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Conserved domains on  [gi|1042053015|gb|ANP74901|]
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Putative AraC family transcriptional regulator (plasmid) [Cryobacterium arcticum]

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 ...
 15-315 1.07e-71

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: 224.65  E-value: 1.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  15 MRIGLIAIDGCFGSAIASIIDIVRVADGARGDvdpriDPIELAILGP-KRRVTTTASMTLSVDHPLSESGEFDVVVVPAl 93
Cdd:COG4977     1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGR-----PLYRWRLVSLdGGPVRSSSGLTVAPDHGLADLAAADTLIVPG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  94 GTLTAAATHDALqsrdarsvIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMV 173
Cdd:COG4977    75 GLDPAAAADPAL--------LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLY 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 174 VVDGNLVTAGAAFAHIDLALSLVRSI-SPDLAQHVAKLLIIDER--PSQAAFVAYEHLR-HEDPIVVEFERFVRARLDEP 249
Cdd:COG4977   147 VDDGDILTSAGGTAGIDLALHLVERDhGAELANAVARRLVVDPRrpGGQAQFSPLLVPLgHRDPRLARAQAWMEANLEEP 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1042053015 250 FNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYANAET 315
Cdd:COG4977   227 LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-315 1.07e-71

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: 224.65  E-value: 1.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  15 MRIGLIAIDGCFGSAIASIIDIVRVADGARGDvdpriDPIELAILGP-KRRVTTTASMTLSVDHPLSESGEFDVVVVPAl 93
Cdd:COG4977     1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGR-----PLYRWRLVSLdGGPVRSSSGLTVAPDHGLADLAAADTLIVPG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  94 GTLTAAATHDALqsrdarsvIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMV 173
Cdd:COG4977    75 GLDPAAAADPAL--------LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLY 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 174 VVDGNLVTAGAAFAHIDLALSLVRSI-SPDLAQHVAKLLIIDER--PSQAAFVAYEHLR-HEDPIVVEFERFVRARLDEP 249
Cdd:COG4977   147 VDDGDILTSAGGTAGIDLALHLVERDhGAELANAVARRLVVDPRrpGGQAQFSPLLVPLgHRDPRLARAQAWMEANLEEP 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1042053015 250 FNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYANAET 315
Cdd:COG4977   227 LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 17-214 4.08e-61

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: 193.63  E-value: 4.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  17 IGLIAIDGCFGSAIASIIDIVRVADGARGDVDPRIDPIELAILGPKRRVTTTASM-TLSVDHPLSESGEFDVVVVPALGt 95
Cdd:cd03138     1 VTLLAYPGALASSLAGLLDLLRAANRLARRQQGGAPPFEVRLVSLDGGPVLLAGGiLILPDATLADVPAPDLVIVPGLG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  96 ltaaATHDALQSRDARSVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMVVV 175
Cdd:cd03138    80 ----GDPDELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1042053015 176 DGNLVTAGAAFAHIDLALSLVRSI-SPDLAQHVAKLLIID 214
Cdd:cd03138   156 DGNLITAGGAMAWADLALHLIERLaGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 72-315 7.81e-29

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 113.14  E-value: 7.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  72 TLSVDHPLSESGEFDVVVVP---ALGTLTAAATHDALQSRDARSviaslgrldeatTRIAAACTGVFAVAETGRMHHRRA 148
Cdd:PRK09393   63 TVVADGGLELLDRADTIVIPgwrGPDAPVPEPLLEALRAAHARG------------ARLCSICSGVFVLAAAGLLDGRRA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 149 TTSWFLGPEFRKRYPTVALDLDTMVVVDGNLVTAGAAFAHIDLALSLVR-SISPDLAQHVAKLLII--DERPSQAAFVAY 225
Cdd:PRK09393  131 TTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRrDFGSEAANRVARRLVVppHRDGGQAQFVPR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 226 EHLRHEDPIVVEFERFVRARLDEPFNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIA 305
Cdd:PRK09393  211 PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIA 290

                         250
                  ....*....|
gi 1042053015 306 LRVGYANAET 315
Cdd:PRK09393  291 ERAGFGSEES 300
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
249-315 3.20e-13

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 64.11  E-value: 3.20e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1042053015  249 PFNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYANAET 315
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSY 67
HTH_18 pfam12833
Helix-turn-helix domain;
255-315 1.37e-12

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 62.22  E-value: 1.37e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1042053015 255 VAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARH-LSATTDFTSAEIALRVGYANAET 315
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRlLLEDTGLSVAEIALALGFSDASH 62
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-315 1.07e-71

