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Conserved domains on  [gi|1829481091|ref|XP_033151881|]
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voltage-dependent calcium channel subunit alpha-2/delta-3 isoform X5 [Drosophila mauritiana]

Protein Classification

methyl-accepting chemotaxis protein( domain architecture ID 13750223)

methyl-accepting chemotaxis protein (MCP) is a bacterial receptor that mediates chemotaxis to diverse signals, responding to changes in the concentration of attractants and repellents in the environment by altering swimming behavior

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 ...
 253-439 1.46e-100

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: 317.41  E-value: 1.46e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  253 RLRSWYMEAATSPKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIR 332
Cdd:cd01463      1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  333 ELKEGIELFRPKSIANYTAALTKAFELLEE---TKLSSRGAQCNQAIMIIGDGAPENNREVFELHNWRDPPYKPVRVFTY 409
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNSEIPVRVFTY 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1829481091  410 LIGKEVANWDDIRWMACENQGYYVHLSDTA 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 ...
 107-241 5.31e-51

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


:

Pssm-ID: 462464  Cd Length: 122  Bit Score: 175.56  E-value: 5.31e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  107 AENTALSHQ-NDMADKMFSYYSAKEMLEPGDpvppiptpapdmdkDIGEPLIYVQPKVVVLEPRPEFHNTPVNFSVSSVH 185
Cdd:pfam08399    1 AEKAAEDHEwNDNVPNDFQYYNAKYSNDVGE--------------DYEKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVH 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  186 VPVNVFDRAPDVIKAIQWSENLDQIFRDNYKNDPTLSWQFFGSSTGFMRQFPASKW 241
Cdd:pfam08399   67 VPTNVYDRAPDVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VGCC_alpha2 super family cl07190
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 852-1066 2.59e-14

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: 76.65  E-value: 2.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  852 GVTVAFLATHSGLTRWheFHSNAAEESGVGETFSQNNtraideiWYKRAVDQHF-----VREESFVYSVPFDagESNSEI 926
Cdd:pfam08473   84 GLLAVFAATDGGITRV--PPKSAGDWWEEAEETYESS-------FYRRSLDNDYyfftpPYFNSSYRPNEEE--DDTSGI 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  927 LVTAshAVFHNEGGKTAPAAVVGFQFQHSALYKLFHNITGN--------ACAVDDK--DCYILDNNGYVIISTRVH---E 993
Cdd:pfam08473  153 LVSA--AVELIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRKdqcdeeccGCKGNDDllCCVLDDDGGFLMMSNQDDyieQ 230

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  994 TGRFFGEVNGAIMKRLLEENVYRQVTVYDYQAVCfESKNDNNASSMLLS---PLFHLLRVGKWLLHTALWYIVQLL 1066
Cdd:pfam08473  231 IGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCC-PPKESSKAAAGRRSvvvPTIADLLNLWWWTSAAAWSIQQQL 305
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 587-709 3.04e-08

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: 52.38  E-value: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  587 EIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDfrpifQGYILKPAYnsvdmievelldddrparDFNPVLMTIRDSIINQS 666
Cdd:cd12912      1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD-----KELVGKKIS------------------DDEAAEEELAKKMLAGK 57

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1829481091  667 TGSKWMLVKNhfdemkrvarIKRQYYWTAIKKTPFTLVISYPE 709
Cdd:cd12912     58 SGSVEYTFNG----------EKKYVAYAPIPGTGWSLVVVVPE 90
 
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 ...
 253-439 1.46e-100

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: 317.41  E-value: 1.46e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  253 RLRSWYMEAATSPKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIR 332
Cdd:cd01463      1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  333 ELKEGIELFRPKSIANYTAALTKAFELLEE---TKLSSRGAQCNQAIMIIGDGAPENNREVFELHNWRDPPYKPVRVFTY 409
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNSEIPVRVFTY 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1829481091  410 LIGKEVANWDDIRWMACENQGYYVHLSDTA 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 ...
 107-241 5.31e-51

