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Conserved domains on  [gi|550718760|ref|WP_022648419|]
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MULTISPECIES: GlxA family transcriptional regulator [Enterobacter]

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 ...
 2-326 1.00e-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: 311.71  E-value: 1.00e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   2 KKILIIVPDGGMLFEAAGIADILMQANRLhpdgLAQPRYRIIIATTQPHLViHGQSGLNLLADYRLPELDPrepLDTIII 81
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRL----AGRPLYRWRLVSLDGGPV-RSSSGLTVAPDHGLADLAA---ADTLIV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  82 TG-RGMNEQESTAVVDWLHLAAPHAGRVASVCggalllaqagllDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPV 160
Cdd:COG4977   73 PGgLDPAAAADPALLAWLRRAAARGARLASICtgafllaaagllDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 161 WTSGGVSSGFDLTLALVEDDYGFTLARNVAQDMVMYLRRPGGQLQFSRYNLEQSGATGPVSELQSWILQNLTADLCVERL 240
Cdd:COG4977  153 LTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDEL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 241 AERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:COG4977  233 ARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312


                 ....*.
gi 550718760 321 HCRRMA 326
Cdd:COG4977  313 RARAAA 318
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 2-326 1.00e-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: 311.71  E-value: 1.00e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   2 KKILIIVPDGGMLFEAAGIADILMQANRLhpdgLAQPRYRIIIATTQPHLViHGQSGLNLLADYRLPELDPrepLDTIII 81
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRL----AGRPLYRWRLVSLDGGPV-RSSSGLTVAPDHGLADLAA---ADTLIV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  82 TG-RGMNEQESTAVVDWLHLAAPHAGRVASVCggalllaqagllDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPV 160
Cdd:COG4977   73 PGgLDPAAAADPALLAWLRRAAARGARLASICtgafllaaagllDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 161 WTSGGVSSGFDLTLALVEDDYGFTLARNVAQDMVMYLRRPGGQLQFSRYNLEQSGATGPVSELQSWILQNLTADLCVERL 240
Cdd:COG4977  153 LTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDEL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 241 AERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:COG4977  233 ARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312


                 ....*.
gi 550718760 321 HCRRMA 326
Cdd:COG4977  313 RARAAA 318
ftrA PRK09393
transcriptional activator FtrA; Provisional
 34-320 2.82e-64

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 205.97  E-value: 2.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  34 GLAQPR-----YRIIIATTQPHlVIHGQSGLNLLADYRLPELdprEPLDTIIITG-RGMNEQESTAVVDWLHLAAPHAGR 107
Cdd:PRK09393  33 GLPRPElgvdwYRFAVAAVEPG-PLRAAGGITVVADGGLELL---DRADTIVIPGwRGPDAPVPEPLLEALRAAHARGAR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 108 VASVCGGALLLAQAGLLDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPVWTSGGVSSGFDLTLALVEDDYGFTLAR 187
Cdd:PRK09393 109 LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAAN 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 188 NVAQDMVMYLRRPGGQLQFSRYNLEQSGAtGPVSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYV 267
Cdd:PRK09393 189 RVARRLVVPPHRDGGQAQFVPRPVASRES-DRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWL 267

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 550718760 268 TEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:PRK09393 268 LRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-196 1.79e-54

