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Conserved domains on  [gi|738070636|ref|WP_036029515|]
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MULTISPECIES: chemoreceptor glutamine deamidase CheD [Burkholderia]

Protein Classification

chemoreceptor glutamine deamidase CheD; chemotaxis protein CheD( domain architecture ID 10014254)

chemoreceptor glutamine deamidase CheD probably deamidates glutamine residues to glutamate on methyl-accepting chemotaxis receptors (MCPs), playing an important role in chemotaxis| chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins, binds to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system, and deamidates selected residues to activate chemoreceptors, enabling them to mediate amino acid chemotaxis

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRK13489 PRK13489
chemoreceptor glutamine deamidase CheD; Provisional
 1-228 1.94e-142

chemoreceptor glutamine deamidase CheD; Provisional


:

Pssm-ID: 237398  Cd Length: 233  Bit Score: 397.27  E-value: 1.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636   1 MSALPIASNHYFDNHFGRPGVKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADARAPASDSMR 80
Cdd:PRK13489   1 MSGLPIATNRYFDNHFHRPGVKLLPNEFYTTREDMVLVTVLGSCVAACLHDPVAGIGGMNHFMLPDDGADAGAAASESMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  81 YGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRT 160
Cdd:PRK13489  81 YGAYAMEVLINELIKAGGRRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALERIRITAEDLQGVHPRKVAFMPRT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738070636 161 GQAMVKKLRLSVPGVAEreaALARSAAEARAARAQRARAHVELFAA-----PAAPKPRVELFGSTAT---TKKQEA 228
Cdd:PRK13489 161 GRAMVKKLRLQVPGVAE---REAALAREAHGERAARARARVELFAApapsaPAPARPRIELFGRRATqnaTRKQEA 233
 
Name Accession Description Interval E-value
PRK13489 PRK13489
chemoreceptor glutamine deamidase CheD; Provisional
 1-228 1.94e-142

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 237398  Cd Length: 233  Bit Score: 397.27  E-value: 1.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636   1 MSALPIASNHYFDNHFGRPGVKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADARAPASDSMR 80
Cdd:PRK13489   1 MSGLPIATNRYFDNHFHRPGVKLLPNEFYTTREDMVLVTVLGSCVAACLHDPVAGIGGMNHFMLPDDGADAGAAASESMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  81 YGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRT 160
Cdd:PRK13489  81 YGAYAMEVLINELIKAGGRRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALERIRITAEDLQGVHPRKVAFMPRT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738070636 161 GQAMVKKLRLSVPGVAEreaALARSAAEARAARAQRARAHVELFAA-----PAAPKPRVELFGSTAT---TKKQEA 228
Cdd:PRK13489 161 GRAMVKKLRLQVPGVAE---REAALAREAHGERAARARARVELFAApapsaPAPARPRIELFGRRATqnaTRKQEA 233
CheD COG1871
Chemotaxis receptor (MCP) glutamine deamidase CheD [Signal transduction mechanisms];
14-169 4.00e-70

Chemotaxis receptor (MCP) glutamine deamidase CheD [Signal transduction mechanisms];


Pssm-ID: 441475  Cd Length: 164  Bit Score: 211.58  E-value: 4.00e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  14 NHFGRPGVKLLPNEF-FTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADarAPASDSMRYGAYAMEVLINE 92
Cdd:COG1871    2 SNAGMKEIKVGPGEYyVSTDPDTLITTGLGSCVAVCLYDPVAKIGGMNHFMLPDSSGA--KAAGNPAKYGDTAMELLINE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738070636  93 LIKAGGKRERFEAKVFGGAAVLAGMT--TINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVKKLR 169
Cdd:COG1871   80 LLKLGARRERLEAKIFGGANMFSGLSsdSLNIGERNVEAAREYLAEEGIPIVAEDVGGNYGRTVEFDPATGRVLVKTLG 158
CheD cd16352
chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins; This ...
 21-166 3.57e-63

chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins; This family contains bacterial chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). The CheD chemotaxis gene is not found in the Escherichia coli genome, but is present in many other organisms, including B. subtilis, where CheD appears to have two separate roles; it binds to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system, and it deamidates selected residues to activate chemoreceptors, enabling them to mediate amino acid chemotaxis. CheD has been shown to catalyze amide hydrolysis of specific glutaminyl side chains of the B. subtilis chemoreceptors McpA, McpB and McpC; deamination by CheD is required for the chemoreceptors to effectively transduce signals to the CheA kinase. CheD's ability to bind the receptors is controlled by CheC via a competitive binding mechanism; substituting Gln into the receptor motif of the signal-terminating phosphatase, CheC, turns the inhibitor into a receptor-modifying deamidase CheD substrate. Also, CheYp increases the affinity of CheD for CheC, controlling CheD binding to the receptors through its interactions with CheC. Thus, high levels of CheYp means CheC is a better binding target for CheD than the receptors, resulting in decreased CheA activity. The CheD structure reveals a distant homology with a class of bacterial toxins represented by the cytotoxic necrotizing factor 1 (CNF1) as well as a class of proteins of unknown function represented by B. subtilis YfiH. An invariant Cys-His pair forming a catalytic dyad is observed, and is required by the toxins for deamidation activity.


Pssm-ID: 319352  Cd Length: 146  Bit Score: 193.45  E-value: 3.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  21 VKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADarAPASDSMRYGAYAMEVLINELIKAGGKR 100
Cdd:cd16352    2 IFVGPGEYYVSRGPTVLSTLLGSCVAVCLYDPVAKIGGMNHFMLPESSGD--KEASNPGKYADTAIELLLNELLKLGARR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738070636 101 ERFEAKVFGGAAVLAGM-TTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVK 166
Cdd:cd16352   80 SRLEAKLFGGANMFPGSsGLLNIGERNIEAARELLAKEGIPIVAEDVGGNYGRTVRFDPATGEVLVK 146
CheD pfam03975
CheD chemotactic sensory transduction; This chemotaxis protein stimulates methylation of MCP ...
 63-167 4.69e-43

CheD chemotactic sensory transduction; This chemotaxis protein stimulates methylation of MCP proteins. The chemotaxis machinery of Bacillus subtilis is similar to that of the well characterized system of Escherichia coli. However, B. subtilis contains several chemotaxis genes not found in the E. coli genome, such as CheC and CheD, indicating that the B. subtilis chemotactic system is more complex. CheD plays an important role in chemotactic sensory transduction for many organizms. CheD deamidates other B. subtilis chemoreceptors including McpB and McpC. Deamidation by CheD is required for B. subtilis chemoreceptors to effectively transduce signals to the CheA kinase. The structure of a complex between the signal-terminating phosphatase, CheC, and the receptor-modifying deamidase, CheD, reveals how CheC mimics receptor substrates to inhibit CheD and how CheD stimulates CheC phosphatase activity. CheD resembles other cysteine deamidases from bacterial pathogens that inactivate host Rho-GTPases. Phospho-CheY, the intracellular signal and CheC target, stabilizes the CheC-CheD complex and reduces availability of CheD. A model is proposed whereby CheC acts as a CheY-P-induced regulator of CheD; CheY-P would cause CheC to sequester CheD from the chemoreceptors, inducing adaptation of the chemotaxis system.


Pssm-ID: 461116  Cd Length: 106  Bit Score: 140.67  E-value: 4.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636   63 MLPDDGADARAPASDSMRYGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAGM-TTINIGDRNADFVRRYLALEKIRI 141
Cdd:pfam03975   1 MLPDSSQARNGAASNPAKYADTAIELLINELLKLGARRERLEAKIAGGAQMFAGSsDVMNIGERNVEAVKEYLKEEGIPI 80

                          90       100
                  ....*....|....*....|....*.
gi 738070636  142 AAEDLQGTHPRKVAFMPRTGQAMVKK 167
Cdd:pfam03975  81 VAEDVGGNYGRTVEFDPATGRVLVKT 106
CheD_Thtga NF041119
chemoreceptor glutamine deamidase/glutamate methylesterase CheD;
27-167 5.17e-36

chemoreceptor glutamine deamidase/glutamate methylesterase CheD;


Pssm-ID: 469042  Cd Length: 158  Bit Score: 124.41  E-value: 5.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  27 EFFTTREDMVLVTV-LGSCVAACLHDPFAGLGGMNHFMLPD-DGADARAPAsdsmRYGAYAMEVLINELIKAGGKRERFE 104
Cdd:NF041119   9 EYAVEKNPAILVTLgLGSCVGVCIRDKVAKIGGMVHVMLPDsRGGKTPKPG----KYADTGIKLLVEELKKMGANLSRLE 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738070636 105 AKVFGGAAVLAGmTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVKK 167
Cdd:NF041119  85 AKIAGGASMFES-KTMDIGKRNVEAVKKWLKYLGIRLVAEDTGGNRARSIEYNIETGKLLVRK 146
 
