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Conserved domains on  [gi|495288737|ref|WP_008013491|]
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GlxA family transcriptional regulator [Pseudomonas sp. GM50]

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 ...
 6-325 1.18e-124

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: 359.86  E-value: 1.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   6 KTIHVLAFANVQVLDVTGPLQVFASANDIARQqglpPPYTPSVIASGGGAVMSSAGLALLAEPLAK--QGSDTLIIAGGW 83
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGR----PLYRWRLVSLDGGPVRSSSGLTVAPDHGLAdlAAADTLIVPGGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  84 GVyAAAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTS 163
Cdd:COG4977   77 DP-AAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 164 AGVTAGIDLALAMVEEDLGRTMALDVARQLVVFLKRPGGQSQFSVTLSLQKEGN-RFDDLHAWISENLTKDLGIPTLALQ 242
Cdd:COG4977  156 AGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDpRLARAQAWMEANLEEPLSVDELARR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 243 AGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRERFSVS 322
Cdd:COG4977  236 AGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRAR 315


                 ...
gi 495288737 323 PPA 325
Cdd:COG4977  316 AAA 318
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 6-325 1.18e-124

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: 359.86  E-value: 1.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   6 KTIHVLAFANVQVLDVTGPLQVFASANDIARQqglpPPYTPSVIASGGGAVMSSAGLALLAEPLAK--QGSDTLIIAGGW 83
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGR----PLYRWRLVSLDGGPVRSSSGLTVAPDHGLAdlAAADTLIVPGGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  84 GVyAAAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTS 163
Cdd:COG4977   77 DP-AAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 164 AGVTAGIDLALAMVEEDLGRTMALDVARQLVVFLKRPGGQSQFSVTLSLQKEGN-RFDDLHAWISENLTKDLGIPTLALQ 242
Cdd:COG4977  156 AGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDpRLARAQAWMEANLEEPLSVDELARR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 243 AGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRERFSVS 322
Cdd:COG4977  236 AGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRAR 315


                 ...
gi 495288737 323 PPA 325
Cdd:COG4977  316 AAA 318
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 10-196 2.56e-81

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: 244.72  E-value: 2.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  10 VLAFANVQVLDVTGPLQVFASANDIARqqglPPPYTPSVIASGGGAVMSSAGLALLAEPLAKQGS--DTLIIAGGWGVYA 87
Cdd:cd03137    3 VLVFPGVSLLDLSGPAEVFGEANRALG----PPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAaaDTVIVPGGPDVDG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  88 AAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTSAGVT 167
Cdd:cd03137   79 RPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVT 158

                        170       180
                 ....*....|....*....|....*....
gi 495288737 168 AGIDLALAMVEEDLGRTMALDVARQLVVF 196
Cdd:cd03137  159 AGIDLCLHLVREDLGAAVANRVARRLVVP 187
ftrA PRK09393
transcriptional activator FtrA; Provisional
 50-320 7.12e-79

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 243.33  E-value: 7.12e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  50 ASGGGAVMSSAGLALLAEplakqgSDTLIIAGGWGVYAAAKDESLVAWVREHATGCRrVASVCTGAFLLAASGWLDGRRV 129
Cdd:PRK09393  58 AAGGITVVADGGLELLDR------ADTIVIPGWRGPDAPVPEPLLEALRAAHARGAR-LCSICSGVFVLAAAGLLDGRRA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 130 VTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTSAGVTAGIDLALAMVEEDLGRTMALDVARQLVVFLKRPGGQSQFSVT 209
Cdd:PRK09393 131 TTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPR 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 210 LSLQKEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVA 289
Cdd:PRK09393 211 PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIA 290

                        250       260       270
                 ....*....|....*....|....*....|.
gi 495288737 290 VQCGFGSEETLRRSFLRAMGVTPQAYRERFS 320
Cdd:PRK09393 291 ERAGFGSEESLRHHFRRRAATSPAAYRKRFG 321
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
233-316 3.77e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 88.38  E-value: 3.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   233 DLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTP 312
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 495288737   313 QAYR 316
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
239-318 3.43e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.72  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  239 LALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLL-SDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRE 317
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 495288737  318 R 318
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 ...
 6-325 1.18e-124

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: 359.86  E-value: 1.18e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   6 KTIHVLAFANVQVLDVTGPLQVFASANDIARQqglpPPYTPSVIASGGGAVMSSAGLALLAEPLAK--QGSDTLIIAGGW 83
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGR----PLYRWRLVSLDGGPVRSSSGLTVAPDHGLAdlAAADTLIVPGGL 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  84 GVyAAAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTS 163
Cdd:COG4977   77 DP-AAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTS 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 164 AGVTAGIDLALAMVEEDLGRTMALDVARQLVVFLKRPGGQSQFSVTLSLQKEGN-RFDDLHAWISENLTKDLGIPTLALQ 242
Cdd:COG4977  156 AGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDpRLARAQAWMEANLEEPLSVDELARR 235

