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Conserved domains on  [gi|635773343|gb|KDF54795|]
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hypothetical protein AF40_03748 [Enterobacter roggenkampii MGH 54]

Protein Classification

GlxA family transcriptional regulator( domain architecture ID 11471967)

GlxA family transcriptional regulator contains an amidase domain and an AraC-type DNA-binding helix-turn-helix (HTH) domain

Gene Ontology:  GO:0003677|GO:0003700|GO:0006355
PubMed:  15808743|33837749|15070401|11282467

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 3-300 7.12e-85

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


:

Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 257.78  E-value: 7.12e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   3 IDVWFVMLPGVLSLDMTGPAETFVLAGD-----AFRLHYIGPQPE-VPTSIGLTMSGIQPLPErLPEGCLLVLPGVSDSR 76
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRlagrpLYRWRLVSLDGGpVRSSSGLTVAPDHGLAD-LAAADTLIVPGGLDPA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  77 SQfsTPQALRiqHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIKENRIFVQDEN 156
Cdd:COG4977   80 AA--ADPALL--AWLRRAA----ARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 157 IWTSAGITSGIDLALHMINRLCGPEKALNVAREMVVWFRRSGDDPQLSPWLRYRNHLHPAIHRAQDALTAEPQKAWSLPD 236
Cdd:COG4977  152 ILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDE 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635773343 237 IAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGR-GVEQASLAAGFSSP----RQYHRA 300
Cdd:COG4977  232 LARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDlSIEEIAAACGFGSAshfrRAFRRR 300
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 3-300 7.12e-85

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 257.78  E-value: 7.12e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   3 IDVWFVMLPGVLSLDMTGPAETFVLAGD-----AFRLHYIGPQPE-VPTSIGLTMSGIQPLPErLPEGCLLVLPGVSDSR 76
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRlagrpLYRWRLVSLDGGpVRSSSGLTVAPDHGLAD-LAAADTLIVPGGLDPA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  77 SQfsTPQALRiqHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIKENRIFVQDEN 156
Cdd:COG4977   80 AA--ADPALL--AWLRRAA----ARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 157 IWTSAGITSGIDLALHMINRLCGPEKALNVAREMVVWFRRSGDDPQLSPWLRYRNHLHPAIHRAQDALTAEPQKAWSLPD 236
Cdd:COG4977  152 ILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDE 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635773343 237 IAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGR-GVEQASLAAGFSSP----RQYHRA 300
Cdd:COG4977  232 LARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDlSIEEIAAACGFGSAshfrRAFRRR 300
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 5-192 1.51e-54

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 175.77  E-value: 1.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   5 VWFVMLPGVLSLDMTGPAETFVLA-----GDAFRLHYIGPQP-EVPTSIGLTMSGiQPLPERLPEGCLLVLPGVSDSRSQ 78
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEAnralgPPAYELRVCSPEGgPVRSSSGLSLVA-DAGLDALAAADTVIVPGGPDVDGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  79 FSTPQALriqHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIKENRIFVQDENIW 158
Cdd:cd03137   80 PPPPALL---AALRRAA----ARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVW 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 635773343 159 TSAGITSGIDLALHMINRLCGPEKALNVAREMVV 192
Cdd:cd03137  153 TSAGVTAGIDLCLHLVREDLGAAVANRVARRLVV 186
ftrA PRK09393
transcriptional activator FtrA; Provisional
 58-293 1.05e-25

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 103.89  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  58 PERLPEGCLLVLPGVSDSRSQFSTP--QALRIQHwlmrlqpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISR 135
Cdd:PRK09393  70 LELLDRADTIVIPGWRGPDAPVPEPllEALRAAH----------ARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAER 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 136 LRTAAPTATIKENRIFVQDENIWTSAGITSGIDLALHMINRLCGPEKALNVAREMVVWFRRSGDDPQLSPW---LRYRNH 212
Cdd:PRK09393 140 LQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRpvaSRESDR 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 213 LHPAIHRAQDALTAEpqkaWSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGR-GVEQASLAAGF 291
Cdd:PRK09393 220 LGPLIDWMRAHLAEP----HTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSAlSIDQIAERAGF 295


                 ..
gi 635773343 292 SS 293
Cdd:PRK09393 296 GS 297
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
232-300 1.00e-16

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 73.74  E-value: 1.00e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   232 WSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRG-VEQASLAAGFSSPRQYHRA 300
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLsVTEIALRVGFSSQSYFSRA 71
HTH_18 pfam12833
Helix-turn-helix domain;
237-300 2.30e-15

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 69.93  E-value: 2.30e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635773343  237 IAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRG--VEQASLAAGFSSPRQYHRA 300
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTGlsVAEIALALGFSDASHFSRA 66
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 3-300 7.12e-85

