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Conserved domains on  [gi|499254896|ref|WP_010952436|]
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MULTISPECIES: GlxA family transcriptional regulator [Pseudomonas]

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 ...
 23-302 1.12e-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: 300.54  E-value: 1.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  23 QPMFDIRLVSPDSQPVDSFSNVQLPVDGGLDD---ADVIILPAYWDDfdnLLQRYPQVLPWLREQHARGAVLCAEASGVF 99
Cdd:COG4977   32 RPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADlaaADTLIVPGGLDP---AAAADPALLAWLRRAAARGARLASICTGAF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 100 WLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDILYE 179
Cdd:COG4977  109 LLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 180 VQRNY-TPGRMGFGGQKLHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAK 258
Cdd:COG4977  189 PRRPGgQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERAR 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499254896 259 GLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYRQQF 302
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 ...
 23-302 1.12e-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: 300.54  E-value: 1.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  23 QPMFDIRLVSPDSQPVDSFSNVQLPVDGGLDD---ADVIILPAYWDDfdnLLQRYPQVLPWLREQHARGAVLCAEASGVF 99
Cdd:COG4977   32 RPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADlaaADTLIVPGGLDP---AAAADPALLAWLRRAAARGARLASICTGAF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 100 WLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDILYE 179
Cdd:COG4977  109 LLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 180 VQRNY-TPGRMGFGGQKLHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAK 258
Cdd:COG4977  189 PRRPGgQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERAR 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499254896 259 GLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYRQQF 302
Cdd:COG4977  269 RLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-179 1.21e-65

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: 204.42  E-value: 1.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896   1 MQAKDFFHLASLRysKQLGLGLQPMFDIRLVSPDSQPVDSFSNVQLPVD---GGLDDADVIILPAYWDDFDN-LLQRYPQ 76
Cdd:cd03138   15 AGLLDLLRAANRL--ARRQQGGAPPFEVRLVSLDGGPVLLAGGILILPDatlADVPAPDLVIVPGLGGDPDElLLADNPA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  77 VLPWLREQHARGAVLCAEASGVFWLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLY 156
Cdd:cd03138   93 LIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLA 172

                        170       180
                 ....*....|....*....|...
gi 499254896 157 IYLIERFCGANVARAVSRDILYE 179
Cdd:cd03138  173 LHLIERLAGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 44-302 1.11e-48

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 164.75  E-value: 1.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  44 VQLPVDGG---LDDADVIILPAyWDDFDnllQRYPQVL-PWLREQHARGAVLCAEASGVFWLAESGLLDGKEATTYWRFF 119
Cdd:PRK09393  62 ITVVADGGlelLDRADTIVIPG-WRGPD---APVPEPLlEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 120 NSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDILYEVQRNytpgrmgfGGQK---- 195
Cdd:PRK09393 138 ERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRD--------GGQAqfvp 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 196 ----LHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTI 271
Cdd:PRK09393 210 rpvaSRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQI 289

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499254896 272 SYEVGYDDASFFARLFRQHTELSPNQYRQQF 302
Cdd:PRK09393 290 AERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
220-299 3.46e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 91.08  E-value: 3.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896   220 EDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYR 299
Cdd:smart00342   5 EDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
227-301 1.03e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.48  E-value: 1.03e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499254896  227 GMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLL-SSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYRQQ 301
Cdd:pfam12833   6 GMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 23-302 1.12e-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: 300.54  E-value: 1.12e-101
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  23 QPMFDIRLVSPDSQPVDSFSNVQLPVDGGLDD---ADVIILPAYWDDfdnLLQRYPQVLPWLREQHARGAVLCAEASGVF 99
Cdd:COG4977   32 RPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADlaaADTLIVPGGLDP---AAAADPALLAWLRRAAARGARLASICTGAF 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 100 WLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDILYE 179
Cdd:COG4977  109 LLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVD 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 180 VQRNY-TPGRMGFGGQKLHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAK 258
Cdd:COG4977  189 PRRPGgQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERAR 268

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 499254896 259 GLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYRQQF 302
Cdd:COG4977  269 RLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-179 1.21e-65

