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Conserved domains on  [gi|549799425|ref|WP_022562854|]
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GlxA family transcriptional regulator [Agrobacterium pusense]

Protein Classification

GlxA family transcriptional regulator( domain architecture ID 11471967)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-335 3.45e-104

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: 308.62  E-value: 3.45e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  15 LSVAFLLADRFTLSAFANFVDVLRLAADEADRSrpiLCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGlI 94
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGRP---LYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGG-L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  95 SDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLTCS 174
Cdd:COG4977   77 DPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 175 GGHGAAHLAAFLVERHVGQSAAIKSLNIMMIDSALSGEKPQPGQQSTRKA-SDPLVKKAILRMQQNIEVPKTVLELASDL 253
Cdd:COG4977  157 GGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGhRDPRLARAQAWMEANLEEPLSVDELARRA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 254 GLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRKTQAGHT 333
Cdd:COG4977  237 GMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316


                 ..
gi 549799425 334 AT 335
Cdd:COG4977  317 AA 318
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-335 3.45e-104

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: 308.62  E-value: 3.45e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  15 LSVAFLLADRFTLSAFANFVDVLRLAADEADRSrpiLCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGlI 94
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGRP---LYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGG-L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  95 SDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLTCS 174
Cdd:COG4977   77 DPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 175 GGHGAAHLAAFLVERHVGQSAAIKSLNIMMIDSALSGEKPQPGQQSTRKA-SDPLVKKAILRMQQNIEVPKTVLELASDL 253
Cdd:COG4977  157 GGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGhRDPRLARAQAWMEANLEEPLSVDELARRA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 254 GLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRKTQAGHT 333
Cdd:COG4977  237 GMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316


                 ..
gi 549799425 334 AT 335
Cdd:COG4977  317 AA 318
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 17-206 2.68e-72

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: 222.46  E-value: 2.68e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEADRsrpILCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGLISD 96
Cdd:cd03136    1 FGFLLLPGFSLLALASAIEPLRAANRLAGR---ELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  97 HSAlPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMiSDQIFVIDRDRLTCSGG 176
Cdd:cd03136   78 RAV-TPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEIDGDRLTCAGG 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 549799425 177 HGAAHLAAFLVERHVGQSAAIKSLNIMMID 206
Cdd:cd03136  156 TAALDLMLELIARDHGAALAARVAEQFLHD 185
ftrA PRK09393
transcriptional activator FtrA; Provisional
 53-327 1.51e-23

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 98.88  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  53 EWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGliSDHSALPPEAL-RFLKDRATAGVPIVGLCTGVFILHEA 131
Cdd:PRK09393  45 RFAVAAVEPGPLRAAGGITVVADGGLELLDRADTIVIPGW--RGPDAPVPEPLlEALRAAHARGARLCSICSGVFVLAAA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 132 GLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLTCSGGHGAAHLAAFLVERHVGQSAAIKSLNIMMIDSALSG 211
Cdd:PRK09393 123 GLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 212 EKPQPGQQSTRKASDPLVKKAILRMQQNIEVPKTVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTT 291
Cdd:PRK09393 203 GQAQFVPRPVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESS 282

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 549799425 292 HDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRK 327
Cdd:PRK09393 283 ALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRK 318
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
245-326 5.99e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 80.29  E-value: 5.99e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425   245 TVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSE 324
Cdd:smart00342   3 TLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSE 82


                   ..
gi 549799425   325 YR 326
Cdd:smart00342  83 YR 84
HTH_18 pfam12833
Helix-turn-helix domain;
249-327 3.85e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 75.32  E-value: 3.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  249 LASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLL-RTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRK 327
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-335 3.45e-104

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: 308.62  E-value: 3.45e-104
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  15 LSVAFLLADRFTLSAFANFVDVLRLAADEADRSrpiLCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGlI 94
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGRP---LYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGG-L 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  95 SDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLTCS 174
Cdd:COG4977   77 DPAAAADPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSA 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 175 GGHGAAHLAAFLVERHVGQSAAIKSLNIMMIDSALSGEKPQPGQQSTRKA-SDPLVKKAILRMQQNIEVPKTVLELASDL 253
Cdd:COG4977  157 GGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGhRDPRLARAQAWMEANLEEPLSVDELARRA 236

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 254 GLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRKTQAGHT 333
Cdd:COG4977  237 GMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316


                 ..
gi 549799425 334 AT 335
Cdd:COG4977  317 AA 318
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 17-206 2.68e-72

