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Conserved domains on  [gi|2181841798|ref|WP_235437897|]
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GlxA family transcriptional regulator [Kitasatospora griseola]

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 ...
 24-286 8.10e-105

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: 308.24  E-value: 8.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  24 DPVQSCDACRIDRLCSLDELAKAHTVIVPGWPDVTQAPPTALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATH 103
Cdd:COG4977    45 GPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTH 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 104 WAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVMPHQTPDEQA-PSSSPSE 182
Cdd:COG4977   125 WEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAqFSPLLVP 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 183 PGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQ 262
Cdd:COG4977   205 LGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAA 284

                         250       260
                  ....*....|....*....|....
gi 2181841798 263 TGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:COG4977   285 CGFGSASHFRRAFRRRFGVSPSAY 308
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 24-286 8.10e-105

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: 308.24  E-value: 8.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  24 DPVQSCDACRIDRLCSLDELAKAHTVIVPGWPDVTQAPPTALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATH 103
Cdd:COG4977    45 GPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTH 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 104 WAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVMPHQTPDEQA-PSSSPSE 182
Cdd:COG4977   125 WEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAqFSPLLVP 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 183 PGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQ 262
Cdd:COG4977   205 LGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAA 284

                         250       260
                  ....*....|....*....|....
gi 2181841798 263 TGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:COG4977   285 CGFGSASHFRRAFRRRFGVSPSAY 308
ftrA PRK09393
transcriptional activator FtrA; Provisional
 1-286 1.86e-102

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 302.65  E-value: 1.86e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798   1 MFGVNRAGAGlvDPWYDFAAYVVDPVQSCDACRIDRLC--SLDELAKAHTVIVPGWPDVTQAPPTALVNAIRDAHEAGAR 78
Cdd:PRK09393   31 IFGLPRPELG--VDWYRFAVAAVEPGPLRAAGGITVVAdgGLELLDRADTIVIPGWRGPDAPVPEPLLEALRAAHARGAR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  79 IVSAGTGAFVLAAAGLLDGRRVATHWAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAK 158
Cdd:PRK09393  109 LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAAN 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 159 ALAHRLVMPHQTPDEQAPSSSPSEPGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLL 238
Cdd:PRK09393  189 RVARRLVVPPHRDGGQAQFVPRPVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLL 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2181841798 239 TQRVQLAQRLLETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:PRK09393  269 RERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAY 316
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 13-167 1.40e-58

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: 185.78  E-value: 1.40e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  13 DPWYDFAAYVVDP--VQSCDACRIDRLCSLDELAKAHTVIVPGWPDV-TQAPPTALVNAIRDAHEAGARIVSAGTGAFVL 89
Cdd:cd03137    30 PPAYELRVCSPEGgpVRSSSGLSLVADAGLDALAAADTVIVPGGPDVdGRPPPPALLAALRRAAARGARVASVCTGAFVL 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181841798  90 AAAGLLDGRRVATHWAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVMP 167
Cdd:cd03137   110 AEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVARRLVVP 187
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
204-286 6.53e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 90.30  E-value: 6.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  204 QVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPP 283
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ...
gi 2181841798  284 DSY 286
Cdd:smart00342  81 SEY 83
HTH_18 pfam12833
Helix-turn-helix domain;
210-286 6.10e-18

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 76.86  E-value: 6.10e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181841798 210 MAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLL-ETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEY 78
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 24-286 8.10e-105

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: 308.24  E-value: 8.10e-105
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  24 DPVQSCDACRIDRLCSLDELAKAHTVIVPGWPDVTQAPPTALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATH 103
Cdd:COG4977    45 GPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTH 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 104 WAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVMPHQTPDEQA-PSSSPSE 182
Cdd:COG4977   125 WEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAqFSPLLVP 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 183 PGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQ 262
Cdd:COG4977   205 LGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAA 284

                         250       260
                  ....*....|....*....|....
gi 2181841798 263 TGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:COG4977   285 CGFGSASHFRRAFRRRFGVSPSAY 308
ftrA PRK09393
transcriptional activator FtrA; Provisional
 1-286 1.86e-102

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 302.65  E-value: 1.86e-102
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798   1 MFGVNRAGAGlvDPWYDFAAYVVDPVQSCDACRIDRLC--SLDELAKAHTVIVPGWPDVTQAPPTALVNAIRDAHEAGAR 78
Cdd:PRK09393   31 IFGLPRPELG--VDWYRFAVAAVEPGPLRAAGGITVVAdgGLELLDRADTIVIPGWRGPDAPVPEPLLEALRAAHARGAR 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  79 IVSAGTGAFVLAAAGLLDGRRVATHWAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAK 158
Cdd:PRK09393  109 LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAAN 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 159 ALAHRLVMPHQTPDEQAPSSSPSEPGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLL 238
Cdd:PRK09393  189 RVARRLVVPPHRDGGQAQFVPRPVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLL 268

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 2181841798 239 TQRVQLAQRLLETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:PRK09393  269 RERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAY 316
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 13-167 1.40e-58