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: 224.65  E-value: 1.07e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  15 MRIGLIAIDGCFGSAIASIIDIVRVADGARGDvdpriDPIELAILGP-KRRVTTTASMTLSVDHPLSESGEFDVVVVPAl 93
Cdd:COG4977     1 LRVAFLLLPGFSLLDLAGPLEVFRLANRLAGR-----PLYRWRLVSLdGGPVRSSSGLTVAPDHGLADLAAADTLIVPG- 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  94 GTLTAAATHDALqsrdarsvIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMV 173
Cdd:COG4977    75 GLDPAAAADPAL--------LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLY 146

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 174 VVDGNLVTAGAAFAHIDLALSLVRSI-SPDLAQHVAKLLIIDER--PSQAAFVAYEHLR-HEDPIVVEFERFVRARLDEP 249
Cdd:COG4977   147 VDDGDILTSAGGTAGIDLALHLVERDhGAELANAVARRLVVDPRrpGGQAQFSPLLVPLgHRDPRLARAQAWMEANLEEP 226

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1042053015 250 FNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYANAET 315
Cdd:COG4977   227 LSVDELARRAGMSPRTLERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASH 292
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 17-214 4.08e-61

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: 193.63  E-value: 4.08e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  17 IGLIAIDGCFGSAIASIIDIVRVADGARGDVDPRIDPIELAILGPKRRVTTTASM-TLSVDHPLSESGEFDVVVVPALGt 95
Cdd:cd03138     1 VTLLAYPGALASSLAGLLDLLRAANRLARRQQGGAPPFEVRLVSLDGGPVLLAGGiLILPDATLADVPAPDLVIVPGLG- 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  96 ltaaATHDALQSRDARSVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMVVV 175
Cdd:cd03138    80 ----GDPDELLLADNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVT 155

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1042053015 176 DGNLVTAGAAFAHIDLALSLVRSI-SPDLAQHVAKLLIID 214
Cdd:cd03138   156 DGNLITAGGAMAWADLALHLIERLaGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 72-315 7.81e-29

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 113.14  E-value: 7.81e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  72 TLSVDHPLSESGEFDVVVVP---ALGTLTAAATHDALQSRDARSviaslgrldeatTRIAAACTGVFAVAETGRMHHRRA 148
Cdd:PRK09393   63 TVVADGGLELLDRADTIVIPgwrGPDAPVPEPLLEALRAAHARG------------ARLCSICSGVFVLAAAGLLDGRRA 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 149 TTSWFLGPEFRKRYPTVALDLDTMVVVDGNLVTAGAAFAHIDLALSLVR-SISPDLAQHVAKLLII--DERPSQAAFVAY 225
Cdd:PRK09393  131 TTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRrDFGSEAANRVARRLVVppHRDGGQAQFVPR 210

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 226 EHLRHEDPIVVEFERFVRARLDEPFNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIA 305
Cdd:PRK09393  211 PVASRESDRLGPLIDWMRAHLAEPHTVASLAARAAMSPRTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIA 290

                         250
                  ....*....|
gi 1042053015 306 LRVGYANAET 315
Cdd:PRK09393  291 ERAGFGSEES 300
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 55-213 1.66e-26

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: 103.35  E-value: 1.66e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  55 ELAILGPKR-RVTTTASMTLSVDHPLSESGEFDVVVVPAlgtltaaaTHDALQSRDARSVIASLGRLDEATTRIAAACTG 133
Cdd:cd03137    34 ELRVCSPEGgPVRSSSGLSLVADAGLDALAAADTVIVPG--------GPDVDGRPPPPALLAALRRAAARGARVASVCTG 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 134 VFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMVVVDGNLVT-AGAAfAHIDLALSLVRS-ISPDLAQHVAKLL 211
Cdd:cd03137   106 AFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTsAGVT-AGIDLCLHLVREdLGAAVANRVARRL 184


                  ..
gi 1042053015 212 II 213
Cdd:cd03137   185 VV 186
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 17-214 8.74e-22

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: 90.72  E-value: 8.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  17 IGLIAIDGCFGSAIASIIDIVRVADGARGDVDPRIDpielaILGPK-RRVTTTASMTLSVDHPLSESGEFDVVVVPALGT 95
Cdd:cd03136     1 FGFLLLPGFSLLALASAIEPLRAANRLAGRELYRWR-----VLSLDgAPVTSSNGLRVAPDAALEDAPPLDYLFVVGGLG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  96 LTAAAThdalqsrdaRSVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALdLDTMVVV 175
Cdd:cd03136    76 ARRAVT---------PALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEI 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1042053015 176 DGNLVTAGAAFAHIDLALSLV-RSISPDLAQHVAKLLIID 214
Cdd:cd03136   146 DGDRLTCAGGTAALDLMLELIaRDHGAALAARVAEQFLHD 185
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 65-211 3.07e-19