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: 222.46  E-value: 2.68e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEADRsrpILCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGLISD 96
Cdd:cd03136    1 FGFLLLPGFSLLALASAIEPLRAANRLAGR---ELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGAR 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  97 HSAlPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMiSDQIFVIDRDRLTCSGG 176
Cdd:cd03136   78 RAV-TPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEIDGDRLTCAGG 155

                        170       180       190
                 ....*....|....*....|....*....|
gi 549799425 177 HGAAHLAAFLVERHVGQSAAIKSLNIMMID 206
Cdd:cd03136  156 TAALDLMLELIARDHGAALAARVAEQFLHD 185
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 17-206 5.48e-34

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: 123.91  E-value: 5.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEADRSRPI--LCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVG-GL 93
Cdd:cd03138    1 VTLLAYPGALASSLAGLLDLLRAANRLARRQQGGapPFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVPGlGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  94 ISDHSALP--PEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRL 171
Cdd:cd03138   81 DPDELLLAdnPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLI 160

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 549799425 172 TCSGGHGAAHLAAFLVERHVGQSAAIKSLNIMMID 206
Cdd:cd03138  161 TAGGAMAWADLALHLIERLAGPELAQLVARFLLID 195
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 17-196 1.47e-30

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: 114.52  E-value: 1.47e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEADRSRpilCEWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGLISD 96
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRALGPPA---YELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVPGGPDVD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  97 HSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLTcSGG 176
Cdd:cd03137   78 GRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWT-SAG 156

                        170       180
                 ....*....|....*....|.
gi 549799425 177 HGAA-HLAAFLVERHVGQSAA 196
Cdd:cd03137  157 VTAGiDLCLHLVREDLGAAVA 177
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 17-196 3.29e-24

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: 97.61  E-value: 3.29e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEADRSRPILcewsvLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGLISD 96
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFL-----VSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGGGTR 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  97 HSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQmiSDQIFVIDRDRLTcSGG 176
Cdd:cd03139   76 ALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVV--VDARWVVDGNIWT-SGG 152

                        170       180
                 ....*....|....*....|.
gi 549799425 177 HGAAH-LAAFLVERHVGQSAA 196
Cdd:cd03139  153 VSAGIdMALALVARLFGEELA 173
ftrA PRK09393
transcriptional activator FtrA; Provisional
 53-327 1.51e-23

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 98.88  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  53 EWSVLSATLGSVQSSCGVKVQPDTRLSDAGHYDYIVVVGGliSDHSALPPEAL-RFLKDRATAGVPIVGLCTGVFILHEA 131
Cdd:PRK09393  45 RFAVAAVEPGPLRAAGGITVVADGGLELLDRADTIVIPGW--RGPDAPVPEPLlEALRAAHARGARLCSICSGVFVLAAA 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 132 GLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLTCSGGHGAAHLAAFLVERHVGQSAAIKSLNIMMIDSALSG 211
Cdd:PRK09393 123 GLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRLVVPPHRDG 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 212 EKPQPGQQSTRKASDPLVKKAILRMQQNIEVPKTVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTT 291
Cdd:PRK09393 203 GQAQFVPRPVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESS 282

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 549799425 292 HDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRK 327
Cdd:PRK09393 283 ALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRK 318
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
245-326 5.99e-19

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 80.29  E-value: 5.99e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425   245 TVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSE 324
Cdd:smart00342   3 TLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTPSE 82


                   ..
gi 549799425   325 YR 326
Cdd:smart00342  83 YR 84
HTH_18 pfam12833
Helix-turn-helix domain;
249-327 3.85e-17

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 75.32  E-value: 3.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  249 LASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLL-RTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRK 327
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
93-330 6.64e-17

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 79.44  E-value: 6.64e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  93 LISDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRCCVSWFHHQDFLDRFDTVQMISDQIFVIDRDRLT 172
Cdd:COG2207   26 LLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLLL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 173 CSGGHGAAHLAAFLVERHVGQSAAIKSLNIMMIDSALSGEKPQPGQQSTRKASDPLVKKAILRMqqnievpkTVLELASD 252
Cdd:COG2207  106 LLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLL--------TLEELARE 177

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 549799425 253 LGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRKTQA 330
Cdd:COG2207  178 LGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLR 255
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 16-175 1.77e-14

