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Conserved domains on  [gi|15599632|ref|NP_253126|]
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transcriptional regulator [Pseudomonas aeruginosa PAO1]

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 ...
 15-294 8.96e-101

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: 297.84  E-value: 8.96e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  15 QPAFRTRILSPDGQPVRSFSGDSIAVDGPLAA---CDIVVLPafwGDFDALERRYPQIVPWLRRSHAEGTALCGEATGVF 91
Cdd:COG4977  32 RPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADlaaADTLIVP---GGLDPAAAADPALLAWLRRAAARGARLASICTGAF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  92 WLAQAGLLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFCGGSVAQAVARDTLYE 171
Cdd:COG4977 109 LLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVD 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632 172 VQRSY-TPGRIGFGGQKLHHDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAK 250
Cdd:COG4977 189 PRRPGgQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERAR 268

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15599632 251 GMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRRQF 294
Cdd:COG4977 269 RLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-294 8.96e-101

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: 297.84  E-value: 8.96e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  15 QPAFRTRILSPDGQPVRSFSGDSIAVDGPLAA---CDIVVLPafwGDFDALERRYPQIVPWLRRSHAEGTALCGEATGVF 91
Cdd:COG4977  32 RPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADlaaADTLIVP---GGLDPAAAADPALLAWLRRAAARGARLASICTGAF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  92 WLAQAGLLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFCGGSVAQAVARDTLYE 171
Cdd:COG4977 109 LLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVD 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632 172 VQRSY-TPGRIGFGGQKLHHDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAK 250
Cdd:COG4977 189 PRRPGgQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERAR 268

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15599632 251 GMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRRQF 294
Cdd:COG4977 269 RLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-171 3.47e-67

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: 207.88  E-value: 3.47e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   1 MASLRHGKQQGLglQPAFRTRILSPDGQPVRSFSGDSIAVD---GPLAACDIVVLPAFWGDFDALER-RYPQIVPWLRRS 76
Cdd:cd03138  23 AANRLARRQQGG--APPFEVRLVSLDGGPVLLAGGILILPDatlADVPAPDLVIVPGLGGDPDELLLaDNPALIAWLRRQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  77 HAEGTALCGEATGVFWLAQAGLLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFC 156
Cdd:cd03138 101 HANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLALHLIERLA 180

                       170
                ....*....|....*
gi 15599632 157 GGSVAQAVARDTLYE 171
Cdd:cd03138 181 GPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 26-294 1.49e-43

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 151.27  E-value: 1.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   26 DGQPVRSFSGDSIAVDGP---LAACDIVVLPAfWGDFDALerrypqiVP-----WLRRSHAEGTALCGEATGVFWLAQAG 97
Cdd:PRK09393  52 EPGPLRAAGGITVVADGGlelLDRADTIVIPG-WRGPDAP-------VPeplleALRAAHARGARLCSICSGVFVLAAAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   98 LLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFCGGSVAQAVARDTLYEVQRSyt 177
Cdd:PRK09393 124 LLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRD-- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  178 pgrigfGGQK--------LHHDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETA 249
Cdd:PRK09393 202 ------GGQAqfvprpvaSRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARA 275

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15599632  250 KGMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRRQF 294
Cdd:PRK09393 276 RDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
212-291 8.68e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 92.23  E-value: 8.68e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632    212 EDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYR 291
Cdd:smart00342   5 EDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
214-293 9.27e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.48  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   214 VARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGML-SSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRR 292
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 15599632   293 Q 293
Cdd:pfam12833  81 R 81
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-294 8.96e-101

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: 297.84  E-value: 8.96e-101
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  15 QPAFRTRILSPDGQPVRSFSGDSIAVDGPLAA---CDIVVLPafwGDFDALERRYPQIVPWLRRSHAEGTALCGEATGVF 91
Cdd:COG4977  32 RPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADlaaADTLIVP---GGLDPAAAADPALLAWLRRAAARGARLASICTGAF 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  92 WLAQAGLLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFCGGSVAQAVARDTLYE 171
Cdd:COG4977 109 LLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVD 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632 172 VQRSY-TPGRIGFGGQKLHHDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAK 250
Cdd:COG4977 189 PRRPGgQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERAR 268