Name Accession Description Interval E-value
PRK13489 PRK13489
chemoreceptor glutamine deamidase CheD; Provisional
 1-228 1.94e-142

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 237398  Cd Length: 233  Bit Score: 397.27  E-value: 1.94e-142
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636   1 MSALPIASNHYFDNHFGRPGVKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADARAPASDSMR 80
Cdd:PRK13489   1 MSGLPIATNRYFDNHFHRPGVKLLPNEFYTTREDMVLVTVLGSCVAACLHDPVAGIGGMNHFMLPDDGADAGAAASESMR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  81 YGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRT 160
Cdd:PRK13489  81 YGAYAMEVLINELIKAGGRRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALERIRITAEDLQGVHPRKVAFMPRT 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 738070636 161 GQAMVKKLRLSVPGVAEreaALARSAAEARAARAQRARAHVELFAA-----PAAPKPRVELFGSTAT---TKKQEA 228
Cdd:PRK13489 161 GRAMVKKLRLQVPGVAE---REAALAREAHGERAARARARVELFAApapsaPAPARPRIELFGRRATqnaTRKQEA 233
PRK13487 PRK13487
chemoreceptor glutamine deamidase CheD; Provisional
 6-169 4.36e-98

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 237396  Cd Length: 201  Bit Score: 283.76  E-value: 4.36e-98
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636   6 IASNHYFDNHFGRPGVKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADArAPASDSMRYGAYA 85
Cdd:PRK13487   9 EASNRYFDRHFQCDAAKILPGEYFVTDDDTAIVTVLGSCVSACLRDPVLGIGGMNHFMLPDGGDSD-GPLSASARYGSYA 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  86 MEVLINELIKAGGKRERFEAKVFGGAAVLAGMTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMV 165
Cdd:PRK13487  88 MELLINDLLKLGARRENLEAKVFGGGNVLRGFTSMNVGERNAEFVRDYLQTERIPIVAEDLLDIYPRKVYFFPTTGKVLV 167


                 ....
gi 738070636 166 KKLR 169
Cdd:PRK13487 168 KKLK 171
CheD COG1871
Chemotaxis receptor (MCP) glutamine deamidase CheD [Signal transduction mechanisms];
14-169 4.00e-70

Chemotaxis receptor (MCP) glutamine deamidase CheD [Signal transduction mechanisms];


Pssm-ID: 441475  Cd Length: 164  Bit Score: 211.58  E-value: 4.00e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  14 NHFGRPGVKLLPNEF-FTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADarAPASDSMRYGAYAMEVLINE 92
Cdd:COG1871    2 SNAGMKEIKVGPGEYyVSTDPDTLITTGLGSCVAVCLYDPVAKIGGMNHFMLPDSSGA--KAAGNPAKYGDTAMELLINE 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738070636  93 LIKAGGKRERFEAKVFGGAAVLAGMT--TINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVKKLR 169
Cdd:COG1871   80 LLKLGARRERLEAKIFGGANMFSGLSsdSLNIGERNVEAAREYLAEEGIPIVAEDVGGNYGRTVEFDPATGRVLVKTLG 158
CheD cd16352
chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins; This ...
 21-166 3.57e-63

chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins; This family contains bacterial chemotaxis protein CheD that stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). The CheD chemotaxis gene is not found in the Escherichia coli genome, but is present in many other organisms, including B. subtilis, where CheD appears to have two separate roles; it binds to chemoreceptors to activate them as part of the CheC/CheD/CheYp adaptation system, and it deamidates selected residues to activate chemoreceptors, enabling them to mediate amino acid chemotaxis. CheD has been shown to catalyze amide hydrolysis of specific glutaminyl side chains of the B. subtilis chemoreceptors McpA, McpB and McpC; deamination by CheD is required for the chemoreceptors to effectively transduce signals to the CheA kinase. CheD's ability to bind the receptors is controlled by CheC via a competitive binding mechanism; substituting Gln into the receptor motif of the signal-terminating phosphatase, CheC, turns the inhibitor into a receptor-modifying deamidase CheD substrate. Also, CheYp increases the affinity of CheD for CheC, controlling CheD binding to the receptors through its interactions with CheC. Thus, high levels of CheYp means CheC is a better binding target for CheD than the receptors, resulting in decreased CheA activity. The CheD structure reveals a distant homology with a class of bacterial toxins represented by the cytotoxic necrotizing factor 1 (CNF1) as well as a class of proteins of unknown function represented by B. subtilis YfiH. An invariant Cys-His pair forming a catalytic dyad is observed, and is required by the toxins for deamidation activity.