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


Pssm-ID: 462464  Cd Length: 122  Bit Score: 175.56  E-value: 5.31e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  107 AENTALSHQ-NDMADKMFSYYSAKEMLEPGDpvppiptpapdmdkDIGEPLIYVQPKVVVLEPRPEFHNTPVNFSVSSVH 185
Cdd:pfam08399    1 AEKAAEDHEwNDNVPNDFQYYNAKYSNDVGE--------------DYEKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVH 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  186 VPVNVFDRAPDVIKAIQWSENLDQIFRDNYKNDPTLSWQFFGSSTGFMRQFPASKW 241
Cdd:pfam08399   67 VPTNVYDRAPDVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 267-440 1.19e-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: 79.04  E-value: 1.19e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091   267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTL---GTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIRELKegielFRP 343
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS-----YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091   344 KSIANYTAALTKAFELLEETKLSSRgAQCNQAIMIIGDGAPENNREVF-----ELHNwrdppyKPVRVFTYLIGKEVaNW 418
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAGSR-RGAPKVVILITDGESNDGPKDLlkaakELKR------SGVKVFVVGVGNDV-DE 147

                           170       180
                    ....*....|....*....|..
gi 1829481091   419 DDIRWMACENQGYYVHLSDTAE 440
Cdd:smart00327  148 EELKKLASAPGGVYVFLPELLD 169
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 852-1066 2.59e-14

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: 76.65  E-value: 2.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  852 GVTVAFLATHSGLTRWheFHSNAAEESGVGETFSQNNtraideiWYKRAVDQHF-----VREESFVYSVPFDagESNSEI 926
Cdd:pfam08473   84 GLLAVFAATDGGITRV--PPKSAGDWWEEAEETYESS-------FYRRSLDNDYyfftpPYFNSSYRPNEEE--DDTSGI 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  927 LVTAshAVFHNEGGKTAPAAVVGFQFQHSALYKLFHNITGN--------ACAVDDK--DCYILDNNGYVIISTRVH---E 993
Cdd:pfam08473  153 LVSA--AVELIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRKdqcdeeccGCKGNDDllCCVLDDDGGFLMMSNQDDyieQ 230

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  994 TGRFFGEVNGAIMKRLLEENVYRQVTVYDYQAVCfESKNDNNASSMLLS---PLFHLLRVGKWLLHTALWYIVQLL 1066
Cdd:pfam08473  231 IGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCC-PPKESSKAAAGRRSvvvPTIADLLNLWWWTSAAAWSIQQQL 305
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 260-470 3.06e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 68.59  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  260 EAATSPKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPcfedtliQANLGNIRELKEGIE 339
Cdd:COG2304     86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-------PTPATDRAKILAAID 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  340 LFRPKSIANYTAALTKAFELLEETKLSSRgaqcNQAIMIIGDGAPENNREVFE-----LHNWRDppyKPVRVFTYLIGke 414
Cdd:COG2304    159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTDGDANVGITDPEellklAEEARE---EGITLTTLGVG-- 229

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829481091  415 vANWDD--IRWMACENQGYYVHLSDTAEVREMV---LNYIPVmaRPLVLGRHDHPVIWSQV 470
Cdd:COG2304    230 -SDYNEdlLERLADAGGGNYYYIDDPEEAEKVFvreFSRIGY--ENRALATEDFPLPYGTL 287
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 587-709 3.04e-08

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: 52.38  E-value: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  587 EIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDfrpifQGYILKPAYnsvdmievelldddrparDFNPVLMTIRDSIINQS 666
Cdd:cd12912      1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD-----KELVGKKIS------------------DDEAAEEELAKKMLAGK 57

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1829481091  667 TGSKWMLVKNhfdemkrvarIKRQYYWTAIKKTPFTLVISYPE 709
Cdd:cd12912     58 SGSVEYTFNG----------EKKYVAYAPIPGTGWSLVVVVPE 90
VWA_2 pfam13519
von Willebrand factor type A domain;
268-379 3.48e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 52.68  E-value: 3.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  268 IVILMDGSGSMLG-----QRLDIAKHVVNTILDTLGtNDFVNIFTFDKEVSPVVPcFEDtliqanlgNIRELKEGIELFR 342
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEVLIP-LTK--------DRAKILRALRRLE 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1829481091  343 PKSIA-NYTAALTKAFELLEEtklssRGAQCNQAIMII 379
Cdd:pfam13519   71 PKGGGtNLAAALQLARAALKH-----RRKNQPRRIVLI 103
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 574-625 9.79e-06

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: 48.49  E-value: 9.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1829481091  574 NILGVAGTDVPINEIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDFRPIFQGY 625
Cdd:pfam02743  140 EVIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLL 191
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 265-349 6.00e-03