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 257.78  E-value: 7.12e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   3 IDVWFVMLPGVLSLDMTGPAETFVLAGD-----AFRLHYIGPQPE-VPTSIGLTMSGIQPLPErLPEGCLLVLPGVSDSR 76
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRlagrpLYRWRLVSLDGGpVRSSSGLTVAPDHGLAD-LAAADTLIVPGGLDPA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  77 SQfsTPQALRiqHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIKENRIFVQDEN 156
Cdd:COG4977   80 AA--ADPALL--AWLRRAA----ARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGD 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 157 IWTSAGITSGIDLALHMINRLCGPEKALNVAREMVVWFRRSGDDPQLSPWLRYRNHLHPAIHRAQDALTAEPQKAWSLPD 236
Cdd:COG4977  152 ILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDE 231

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 635773343 237 IAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGR-GVEQASLAAGFSSP----RQYHRA 300
Cdd:COG4977  232 LARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDlSIEEIAAACGFGSAshfrRAFRRR 300
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 5-192 1.51e-54

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 175.77  E-value: 1.51e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   5 VWFVMLPGVLSLDMTGPAETFVLA-----GDAFRLHYIGPQP-EVPTSIGLTMSGiQPLPERLPEGCLLVLPGVSDSRSQ 78
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEAnralgPPAYELRVCSPEGgPVRSSSGLSLVA-DAGLDALAAADTVIVPGGPDVDGR 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  79 FSTPQALriqHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIKENRIFVQDENIW 158
Cdd:cd03137   80 PPPPALL---AALRRAA----ARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVW 152

                        170       180       190
                 ....*....|....*....|....*....|....
gi 635773343 159 TSAGITSGIDLALHMINRLCGPEKALNVAREMVV 192
Cdd:cd03137  153 TSAGVTAGIDLCLHLVREDLGAAVANRVARRLVV 186
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 7-190 7.51e-34

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 121.88  E-value: 7.51e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   7 FVMLPGVLSLDMTGPAETFVLAGDA---FRLHYIGPQPE-VPTSIGLTMsgiqpLPERLPEGC----LLVLPGVSDSRSQ 78
Cdd:cd03139    3 ILLFPGVEVLDVIGPYEVFGRAPRLaapFEVFLVSETGGpVSSRSGLTV-----LPDTSFADPpdldVLLVPGGGGTRAL 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  79 FSTPQALriqHWLMRLQPiiqrRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTatIKENRIFVQDENIW 158
Cdd:cd03139   78 VNDPALL---DFIRRQAA----RAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAI--VVVDARWVVDGNIW 148

                        170       180       190
                 ....*....|....*....|....*....|..
gi 635773343 159 TSAGITSGIDLALHMINRLCGPEKALNVAREM 190
Cdd:cd03139  149 TSGGVSAGIDMALALVARLFGEELAQAVALLI 180
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 7-192 5.90e-26

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 101.57  E-value: 5.90e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   7 FVMLPGVLSLDMTGPAETFVLAG----------DAFRLHYIGPQPEVPTSIGLTMSGIQPLPERLPEGCLLVLPGVSDSR 76
Cdd:cd03138    3 LLAYPGALASSLAGLLDLLRAANrlarrqqggaPPFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVPGLGGDP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  77 SQFSTPQALRIQHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIKENRIFVQDEN 156
Cdd:cd03138   83 DELLLADNPALIAWLRRQH----ANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGN 158

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 635773343 157 IWTSAGITSGIDLALHMINRLCGPEKALNVAREMVV 192
Cdd:cd03138  159 LITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
ftrA PRK09393
transcriptional activator FtrA; Provisional
 58-293 1.05e-25

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 103.89  E-value: 1.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  58 PERLPEGCLLVLPGVSDSRSQFSTP--QALRIQHwlmrlqpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISR 135
Cdd:PRK09393  70 LELLDRADTIVIPGWRGPDAPVPEPllEALRAAH----------ARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAER 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 136 LRTAAPTATIKENRIFVQDENIWTSAGITSGIDLALHMINRLCGPEKALNVAREMVVWFRRSGDDPQLSPW---LRYRNH 212
Cdd:PRK09393 140 LQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRpvaSRESDR 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 213 LHPAIHRAQDALTAEpqkaWSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGR-GVEQASLAAGF 291
Cdd:PRK09393 220 LGPLIDWMRAHLAEP----HTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSAlSIDQIAERAGF 295


                 ..
gi 635773343 292 SS 293
Cdd:PRK09393 296 GS 297
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 5-192 3.48e-22

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 91.49  E-value: 3.48e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   5 VWFVMLPGVLSLDMTGPAETFVLAGD-----AFRLHYIGPQPE-VPTSIGLTMSGIQPLPERLPEGCLLVLPGVSDSRSQ 78
Cdd:cd03136    1 FGFLLLPGFSLLALASAIEPLRAANRlagreLYRWRVLSLDGApVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGARRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  79 fsTPQALRiqhWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAPTATIkENRIFVQDENIW 158
Cdd:cd03136   81 --TPALLA---WLRRAA----RRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEIDGDRL 150