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: 176.15  E-value: 1.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   4 ILIIVPDGGMLFEAAGIADILMQANRLhpdgLAQPRYRIIIATTQPHLViHGQSGLNLLADYRLPELDPrepLDTIIITG 83
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRA----LGPPAYELRVCSPEGGPV-RSSSGLSLVADAGLDALAA---ADTVIVPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  84 RGM--NEQESTAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPVW 161
Cdd:cd03137   73 GPDvdGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVW 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 550718760 162 TSGGVSSGFDLTLALVEDDYGFTLARNVAQDMVMY 196
Cdd:cd03137  153 TSAGVTAGIDLCLHLVREDLGAAVANRVARRLVVP 187
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
234-317 1.91e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 86.45  E-value: 1.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   234 DLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTP 313
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 550718760   314 GEYR 317
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
240-319 9.52e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 84.56  E-value: 9.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  240 LAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLL-EQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQ 318
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 550718760  319 R 319
Cdd:pfam12833  81 R 81
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 2-326 1.00e-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: 311.71  E-value: 1.00e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   2 KKILIIVPDGGMLFEAAGIADILMQANRLhpdgLAQPRYRIIIATTQPHLViHGQSGLNLLADYRLPELDPrepLDTIII 81
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLANRL----AGRPLYRWRLVSLDGGPV-RSSSGLTVAPDHGLADLAA---ADTLIV 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  82 TG-RGMNEQESTAVVDWLHLAAPHAGRVASVCggalllaqagllDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPV 160
Cdd:COG4977   73 PGgLDPAAAADPALLAWLRRAAARGARLASICtgafllaaagllDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDI 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 161 WTSGGVSSGFDLTLALVEDDYGFTLARNVAQDMVMYLRRPGGQLQFSRYNLEQSGATGPVSELQSWILQNLTADLCVERL 240
Cdd:COG4977  153 LTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDEL 232

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 241 AERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:COG4977  233 ARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRF 312


                 ....*.
gi 550718760 321 HCRRMA 326
Cdd:COG4977  313 RARAAA 318
ftrA PRK09393
transcriptional activator FtrA; Provisional
 34-320 2.82e-64

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 205.97  E-value: 2.82e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  34 GLAQPR-----YRIIIATTQPHlVIHGQSGLNLLADYRLPELdprEPLDTIIITG-RGMNEQESTAVVDWLHLAAPHAGR 107
Cdd:PRK09393  33 GLPRPElgvdwYRFAVAAVEPG-PLRAAGGITVVADGGLELL---DRADTIVIPGwRGPDAPVPEPLLEALRAAHARGAR 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 108 VASVCGGALLLAQAGLLDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPVWTSGGVSSGFDLTLALVEDDYGFTLAR 187
Cdd:PRK09393 109 LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAAN 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 188 NVAQDMVMYLRRPGGQLQFSRYNLEQSGAtGPVSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYV 267
Cdd:PRK09393 189 RVARRLVVPPHRDGGQAQFVPRPVASRES-DRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWL 267

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 550718760 268 TEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:PRK09393 268 LRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRF 320
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-196 1.79e-54

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: 176.15  E-value: 1.79e-54
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   4 ILIIVPDGGMLFEAAGIADILMQANRLhpdgLAQPRYRIIIATTQPHLViHGQSGLNLLADYRLPELDPrepLDTIIITG 83
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRA----LGPPAYELRVCSPEGGPV-RSSSGLSLVADAGLDALAA---ADTVIVPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  84 RGM--NEQESTAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATTHWRLLETLKTRYPAVNVEGGPLYVQDGPVW 161
Cdd:cd03137   73 GPDvdGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVW 152

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 550718760 162 TSGGVSSGFDLTLALVEDDYGFTLARNVAQDMVMY 196
Cdd:cd03137  153 TSAGVTAGIDLCLHLVREDLGAAVANRVARRLVVP 187
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-195 2.49e-27

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: 105.81  E-value: 2.49e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   4 ILIIVPDGGMLFEAAGIADILMQANRLHPDGL---AQPRYRIIIATTQPHLVIHGQSGLNLLAdyrlpeLDPREPLDTII 80
Cdd:cd03138    1 VTLLAYPGALASSLAGLLDLLRAANRLARRQQggaPPFEVRLVSLDGGPVLLAGGILILPDAT------LADVPAPDLVI 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  81 ITGRGMNEQE-----STAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATTHWRLLETLKTRYPAVNVEGGPLYV 155
Cdd:cd03138   75 VPGLGGDPDEllladNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVV 154

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 550718760 156 QDGPVWTSGGVSSGFDLTLALVEDDYGFTLARNVAQDMVM 195
Cdd:cd03138  155 TDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 4-193 1.72e-23