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 40.37  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  265 PKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPcFEDtliqanlgNIRELKEGIELFRPK 344
Cdd:TIGR03436   53 PLTVGLVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRLLQD-FTS--------DPRLLEAALNRLKPP 123


                   ....*
gi 1829481091  345 SIANY 349
Cdd:TIGR03436  124 LRTDY 128
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
 587-624 6.87e-03

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995 [Multi-domain]  Cd Length: 91  Bit Score: 37.23  E-value: 6.87e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1829481091   587 EIKKLLSPFTLGVNGYAFIVTNNGYVLFHPdFRPIFQG 624
Cdd:smart01049   40 QAKAALRALRYGGDGYFFVYDSDGVMLMHP-AKPELEG 76
 
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 ...
 253-439 1.46e-100

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: 317.41  E-value: 1.46e-100
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  253 RLRSWYMEAATSPKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIR 332
Cdd:cd01463      1 RNRSWYIQAATSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNPVVPCFNDTLVQATTSNKK 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  333 ELKEGIELFRPKSIANYTAALTKAFELLEE---TKLSSRGAQCNQAIMIIGDGAPENNREVFELHNWRDPPYKPVRVFTY 409
Cdd:cd01463     81 VLKEALDMLEAKGIANYTKALEFAFSLLLKnlqSNHSGSRSQCNQAIMLITDGVPENYKEIFDKYNWDKNSEIPVRVFTY 160

                          170       180       190
                   ....*....|....*....|....*....|
gi 1829481091  410 LIGKEVANWDDIRWMACENQGYYVHLSDTA 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 ...
 107-241 5.31e-51

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


Pssm-ID: 462464  Cd Length: 122  Bit Score: 175.56  E-value: 5.31e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  107 AENTALSHQ-NDMADKMFSYYSAKEMLEPGDpvppiptpapdmdkDIGEPLIYVQPKVVVLEPRPEFHNTPVNFSVSSVH 185
Cdd:pfam08399    1 AEKAAEDHEwNDNVPNDFQYYNAKYSNDVGE--------------DYEKGNNVPLSKEFVLTPNPHFYNIPVNTNYSAVH 66

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  186 VPVNVFDRAPDVIKAIQWSENLDQIFRDNYKNDPTLSWQFFGSSTGFMRQFPASKW 241
Cdd:pfam08399   67 VPTNVYDRAPDVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 267-440 1.19e-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: 79.04  E-value: 1.19e-16
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091   267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTL---GTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIRELKegielFRP 343
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLdigPDGDRVGLVTFSDDARVLFPLNDSRSKDALLEALASLS-----YKL 75

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091   344 KSIANYTAALTKAFELLEETKLSSRgAQCNQAIMIIGDGAPENNREVF-----ELHNwrdppyKPVRVFTYLIGKEVaNW 418
Cdd:smart00327   76 GGGTNLGAALQYALENLFSKSAGSR-RGAPKVVILITDGESNDGPKDLlkaakELKR------SGVKVFVVGVGNDV-DE 147

                           170       180
                    ....*....|....*....|..
gi 1829481091   419 DDIRWMACENQGYYVHLSDTAE 440
Cdd:smart00327  148 EELKKLASAPGGVYVFLPELLD 169
vWA_interalpha_trypsin_inhibitor cd01461
vWA_interalpha trypsin inhibitor (ITI): ITI is a glycoprotein composed of three polypeptides- ...
 265-441 1.86e-15

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: 75.33  E-value: 1.86e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  265 PKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCfedtLIQANLGNIRELKEGIELFRPK 344
Cdd:cd01461      2 PKEVVFVIDTSGSMSGTKIEQTKEALLTALKDLPPGDYFNIIGFSDTVEEFSPS----SVSATAENVAAAIEYVNRLQAL 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  345 SIANYTAALTKAFELLEETKLSSRGaqcnqaIMIIGDGAPENNREVfeLHNWRDPPYKPVRVFTYLIGKEVaNWDDIRWM 424
Cdd:cd01461     78 GGTNMNDALEAALELLNSSPGSVPQ------IILLTDGEVTNESQI--LKNVREALSGRIRLFTFGIGSDV-NTYLLERL 148

                          170
                   ....*....|....*..
gi 1829481091  425 ACENQGYYVHLSDTAEV 441
Cdd:cd01461    149 AREGRGIARRIYETDDI 165
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 267-433 9.15e-15