                        170       180       190
                 ....*....|....*....|....*....|....
gi 635773343 159 TSAGITSGIDLALHMINRLCGPEKALNVAREMVV 192
Cdd:cd03136  151 TCAGGTAALDLMLELIARDHGAALAARVAEQFLH 184
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
232-300 1.00e-16

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 73.74  E-value: 1.00e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   232 WSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRG-VEQASLAAGFSSPRQYHRA 300
Cdd:smart00342   2 LTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLsVTEIALRVGFSSQSYFSRA 71
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 214-300 1.39e-16

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 78.94  E-value: 1.39e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 214 HPAIHRAQDALTAEPQKAWSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRGVEQASLAAGFSS 293
Cdd:COG2169   83 ADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGLSVTDAAYAAGFGS 162


                 ....*..
gi 635773343 294 PRQYHRA 300
Cdd:COG2169  163 LSRFYEA 169
HTH_18 pfam12833
Helix-turn-helix domain;
237-300 2.30e-15

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 69.93  E-value: 2.30e-15
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635773343  237 IAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRG--VEQASLAAGFSSPRQYHRA 300
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLLEDTGlsVAEIALALGFSDASHFSRA 66
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
207-300 1.45e-13

AraC-type DNA-binding domain and AraC-containing proteins [Transcription];


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 69.42  E-value: 1.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 207 LRYRNHLHPAIHRAQDALTAEPQKAWSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRG-VEQA 285
Cdd:COG2207  144 LLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLsISEI 223

                         90
                 ....*....|....*
gi 635773343 286 SLAAGFSSPRQYHRA 300
Cdd:COG2207  224 AYELGFSSQSHFSRA 238
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 5-171 8.67e-12

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 396514 [Multi-domain]  Cd Length: 165  Bit Score: 62.27  E-value: 8.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343    5 VWFVMLPGVLSLDMTGPAETFVLAGdaFRLHYIGPQP-EVPTSIGLTMSGIQPLPERLPEGC-LLVLPGvsdsrsQFSTP 82
Cdd:pfam01965   3 VLVLLADGFEDIELIYPADVLRRAG--IKVTVVSVDGgEVKGSRGVKVTVDASLDDVKPDDYdALVLPG------GRAGP 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343   83 QALR----IQHWLMRLQpiiqRRDITVMCVCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAptATIKEnRIFVQDENIW 158
Cdd:pfam01965  75 ERLRdnekLVEFVKDFY----EKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAG--ATYVD-KPVVVDGNLV 147

                         170
                  ....*....|...
gi 635773343  159 TSAGITSGIDLAL 171
Cdd:pfam01965 148 TSRGPGDAPEFAL 160
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 228-264 9.48e-06

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 41.76  E-value: 9.48e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 635773343  228 PQKAWSLPDIAALAHVSPRHLTRLFQTHLGISVRDYL 264
Cdd:pfam00165   5 LSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 108-177 6.72e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 39.46  E-value: 6.72e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 108 VCSGALLAAKSGLLNNKQCTTHHDVISRLrtaaPTATIKENRIfVQDENIWTSAGITSGIDLALHMINRL 177
Cdd:cd03135   99 ICAAPAVLAKAGLLKGKKATCYPGFEDKL----GGANYVDEPV-VVDGNIITSRGPGTAFEFALKIVEAL 163
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 29-162 8.88e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 39.51  E-value: 8.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343  29 GDAFRLHYIGPQPEVPTSIGltmsGIQPLPE------RLPEGCLLVLPGvSDSrsqFSTPQAlriqhwlMRLQPIIQR-- 100
Cdd:cd03140   24 YEGFEVRTVSPTGEPVTSIG----GLRVVPDyslddlPPEDYDLLILPG-GDS---WDNPEA-------PDLAGLVRQal 88

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 635773343 101 -RDITVMCVCSGALLAAKSGLLNNKQCTThhDVISRLRTAAPTATIKENRIF---VQDENIWTSAG 162
Cdd:cd03140   89 kQGKPVAAICGATLALARAGLLNNRKHTS--NSLDFLKAHAPYYGGAEYYDEpqaVSDGNLITANG 152
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 108-177 1.25e-03

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 38.93  E-value: 1.25e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 108 VCSGALLAAKSGLLNNKQCTTHHDVISRLRTAAptATIKENRIfVQDENIWTSAGITSGIDLALHMINRL 177
Cdd:COG0693  103 ICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAG--ATYVDEEV-VVDGNLITSRGPGDAPAFARALLELL 169
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
213-299 1.39e-03

bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 39.78  E-value: 1.39e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 635773343 213 LHPAIHRAQDALTA----EPQKAWSLPDIAALAHVSPRHLTRLFQTHLGISVRDYLEQLRLAVAEQWLLQGRGVEQASLA 288
Cdd:PRK15435  77 ANPQQHRLDKITHAcrllEQETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILN 156

                         90
                 ....*....|.
gi 635773343 289 AGFSSPRQYHR 299
Cdd:PRK15435 157 AGFPDSSSYYR 167
 
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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