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....
gi 15599632 251 GMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRRQF 294
Cdd:COG4977 269 RLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-171 3.47e-67

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: 207.88  E-value: 3.47e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   1 MASLRHGKQQGLglQPAFRTRILSPDGQPVRSFSGDSIAVD---GPLAACDIVVLPAFWGDFDALER-RYPQIVPWLRRS 76
Cdd:cd03138  23 AANRLARRQQGG--APPFEVRLVSLDGGPVLLAGGILILPDatlADVPAPDLVIVPGLGGDPDELLLaDNPALIAWLRRQ 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  77 HAEGTALCGEATGVFWLAQAGLLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFC 156
Cdd:cd03138 101 HANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLALHLIERLA 180

                       170
                ....*....|....*
gi 15599632 157 GGSVAQAVARDTLYE 171
Cdd:cd03138 181 GPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 26-294 1.49e-43

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 151.27  E-value: 1.49e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   26 DGQPVRSFSGDSIAVDGP---LAACDIVVLPAfWGDFDALerrypqiVP-----WLRRSHAEGTALCGEATGVFWLAQAG 97
Cdd:PRK09393  52 EPGPLRAAGGITVVADGGlelLDRADTIVIPG-WRGPDAP-------VPeplleALRAAHARGARLCSICSGVFVLAAAG 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   98 LLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGVTSACDLYIYLIERFCGGSVAQAVARDTLYEVQRSyt 177
Cdd:PRK09393 124 LLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRD-- 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  178 pgrigfGGQK--------LHHDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETA 249
Cdd:PRK09393 202 ------GGQAqfvprpvaSRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARA 275

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 15599632  250 KGMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRRQF 294
Cdd:PRK09393 276 RDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 15-167 4.21e-40

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: 138.40  E-value: 4.21e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  15 QPAFRTRILSPDGQPVRSFSGDSIAVDGPLAA---CDIVVLPAfWGDFDALERRyPQIVPWLRRSHAEGTALCGEATGVF 91
Cdd:cd03137  30 PPAYELRVCSPEGGPVRSSSGLSLVADAGLDAlaaADTVIVPG-GPDVDGRPPP-PALLAALRRAAARGARVASVCTGAF 107

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  92 WLAQAGLLDGKEATTYWRFYREFAERFPNVLLnqekhltDADDLFC-------ASGVTSACDLYIYLIERFCGGSVAQAV 164
Cdd:cd03137 108 VLAEAGLLDGRRATTHWAYAEDLARRFPAVRV-------DPDVLYVddgnvwtSAGVTAGIDLCLHLVREDLGAAVANRV 180


                ...
gi 15599632 165 ARD 167
Cdd:cd03137 181 ARR 183
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 15-171 6.71e-38

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: 132.32  E-value: 6.71e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  15 QPAFRTRILSPDGQPVRSFSGDSIAVDGPL---AACDIVVLPafwGDFDALERRYPQIVPWLRRSHAEGTALCGEATGVF 91
Cdd:cd03136  30 RELYRWRVLSLDGAPVTSSNGLRVAPDAALedaPPLDYLFVV---GGLGARRAVTPALLAWLRRAARRGVALGGIDTGAF 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  92 WLAQAGLLDGKEATTYWRFYREFAERFPNVLLNQEKHLTDADDLFCASGvTSACDLYIYLIERFCGGSVAQAVARDTLYE 171
Cdd:cd03136 107 LLARAGLLDGRRATVHWEHLEAFAEAFPRVQVTRDLFEIDGDRLTCAGG-TAALDLMLELIARDHGAALAARVAEQFLHD 185
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 14-171 2.04e-28

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: 107.63  E-value: 2.04e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  14 LQPAFRTRILSPDGQPVRSFSGDSIAVDGPLA---ACDIVVLPAfwGDFDALERRYPQIVPWLRRSHAEGTALCGEATGV 90
Cdd:cd03139  27 LAAPFEVFLVSETGGPVSSRSGLTVLPDTSFAdppDLDVLLVPG--GGGTRALVNDPALLDFIRRQAARAKYVTSVCTGA 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  91 FWLAQAGLLDGKEATTYWRFYREFAERFPNVllNQEKHLTDADDLFCASGVTSACDLYIYLIERFCGGSVAQAVARDTLY 170
Cdd:cd03139 105 LLLAAAGLLDGRRATTHWAAIDWLKEFGAIV--VVDARWVVDGNIWTSGGVSAGIDMALALVARLFGEELAQAVALLIEY 182