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


Pssm-ID: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 73.37  E-value: 9.15e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTL---GTNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIRELKegielFRP 343
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLsasPPGDRVGLVTFGSNARVVLPLTTDTDKADLLEAIDALK-----KGL 76

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  344 KSIANYTAALTKAFELLEETKLSSRGaqcnQAIMIIGDGAPENNREVFE--LHNWRDppyKPVRVFTYLIGKEvANWDDI 421
Cdd:cd00198     77 GGGTNIGAALRLALELLKSAKRPNAR----RVIILLTDGEPNDGPELLAeaARELRK---LGITVYTIGIGDD-ANEDEL 148

                          170
                   ....*....|..
gi 1829481091  422 RWMACENQGYYV 433
Cdd:cd00198    149 KEIADKTTGGAV 160
VGCC_alpha2 pfam08473
Neuronal voltage-dependent calcium channel alpha 2acd; This eukaryotic domain has been found ...
 852-1066 2.59e-14

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: 76.65  E-value: 2.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  852 GVTVAFLATHSGLTRWheFHSNAAEESGVGETFSQNNtraideiWYKRAVDQHF-----VREESFVYSVPFDagESNSEI 926
Cdd:pfam08473   84 GLLAVFAATDGGITRV--PPKSAGDWWEEAEETYESS-------FYRRSLDNDYyfftpPYFNSSYRPNEEE--DDTSGI 152

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  927 LVTAshAVFHNEGGKTAPAAVVGFQFQHSALYKLFHNITGN--------ACAVDDK--DCYILDNNGYVIISTRVH---E 993
Cdd:pfam08473  153 LVSA--AVELIIDGTLLKPAVVGVKLDDSWWMEFFSNTTRKdqcdeeccGCKGNDDllCCVLDDDGGFLMMSNQDDyieQ 230

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  994 TGRFFGEVNGAIMKRLLEENVYRQVTVYDYQAVCfESKNDNNASSMLLS---PLFHLLRVGKWLLHTALWYIVQLL 1066
Cdd:pfam08473  231 IGFFFGEDDPLLMSLLNNSSFYTKKTSYDYQSCC-PPKESSKAAAGRRSvvvPTIADLLNLWWWTSAAAWSIQQQL 305
YfbK COG2304
Secreted protein containing bacterial Ig-like domain and vWFA domain [General function ...
 260-470 3.06e-12

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


Pssm-ID: 441879 [Multi-domain]  Cd Length: 289  Bit Score: 68.59  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  260 EAATSPKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPcfedtliQANLGNIRELKEGIE 339
Cdd:COG2304     86 AEERPPLNLVFVIDVSGSMSGDKLELAKEAAKLLVDQLRPGDRVSIVTFAGDARVLLP-------PTPATDRAKILAAID 158

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  340 LFRPKSIANYTAALTKAFELLEETKLSSRgaqcNQAIMIIGDGAPENNREVFE-----LHNWRDppyKPVRVFTYLIGke 414
Cdd:COG2304    159 RLQAGGGTALGAGLELAYELARKHFIPGR----VNRVILLTDGDANVGITDPEellklAEEARE---EGITLTTLGVG-- 229

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829481091  415 vANWDD--IRWMACENQGYYVHLSDTAEVREMV---LNYIPVmaRPLVLGRHDHPVIWSQV 470
Cdd:COG2304    230 -SDYNEdlLERLADAGGGNYYYIDDPEEAEKVFvreFSRIGY--ENRALATEDFPLPYGTL 287
ViaA COG2425
Uncharacterized conserved protein, contains a von Willebrand factor type A (vWA) domain ...
 265-425 5.44e-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: 67.78  E-value: 5.44e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  265 PKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCFEDTliqanlgNIRELKEGIELFRPK 344
Cdd:COG2425    118 EGPVVLCVDTSGSMAGSKEAAAKAAALALLRALRPNRRFGVILFDTEVVEDLPLTADD-------GLEDAIEFLSGLFAG 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  345 SIANYTAALTKAFELLEETKLSSRgaqcnqAIMIIGDGAPENNREVFeLHNWRDPPYKpVRVFTYLIGKEvANWDDIRWM 424
Cdd:COG2425    191 GGTDIAPALRAALELLEEPDYRNA------DIVLITDGEAGVSPEEL-LREVRAKESG-VRLFTVAIGDA-GNPGLLEAL 261