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 243 AGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRERFSVS 322
Cdd:COG4977  236 AGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRAR 315


                 ...
gi 495288737 323 PPA 325
Cdd:COG4977  316 AAA 318
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 10-196 2.56e-81

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: 244.72  E-value: 2.56e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  10 VLAFANVQVLDVTGPLQVFASANDIARqqglPPPYTPSVIASGGGAVMSSAGLALLAEPLAKQGS--DTLIIAGGWGVYA 87
Cdd:cd03137    3 VLVFPGVSLLDLSGPAEVFGEANRALG----PPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAaaDTVIVPGGPDVDG 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  88 AAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTSAGVT 167
Cdd:cd03137   79 RPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVT 158

                        170       180
                 ....*....|....*....|....*....
gi 495288737 168 AGIDLALAMVEEDLGRTMALDVARQLVVF 196
Cdd:cd03137  159 AGIDLCLHLVREDLGAAVANRVARRLVVP 187
ftrA PRK09393
transcriptional activator FtrA; Provisional
 50-320 7.12e-79

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 243.33  E-value: 7.12e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  50 ASGGGAVMSSAGLALLAEplakqgSDTLIIAGGWGVYAAAKDESLVAWVREHATGCRrVASVCTGAFLLAASGWLDGRRV 129
Cdd:PRK09393  58 AAGGITVVADGGLELLDR------ADTIVIPGWRGPDAPVPEPLLEALRAAHARGAR-LCSICSGVFVLAAAGLLDGRRA 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 130 VTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTSAGVTAGIDLALAMVEEDLGRTMALDVARQLVVFLKRPGGQSQFSVT 209
Cdd:PRK09393 131 TTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPR 210

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 210 LSLQKEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVA 289
Cdd:PRK09393 211 PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIA 290

                        250       260       270
                 ....*....|....*....|....*....|.
gi 495288737 290 VQCGFGSEETLRRSFLRAMGVTPQAYRERFS 320
Cdd:PRK09393 291 ERAGFGSEESLRHHFRRRAATSPAAYRKRFG 321
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 10-193 2.49e-47

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: 157.70  E-value: 2.49e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  10 VLAFANVQVLDVTGPLQVFASANDiarqqgLPPPYTPSVIASGGGAVMSSAGLALLAEPLAKQGS--DTLIIAGGWGVYA 87
Cdd:cd03139    3 ILLFPGVEVLDVIGPYEVFGRAPR------LAAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPdlDVLLVPGGGGTRA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  88 AAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPklQVEPNPIFINDGPVWTSAGVT 167
Cdd:cd03139   77 LVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGA--IVVVDARWVVDGNIWTSGGVS 154

                        170       180
                 ....*....|....*....|....*.
gi 495288737 168 AGIDLALAMVEEDLGRTMALDVARQL 193
Cdd:cd03139  155 AGIDMALALVARLFGEELAQAVALLI 180
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 8-195 2.39e-41

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: 142.79  E-value: 2.39e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   8 IHVLAFANVQVLDVTGPLQVFASANDIA-RQQGLPPPYTPSVIASGGGAVMSSAGLALLAEPLAKQ--GSDTLIIAGGWG 84
Cdd:cd03138    1 VTLLAYPGALASSLAGLLDLLRAANRLArRQQGGAPPFEVRLVSLDGGPVLLAGGILILPDATLADvpAPDLVIVPGLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  85 VYAA---AKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVW 161
Cdd:cd03138   81 DPDElllADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLI 160

                        170       180       190
                 ....*....|....*....|....*....|....
gi 495288737 162 TSAGVTAGIDLALAMVEEDLGRTMALDVARQLVV 195
Cdd:cd03138  161 TAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 24-195 5.44e-36

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: 128.47  E-value: 5.44e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  24 PLQVFASAND---IARQQGLPPPYTPSVIASGGGAVMSSAGLALLAEPLAKQGS--DTLIIAGGWGVyAAAKDESLVAWV 98
Cdd:cd03136   10 SLLALASAIEplrAANRLAGRELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPplDYLFVVGGLGA-RRAVTPALLAWL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  99 REHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFInDGPVWTSAGVTAGIDLALAMVE 178
Cdd:cd03136   89 RRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQVTRDLFEI-DGDRLTCAGGTAALDLMLELIA 167

