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Conserved domains on  [gi|1417916997|ref|NP_065976|]
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VWFA and cache domain-containing protein 1 isoform 1 precursor [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 89-204 2.41e-24

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: 99.29  E-value: 2.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   89 AKKIREKFN---------RYLDVVNRN---------------KQVVEASYTAHLTSPLTAIQDCCTIPPSMMEfdgnfnt 144
Cdd:pfam08399    1 AEKAAEDHEwndnvpndfQYYNAKYSNdvgedyekgnnvplsKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYD------- 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  145 nvsrtiscdrlSTTVNSRAFNPGRDLNSVLADNLKSNPGIKWQYFSSEEGIFTVFPAHKF 204
Cdd:pfam08399   74 -----------RAPDVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 674-868 1.00e-07

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: 54.27  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  674 TKRMVEHYTAYLSDNTRLIA-NPGLKFSVRNEVMATShvtdewMTQMEMSSLNTYIVRRYIATPNGVLRIYPG-SLMDKA 751
Cdd:pfam02743   18 LAENIESYLDSLEEILELLAsNPDLQDLLSAPAEEEL------AKLESLLRSNPGISSIYLVDADGRVLASSDeSPSYPG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  752 FDPTRRQWYLHAVAN--PGLISLTGPYLDVGGAGYVVTISHTIHSSStqlssGHTVAVMGIDFTLRYFYKVLMDLLPvcn 829
Cdd:pfam02743   92 LDVSERPWYKEALKGggGIIWVFSSPYPSSESGEPVLTIARPIYDDD-----GEVIGVLVADLDLDTLQELLSQIKL--- 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1417916997  830 qdgGNKIRCFIMEDRGYLVAHPTLIDPKGHAPVEQQHIT 868
Cdd:pfam02743  164 ---GEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSL 199
vWFA super family cl00057
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 213-408 1.30e-07

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.


The actual alignment was detected with superfamily member cd01463:

Pssm-ID: 469594 [Multi-domain]  Cd Length: 190  Bit Score: 53.17  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  213 RSRPIYVSTVrPQSKHIVVILDHGASVTDTQLQIAKDAAQVILSAIDEHDKISVLTVADTVRTcsLDQCYKTFLSPATSE 292
Cdd:cd01463      1 RNRSWYIQAA-TSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNP--VVPCFNDTLVQATTS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  293 TKRKMSTFVSSVKSSDSPtQHAVGFQKAFQLIR----STNNNTKFQANTDMVIIylsagitsKDSSEEDKKatlQVINEE 368
Cdd:cd01463     78 NKKVLKEALDMLEAKGIA-NYTKALEFAFSLLLknlqSNHSGSRSQCNQAIMLI--------TDGVPENYK---EIFDKY 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1417916997  369 NSFLNNS--VMILTYaLMNDGVTGLKElafLRDLAEQNSGKY 408
Cdd:cd01463    146 NWDKNSEipVRVFTY-LIGREVTDRRE---IQWMACENKGYY 183
HK_sensor super family cl38916
Sensor domains of Histidine Kinase receptors; Histidine kinase (HK) receptors are part of ...
 449-489 1.03e-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: 40.59  E-value: 1.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1417916997  449 DEAVFSLPFSDEMGDG-LIMTVSKPCYFGNLLLGIVGVDVNL 489
Cdd:cd12913     98 GKPVWTEPYIDEVGTGvLMITISVPIYDNGKFIGVVGVDISL 139
 
Name Accession Description Interval E-value
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 89-204 2.41e-24

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: 99.29  E-value: 2.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   89 AKKIREKFN---------RYLDVVNRN---------------KQVVEASYTAHLTSPLTAIQDCCTIPPSMMEfdgnfnt 144
Cdd:pfam08399    1 AEKAAEDHEwndnvpndfQYYNAKYSNdvgedyekgnnvplsKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYD------- 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  145 nvsrtiscdrlSTTVNSRAFNPGRDLNSVLADNLKSNPGIKWQYFSSEEGIFTVFPAHKF 204
Cdd:pfam08399   74 -----------RAPDVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 674-868 1.00e-07