Pssm-ID: 319352  Cd Length: 146  Bit Score: 193.45  E-value: 3.57e-63
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  21 VKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDGADarAPASDSMRYGAYAMEVLINELIKAGGKR 100
Cdd:cd16352    2 IFVGPGEYYVSRGPTVLSTLLGSCVAVCLYDPVAKIGGMNHFMLPESSGD--KEASNPGKYADTAIELLLNELLKLGARR 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738070636 101 ERFEAKVFGGAAVLAGM-TTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVK 166
Cdd:cd16352   80 SRLEAKLFGGANMFPGSsGLLNIGERNIEAARELLAKEGIPIVAEDVGGNYGRTVRFDPATGEVLVK 146
PRK13497 PRK13497
chemoreceptor glutamine deamidase CheD; Provisional
 34-163 2.71e-43

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 237399  Cd Length: 184  Bit Score: 144.28  E-value: 2.71e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  34 DMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDDgADARAPASDSMRYGAYAMEVLINELIKAGGKRERFEAKVFGGAAV 113
Cdd:PRK13497  24 NVVLSTILGSCVAACLRDPVAGVGGMNHFLLPGS-ATSPTSGGDATRYGVHLMELLINGLLKQGARRDRLEAKIFGGAKT 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 738070636 114 LAGMTtiNIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQA 163
Cdd:PRK13497 103 IATFS--NVGEQNAAFAMQFLRDEGIPVVGSSTGGEHGRKLEYWPVSGRA 150
PRK13493 PRK13493
chemoreceptor glutamine deamidase CheD; Provisional
 11-171 4.27e-43

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 184086  Cd Length: 213  Bit Score: 144.70  E-value: 4.27e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  11 YFDNHFGRPGVKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLP------DDGADARAPASDSMRYGAY 84
Cdd:PRK13493  21 FNHPSDHRHWVKVMPGGVYATSDQEIIHTGLGSCVSACAWDIEMKVGGMNHFLLPfnnqfeSQHWHPQALLSDSSRYGCY 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  85 AMEVLINELIKAGGKRERFEAKVFGGAAVLaGMTTInIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAM 164
Cdd:PRK13493 101 AMEVLINRLLSMGAERERLKFKLFGGAHLM-GYQSL-VGEKNVEFVLEYAKREKLNVVAQDLGGAQPRKLLFDPQTGQAW 178


                 ....*..
gi 738070636 165 VKKLRLS 171
Cdd:PRK13493 179 VKRIGFS 185
CheD pfam03975
CheD chemotactic sensory transduction; This chemotaxis protein stimulates methylation of MCP ...
 63-167 4.69e-43

CheD chemotactic sensory transduction; This chemotaxis protein stimulates methylation of MCP proteins. The chemotaxis machinery of Bacillus subtilis is similar to that of the well characterized system of Escherichia coli. However, B. subtilis contains several chemotaxis genes not found in the E. coli genome, such as CheC and CheD, indicating that the B. subtilis chemotactic system is more complex. CheD plays an important role in chemotactic sensory transduction for many organizms. CheD deamidates other B. subtilis chemoreceptors including McpB and McpC. Deamidation by CheD is required for B. subtilis chemoreceptors to effectively transduce signals to the CheA kinase. The structure of a complex between the signal-terminating phosphatase, CheC, and the receptor-modifying deamidase, CheD, reveals how CheC mimics receptor substrates to inhibit CheD and how CheD stimulates CheC phosphatase activity. CheD resembles other cysteine deamidases from bacterial pathogens that inactivate host Rho-GTPases. Phospho-CheY, the intracellular signal and CheC target, stabilizes the CheC-CheD complex and reduces availability of CheD. A model is proposed whereby CheC acts as a CheY-P-induced regulator of CheD; CheY-P would cause CheC to sequester CheD from the chemoreceptors, inducing adaptation of the chemotaxis system.