                   .
gi 1829481091  425 A 425
Cdd:COG2425    262 A 262
ChlD COG1240
vWFA (von Willebrand factor type A) domain of Mg and Co chelatases [Coenzyme transport and ...
 264-445 5.84e-11

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: 64.57  E-value: 5.84e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  264 SPKDIVILMDGSGSMLGQ-RLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPcFEDtliqanlgNIRELKEGIELFR 342
Cdd:COG1240     91 RGRDVVLVVDASGSMAAEnRLEAAKGALLDFLDDYRPRDRVGLVAFGGEAEVLLP-LTR--------DREALKRALDELP 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  343 PKSIANYTAALTKAFELLEETKLSSRgaqcnQAIMIIGDGapENNREVFELHNW----RDppyKPVRVFTYLIGKEVANW 418
Cdd:COG1240    162 PGGGTPLGDALALALELLKRADPARR-----KVIVLLTDG--RDNAGRIDPLEAaelaAA---AGIRIYTIGVGTEAVDE 231

                          170       180
                   ....*....|....*....|....*..
gi 1829481091  419 DDIRWMACENQGYYVHLSDTAEVREMV 445
Cdd:COG1240    232 GLLREIAEATGGRYFRADDLSELAAIY 258
PDC2_MCP_like cd12912
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 587-709 3.04e-08

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: 52.38  E-value: 3.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  587 EIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDfrpifQGYILKPAYnsvdmievelldddrparDFNPVLMTIRDSIINQS 666
Cdd:cd12912      1 ELSEIISSIKIGETGYAFLVDKDGTIIAHPD-----KELVGKKIS------------------DDEAAEEELAKKMLAGK 57

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1829481091  667 TGSKWMLVKNhfdemkrvarIKRQYYWTAIKKTPFTLVISYPE 709
Cdd:cd12912     58 SGSVEYTFNG----------EKKYVAYAPIPGTGWSLVVVVPE 90
VWA_2 pfam13519
von Willebrand factor type A domain;
268-379 3.48e-08

von Willebrand factor type A domain;


Pssm-ID: 463909 [Multi-domain]  Cd Length: 103  Bit Score: 52.68  E-value: 3.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  268 IVILMDGSGSMLG-----QRLDIAKHVVNTILDTLGtNDFVNIFTFDKEVSPVVPcFEDtliqanlgNIRELKEGIELFR 342
Cdd:pfam13519    1 LVFVLDTSGSMRNgdygpTRLEAAKDAVLALLKSLP-GDRVGLVTFGDGPEVLIP-LTK--------DRAKILRALRRLE 70

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1829481091  343 PKSIA-NYTAALTKAFELLEEtklssRGAQCNQAIMII 379
Cdd:pfam13519   71 PKGGGtNLAAALQLARAALKH-----RRKNQPRRIVLI 103
VWA_3 pfam13768
von Willebrand factor type A domain;
266-433 6.91e-08

von Willebrand factor type A domain;


Pssm-ID: 372716 [Multi-domain]  Cd Length: 155  Bit Score: 53.17  E-value: 6.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  266 KDIVILMDGSGSMLGQRLDIaKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPCFeDTLIQANLgniRELKEGIELFRPKS 345
Cdd:pfam13768    1 GDVVIVVDVSSSMSGEPKLQ-KDALSVALRQLPTGDKFAVLGFGTLPRPLFPGW-RVVSPRSL---QEAFQFIKTLQPPL 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  346 IA-NYTAALTKAFELLEETklssrgaQCNQAIMIIGDGAPENNREVFElHNWRDPPYKpVRVFTYLIGKEVaNWDDIRWM 424
Cdd:pfam13768   76 GGsDLLGALKEAVRAPASP-------GYIRHVLLLTDGSPMQGETRVS-DLISRAPGK-IRFFAYGLGASI-SAPMLQLL 145


                   ....*....
gi 1829481091  425 ACENQGYYV 433
Cdd:pfam13768  146 AEASNGTYE 154
vWA_C3HC4_type cd01466
VWA C3HC4-type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 267-412 3.06e-07