                        170
                 ....*....|....*..
gi 495288737 179 EDLGRTMALDVARQLVV 195
Cdd:cd03136  168 RDHGAALAARVAEQFLH 184
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
233-316 3.77e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 88.38  E-value: 3.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   233 DLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTP 312
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 495288737   313 QAYR 316
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
239-318 3.43e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 85.72  E-value: 3.43e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  239 LALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLL-SDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRE 317
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 495288737  318 R 318
Cdd:pfam12833  81 R 81
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
122-320 8.33e-21

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 89.84  E-value: 8.33e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 122 GWLDGRRVVTHWTRCEQLAQQHPKLQVEPNPIFINDGPVWTSAGVTAGIDLALAMVEEDLGRTMALDVARQLVVFLKRPG 201
Cdd:COG2207   57 LLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALEL 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 202 GQSQFSVTLSLQKEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDT 281
Cdd:COG2207  137 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAET 216

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 495288737 282 GVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRERFS 320
Cdd:COG2207  217 DLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLR 255
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 6-179 1.47e-18

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: 81.53  E-value: 1.47e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737    6 KTIHVLAFANVQVLDVTGPLQVFASANdiarqqglpppYTPSVIASGGGAVMSSAGLALLA----EPLAKQGSDTLIIAG 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAG-----------IKVTVVSVDGGEVKGSRGVKVTVdaslDDVKPDDYDALVLPG 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   82 G--WGVYAAAkDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHPKLQVEPnpiFINDGP 159
Cdd:pfam01965  70 GraGPERLRD-NEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKP---VVVDGN 145

                         170       180
                  ....*....|....*....|
gi 495288737  160 VWTSAGVTAGIDLALAMVEE 179
Cdd:pfam01965 146 LVTSRGPGDAPEFALEILEQ 165
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 224-318 5.80e-12

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: 65.85  E-value: 5.80e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 224 AWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLsDTGVPIKRVAVQCGFGSEETLRRS 303
Cdd:COG2169   91 RLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAGFGSLSRFYEA 169

                         90
                 ....*....|....*
gi 495288737 304 FLRAMGVTPQAYRER 318
Cdd:COG2169  170 FKKLLGMTPSAYRRG 184
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
192-323 8.25e-12

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 64.93  E-value: 8.25e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 192 QLVVFLKRPGGQSQFSVTLSlqkEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRV 271
Cdd:PRK13501 154 QLAIVLKRHRYRAEQAHLLP---DGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRL 230

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495288737 272 ETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRERFSVSP 323
Cdd:PRK13501 231 CHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRFIRSP 282
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
192-316 1.40e-08

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 55.07  E-value: 1.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 192 QLVVFLKrpggQSQFsvTLSLQKEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRV 271
Cdd:PRK13503 152 QLLVLLR----KSSL--QENGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRL 225

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495288737 272 ETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYR 316
Cdd:PRK13503 226 LKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
225-316 8.17e-08

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 50.49  E-value: 8.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 225 WISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSF 304
Cdd:PRK11511  17 WIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQTLTRTF 96

                         90
                 ....*....|..
gi 495288737 305 LRAMGVTPQAYR 316
Cdd:PRK11511  97 KNYFDVPPHKYR 108
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
181-316 1.66e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 51.98  E-value: 1.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 181 LGRTMALDVARQLVVFLKRpggQSQFSVTLSLQKEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQ 260
Cdd:PRK13502 143 LANEMAELLFGQLVMTLKR---HRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGM 219

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 495288737 261 TPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYR 316
Cdd:PRK13502 220 TINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 8-118 2.82e-07

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: 48.36  E-value: 2.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   8 IHVLAFANVQVLDVTGPLQVFASANdiarqqglpppYTPSVIASGGGAVMSSAGLALLaeplakqgsDTLIIAGGWG-VY 86
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAG-----------AEVDVVSPDGGPVESDVDLDDY---------DGLILPGGPGtPD 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495288737  87 AAAKDESLVAWVREHATGCRRVASVCTGAFLL 118
Cdd:cd01653   61 DLARDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 8-118 5.60e-07

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: 47.20  E-value: 5.60e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   8 IHVLAFANVQVLDVTGPLQVFASANdiarqqglpppYTPSVIASGGGAVMSSAGLALLaeplakqgsDTLIIAGGWG-VY 86
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAG-----------AEVDVVSPDGGPVESDVDLDDY---------DGLILPGGPGtPD 60