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: 204.42  E-value: 1.21e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896   1 MQAKDFFHLASLRysKQLGLGLQPMFDIRLVSPDSQPVDSFSNVQLPVD---GGLDDADVIILPAYWDDFDN-LLQRYPQ 76
Cdd:cd03138   15 AGLLDLLRAANRL--ARRQQGGAPPFEVRLVSLDGGPVLLAGGILILPDatlADVPAPDLVIVPGLGGDPDElLLADNPA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  77 VLPWLREQHARGAVLCAEASGVFWLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLY 156
Cdd:cd03138   93 LIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLA 172

                        170       180
                 ....*....|....*....|...
gi 499254896 157 IYLIERFCGANVARAVSRDILYE 179
Cdd:cd03138  173 LHLIERLAGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 44-302 1.11e-48

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 164.75  E-value: 1.11e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  44 VQLPVDGG---LDDADVIILPAyWDDFDnllQRYPQVL-PWLREQHARGAVLCAEASGVFWLAESGLLDGKEATTYWRFF 119
Cdd:PRK09393  62 ITVVADGGlelLDRADTIVIPG-WRGPD---APVPEPLlEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYA 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 120 NSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDILYEVQRNytpgrmgfGGQK---- 195
Cdd:PRK09393 138 ERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRD--------GGQAqfvp 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 196 ----LHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTI 271
Cdd:PRK09393 210 rpvaSRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQI 289

                        250       260       270
                 ....*....|....*....|....*....|.
gi 499254896 272 SYEVGYDDASFFARLFRQHTELSPNQYRQQF 302
Cdd:PRK09393 290 AERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 23-176 1.27e-38

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: 134.55  E-value: 1.27e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  23 QPMFDIRLVSPDSQPVDSFSNVQLPVDGGLD---DADVIILPAyWDDFDNLLQRyPQVLPWLREQHARGAVLCAEASGVF 99
Cdd:cd03137   30 PPAYELRVCSPEGGPVRSSSGLSLVADAGLDalaAADTVIVPG-GPDVDGRPPP-PALLAALRRAAARGARVASVCTGAF 107

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499254896 100 WLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDI 176
Cdd:cd03137  108 VLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVARRL 184
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 23-179 7.54e-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: 132.71  E-value: 7.54e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  23 QPMFDIRLVSPDSQPVDSFSNVQLPVDGGLDDA---DVIILPAYWDDfdnLLQRYPQVLPWLREQHARGAVLCAEASGVF 99
Cdd:cd03136   30 RELYRWRVLSLDGAPVTSSNGLRVAPDAALEDApplDYLFVVGGLGA---RRAVTPALLAWLRRAARRGVALGGIDTGAF 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 100 WLAESGLLDGKEATTYWRFFNSFAERFPQIRLNQDKHLTDADNIYCAGGaTSACDLYIYLIERFCGANVARAVSRDILYE 179
Cdd:cd03136  107 LLARAGLLDGRRATVHWEHLEAFAEAFPRVQVTRDLFEIDGDRLTCAGG-TAALDLMLELIARDHGAALAARVAEQFLHD 185
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 26-179 6.11e-29

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: 109.17  E-value: 6.11e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  26 FDIRLVSPDSQPVDSFSNVQLPVDGGLDDA---DVIILPAywDDFDNLLQRYPQVLPWLREQHARGAVLCAEASGVFWLA 102
Cdd:cd03139   31 FEVFLVSETGGPVSSRSGLTVLPDTSFADPpdlDVLLVPG--GGGTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLA 108

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 499254896 103 ESGLLDGKEATTYWRFFNSFAERFPQIRlnQDKHLTDADNIYCAGGATSACDLYIYLIERFCGANVARAVSRDILYE 179
Cdd:cd03139  109 AAGLLDGRRATTHWAAIDWLKEFGAIVV--VDARWVVDGNIWTSGGVSAGIDMALALVARLFGEELAQAVALLIEYD 183
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
220-299 3.46e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 91.08  E-value: 3.46e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896   220 EDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYR 299
Cdd:smart00342   5 EDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
196-306 4.99e-22

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 92.92  E-value: 4.99e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 196 LHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEV 275
Cdd:COG2207  148 LLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYEL 227