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: 185.78  E-value: 1.40e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  13 DPWYDFAAYVVDP--VQSCDACRIDRLCSLDELAKAHTVIVPGWPDV-TQAPPTALVNAIRDAHEAGARIVSAGTGAFVL 89
Cdd:cd03137    30 PPAYELRVCSPEGgpVRSSSGLSLVADAGLDALAAADTVIVPGGPDVdGRPPPPALLAALRRAAARGARVASVCTGAFVL 109

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181841798  90 AAAGLLDGRRVATHWAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVMP 167
Cdd:cd03137   110 AEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVARRLVVP 187
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 25-167 7.50e-33

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: 119.61  E-value: 7.50e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  25 PVQSCDACRIDRLCSLDELAKAHTVIVPGWPDVTQAPPTALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATHW 104
Cdd:cd03136    44 PVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHW 123

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181841798 105 AHADLLAARYPRVRVdTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVMP 167
Cdd:cd03136   124 EHLEAFAEAFPRVQV-TRDLFEIDGDRLTCAGGTAALDLMLELIARDHGAALAARVAEQFLHD 185
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 38-166 3.34e-31

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: 115.44  E-value: 3.34e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  38 CSLDELAKAHTVIVPG---WPD---VTQAPPtaLVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATHWAHADLLA 111
Cdd:cd03138    62 ATLADVPAPDLVIVPGlggDPDellLADNPA--LIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFR 139

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2181841798 112 ARYPRVRVDTDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRLVM 166
Cdd:cd03138   140 RRFPKVRLDPDRVVVTDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 24-164 4.18e-27

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: 104.16  E-value: 4.18e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  24 DPVQSCDACRIDRLCSLDELAKAHTVIVPGWPDVTQAPP-TALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVAT 102
Cdd:cd03139    41 GPVSSRSGLTVLPDTSFADPPDLDVLLVPGGGGTRALVNdPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATT 120

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2181841798 103 HWAHADLLAARYPRVRVdtDALYVDEGDILSSAGGAATIDLFLHLVRLDHGAAVAKALAHRL 164
Cdd:cd03139   121 HWAAIDWLKEFGAIVVV--DARWVVDGNIWTSGGVSAGIDMALALVARLFGEELAQAVALLI 180
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
204-286 6.53e-23

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 90.30  E-value: 6.53e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  204 QVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPP 283
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ...
gi 2181841798  284 DSY 286
Cdd:smart00342  81 SEY 83
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
64-286 9.72e-22

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 92.15  E-value: 9.72e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  64 ALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATHWAHADLLAARYPRVRVDTDALYVDEGDILSSAGGAATIDL 143
Cdd:COG2207    28 ILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLLLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 144 FLHLVRLDHGAAVAKALAHRLVMPHQTPDEQAPSSSPSEPGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVR 223
Cdd:COG2207   108 LLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSR 187

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2181841798 224 RFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:COG2207   188 LFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250
HTH_18 pfam12833
Helix-turn-helix domain;
210-286 6.10e-18

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 76.86  E-value: 6.10e-18
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2181841798 210 MAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLL-ETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEY 78
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 176-286 1.49e-11

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: 64.30  E-value: 1.49e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 176 PSSSPSEPGAEDRVlTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETThLS 255
Cdd:COG2169    73 PDLAPGSPPRADLV-ARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTG-LS 150

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2181841798 256 IEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:COG2169   151 VTDAAYAAGFGSLSRFYEAFKKLLGMTPSAY 181
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 38-150 1.56e-10

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: 58.81  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  38 CSLDELAKAH--TVIVPG---WPDvTQAPPTALVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATHWAH-ADLLA 111
Cdd:pfam01965  52 ASLDDVKPDDydALVLPGgraGPE-RLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVkDDLIN 130

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2181841798 112 ARYPRVrvdtDALYVDEGDILSSAGGAATIDLFLHLVRL 150
Cdd:pfam01965 131 AGATYV----DKPVVVDGNLVTSRGPGDAPEFALEILEQ 165
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
149-286 4.82e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 56.22  E-value: 4.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 149 RLDHGAAVAKALAHRLVMP---HQTPDEQAPSSSpsepgaEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRF 225
Cdd:PRK13502  140 RDPLANEMAELLFGQLVMTlkrHRYATDDLPATS------RETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQF 213

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2181841798 226 RAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:PRK13502  214 RAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQW 274
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
188-286 5.82e-08

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 53.05  E-value: 5.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 188 RVLtEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGT 267
Cdd:PRK10572  184 RVR-EACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDD 262

                          90
                  ....*....|....*....
gi 2181841798 268 AATLRRHFSRTVGVPPDSY 286
Cdd:PRK10572  263 QLYFSRVFKKCTGASPSEF 281
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
177-286 2.65e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 51.26  E-value: 2.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 177 SSSPSEPGAEDRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSI 256
Cdd:PRK13500  195 TSDSLPPTSSETLLDKLITRLAASLKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLI 274

                          90       100       110
                  ....*....|....*....|....*....|
gi 2181841798 257 EQVATQTGMGTAATLRRHFSRTVGVPPDSY 286
Cdd:PRK13500  275 SDISTECGFEDSNYFSVVFTRETGMTPSQW 304
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 201-237 7.37e-07