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: 95.30  E-value: 1.72e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   4 ILIIVPDGGMLFEAAGIADILMQANRLHPDglAQPRYriIIATTQPhlvIHGQSGLNLLADYRLPELDPrepLDTIIITG 83
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAP--FEVFL--VSETGGP---VSSRSGLTVLPDTSFADPPD---LDVLLVPG 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  84 rGMN---EQESTAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATTHWRLLETLKTRYPAVNVEGgpLYVQDGPV 160
Cdd:cd03139   71 -GGGtraLVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDA--RWVVDGNI 147

                        170       180       190
                 ....*....|....*....|....*....|...
gi 550718760 161 WTSGGVSSGFDLTLALVEDDYGFTLARNVAQDM 193
Cdd:cd03139  148 WTSGGVSAGIDMALALVARLFGEELAQAVALLI 180
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
234-317 1.91e-21

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 86.45  E-value: 1.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   234 DLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTP 313
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 550718760   314 GEYR 317
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
240-319 9.52e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 84.56  E-value: 9.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  240 LAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLL-EQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQ 318
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80


                  .
gi 550718760  319 R 319
Cdd:pfam12833  81 R 81
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
170-324 1.04e-19

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 86.76  E-value: 1.04e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 170 FDLTLALVEDDYGFTLARNVAQDMVMYLRRPGGQLQFSRYNLEQSGATGPVSELQSWILQNLTADLCVERLAERVAMSPR 249
Cdd:COG2207  104 LLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPR 183

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 550718760 250 NFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRFHCRR 324
Cdd:COG2207  184 TLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRARA 258
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 57-194 3.33e-18

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: 80.71  E-value: 3.33e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  57 SGLNLLADYRLPELDPREPLdtIIITGRGMNEQESTAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATTHWRLL 136
Cdd:cd03136   49 NGLRVAPDAALEDAPPLDYL--FVVGGLGARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHL 126

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 550718760 137 ETLKTRYPAVNVEGGpLYVQDGPVWTSGGVSSGFDLTLALVEDDYGFTLARNVAQDMV 194
Cdd:cd03136  127 EAFAEAFPRVQVTRD-LFEIDGDRLTCAGGTAALDLMLELIARDHGAALAARVAEQFL 183
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 226-319 1.19e-12

Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), contains Zn-binding and two AraC-type DNA-binding domains [Replication, recombination and repair];


Pssm-ID: 441772 [Multi-domain]  Cd Length: 358  Bit Score: 67.77  E-value: 1.19e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 226 WILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPyPLEVIAEKSGFGTSINLRRVF 305
Cdd:COG2169   92 LIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGL-SVTDAAYAAGFGSLSRFYEAF 170

                         90
                 ....*....|....
gi 550718760 306 EKQLHLTPGEYRQR 319
Cdd:COG2169  171 KKLLGMTPSAYRRG 184
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
220-325 1.17e-10

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 61.14  E-value: 1.17e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 220 VSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSI 299
Cdd:PRK10572 185 VREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPIATIGRNVGYDDQL 264

                         90       100
                 ....*....|....*....|....*.
gi 550718760 300 NLRRVFEKQLHLTPGEYRQRfhCRRM 325
Cdd:PRK10572 265 YFSRVFKKCTGASPSEFRAR--CEEK 288
PRK11511 PRK11511
MDR efflux pump AcrAB transcriptional activator MarA;
220-317 1.42e-10

MDR efflux pump AcrAB transcriptional activator MarA;


Pssm-ID: 236920 [Multi-domain]  Cd Length: 127  Bit Score: 58.19  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 220 VSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSI 299
Cdd:PRK11511  11 IHSILDWIEDNLESPLSLEKVSERSGYSKWHLQRMFKKETGHSLGQYIRSRKMTEIAQKLKESNEPILYLAERYGFESQQ 90

                         90
                 ....*....|....*...
gi 550718760 300 NLRRVFEKQLHLTPGEYR 317
Cdd:PRK11511  91 TLTRTFKNYFDVPPHKYR 108
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
203-318 1.73e-10

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 60.85  E-value: 1.73e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 203 QLQFSRYNLEQSGATGPVSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQT 282
Cdd:PRK13503 156 LLRKSSLQENGENSDARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHS 235