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: 54.27  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  674 TKRMVEHYTAYLSDNTRLIA-NPGLKFSVRNEVMATShvtdewMTQMEMSSLNTYIVRRYIATPNGVLRIYPG-SLMDKA 751
Cdd:pfam02743   18 LAENIESYLDSLEEILELLAsNPDLQDLLSAPAEEEL------AKLESLLRSNPGISSIYLVDADGRVLASSDeSPSYPG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  752 FDPTRRQWYLHAVAN--PGLISLTGPYLDVGGAGYVVTISHTIHSSStqlssGHTVAVMGIDFTLRYFYKVLMDLLPvcn 829
Cdd:pfam02743   92 LDVSERPWYKEALKGggGIIWVFSSPYPSSESGEPVLTIARPIYDDD-----GEVIGVLVADLDLDTLQELLSQIKL--- 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1417916997  830 qdgGNKIRCFIMEDRGYLVAHPTLIDPKGHAPVEQQHIT 868
Cdd:pfam02743  164 ---GEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSL 199
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 213-408 1.30e-07

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: 53.17  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  213 RSRPIYVSTVrPQSKHIVVILDHGASVTDTQLQIAKDAAQVILSAIDEHDKISVLTVADTVRTcsLDQCYKTFLSPATSE 292
Cdd:cd01463      1 RNRSWYIQAA-TSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNP--VVPCFNDTLVQATTS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  293 TKRKMSTFVSSVKSSDSPtQHAVGFQKAFQLIR----STNNNTKFQANTDMVIIylsagitsKDSSEEDKKatlQVINEE 368
Cdd:cd01463     78 NKKVLKEALDMLEAKGIA-NYTKALEFAFSLLLknlqSNHSGSRSQCNQAIMLI--------TDGVPENYK---EIFDKY 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1417916997  369 NSFLNNS--VMILTYaLMNDGVTGLKElafLRDLAEQNSGKY 408
Cdd:cd01463    146 NWDKNSEipVRVFTY-LIGREVTDRRE---IQWMACENKGYY 183
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 752-814 5.90e-06

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: 47.14  E-value: 5.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1417916997  752 FDPTRRQWYLHAVANpGLISLTGPYLDVGGAG-YVVTISHTIHssstqlSSGHTVAVMGIDFTL 814
Cdd:cd12913     83 YDYRTRDWYKLAKET-GKPVWTEPYIDEVGTGvLMITISVPIY------DNGKFIGVVGVDISL 139
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 228-408 2.54e-04

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: 43.21  E-value: 2.54e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   228 HIVVILDHGASVTDTQLQIAKDAAQVILSAIDE---HDKISVLTVADTVRtcsldqcykTFLSPATSETKRKMSTFVSSV 304
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDAR---------VLFPLNDSRSKDALLEALASL 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   305 K---SSDSPTQHAVgfQKAFQLIRSTNNNTKFQANTdmVIIYLSAGItsKDSSEEDKKATLQVINEENsflnnsvmILTY 381
Cdd:smart00327   72 SyklGGGTNLGAAL--QYALENLFSKSAGSRRGAPK--VVILITDGE--SNDGPKDLLKAAKELKRSG--------VKVF 137

                           170       180
                    ....*....|....*....|....*..
gi 1417916997   382 ALmndGVTGLKELAFLRDLAEQNSGKY 408
Cdd:smart00327  138 VV---GVGNDVDEEELKKLASAPGGVY 161
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 449-489 1.03e-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: 40.59  E-value: 1.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1417916997  449 DEAVFSLPFSDEMGDG-LIMTVSKPCYFGNLLLGIVGVDVNL 489
Cdd:cd12913     98 GKPVWTEPYIDEVGTGvLMITISVPIYDNGKFIGVVGVDISL 139
VWA pfam00092
von Willebrand factor type A domain;
229-395 2.27e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 40.34  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  229 IVVILDHGASVTDTQLQIAKDAAQVILSAID---EHDKISVLTVADTVRtcsldqcykTFLSPATSETKRKMSTFVSSVK 305
Cdd:pfam00092    2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVR---------TEFPLNDYSSKEELLSAVDNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  306 SSDSPTQH-AVGFQKAFQLIRSTNNNTKFQANTDMVIiylsagITSKDSSEEDKKATLQVINEENsflnnsVMILTYALM 384
Cdd:pfam00092   73 YLGGGTTNtGKALKYALENLFSSAAGARPGAPKVVVL------LTDGRSQDGDPEEVARELKSAG------VTVFAVGVG 140

                          170
                   ....*....|.
gi 1417916997  385 NDGVTGLKELA 395
Cdd:pfam00092  141 NADDEELRKIA 151
 
Name Accession Description Interval E-value
VWA_N pfam08399
VWA N-terminal; This domain is found at the N-terminus of proteins containing von Willebrand ...
 89-204 2.41e-24

