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Conserved domains on  [gi|2519556413|ref|WP_285091816|]
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GlxA family transcriptional regulator, partial [Serratia nevei]

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 ...
 1-227 1.14e-101

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


:

Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 297.45  E-value: 1.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:COG4977    87 LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLAL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  81 ALIEDDLGATMAAGVARQLVVYHRRPGGQSQYS-LLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRL 159
Cdd:COG4977   167 HLVERDHGAELANAVARRLVVDPRRPGGQAQFSpLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERR 246

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519556413 160 FRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRRLGRA 227
Cdd:COG4977   247 FRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRA 314
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 1-227 1.14e-101

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 297.45  E-value: 1.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:COG4977    87 LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLAL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  81 ALIEDDLGATMAAGVARQLVVYHRRPGGQSQYS-LLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRL 159
Cdd:COG4977   167 HLVERDHGAELANAVARRLVVDPRRPGGQAQFSpLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERR 246

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519556413 160 FRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRRLGRA 227
Cdd:COG4977   247 FRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRA 314
ftrA PRK09393
transcriptional activator FtrA; Provisional
 7-223 7.81e-66

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 206.35  E-value: 7.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   7 HSRRARrIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLALALIEDD 86
Cdd:PRK09393  103 HARGAR-LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRD 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  87 LGATMAAGVARQLVVYHRRPGGQSQYSLLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQ 166
Cdd:PRK09393  182 FGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGM 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2519556413 167 TPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRR 223
Cdd:PRK09393  262 TPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRK 318
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-102 2.84e-53

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: 169.60  E-value: 2.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:cd03137    86 LAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAGIDLCL 165

                          90       100
                  ....*....|....*....|..
gi 2519556413  81 ALIEDDLGATMAAGVARQLVVY 102
Cdd:cd03137   166 HLVREDLGAAVANRVARRLVVP 187
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
139-222 1.24e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.91  E-value: 1.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  139 PLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSP 218
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2519556413  219 QAIR 222
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
145-223 4.36e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 78.40  E-value: 4.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 145 LADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGR-IEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRR 223
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 ...
 1-227 1.14e-101

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 297.45  E-value: 1.14e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:COG4977    87 LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGIDLAL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  81 ALIEDDLGATMAAGVARQLVVYHRRPGGQSQYS-LLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRL 159
Cdd:COG4977   167 HLVERDHGAELANAVARRLVVDPRRPGGQAQFSpLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRTLERR 246

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2519556413 160 FRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRRLGRA 227
Cdd:COG4977   247 FRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRA 314
ftrA PRK09393
transcriptional activator FtrA; Provisional
 7-223 7.81e-66

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 206.35  E-value: 7.81e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   7 HSRRARrIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLALALIEDD 86
Cdd:PRK09393  103 HARGAR-LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRD 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  87 LGATMAAGVARQLVVYHRRPGGQSQYSLLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQ 166
Cdd:PRK09393  182 FGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGM 261

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2519556413 167 TPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRR 223
Cdd:PRK09393  262 TPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRK 318
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-102 2.84e-53

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: 169.60  E-value: 2.84e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:cd03137    86 LAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAGIDLCL 165

                          90       100
                  ....*....|....*....|..
gi 2519556413  81 ALIEDDLGATMAAGVARQLVVY 102
Cdd:cd03137   166 HLVREDLGAAVANRVARRLVVP 187
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 2-99 5.56e-37

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: 127.66  E-value: 5.56e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   2 AFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNriFIRDGDIWTSAGISAGIDLALA 81
Cdd:cd03139    85 DFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDAR--WVVDGNIWTSGGVSAGIDMALA 162

                          90
                  ....*....|....*...
gi 2519556413  82 LIEDDLGATMAAGVARQL 99
Cdd:cd03139   163 LVARLFGEELAQAVALLI 180
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 1-101 2.09e-32

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: 116.21  E-value: 2.09e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVDSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:cd03138    94 IAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLAL 173

                          90       100
                  ....*....|....*....|.
gi 2519556413  81 ALIEDDLGATMAAGVARQLVV 101
Cdd:cd03138   174 HLIERLAGPELAQLVARFLLI 194
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 2-101 2.53e-29

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: 108.06  E-value: 2.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   2 AFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWYHAARLQQSYPRIRVdSNRIFIRDGDIWTSAGISAGIDLALA 81
Cdd:cd03136    86 AWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEIDGDRLTCAGGTAALDLMLE 164

                          90       100
                  ....*....|....*....|
gi 2519556413  82 LIEDDLGATMAAGVARQLVV 101
Cdd:cd03136   165 LIARDHGAALAARVAEQFLH 184
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
139-222 1.24e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 84.91  E-value: 1.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  139 PLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSP 218
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 2519556413  219 QAIR 222
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
114-227 1.05e-20

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 87.53  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 114 LLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEA 193
Cdd:COG2207   143 LLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISE 222

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2519556413 194 IARSVGFSDPERMRRAFIRVFGLSPQAIRRLGRA 227
Cdd:COG2207   223 IAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
HTH_18 pfam12833
Helix-turn-helix domain;
145-223 4.36e-19

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 78.40  E-value: 4.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 145 LADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGR-IEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRR 223
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLlLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-84 4.80e-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: 67.28  E-value: 4.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATTHWyhAARLQQSYPRIRVdSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:pfam01965  84 VEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHP--AVKDDLINAGATY-VDKPVVVDGNLVTSRGPGDAPEFAL 160


                  ....
gi 2519556413  81 ALIE 84
Cdd:pfam01965 161 EILE 164
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 120-227 3.48e-13