                .
gi 15599632 171 E 171
Cdd:cd03139 183 D 183
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
212-291 8.68e-24

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 92.23  E-value: 8.68e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632    212 EDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYR 291
Cdd:smart00342   5 EDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
188-298 1.12e-21

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 91.77  E-value: 1.12e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632 188 LHHDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEV 267
Cdd:COG2207 148 LLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYEL 227

                        90       100       110
                ....*....|....*....|....*....|.
gi 15599632 268 GYDDASFFARLFRQHTELSPHHYRRQFMQKE 298
Cdd:COG2207 228 GFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
214-293 9.27e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.48  E-value: 9.27e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632   214 VARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGML-SSTRKSIKTISYEVGYDDASFFARLFRQHTELSPHHYRR 292
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 15599632   293 Q 293
Cdd:pfam12833  81 R 81
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
196-293 8.01e-16

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 75.87  E-value: 8.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  196 QIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDASFF 275
Cdd:PRK13503 175 QLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHF 254

                         90
                 ....*....|....*...
gi 15599632  276 ARLFRQHTELSPHHYRRQ 293
Cdd:PRK13503 255 STLFRREFSWSPRDIRQG 272
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
190-297 2.65e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 74.62  E-value: 2.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  190 HDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGY 269
Cdd:PRK10572 181 MDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGY 260

                         90       100
                 ....*....|....*....|....*...
gi 15599632  270 DDASFFARLFRQHTELSPHHYRRQFMQK 297
Cdd:PRK10572 261 DDQLYFSRVFKKCTGASPSEFRARCEEK 288
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 190-293 1.98e-14

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: 72.78  E-value: 1.98e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632 190 HDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLsSTRKSIKTISYEVGY 269
Cdd:COG2169  82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGF 160

                        90       100
                ....*....|....*....|....
gi 15599632 270 DDASFFARLFRQHTELSPHHYRRQ 293
Cdd:COG2169 161 GSLSRFYEAFKKLLGMTPSAYRRG 184
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
201-296 4.29e-10

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 59.53  E-value: 4.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  201 LEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDASFFARLFR 280
Cdd:PRK13501 185 LQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFT 264

                         90
                 ....*....|....*.
gi 15599632  281 QHTELSPHHYRRQFMQ 296
Cdd:PRK13501 265 REAGMTPRDYRQRFIR 280
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
190-293 7.58e-10

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 55.32  E-value: 7.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  190 HDPTILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGY 269
Cdd:PRK10219   3 HQKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGY 82

                         90       100
                 ....*....|....*....|....
gi 15599632  270 DDASFFARLFRQHTELSPHHYRRQ 293
Cdd:PRK10219  83 VSQQTFSRVFRRQFDRTPSDYRHR 106
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 212-294 1.90e-09

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 57.35  E-value: 1.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  212 EDVARDHGMSIRNFMRRFqAATGDKPLHYLQRLRIETAKGMLSS--TRKSIKTISYEVGYDDASFFARLFRQHTELSPHH 289
Cdd:PRK09685 218 EWIAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLDRCADDLRPaaDDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGE 296


                 ....*
gi 15599632  290 YRRQF 294
Cdd:PRK09685 297 YRRKF 301
PRK10371 PRK10371
transcriptional regulator MelR;
151-298 3.90e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 56.75  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  151 LIERFCGGSVAQAVARD--TLYEVQR------SYTPGR-------IGF--------GGQKLHHDPT------------IL 195
Cdd:PRK10371 112 LINHVTHGMVIKSLATQqlSPFEVRRwqqelnSPNEQIrqlaideIGLmlkrfslsGWEPILVNKTsrthknsvsrhaQF 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  196 QIQQWLE---DHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDA 272
Cdd:PRK10371 192 YVSQMLGfiaENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSS 271