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 550718760 283 PYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQ 318
Cdd:PRK13503 236 DASVTDIAYRCGFGDSNHFSTLFRREFSWSPRDIRQ 271
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 2-178 2.01e-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: 2.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760    2 KKILIIVPDGGMLFEAAGIADILMQANrlhpdglaqprYRIIIATTQPhLVIHGQSGLNLLADYRLPELDPREPlDTIII 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAG-----------IKVTVVSVDG-GEVKGSRGVKVTVDASLDDVKPDDY-DALVL 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   82 TG-RGMNEQ--ESTAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATTHWRLLETLKtrYPAVNVEGGPlYVQDG 158
Cdd:pfam01965  68 PGgRAGPERlrDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLI--NAGATYVDKP-VVVDG 144

                         170       180
                  ....*....|....*....|
gi 550718760  159 PVWTSGGVSSGFDLTLALVE 178
Cdd:pfam01965 145 NLVTSRGPGDAPEFALEILE 164
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
220-319 7.49e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 49.92  E-value: 7.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 220 VSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSI 299
Cdd:PRK10219   7 IQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQ 86

                         90       100
                 ....*....|....*....|
gi 550718760 300 NLRRVFEKQLHLTPGEYRQR 319
Cdd:PRK10219  87 TFSRVFRRQFDRTPSDYRHR 106
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 190-320 1.59e-07

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 51.96  E-value: 1.59e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 190 AQDMVMYLRRPGgqlqFSRYNLEQSGATGPVSELQSWILQNLTAD-LCVERLAERVAMSPRNFTRVFTRDvGVPPARYVT 268
Cdd:PRK09685 173 LLEALIALLRPA----LHQRESVQPRRERQFQKVVALIDQSIQEEiLRPEWIAGELGISVRSLYRLFAEQ-GLVVAQYIR 247

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550718760 269 EARL---------AAARQLLEQtpyplevIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:PRK09685 248 NRRLdrcaddlrpAADDEKITS-------IAYKWGFSDSSHFSTAFKQRFGVSPGEYRRKF 301
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
204-320 1.98e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 51.44  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 204 LQFSRYNLEQSGATgPVSE----LQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLL 279
Cdd:PRK13501 159 LKRHRYRAEQAHLL-PDGEqldlIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLL 237

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 550718760 280 EQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRF 320
Cdd:PRK13501 238 RGSEHRISDIAARCGFEDSNYFSAVFTREAGMTPRDYRQRF 278
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-178 2.49e-07

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: 49.72  E-value: 2.49e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   1 MKKILIIVPDGGMLFEAAGIADILMQANrlhpdglaqprYRIIIATTQPHLVIHGQSGLNLLADYRLPELDPREpLDTII 80
Cdd:COG0693    2 MKKVLILLTDGFEDEELTVPYDALREAG-----------AEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDD-YDALV 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  81 ITGrGM----NEQESTAVVDWL-HLAAphAGR-VASVCGGALLLAQAGLLDGRRATTHWRLLETLK---TRYPAVNVegg 151
Cdd:COG0693   70 LPG-GHgapdDLREDPDVVALVrEFYE--AGKpVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKnagATYVDEEV--- 143

                        170       180
                 ....*....|....*....|....*..
gi 550718760 152 plyVQDGPVWTSGGVSSGFDLTLALVE 178
Cdd:COG0693  144 ---VVDGNLITSRGPGDAPAFARALLE 167
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
185-318 6.18e-05

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 43.89  E-value: 6.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 185 LARNVAQ----DMVMYLRRpggqLQFSRYNLEQSGATGPVSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVG 260
Cdd:PRK13502 143 LANEMAEllfgQLVMTLKR----HRYATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTG 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 550718760 261 VPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQ 318
Cdd:PRK13502 219 MTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWRH 276
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 227-268 1.77e-04

Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the N-terminal arm of AraC binds to the DNA binding domain (pfam00165) and helps to hold the two DNA binding domains in a relative orientation that favours DNA looping. In the presence of arabinose, the arms bind over the arabinose on the dimerization domain, thus freeing the DNA-binding domains. The freed DNA-binding domains are then able to assume a conformation suitable for binding to the adjacent DNA sites that are utilized when AraC activates transcription, and hence AraC ceases looping the DNA when arabinose is added.