                         90       100       110
                 ....*....|....*....|....*....|.
gi 499254896 276 GYDDASFFARLFRQHTELSPNQYRQQFMQEA 306
Cdd:COG2207  228 GFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
HTH_18 pfam12833
Helix-turn-helix domain;
227-301 1.03e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 81.48  E-value: 1.03e-19
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499254896  227 GMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLL-SSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYRQQ 301
Cdd:pfam12833   6 GMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRRR 81
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
197-301 5.06e-17

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 79.34  E-value: 5.06e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 197 HQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEVG 276
Cdd:PRK13503 168 NSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCG 247

                         90       100
                 ....*....|....*....|....*
gi 499254896 277 YDDASFFARLFRQHTELSPNQYRQQ 301
Cdd:PRK13503 248 FGDSNHFSTLFRREFSWSPRDIRQG 272
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 193-301 2.78e-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: 72.39  E-value: 2.78e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 193 GQKLHQDLIIlQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLsSTRKSIKTIS 272
Cdd:COG2169   78 GSPPRADLVA-RACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAA 155

                         90       100
                 ....*....|....*....|....*....
gi 499254896 273 YEVGYDDASFFARLFRQHTELSPNQYRQQ 301
Cdd:COG2169  156 YAAGFGSLSRFYEAFKKLLGMTPSAYRRG 184
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
202-301 7.84e-13

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 67.31  E-value: 7.84e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 202 ILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEVGYDDAS 281
Cdd:PRK10572 185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQL 264

                         90       100
                 ....*....|....*....|
gi 499254896 282 FFARLFRQHTELSPNQYRQQ 301
Cdd:PRK10572 265 YFSRVFKKCTGASPSEFRAR 284
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
193-306 8.31e-12

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 64.54  E-value: 8.31e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 193 GQKLhqDLIILQIQhwleEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTIS 272
Cdd:PRK13501 175 GEQL--DLIMSALQ----QSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIA 248

                         90       100       110
                 ....*....|....*....|....*....|....
gi 499254896 273 YEVGYDDASFFARLFRQHTELSPNQYRQQFMQEA 306
Cdd:PRK13501 249 ARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRSP 282
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
196-301 4.75e-11

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 58.78  E-value: 4.75e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 196 LHQDlIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEV 275
Cdd:PRK10219   2 SHQK-IIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDL 80

                         90       100
                 ....*....|....*....|....*.
gi 499254896 276 GYDDASFFARLFRQHTELSPNQYRQQ 301
Cdd:PRK10219  81 GYVSQQTFSRVFRRQFDRTPSDYRHR 106
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 26-114 1.20e-09

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: 56.46  E-value: 1.20e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  26 FDIRLVSPDSQPVDSFSNVQLPVDGGLD-----DADVIILPA--YWDDFDNllqryPQVLPWLREQHARGAVLCAEASGV 98
Cdd:cd03140   27 FEVRTVSPTGEPVTSIGGLRVVPDYSLDdlppeDYDLLILPGgdSWDNPEA-----PDLAGLVRQALKQGKPVAAICGAT 101

                         90
                 ....*....|....*.
gi 499254896  99 FWLAESGLLDGKEATT 114
Cdd:cd03140  102 LALARAGLLNNRKHTS 117
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 220-302 1.74e-09

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 57.73  E-value: 1.74e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 220 EDVARNHGMSIRNFMRRFQgATGDKPLHYLQRLRIETAKGLLSS--TRKSIKTISYEVGYDDASFFARLFRQHTELSPNQ 297
Cdd:PRK09685 218 EWIAGELGISVRSLYRLFA-EQGLVVAQYIRNRRLDRCADDLRPaaDDEKITSIAYKWGFSDSSHFSTAFKQRFGVSPGE 296


                 ....*
gi 499254896 298 YRQQF 302
Cdd:PRK09685 297 YRRKF 301
PRK10371 PRK10371
transcriptional regulator MelR;
197-306 5.77e-09

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 55.98  E-value: 5.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 197 HQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEVG 276
Cdd:PRK10371 188 HAQFYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAG 267

                         90       100       110
                 ....*....|....*....|....*....|
gi 499254896 277 YDDASFFARLFRQHTELSPNQYRQQFMQEA 306
Cdd:PRK10371 268 FRSSSRFYSTFGKYVGMSPQQYRKLSQQRR 297
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 26-116 1.07e-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: 53.41  E-value: 1.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896   26 FDIRLVSPDSQPVDSFSNVQLPVDGGLDDA-----DVIILPAyWDDFDNLLQRYPQVLPWLREQHARGAVLCAEASGVFW 100
Cdd:pfam01965  28 IKVTVVSVDGGEVKGSRGVKVTVDASLDDVkpddyDALVLPG-GRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQV 106