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: 45.22  E-value: 7.37e-07
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2181841798 201 LDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWL 237
Cdd:pfam00165   5 LSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
193-286 3.36e-06

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 45.48  E-value: 3.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 193 VLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRV-QLAQRLLETTHlSIEQVATQTGMGTAATL 271
Cdd:PRK11511   14 ILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMtEIAQKLKESNE-PILYLAERYGFESQQTL 92

                          90
                  ....*....|....*
gi 2181841798 272 RRHFSRTVGVPPDSY 286
Cdd:PRK11511   93 TRTFKNYFDVPPHKY 107
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
187-286 1.05e-05

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 43.76  E-value: 1.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 187 DRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMG 266
Cdd:PRK10219    4 QKIIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYV 83

                          90       100
                  ....*....|....*....|
gi 2181841798 267 TAATLRRHFSRTVGVPPDSY 286
Cdd:PRK10219   84 SQQTFSRVFRRQFDRTPSDY 103
PRK10130 PRK10130
HTH-type transcriptional regulator EutR;
152-264 1.87e-05

HTH-type transcriptional regulator EutR;


Pssm-ID: 182258 [Multi-domain]  Cd Length: 350  Bit Score: 45.68  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 152 HGAAVAKALAHRLVMPHQTPDEQAPSSSPSEPGAED---RVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAG 228
Cdd:PRK10130  201 HQPAVRKVLGDNLLMAMGAMLEEAQPMVTAESISHQsyrRLLSRAREYVLENMSEPVTVLDLCNQLHVSRRTLQNAFHAI 280

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2181841798 229 TGMAPLQWLLTQRVQLAQRLL---ETTHLSIEQVATQTG 264
Cdd:PRK10130  281 LGIGPNAWLKRIRLNAVRRELispWSQSTTVKDAAMQWG 319
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
187-276 1.14e-04

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 43.13  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 187 DRVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMG 266
Cdd:PRK13503  170 DARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFG 249

                          90
                  ....*....|....
gi 2181841798 267 TA---ATL-RRHFS 276
Cdd:PRK13503  250 DSnhfSTLfRREFS 263
PRK10371 PRK10371
transcriptional regulator MelR;
188-286 3.87e-04

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 41.34  E-value: 3.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 188 RVLTEVLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGT 267
Cdd:PRK10371  191 FYVSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRS 270

                          90
                  ....*....|....*....
gi 2181841798 268 AATLRRHFSRTVGVPPDSY 286
Cdd:PRK10371  271 SSRFYSTFGKYVGMSPQQY 289
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
197-286 4.95e-04

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 41.32  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 197 AAGRL---DQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWlltQRVQLAQRLLE--TTHLSIEQVATQTGMGTAATL 271
Cdd:PRK15435   89 HACRLleqETPVTLEALADQVAMSPFHLHRLFKATTGMTPKAW---QQAWRARRLREalAKGESVTTSILNAGFPDSSSY 165

                          90
                  ....*....|....*
gi 2181841798 272 RRHFSRTVGVPPDSY 286
Cdd:PRK15435  166 YRKADETLGMTAKQF 180
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
193-286 1.12e-03

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 39.89  E-value: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798 193 VLSWAAGRLDQQVTVEDMAQQANVSRRTLVRRFRAGTGMAPLQWLLTQRVQLAQRLLETTHLSIEQVATQTGMGTAATLR 272
Cdd:PRK13501  181 IMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFS 260

                          90
                  ....*....|....
gi 2181841798 273 RHFSRTVGVPPDSY 286
Cdd:PRK13501  261 AVFTREAGMTPRDY 274
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 65-105 3.07e-03

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: 38.01  E-value: 3.07e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2181841798  65 LVNAIRDAHEAGARIVSAGTGAFVLAAAGLLDGRRVATHWA 105
Cdd:cd03169    97 VLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPA 137
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 64-150 3.35e-03

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


Pssm-ID: 440457 [Multi-domain]  Cd Length: 170  Bit Score: 37.78  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2181841798  64 ALVNAIRDAHEAGaRIVSA-GTGAFVLAAAGLLDGRRVATHWAHADLLAARyprvrvdtDALYVDE-----GDILSSAGG 137
Cdd:COG0693    85 DVVALVREFYEAG-KPVAAiCHGPAVLAAAGLLKGRKVTSFPNIEDDLKNA--------GATYVDEevvvdGNLITSRGP 155

                          90
                  ....*....|...
gi 2181841798 138 AATIDLFLHLVRL 150
Cdd:COG0693   156 GDAPAFARALLEL 168
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 35-89 7.49e-03

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: 35.25  E-value: 7.49e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2181841798  35 DRLCSLDELAKAHTVIVPGWPDVTQAPP--TALVNAIRDAHEAGARIVSAGTGAFVL 89
Cdd:cd03128    36 GPVESDVDLDDYDGLILPGGPGTPDDLAwdEALLALLREAAAAGKPVLGICLGAQLL 92
 
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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