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: 99.29  E-value: 2.41e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   89 AKKIREKFN---------RYLDVVNRN---------------KQVVEASYTAHLTSPLTAIQDCCTIPPSMMEfdgnfnt 144
Cdd:pfam08399    1 AEKAAEDHEwndnvpndfQYYNAKYSNdvgedyekgnnvplsKEFVLTPNPHFYNIPVNTNYSAVHVPTNVYD------- 73

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  145 nvsrtiscdrlSTTVNSRAFNPGRDLNSVLADNLKSNPGIKWQYFSSEEGIFTVFPAHKF 204
Cdd:pfam08399   74 -----------RAPDVLNGINWSEALDDVFRDNYEEDPSLSWQYFGSATGFFRYYPASKW 122
dCache_1 pfam02743
Cache domain; Double cache domain 1 covers the last three strands from the membrane distal ...
 674-868 1.00e-07

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: 54.27  E-value: 1.00e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  674 TKRMVEHYTAYLSDNTRLIA-NPGLKFSVRNEVMATShvtdewMTQMEMSSLNTYIVRRYIATPNGVLRIYPG-SLMDKA 751
Cdd:pfam02743   18 LAENIESYLDSLEEILELLAsNPDLQDLLSAPAEEEL------AKLESLLRSNPGISSIYLVDADGRVLASSDeSPSYPG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  752 FDPTRRQWYLHAVAN--PGLISLTGPYLDVGGAGYVVTISHTIHSSStqlssGHTVAVMGIDFTLRYFYKVLMDLLPvcn 829
Cdd:pfam02743   92 LDVSERPWYKEALKGggGIIWVFSSPYPSSESGEPVLTIARPIYDDD-----GEVIGVLVADLDLDTLQELLSQIKL--- 163

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1417916997  830 qdgGNKIRCFIMEDRGYLVAHPTLIDPKGHAPVEQQHIT 868
Cdd:pfam02743  164 ---GEGGYVFIVDSDGRILAHPLGKNLRSLLAPFLGKSL 199
vWA_VGCC_like cd01463
VWA Voltage gated Calcium channel like: Voltage-gated calcium channels are a complex of five ...
 213-408 1.30e-07

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: 53.17  E-value: 1.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  213 RSRPIYVSTVrPQSKHIVVILDHGASVTDTQLQIAKDAAQVILSAIDEHDKISVLTVADTVRTcsLDQCYKTFLSPATSE 292
Cdd:cd01463      1 RNRSWYIQAA-TSPKDIVILLDVSGSMTGQRLHLAKQTVSSILDTLSDNDFFNIITFSNEVNP--VVPCFNDTLVQATTS 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  293 TKRKMSTFVSSVKSSDSPtQHAVGFQKAFQLIR----STNNNTKFQANTDMVIIylsagitsKDSSEEDKKatlQVINEE 368
Cdd:cd01463     78 NKKVLKEALDMLEAKGIA-NYTKALEFAFSLLLknlqSNHSGSRSQCNQAIMLI--------TDGVPENYK---EIFDKY 145

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1417916997  369 NSFLNNS--VMILTYaLMNDGVTGLKElafLRDLAEQNSGKY 408
Cdd:cd01463    146 NWDKNSEipVRVFTY-LIGREVTDRRE---IQWMACENKGYY 183
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 752-814 5.90e-06

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: 47.14  E-value: 5.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1417916997  752 FDPTRRQWYLHAVANpGLISLTGPYLDVGGAG-YVVTISHTIHssstqlSSGHTVAVMGIDFTL 814
Cdd:cd12913     83 YDYRTRDWYKLAKET-GKPVWTEPYIDEVGTGvLMITISVPIY------DNGKFIGVVGVDISL 139
VWA smart00327
von Willebrand factor (vWF) type A domain; VWA domains in extracellular eukaryotic proteins ...
 228-408 2.54e-04

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: 43.21  E-value: 2.54e-04
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   228 HIVVILDHGASVTDTQLQIAKDAAQVILSAIDE---HDKISVLTVADTVRtcsldqcykTFLSPATSETKRKMSTFVSSV 304
Cdd:smart00327    1 DVVFLLDGSGSMGGNRFELAKEFVLKLVEQLDIgpdGDRVGLVTFSDDAR---------VLFPLNDSRSKDALLEALASL 71

                            90       100       110       120       130       140       150       160
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997   305 K---SSDSPTQHAVgfQKAFQLIRSTNNNTKFQANTdmVIIYLSAGItsKDSSEEDKKATLQVINEENsflnnsvmILTY 381
Cdd:smart00327   72 SyklGGGTNLGAAL--QYALENLFSKSAGSRRGAPK--VVILITDGE--SNDGPKDLLKAAKELKRSG--------VKVF 137