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: 70.36  E-value: 1.77e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425   16 SVAFLLADRFTLSAFANFVDVLRlaadEADrsrpilCEWSVLSATLGSVQSSCGVKVQPDTRLSDA--GHYDYIVVVGGL 93
Cdd:pfam01965   2 KVLVLLADGFEDIELIYPADVLR----RAG------IKVTVVSVDGGEVKGSRGVKVTVDASLDDVkpDDYDALVLPGGR 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425   94 -ISDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRcCVSWFHHQDFLDRfdTVQMISDQIFVIDRDRLT 172
Cdd:pfam01965  72 aGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRK-VTSHPAVKDDLIN--AGATYVDKPVVVDGNLVT 148


                  ...
gi 549799425  173 CSG 175
Cdd:pfam01965 149 SRG 151
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 17-139 9.14e-12

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: 62.81  E-value: 9.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEADrsrpilcewsVLSATLG-SVQSSCGVKVQPDTRLSD--AGHYDYIVVVGGL 93
Cdd:COG0693    5 VLILLTDGFEDEELTVPYDALREAGAEVD----------VASPEGGpPVTSKHGITVTADKTLDDvdPDDYDALVLPGGH 74

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 549799425  94 IS-DHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRC 139
Cdd:COG0693   75 GApDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKV 121
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 215-334 3.62e-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: 63.53  E-value: 3.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 215 QPGQQSTRKASDPLVKKAILRMQQNIEVPKTVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLrTTHDP 294
Cdd:COG2169   72 RPDLAPGSPPRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLS 150

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 549799425 295 ITQISLATGFCDAPHLSRTLRTERGFTPSEYRKTQAGHTA 334
Cdd:COG2169  151 VTDAAYAAGFGSLSRFYEAFKKLLGMTPSAYRRGGAGAAI 190
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 54-144 1.29e-09

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: 56.40  E-value: 1.29e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  54 WSVLSATLGSVQSSCG----VKVQPDTRLSDAGHYDYIVVV--GGLISDHSALPPEALRFLKDRATAGVPIVGLCTGVFI 127
Cdd:cd03134   27 AEVVVAGPEAGGEIQGkhgyDTVTVDLTIADVDADDYDALVipGGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWV 106

                         90
                 ....*....|....*..
gi 549799425 128 LHEAGLLDGYRCCvSWF 144
Cdd:cd03134  107 LISAGVVRGRKLT-SYP 122
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 17-128 6.99e-09

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: 52.99  E-value: 6.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAAdeadrsrpilCEWSVLSATLGSVQSscgvkvqpdtrLSDAGHYDYIVVVGGLISD 96
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAG----------AEVDVVSPDGGPVES-----------DVDLDDYDGLILPGGPGTP 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 549799425  97 HSALP-PEALRFLKDRATAGVPIVGLCTGVFIL 128
Cdd:cd01653   60 DDLARdEALLALLREAAAAGKPILGICLGAQLL 92
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 54-138 8.46e-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: 54.15  E-value: 8.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  54 WSVLSATLGS--VQSSCGVKVQPDTRLSD--AGHYDYIVVVGGLISDHSAlPPEALRFLKDRATAGVPIVGLCTGVFILH 129
Cdd:cd03140   27 FEVRTVSPTGepVTSIGGLRVVPDYSLDDlpPEDYDLLILPGGDSWDNPE-APDLAGLVRQALKQGKPVAAICGATLALA 105


                 ....*....
gi 549799425 130 EAGLLDGYR 138
Cdd:cd03140  106 RAGLLNNRK 114
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 17-128 1.78e-08

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: 51.43  E-value: 1.78e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAAdeadrsrpilCEWSVLSATLGSVQSscgvkvqpdtrLSDAGHYDYIVVVGGLISD 96
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAG----------AEVDVVSPDGGPVES-----------DVDLDDYDGLILPGGPGTP 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 549799425  97 HSALP-PEALRFLKDRATAGVPIVGLCTGVFIL 128
Cdd:cd03128   60 DDLAWdEALLALLREAAAAGKPVLGICLGAQLL 92
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
236-328 6.77e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 50.31  E-value: 6.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 236 MQQNIEVPKTVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLR 315
Cdd:PRK10219  14 IDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVFR 93

                         90
                 ....*....|...
gi 549799425 316 TERGFTPSEYRKT 328
Cdd:PRK10219  94 RQFDRTPSDYRHR 106
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 71-139 3.44e-06