                          90
                  ....*....|....*.
gi 499254896  101 LAESGLLDGKEATTYW 116
Cdd:pfam01965 107 LAAAGVLKGRKVTSHP 122
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 234-302 4.77e-07

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 50.14  E-value: 4.77e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 499254896 234 MRRFQGATgdkPLHYLQRLRIETAKGLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPNQYRQQF 302
Cdd:PRK10296 209 TRRYYGKT---PMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKL 274
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
217-300 1.93e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 48.51  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 217 FRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRLRIETAKGLLSSTRKSIKTISYEVGYDDASFFARLFRQHTELSPN 296
Cdd:PRK13502 193 FALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPS 272


                 ....
gi 499254896 297 QYRQ 300
Cdd:PRK13502 273 QWRH 276
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 26-115 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 499254896  26 FDIRLVSPDS-QPVDSFSNVQLPVDGGLDDA-----DVIILP----AYWDdfdnlLQRYPQVLPWLREQHARG---AVLC 92
Cdd:COG0693   30 AEVDVASPEGgPPVTSKHGITVTADKTLDDVdpddyDALVLPgghgAPDD-----LREDPDVVALVREFYEAGkpvAAIC 104

                         90       100
                 ....*....|....*....|...
gi 499254896  93 AeASGVfwLAESGLLDGKEATTY 115
Cdd:COG0693  105 H-GPAV--LAAAGLLKGRKVTSF 124
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 263-300 3.21e-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: 40.60  E-value: 3.21e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 499254896  263 STRKSIKTISYEVGYDdASFFARLFRQHTELSPNQYRQ 300
Cdd:pfam00165   6 STNLTIADIADELGFS-RSYFSRLFKKYTGVTPSQYRH 42
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 194-298 6.53e-05

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 43.90  E-value: 6.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896 194 QKLHQDLIILQIQHWLEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQRlRIETAKGLLSSTRKSIKTISY 273
Cdd:PRK15186 175 RELSQNTLAENIYNIIISDISRKWALKDISDSLYMSCSTLKRKLKQENTSFSEVYLNA-RMNKATKLLRNSEYNITRVAY 253

                         90       100
                 ....*....|....*....|....*
gi 499254896 274 EVGYDDASFFARLFRQHTELSPNQY 298
Cdd:PRK15186 254 MCGYDSASYFTCVFKKHFKTTPSEF 278
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 209-250 1.56e-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: 38.67  E-value: 1.56e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 499254896  209 LEEHFADKFRFEDVARNHGMSIRNFMRRFQGATGDKPLHYLQ 250
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 26-101 2.35e-04

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 39.89  E-value: 2.35e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499254896  26 FDIRLVSPDSQPVDSFSNvqlpvdggLDDADVIILPAYWDDFDNLLqRYPQVLPWLREQHARGAVLCAEASGVFWL 101
Cdd:cd01653   26 AEVDVVSPDGGPVESDVD--------LDDYDGLILPGGPGTPDDLA-RDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 26-101 3.41e-04

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 39.11  E-value: 3.41e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 499254896  26 FDIRLVSPDSQPVDSFSNvqlpvdggLDDADVIILPAYWDDfDNLLQRYPQVLPWLREQHARGAVLCAEASGVFWL 101
Cdd:cd03128   26 AEVDVVSPDGGPVESDVD--------LDDYDGLILPGGPGT-PDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 34-115 5.35e-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: 39.84  E-value: 5.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 499254896  34 DSQPVDSFSNVQLPVDGGLDDA-----DVIILPAYWDDFDNLLQRyPQVLPWLREQHARG---AVLCAeASGVfwLAESG 105
Cdd:cd03135   35 KKLAVGSSHGIKVKADKTLSDVnlddyDAIVIPGGLPGAQNLADN-EKLIKLLKEFNAKGkliAAICA-APAV--LAKAG 110

                         90
                 ....*....|
gi 499254896 106 LLDGKEATTY 115
Cdd:cd03135  111 LLKGKKATCY 120
 
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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