                           170       180
                    ....*....|....*....|....*..
gi 1417916997   382 ALmndGVTGLKELAFLRDLAEQNSGKY 408
Cdd:smart00327  138 VV---GVGNDVDEEELKKLASAPGGVY 161
PDC1_HK_sensor cd18773
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins, diguanylate-cyclase ...
 732-814 5.24e-04

first 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: 350341 [Multi-domain]  Cd Length: 125  Bit Score: 41.39  E-value: 5.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  732 YIATPNGVLRIY--PGSLMDKAFDPTRRQWYLHAVANPGLIsLTGPYLDVGGAGYVVTISHTIHSsstqlSSGHTVAVMG 809
Cdd:cd18773     47 YVVDADGRVVASsdRDPGGGDDDDDRDRFWYQAAKATGKLV-ISEPYISRVTGKPVITLSRPIRD-----ADGRFIGVVG 120


                   ....*
gi 1417916997  810 IDFTL 814
Cdd:cd18773    121 ADIDL 125
PDC1_MCP_like cd12913
first PDC (PhoQ/DcuS/CitA) domain of methyl-accepting chemotaxis proteins and similar domains; ...
 449-489 1.03e-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: 40.59  E-value: 1.03e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1417916997  449 DEAVFSLPFSDEMGDG-LIMTVSKPCYFGNLLLGIVGVDVNL 489
Cdd:cd12913     98 GKPVWTEPYIDEVGTGvLMITISVPIYDNGKFIGVVGVDISL 139
vWA_subgroup cd01465
VWA subgroup: Von Willebrand factor type A (vWA) domain was originally found in the blood ...
 230-324 1.50e-03

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: 40.72  E-value: 1.50e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  230 VVILDHGASVTDTQLQIAKDAAQVILSAIDEHDKISVLTVADTVRTcsldqcyktfLSPATSET-KRKMSTFVSSVKSSD 308
Cdd:cd01465      4 VFVIDRSGSMDGPKLPLVKSALKLLVDQLRPDDRLAIVTYDGAAET----------VLPATPVRdKAAILAAIDRLTAGG 73

                           90
                   ....*....|....*.
gi 1417916997  309 SpTQHAVGFQKAFQLI 324
Cdd:cd01465     74 S-TAGGAGIQLGYQEA 88
vWFA cd00198
Von Willebrand factor type A (vWA) domain was originally found in the blood coagulation ...
 228-360 1.72e-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: 238119 [Multi-domain]  Cd Length: 161  Bit Score: 40.63  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  228 HIVVILDHGASVTDTQLQIAKDAAQVILSAID---EHDKISVLTVADTVRTcsldqcYKTFLSPATSETKRKMSTFVSSV 304
Cdd:cd00198      2 DIVFLLDVSGSMGGEKLDKAKEALKALVSSLSaspPGDRVGLVTFGSNARV------VLPLTTDTDKADLLEAIDALKKG 75

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1417916997  305 KSSDSPTqhAVGFQKAFQLIRSTNNNtkfqaNTDMVIIYLSAGITSKDSSEEDKKA 360
Cdd:cd00198     76 LGGGTNI--GAALRLALELLKSAKRP-----NARRVIILLTDGEPNDGPELLAEAA 124
VWA pfam00092
von Willebrand factor type A domain;
229-395 2.27e-03

von Willebrand factor type A domain;


Pssm-ID: 459670 [Multi-domain]  Cd Length: 174  Bit Score: 40.34  E-value: 2.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  229 IVVILDHGASVTDTQLQIAKDAAQVILSAID---EHDKISVLTVADTVRtcsldqcykTFLSPATSETKRKMSTFVSSVK 305
Cdd:pfam00092    2 IVFLLDGSGSIGGDNFEKVKEFLKKLVESLDigpDGTRVGLVQYSSDVR---------TEFPLNDYSSKEELLSAVDNLR 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1417916997  306 SSDSPTQH-AVGFQKAFQLIRSTNNNTKFQANTDMVIiylsagITSKDSSEEDKKATLQVINEENsflnnsVMILTYALM 384
Cdd:pfam00092   73 YLGGGTTNtGKALKYALENLFSSAAGARPGAPKVVVL------LTDGRSQDGDPEEVARELKSAG------VTVFAVGVG 140

                          170
                   ....*....|.
gi 1417916997  385 NDGVTGLKELA 395
Cdd:pfam00092  141 NADDEELRKIA 151
 
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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