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


Pssm-ID: 238743 [Multi-domain]  Cd Length: 155  Bit Score: 51.24  E-value: 3.06e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPcfedtLIQANLGNIRELKEGIELFRPKSI 346
Cdd:cd01466      2 DLVAVLDVSGSMAGDKLQLVKHALRFVISSLGDADRLSIVTFSTSAKRLSP-----LRRMTAKGKRSAKRVVDGLQAGGG 76

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1829481091  347 ANYTAALTKAFELLEETKLSSRGAqcnqAIMIIGDGAPenNREVFELHnwRDPPykPVRVFTYLIG 412
Cdd:cd01466     77 TNVVGGLKKALKVLGDRRQKNPVA----SIMLLSDGQD--NHGAVVLR--ADNA--PIPIHTFGLG 132
PDC2_HK_sensor cd18774
second PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, ...
 587-709 6.96e-07

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: 48.59  E-value: 6.96e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  587 EIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDFRPIFQGyilkpaynsvdmievelldddrparDFNPVLMTIRDSIINQS 666
Cdd:cd18774      1 YLSDLLSSIKLGETGYAFLVDSDGTILAHPPKELVGKG-------------------------KSLDDLALLAALLLAGE 55

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1829481091  667 TGskwmlvknhFDEMKRVARIKRQYYWTAIKKTPFTLVISYPE 709
Cdd:cd18774     56 SG---------TFEYTSDDGVERLVAYRPVPGTPWVVVVGVPE 89
VWA pfam00092
von Willebrand factor type A domain;
267-445 1.43e-06

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 49.97  E-value: 1.43e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTLG---TNDFVNIFTFDKEVSPVVPCFEDTLIQANLGNIRELKegielFRP 343
Cdd:pfam00092    1 DIVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVRTEFPLNDYSSKEELLSAVDNLR-----YLG 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  344 KSIANYTAALTKAFELLEETKLSSRgAQCNQAIMIIGDGAPENNREVFELHNwrdppYKPVRVFTYLIGKEVANWDDIRW 423
Cdd:pfam00092   76 GGTTNTGKALKYALENLFSSAAGAR-PGAPKVVVLLTDGRSQDGDPEEVARE-----LKSAGVTVFAVGVGNADDEELRK 149

                          170       180
                   ....*....|....*....|...
gi 1829481091  424 MACE-NQGYYVHLSDTAEVREMV 445
Cdd:pfam00092  150 IASEpGEGHVFTVSDFEALEDLQ 172
TerY COG4245
Uncharacterized conserved protein YegL, contains vWA domain of TerY type [Function unknown];
267-384 3.99e-06

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


Pssm-ID: 443387 [Multi-domain]  Cd Length: 196  Bit Score: 48.77  E-value: 3.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTND------FVNIFTFDKEVSPVVPcFEDtliqanlgnirelkegIEL 340
Cdd:COG4245      7 PVYLLLDTSGSMSGEPIEALNEGLQALIDELRQDPyaletvEVSVITFDGEAKVLLP-LTD----------------LED 69

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1829481091  341 FRPKSIA-----NYTAALTKAFELLEETKLSSRGAQ---CNQAIMIIGDGAP 384
Cdd:COG4245     70 FQPPDLSasggtPLGAALELLLDLIERRVQKYTAEGkgdWRPVVFLITDGEP 121
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 269-317 9.06e-06

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


Pssm-ID: 238742 [Multi-domain]  Cd Length: 170  Bit Score: 47.27  E-value: 9.06e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1829481091  269 VILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVP 317
Cdd:cd01465      4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAETVLP 52
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 574-625 9.79e-06

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: 48.49  E-value: 9.79e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1829481091  574 NILGVAGTDVPINEIKKLLSPFTLGVNGYAFIVTNNGYVLFHPDFRPIFQGY 625
Cdd:pfam02743  140 EVIGVLVADLDLDTLQELLSQIKLGEGGYVFIVDSDGRILAHPLGKNLRSLL 191
vWFA_subfamily_ECM cd01450
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 267-392 1.14e-03

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: 41.12  E-value: 1.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  267 DIVILMDGSGSMLGQRLDIAKHVVNTILDTL---GTNDFVNIFTFDKEVSPVVPCFEDTliqanlgNIRELKEGIELFRP 343
Cdd:cd01450      2 DIVFLLDGSESVGPENFEKVKDFIEKLVEKLdigPDKTRVGLVQYSDDVRVEFSLNDYK-------SKDDLLKAVKNLKY 74