Pssm-ID: 461116  Cd Length: 106  Bit Score: 140.67  E-value: 4.69e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636   63 MLPDDGADARAPASDSMRYGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAGM-TTINIGDRNADFVRRYLALEKIRI 141
Cdd:pfam03975   1 MLPDSSQARNGAASNPAKYADTAIELLINELLKLGARRERLEAKIAGGAQMFAGSsDVMNIGERNVEAVKEYLKEEGIPI 80

                          90       100
                  ....*....|....*....|....*.
gi 738070636  142 AAEDLQGTHPRKVAFMPRTGQAMVKK 167
Cdd:pfam03975  81 VAEDVGGNYGRTVEFDPATGRVLVKT 106
PRK13491 PRK13491
chemoreceptor glutamine deamidase CheD; Provisional
 25-162 2.91e-37

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 184085  Cd Length: 199  Bit Score: 128.94  E-value: 2.91e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  25 PNEFFTTredmvlvtVLGSCVAACLHDPFAGLGGMNHFMLPDDGADarapASDSMRYGAYAMEVLINELIKAGGKRERFE 104
Cdd:PRK13491  29 PNEVYAT--------ILGSCICTCMCDPVAGVGGMNHFLLPSADVE----DAQHLRYGSHAMELLINALLKLGAARQRIE 96

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 738070636 105 AKVFGGAAVLAGMTTinIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQ 162
Cdd:PRK13491  97 AKIFGGAMMTPQLGA--IGQANAAFARRYLRDEGIRCTAHSLGGNRARRIRFWPKTGR 152
CheD_Thtga NF041119
chemoreceptor glutamine deamidase/glutamate methylesterase CheD;
27-167 5.17e-36

chemoreceptor glutamine deamidase/glutamate methylesterase CheD;


Pssm-ID: 469042  Cd Length: 158  Bit Score: 124.41  E-value: 5.17e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  27 EFFTTREDMVLVTV-LGSCVAACLHDPFAGLGGMNHFMLPD-DGADARAPAsdsmRYGAYAMEVLINELIKAGGKRERFE 104
Cdd:NF041119   9 EYAVEKNPAILVTLgLGSCVGVCIRDKVAKIGGMVHVMLPDsRGGKTPKPG----KYADTGIKLLVEELKKMGANLSRLE 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 738070636 105 AKVFGGAAVLAGmTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVKK 167
Cdd:NF041119  85 AKIAGGASMFES-KTMDIGKRNVEAVKKWLKYLGIRLVAEDTGGNRARSIEYNIETGKLLVRK 146
PRK13488 PRK13488
chemoreceptor glutamine deamidase CheD; Provisional
 41-167 3.38e-35

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 237397  Cd Length: 157  Bit Score: 122.32  E-value: 3.38e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  41 LGSCVAACLHDPFAGLGGMNHFMLPD-DGADARAPAsdsmRYGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAGMT- 118
Cdd:PRK13488  25 LGSCVGIILYDRGKKIGGLAHVMLPEsSGAGDRNPG----KYADTAIPLLIEEMVKLGARKSKLEAKLAGGAAMFDFSSn 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 738070636 119 TINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVKK 167
Cdd:PRK13488 101 NLNIGERNIESAKETLKKLGIRIVAEDVGGDYGRTVKFDLKTGKVIVRK 149
PRK13495 PRK13495
chemoreceptor glutamine deamidase CheD; Provisional
 27-169 4.62e-34

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 184088  Cd Length: 159  Bit Score: 119.59  E-value: 4.62e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  27 EFFTTREDMVLVTV-LGSCVAACLHDPFAGLGGMNHFMLPD-DGADARAPAsdsmRYGAYAMEVLINELIKAGGKRERFE 104
Cdd:PRK13495  10 EYAVMKNPGVIVTLgLGSCVGVCMRDPVAKVGAMAHVMLPDsGGKETDKPG----KYADTAIKTLVEELKKMGAKVERLE 85

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 738070636 105 AKVFGGAAVLAGmTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVKKLR 169
Cdd:PRK13495  86 AKIAGGASMFES-SGMNIGARNVEAVKKHLKDFGIKLVAEDTGGNRARSIEYNIETGKLLVRKVG 149
PRK13494 PRK13494
chemoreceptor glutamine deamidase CheD; Provisional
 14-166 1.29e-23