                        170       180
                 ....*....|....*....|....*.
gi 15599632  273 SFFARLFRQHTELSPHHYRRQFMQKE 298
Cdd:PRK10371 272 SRFYSTFGKYVGMSPQQYRKLSQQRR 297
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 18-108 2.58e-08

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: 52.26  E-value: 2.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632    18 FRTRILSPDGQPVRSFSGDSIAVDGPLAAC-----DIVVLPAFWGDFDALeRRYPQIVPWLRRSHAEGT---ALCgeaTG 89
Cdd:pfam01965  28 IKVTVVSVDGGEVKGSRGVKVTVDASLDDVkpddyDALVLPGGRAGPERL-RDNEKLVEFVKDFYEKGKpvaAIC---HG 103

                          90
                  ....*....|....*....
gi 15599632    90 VFWLAQAGLLDGKEATTYW 108
Cdd:pfam01965 104 PQVLAAAGVLKGRKVTSHP 122
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 197-294 1.05e-07

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 52.07  E-value: 1.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  197 IQQWLE---DHFADKFRF-----EDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVG 268
Cdd:PRK10296 169 IPQWLKatvEKMHDKEQFsesalENMVRLSGKSQEYLTRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAG 248

                         90       100
                 ....*....|....*....|....*.
gi 15599632  269 YDDASFFARLFRQHTELSPHHYRRQF 294
Cdd:PRK10296 249 YSSPSLFIKTFKKLTSFTPGSYRKKL 274
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
193-299 2.00e-07

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 48.94  E-value: 2.00e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  193 TILQIQQWLEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDA 272
Cdd:PRK11511  10 TIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQ 89

                         90       100
                 ....*....|....*....|....*..
gi 15599632  273 SFFARLFRQHTELSPHHYRRQFMQKES 299
Cdd:PRK11511  90 QTLTRTFKNYFDVPPHKYRMTNMQGES 116
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 18-106 4.42e-07

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: 48.76  E-value: 4.42e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  18 FRTRILSPDGQPVRSFSGDSIAVDG-----PLAACDIVVLPAfwGD-FDALErrYPQIVPWLRRSHAEGT---ALCGeat 88
Cdd:cd03140  27 FEVRTVSPTGEPVTSIGGLRVVPDYslddlPPEDYDLLILPG--GDsWDNPE--APDLAGLVRQALKQGKpvaAICG--- 99

                        90
                ....*....|....*...
gi 15599632  89 GVFWLAQAGLLDGKEATT 106
Cdd:cd03140 100 ATLALARAGLLNNRKHTS 117
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 18-107 2.49e-06

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: 46.64  E-value: 2.49e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  18 FRTRILSPD-GQPVRSFSGDSIAVDGPLAAC-----DIVVLPAFWGDFDALeRRYPQIVPWLRRSHAEGT---ALCGeAT 88
Cdd:COG0693  30 AEVDVASPEgGPPVTSKHGITVTADKTLDDVdpddyDALVLPGGHGAPDDL-REDPDVVALVREFYEAGKpvaAICH-GP 107

                        90
                ....*....|....*....
gi 15599632  89 GVfwLAQAGLLDGKEATTY 107
Cdd:COG0693 108 AV--LAAAGLLKGRKVTSF 124
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
209-298 5.07e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 46.97  E-value: 5.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  209 FRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRLRIETAKGMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPH 288
Cdd:PRK13502 193 FALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPS 272

                         90
                 ....*....|
gi 15599632  289 HYRRQFMQKE 298
Cdd:PRK13502 273 QWRHLSNQSD 282
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 201-242 2.03e-05

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: 40.99  E-value: 2.03e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 15599632   201 LEDHFADKFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQ 242
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 255-292 6.95e-04

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: 36.75  E-value: 6.95e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 15599632   255 STRKSIKTISYEVGYDdASFFARLFRQHTELSPHHYRR 292
Cdd:pfam00165   6 STNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQYRH 42
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 208-290 9.99e-04

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 40.05  E-value: 9.99e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15599632  208 KFRFEDVARDHGMSIRNFMRRFQAATGDKPLHYLQRlRIETAKGMLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSP 287
Cdd:PRK15186 197 KWALKDISDSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTP 275


                 ...
gi 15599632  288 HHY 290
Cdd:PRK15186 276 SEF 278
 
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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