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1829481091  344 K--SIANYTAALTKAFELLEETKLSSRGAqcNQAIMIIGDGAPENNREVFE 392
Cdd:cd01450     75 LggGGTNTGKALQYALEQLFSESNARENV--PKVIIVLTDGRSDDGGDPKE 123
VWA_YIEM_type cd01462
VWA YIEM type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 266-395 2.06e-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: 40.02  E-value: 2.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  266 KDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTN--DFVNIF---TFDKEVSPVVPCFEDTL-----IQANLGnirelk 335
Cdd:cd01462      1 GPVILLVDQSGSMYGAPEEVAKAVALALLRIALAEnrDTYLILfdsEFQTKIVDKTDDLEEPVeflsgVQLGGG------ 74

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1829481091  336 egielfrpksiANYTAALTKAFELLEETKLssRGAQcnqaIMIIGDG-APENNREVFELHN 395
Cdd:cd01462     75 -----------TDINKALRYALELIERRDP--RKAD----IVLITDGyEGGVSDELLREVE 118
vWA_BatA_type cd01467
VWA BatA type: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 267-387 4.08e-03

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: 39.62  E-value: 4.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  267 DIVILMDGSGSMLGQ------RLDIAKHVVNTILDTLgTNDFVNIFTFDKEVSPVVPCfedTLIQANLGN-IRELKEGIe 339
Cdd:cd01467      4 DIMIALDVSGSMLAQdfvkpsRLEAAKEVLSDFIDRR-ENDRIGLVVFAGAAFTQAPL---TLDRESLKElLEDIKIGL- 78

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1829481091  340 lfrpksIANYTA---ALTKAFELLEETKLSSRgaqcnqAIMIIGDGapENN 387
Cdd:cd01467     79 ------AGQGTAigdAIGLAIKRLKNSEAKER------VIVLLTDG--ENN 115
acidobact_VWFA TIGR03436
VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include ...
 265-349 6.00e-03

VWFA-related Acidobacterial domain; Members of this family are bacterial domains that include a region related to the von Willebrand factor type A (VWFA) domain (pfam00092). These domains are restricted to, and have undergone a large paralogous family expansion in, the Acidobacteria, including Solibacter usitatus and Acidobacterium capsulatum ATCC 51196.


Pssm-ID: 274577 [Multi-domain]  Cd Length: 296  Bit Score: 40.37  E-value: 6.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1829481091  265 PKDIVILMDGSGSMLGQRLDIAKHVVNTILDTLGTNDFVNIFTFDKEVSPVVPcFEDtliqanlgNIRELKEGIELFRPK 344
Cdd:TIGR03436   53 PLTVGLVIDTSGSMRNDLDRARAAAIRFLKTVLRPNDRVFVVTFNTRLRLLQD-FTS--------DPRLLEAALNRLKPP 123


                   ....*
gi 1829481091  345 SIANY 349
Cdd:TIGR03436  124 LRTDY 128
Cache_2 smart01049
Cache is an extracellular domain that is predicted to have a role in small-molecule ...
 587-624 6.87e-03

Cache is an extracellular domain that is predicted to have a role in small-molecule recognition in a wide range of proteins; Members include the animal dihydropyridine-sensitive voltage-gated Ca2+ channel; alpha-2delta subunit, and various bacterial chemotaxis receptors. The name Cache comes from CAlcium channels and CHEmotaxis receptors. This domain consists of an N-terminal part with three predicted strands and an alpha-helix, and a C-terminal part with a strand dyad followed by a relatively unstructured region. The N-terminal portion of the (unpermuted) Cache domain contains three predicted strands that could form a sheet analogous to that present in the core of the PAS domain structure. Cache domains are particularly widespread in bacteria, with Vibrio cholerae. The animal calcium channel alpha-2delta subunits might have acquired a part of their extracellular domains from a bacterial source. The Cache domain appears to have arisen from the GAF-PAS fold despite their divergent functions.


Pssm-ID: 214995 [Multi-domain]  Cd Length: 91  Bit Score: 37.23  E-value: 6.87e-03
                            10        20        30
                    ....*....|....*....|....*....|....*...
gi 1829481091   587 EIKKLLSPFTLGVNGYAFIVTNNGYVLFHPdFRPIFQG 624
Cdd:smart01049   40 QAKAALRALRYGGDGYFFVYDSDGVMLMHP-AKPELEG 76
 
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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