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 184087  Cd Length: 163  Bit Score: 92.68  E-value: 1.29e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  14 NHFG----RPGVKLLPNEFFTTrEDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPDdgADARAPASDSMRYGAYAMEVL 89
Cdd:PRK13494   3 NHFNfklkRDVTIIVPGEAFVS-NDRVISTILGSCVAVVLYDESRNLIGMNHYVLVK--SDLVISPLQRGRYGVYAIPML 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 738070636  90 INELIKAGGKRERFEAKVFGGAAVLAgMTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVK 166
Cdd:PRK13494  80 IDAMLENGASKSNLKAKLFGGTNFMA-KGTIKVGLENSEFAVNTLNKYGIPILAKDFDQSKSRKIFVFPENFKVIVE 155
PRK13498 PRK13498
chemoreceptor glutamine deamidase CheD; Provisional
 21-172 2.63e-18

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 237400  Cd Length: 167  Bit Score: 78.68  E-value: 2.63e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  21 VKLLPNEFFTTREDMVLVTVLGSCVAACLHDPFAGLGGMNHFMLPddgADARAPASDSMRYGAYAMEVLINELIKAGGKR 100
Cdd:PRK13498  10 IVLQPGEVVFATRPTRLRTLLGSCVAITFWHPQQHIGGMCHFMLP---GRIRKHQPLDGRYADEAMELLIRHALANGTPP 86

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 738070636 101 ERFEAKVFGGAAVL----AGMTTINIGDRNadfVRRYLALEK---IRIAAEDLQGTHPRKVAFMPRTGQAMVKKLRLSV 172
Cdd:PRK13498  87 EDYQVKLFGGGNMFpelqQDLHTLNVADKN---IHAALALAEqngLHLKAQDLGSTGHRSIIFDLWNGNVWVRHQPMEH 162
PRK13490 PRK13490
chemoreceptor glutamine deamidase CheD; Provisional
 37-166 8.70e-17

chemoreceptor glutamine deamidase CheD; Provisional


Pssm-ID: 184084  Cd Length: 162  Bit Score: 74.82  E-value: 8.70e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  37 LVTV-LGSCVAACLHDPFAGLGGMNHFMLPDdgADARAPASDSMRYGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLA 115
Cdd:PRK13490  22 IITVgLGSCIGIALYDGIKCIGGLSHIMLPD--STQFSNVTNPMKFADLAIPILIEKMEKLGANKRNLKAKIAGGASMFN 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 738070636 116 ---GMTTINIGDRNADFVRRYLALEKIRIAAEDLQGTHPRKVAFMPRTGQAMVK 166
Cdd:PRK13490 100 fsdKSMVMDIGNRNGKAVKKKLKELSIPILAEDIGGNKGRTMIFDTSDGKVYIK 153
CNF1_CheD_YfiH-like cd16832
cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant ...
 41-149 9.11e-08

cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and YfiH (DUF152) are distant homologs; This family contains distant homologs that include cytotoxic necrotizing factor 1 (CNF1), chemotaxis protein CheD and a protein of unknown function YfiH. CNF-1 along with dermonecrotic toxin (DNT) from Bordetella species, and Burkholderia Lethal Factor 1 (BLF1, also known as BPSL1549) are Rho-activating toxins. The bacterial chemotaxis protein CheD stimulates methylation of methyl-accepting chemotaxis proteins (MCPs). YfiH, a domain of unknown function, also included in this family reveals a structure with a distant homology between to the CNF1, and CheD, all having an invariant Cys-His pair forming a catalytic dyad that is required by the CNF-1 toxins for deamidation activity.


Pssm-ID: 319353  Cd Length: 145  Bit Score: 49.70  E-value: 9.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 738070636  41 LGSCVAACLHDPFAGLGGMNHFMLPDDGADARapasdSMRYGAYAMEVLINELIKAGGKRERFEAKVFGGAAVLAgMTTI 120
Cdd:cd16832   28 LSGCTTVVARDPGAKYIAKAHTGTTKSLAGFT-----STTGVDKAVEVLVLLTKEPGASENFEDSLITYSSSEKK-PDSM 101

                         90       100
                 ....*....|....*....|....*....
gi 738070636 121 NIGDRNADFVRRYLALEKIRIAAEDLQGT 149
Cdd:cd16832  102 NIGARNVEAVKKHLITIGRDNVSVFPYFL 130
 
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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