Pssm-ID: 425497 [Multi-domain]  Cd Length: 42  Bit Score: 38.29  E-value: 1.77e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 550718760  227 ILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVT 268
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
PRK10371 PRK10371
transcriptional regulator MelR;
220-318 2.33e-04

transcriptional regulator MelR;


Pssm-ID: 182416 [Multi-domain]  Cd Length: 302  Bit Score: 42.11  E-value: 2.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 220 VSELQSWILQNLTADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSI 299
Cdd:PRK10371 193 VSQMLGFIAENYDQALTINDVAEHVKLNANYAMGIFQRVMQLTMKQYITAMRINHVRALLSDTDKSILDIALTAGFRSSS 272

                         90
                 ....*....|....*....
gi 550718760 300 NLRRVFEKQLHLTPGEYRQ 318
Cdd:PRK10371 273 RFYSTFGKYVGMSPQQYRK 291
PRK10296 PRK10296
DNA-binding transcriptional regulator ChbR; Provisional
 252-322 5.70e-04

DNA-binding transcriptional regulator ChbR; Provisional


Pssm-ID: 182362 [Multi-domain]  Cd Length: 278  Bit Score: 40.90  E-value: 5.70e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 550718760 252 TRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEKSGFGTSINLRRVFEKQLHLTPGEYRQRFHC 322
Cdd:PRK10296 206 TRATRRYYGKTPMQIINEIRINFAKKQLEMTNYSVTDIAFEAGYSSPSLFIKTFKKLTSFTPGSYRKKLTE 276
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 4-178 7.83e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1. DJ-1 is involved in multiple physiological processes including cancer, Parkinson's disease and male fertility. It is unclear how DJ-1 functions in these. DJ-1 has been shown to possess chaperone activity. DJ-1 is preferentially expressed in the testis and moderately in other tissues; it is induced together with genes involved in oxidative stress response. The Drosophila homologue (DJ-1A) plays an essential role in oxidative stress response and neuronal maintenance. Inhibition of DJ-1A function through RNAi, results in the cellular accumulation of reactive oxygen species, organismal hypersensitivity to oxidative stress, and dysfunction and degeneration of dopaminergic and photoreceptor neurons. DJ-1 has lacks enzymatic activity and the catalytic triad of typical GATase1 domains, however it does contain the highly conserved cysteine located at the nucelophile elbow region typical of these domains. This cysteine been proposed to be a site of regulation of DJ-1 activity by oxidation. DJ-1 is a dimeric enzyme.


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 39.46  E-value: 7.83e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760   4 ILIIVPDGGMLFEAAGIADILMQANrlhpdglaqprYRIIIATTQPHLVIHGQSGLNLLADYRLPELDPrEPLDTIIITG 83
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAG-----------IEVTTASLEKKLAVGSSHGIKVKADKTLSDVNL-DDYDAIVIPG 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760  84 rGM----NEQESTAVVDWLHLAAPHAGRVASVCGGALLLAQAGLLDGRRATThwrlletlktrYPAVN-VEGGPLY---- 154
Cdd:cd03135   69 -GLpgaqNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATC-----------YPGFEdKLGGANYvdep 136

                        170       180
                 ....*....|....*....|....*
gi 550718760 155 -VQDGPVWTSGGVSSGFDLTLALVE 178
Cdd:cd03135  137 vVVDGNIITSRGPGTAFEFALKIVE 161
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
233-318 9.38e-03

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 37.47  E-value: 9.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 550718760 233 ADLCVERLAERVAMSPRNFTRVFTRDVGVPPARYVTEARLAAARQLLEQTPYPLEVIAEkSGFGTSINLRRVFEKQLHLT 312
Cdd:PRK15435  98 TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGESVTTSILN-AGFPDSSSYYRKADETLGMT 176


                 ....*.
gi 550718760 313 PGEYRQ 318
Cdd:PRK15435 177 AKQFRH 182
 
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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