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: 67.39  E-value: 3.48e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 120 PSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIeESTESLEAIARSVG 199
Cdd:COG2169    81 PRADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLL-QTGLSVTDAAYAAG 159

                          90       100
                  ....*....|....*....|....*...
gi 2519556413 200 FSDPERMRRAFIRVFGLSPQAIRRLGRA 227
Cdd:COG2169   160 FGSLSRFYEAFKKLLGMTPSAYRRGGAG 187
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
124-223 4.51e-12

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 63.84  E-value: 4.51e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 124 RMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDP 203
Cdd:PRK10572  184 RVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQ 263

                          90       100
                  ....*....|....*....|
gi 2519556413 204 ERMRRAFIRVFGLSPQAIRR 223
Cdd:PRK10572  264 LYFSRVFKKCTGASPSEFRA 283
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
111-222 1.93e-09

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 56.22  E-value: 1.93e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 111 QYSLLLALNPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTES 190
Cdd:PRK13503  159 KSSLQENGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDAS 238

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2519556413 191 LEAIARSVGFSDPERMRRAFIRVFGLSPQAIR 222
Cdd:PRK13503  239 VTDIAYRCGFGDSNHFSTLFRREFSWSPRDIR 270
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
98-223 5.71e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 54.91  E-value: 5.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413  98 QLVVYHRRPGGQSQYSLLLalnPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRV 177
Cdd:PRK13501  154 QLAIVLKRHRYRAEQAHLL---PDGEQLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRL 230

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2519556413 178 EAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFGLSPQAIRR 223
Cdd:PRK13501  231 CHAKCLLRGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQ 276
PRK10371 PRK10371
transcriptional regulator MelR;
129-228 9.39e-08

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 51.36  E-value: 9.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 129 LSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRR 208
Cdd:PRK10371  197 LGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSSRFYS 276

                          90       100
                  ....*....|....*....|
gi 2519556413 209 AFIRVFGLSPQAIRRLGRAG 228
Cdd:PRK10371  277 TFGKYVGMSPQQYRKLSQQR 296
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 133-172 4.54e-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: 4.54e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2519556413 133 REHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVI 172
Cdd:pfam00165   2 RENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
119-222 6.79e-07

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 47.02  E-value: 6.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 119 NPSSDRMRAALSFAREHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSV 198
Cdd:PRK11511    5 NTDAITIHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERY 84

                          90       100
                  ....*....|....*....|....
gi 2519556413 199 GFSDPERMRRAFIRVFGLSPQAIR 222
Cdd:PRK11511   85 GFESQQTLTRTFKNYFDVPPHKYR 108
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 1-84 1.57e-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: 46.39  E-value: 1.57e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATThwYHAARLQQSYPRIrvdSNRIFIRDGDIWTSAGISAGIDLAL 80
Cdd:cd03135    83 IKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATC--YPGFEDKLGGANY---VDEPVVVDGNIITSRGPGTAFEFAL 157


                  ....
gi 2519556413  81 ALIE 84
Cdd:cd03135   158 KIVE 161
PRK13500 PRK13500
HTH-type transcriptional activator RhaR;
136-224 1.51e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184091 [Multi-domain]  Cd Length: 312  Bit Score: 45.09  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 136 LHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFG 215
Cdd:PRK13500  219 LKSPFALDKFCDEASCSERVLRQQFRQQTGMTINQYLRQVRVCHAQYLLQHSRLLISDISTECGFEDSNYFSVVFTRETG 298


                  ....*....
gi 2519556413 216 LSPQAIRRL 224
Cdd:PRK13500  299 MTPSQWRHL 307
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-84 3.98e-05

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: 42.78  E-value: 3.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413   1 VAFLTSHSRRARRIASVCTGAFILAACGLLDGKRATthwyhaarlqqSYPRIRVD--------SNRIFIRDGDIWTSAGI 72
Cdd:COG0693    87 VALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVT-----------SFPNIEDDlknagatyVDEEVVVDGNLITSRGP 155

                          90
                  ....*....|..
gi 2519556413  73 SAGIDLALALIE 84
Cdd:COG0693   156 GDAPAFARALLE 167
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 119-223 9.45e-05

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 42.33  E-value: 9.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 119 NPSSDRM-RAALSFAREHLHLP-LSVADLADAACLSERQFGRLFrAETGQTPAKVIEQLRVE--AARGRIEESTESLEAI 194
Cdd:PRK09685  192 QPRRERQfQKVVALIDQSIQEEiLRPEWIAGELGISVRSLYRLF-AEQGLVVAQYIRNRRLDrcADDLRPAADDEKITSI 270

                          90       100
                  ....*....|....*....|....*....
gi 2519556413 195 ARSVGFSDPERMRRAFIRVFGLSPQAIRR 223
Cdd:PRK09685  271 AYKWGFSDSSHFSTAFKQRFGVSPGEYRR 299
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
134-222 1.04e-04

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 40.29  E-value: 1.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 134 EHLHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRV 213
Cdd:PRK10219   16 EHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQTFSRVFRRQ 95


                  ....*....
gi 2519556413 214 FGLSPQAIR 222
Cdd:PRK10219   96 FDRTPSDYR 104
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
136-224 1.58e-04

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 41.96  E-value: 1.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2519556413 136 LHLPLSVADLADAACLSERQFGRLFRAETGQTPAKVIEQLRVEAARGRIEESTESLEAIARSVGFSDPERMRRAFIRVFG 215
Cdd:PRK13502  189 LECPFALDAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETG 268


                  ....*....
gi 2519556413 216 LSPQAIRRL 224
Cdd:PRK13502  269 MTPSQWRHL 277
 
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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