                         90       100       110
                 ....*....|....*....|....*....|..
gi 495288737  87 AAAKDESLVAWVREHATGCRRVASVCTGAFLL 118
Cdd:cd03128   61 DLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 6-179 1.53e-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: 47.41  E-value: 1.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737   6 KTIHVLAFANVQVLDVTGPLQVFASANdiarqqglpppYTPSVIASGGGA-VMSSAGLALLAEPLAKQGS----DTLIIA 80
Cdd:COG0693    3 KKVLILLTDGFEDEELTVPYDALREAG-----------AEVDVASPEGGPpVTSKHGITVTADKTLDDVDpddyDALVLP 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  81 GGWGVYAA-AKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRvVTHWTRCE-QLAQQHPKLQVEPnpiFINDG 158
Cdd:COG0693   72 GGHGAPDDlREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRK-VTSFPNIEdDLKNAGATYVDEE---VVVDG 147

                        170       180
                 ....*....|....*....|.
gi 495288737 159 PVWTSAGVTAGIDLALAMVEE 179
Cdd:COG0693  148 NLITSRGPGDAPAFARALLEL 168
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
192-316 3.28e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 48.17  E-value: 3.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 192 QLVVFLKRpggQSQFSVTLSLQKEGNRFDDLHAWISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTPARAIELIRV 271
Cdd:PRK13500 184 QLVMLLNR---HRYTSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRV 260

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 495288737 272 ETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYR 316
Cdd:PRK13500 261 CHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETGMTPSQWR 305
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
226-318 5.81e-06

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 47.28  E-value: 5.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 226 ISENLTKDLGIPTLALQAGMSErSFVRH-YRADTGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSF 304
Cdd:PRK10572 192 ISDHLASEFDIESVAQHVCLSP-SRLAHlFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVF 270

                         90
                 ....*....|....
gi 495288737 305 LRAMGVTPQAYRER 318
Cdd:PRK10572 271 KKCTGASPSEFRAR 284
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 75-178 1.53e-05

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: 44.47  E-value: 1.53e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737  75 DTLIIAGGW-GVYAAAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTHWTRCEQLAQQHpklqVEPNPI 153
Cdd:cd03135   62 DAIVIPGGLpGAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLGGAN----YVDEPV 137

                         90       100
                 ....*....|....*....|....*
gi 495288737 154 FInDGPVWTSAGVTAGIDLALAMVE 178
Cdd:cd03135  138 VV-DGNIITSRGPGTAFEFALKIVE 161
PRK10371 PRK10371
transcriptional regulator MelR;
259-316 1.96e-05

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 45.58  E-value: 1.96e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495288737 259 GQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYR 316
Cdd:PRK10371 233 QLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYSTFGKYVGMSPQQYR 290
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 75-132 8.71e-05

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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 42.64  E-value: 8.71e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 495288737  75 DTLIIAGGWGVYAAAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRVVTH 132
Cdd:cd03169   78 DALVIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAY 135
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 280-316 1.18e-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: 39.06  E-value: 1.18e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 495288737  280 DTGVPIKRVAVQCGFgSEETLRRSFLRAMGVTPQAYR 316
Cdd:pfam00165   6 STNLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYR 41
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 226-318 1.61e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 42.61  E-value: 1.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495288737 226 ISENLTKDLGIPTLALQAGMSERSFVRHYRADtGQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFL 305
Cdd:PRK09978 151 INNNIAHEWTLARIASELLMSPSLLKKKLREE-ETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFR 229

                         90
                 ....*....|...
gi 495288737 306 RAMGVTPQAYRER 318
Cdd:PRK09978 230 NYYGMTPTEYQER 242
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 75-129 6.61e-04

A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus; A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus furiosus. This group includes proteins similar to PfpI from P. furiosus. and PH1704 from Pyrococcus horikoshii. These enzymes are ATP-independent intracellular proteases and 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. For PH1704, it is believed that this Cys together with a different His in one monomer and Glu (from an adjacent monomer) forms a different catalytic triad from the typical GATase1domain. PfpI is homooligomeric. Protease activity is only found for oligomeric forms of PH1704.


Pssm-ID: 153228 [Multi-domain]  Cd Length: 165  Bit Score: 39.84  E-value: 6.61e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495288737  75 DTLIIAGGWGVYAAAKDESLVAWVREHATGCRRVASVCTGAFLLAASGWLDGRRV 129
Cdd:cd03134   64 DALVIPGGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKL 118
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 248-322 1.76e-03

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 39.36  E-value: 1.76e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495288737 248 RSFVRHYRadtgQTPARAIELIRVETARRLLSDTGVPIKRVAVQCGFGSEETLRRSFLRAMGVTPQAYRERFSVS 322
Cdd:PRK10296 207 RATRRYYG----KTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLTEF 277
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 226-262 4.61e-03

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: 34.44  E-value: 4.61e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 495288737  226 ISENLTKDLGIPTLALQAGMSERSFVRHYRADTGQTP 262
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTP 37
 
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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