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: 46.87  E-value: 3.44e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799425  71 KVQPDTrlsdaghYDYIVVVGGLISDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRC 139
Cdd:cd03169   71 EVDPDD-------YDALVIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRC 132
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 17-189 6.08e-06

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: 45.62  E-value: 6.08e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  17 VAFLLADRFTLSAFANFVDVLRLAADEadrsrpilcewsVLSATLG---SVQSSCGVKVQPDTRLSDA--GHYDYIVVVG 91
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAGIE------------VTTASLEkklAVGSSHGIKVKADKTLSDVnlDDYDAIVIPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425  92 GLI-SDHSALPPEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDGYRcCVSW--FHHQDFLDRFdtvqmiSDQIFVIDR 168
Cdd:cd03135   69 GLPgAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKK-ATCYpgFEDKLGGANY------VDEPVVVDG 141

                        170       180
                 ....*....|....*....|.
gi 549799425 169 DRLTCSGGHGAAHLAAFLVER 189
Cdd:cd03135  142 NIITSRGPGTAFEFALKIVEA 162
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
248-326 7.48e-06

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 46.98  E-value: 7.48e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 549799425 248 ELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYR 326
Cdd:PRK13503 192 ALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
236-327 7.51e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 46.82  E-value: 7.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 236 MQQNIEVPKTVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLR 315
Cdd:PRK13501 185 LQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFT 264

                         90
                 ....*....|..
gi 549799425 316 TERGFTPSEYRK 327
Cdd:PRK13501 265 REAGMTPRDYRQ 276
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 249-328 5.16e-05

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 44.25  E-value: 5.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 249 LASDLGLGRRSLERRFL--NDLKAtpsKVYLELRLDRALSLLRTTHD--PITQISLATGFCDAPHLSRTLRTERGFTPSE 324
Cdd:PRK09685 220 IAGELGISVRSLYRLFAeqGLVVA---QYIRNRRLDRCADDLRPAADdeKITSIAYKWGFSDSSHFSTAFKQRFGVSPGE 296


                 ....
gi 549799425 325 YRKT 328
Cdd:PRK09685 297 YRRK 300
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
280-327 4.57e-04

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 41.50  E-value: 4.57e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 549799425 280 RLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSEYRK 327
Cdd:PRK10572 236 RISRAKLLLQTTRMPIATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
224-330 7.70e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 40.81  E-value: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 224 ASDPLVKKAILRMQQNIEVPKTVLELASDLGLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATG 303
Cdd:PRK13502 173 SRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCG 252

                         90       100
                 ....*....|....*....|....*..
gi 549799425 304 FCDAPHLSRTLRTERGFTPSEYRKTQA 330
Cdd:PRK13502 253 FEDSNYFSVVFTRETGMTPSQWRHLSN 279
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 236-332 1.07e-03

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 40.29  E-value: 1.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 236 MQQNIEVPKTVLELASDLgLGRRSLERRFLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLR 315
Cdd:PRK09978 151 INNNIAHEWTLARIASEL-LMSPSLLKKKLREEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFR 229

                         90
                 ....*....|....*..
gi 549799425 316 TERGFTPSEYRKTQAGH 332
Cdd:PRK09978 230 NYYGMTPTEYQERSAQG 246
PRK15186 PRK15186
AraC family transcriptional regulator; Provisional
 245-325 6.84e-03

AraC family transcriptional regulator; Provisional


Pssm-ID: 185108 [Multi-domain]  Cd Length: 291  Bit Score: 37.74  E-value: 6.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 549799425 245 TVLELASDLGLGRRSLERRfLNDLKATPSKVYLELRLDRALSLLRTTHDPITQISLATGFCDAPHLSRTLRTERGFTPSE 324
Cdd:PRK15186 199 ALKDISDSLYMSCSTLKRK-LKQENTSFSEVYLNARMNKATKLLRNSEYNITRVAYMCGYDSASYFTCVFKKHFKTTPSE 277


                 .
gi 549799425 325 Y 325
Cdd:PRK15186 278 F 278
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
75-136 8.14e-03

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 37.02  E-value: 8.14e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 549799425  75 DTRLSDaghYDYIVVVGGL----------ISDHSalppEALRFLKDRATAGVPIVGLCTGVFILHEAGLLDG 136
Cdd:PRK03619  36 ETDLDG---VDAVVLPGGFsygdylrcgaIAAFS----PIMKAVKEFAEKGKPVLGICNGFQILTEAGLLPG 100
 
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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