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: 83.75  E-value: 3.07e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  65 VTTTASMTLSVDHPLSESGEFDVVVVPAlGTLTAAATHDAlqsrdarSVIASLGRLDEATTRIAAACTGVFAVAETGRMH 144
Cdd:cd03139    43 VSSRSGLTVLPDTSFADPPDLDVLLVPG-GGGTRALVNDP-------ALLDFIRRQAARAKYVTSVCTGALLLAAAGLLD 114

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1042053015 145 HRRATTSWFLGPEFRKRYPTValDLDTMVVVDGNLVTAGAAFAHIDLALSLVRSI-SPDLAQHVAKLL 211
Cdd:cd03139   115 GRRATTHWAAIDWLKEFGAIV--VVDARWVVDGNIWTSGGVSAGIDMALALVARLfGEELAQAVALLI 180
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
96-313 4.83e-14

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 70.96  E-value: 4.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  96 LTAAATHDALQSRDARSVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVALDLDTMVVV 175
Cdd:COG2207    15 ALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGL 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 176 DGNLVTAGAAFAHIDLALSLVRSISPDLAQHVAKLLIIDERPSQAAFVAYEHLRHEDPIVVEFERFVRARLDEPFNVAFV 255
Cdd:COG2207    95 LLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEEL 174

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1042053015 256 AQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYANA 313
Cdd:COG2207   175 ARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQ 232
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
249-315 3.20e-13

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 64.11  E-value: 3.20e-13
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1042053015  249 PFNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYANAET 315
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSY 67
HTH_18 pfam12833
Helix-turn-helix domain;
255-315 1.37e-12

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 62.22  E-value: 1.37e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1042053015 255 VAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARH-LSATTDFTSAEIALRVGYANAET 315
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRlLLEDTGLSVAEIALALGFSDASH 62
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 62-197 1.36e-08

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: 53.41  E-value: 1.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  62 KRRVTTTASMTLSVDHPLSE--SGEFDVVVVPAlGTLTAaathDALqsRDARSVIASLGRLDEATTRIAAACTGVFAVAE 139
Cdd:pfam01965  37 GGEVKGSRGVKVTVDASLDDvkPDDYDALVLPG-GRAGP----ERL--RDNEKLVEFVKDFYEKGKPVAAICHGPQVLAA 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1042053015 140 TGRMHHRRATTSWFLGPEFRKrypTVALDLDTMVVVDGNLVTAGAAFAHIDLALSLVR 197
Cdd:pfam01965 110 AGVLKGRKVTSHPAVKDDLIN---AGATYVDKPVVVDGNLVTSRGPGDAPEFALEILE 164
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 232-312 5.05e-06

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: 47.74  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 232 DPIVVEFERFVRARLDEPFNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDfTSAEIALRVGYA 311
Cdd:COG2169    83 ADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTGL-SVTDAAYAAGFG 161


                  .
gi 1042053015 312 N 312
Cdd:COG2169   162 S 162
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 15-197 1.32e-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: 44.71  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  15 MRIGLIAIDGCFGSAIASIIDIVRVAdGARgdvdpridpIELAILGPKRRVTTTASMTLSVDHPLSE--SGEFDVVVVPA 92
Cdd:COG0693     3 KKVLILLTDGFEDEELTVPYDALREA-GAE---------VDVASPEGGPPVTSKHGITVTADKTLDDvdPDDYDALVLPG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  93 lGTLTAaathDALqsRDARSVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTValdLDTM 172
Cdd:COG0693    73 -GHGAP----DDL--REDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATY---VDEE 142

                         170       180
                  ....*....|....*....|....*
gi 1042053015 173 VVVDGNLVTAGAAFAHIDLALSLVR 197
Cdd:COG0693   143 VVVDGNLITSRGPGDAPAFARALLE 167
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 32-197 7.97e-05

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


Pssm-ID: 153229 [Multi-domain]  Cd Length: 163  Bit Score: 42.54  E-value: 7.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  32 SIIDIVRvadgaRGDVDpridpIELAILGPKRRVTTTASMTLSVDHPLSE--SGEFDVVVVPalGTLTAAATHdalqsRD 109
Cdd:cd03135    16 TPVDVLR-----RAGIE-----VTTASLEKKLAVGSSHGIKVKADKTLSDvnLDDYDAIVIP--GGLPGAQNL-----AD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 110 ARSVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTswFLGPEFRKRYPTValdLDTMVVVDGNLVTAGAAFAHI 189
Cdd:cd03135    79 NEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATC--YPGFEDKLGGANY---VDEPVVVDGNIITSRGPGTAF 153


                  ....*...
gi 1042053015 190 DLALSLVR 197
Cdd:cd03135   154 EFALKIVE 161
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
228-315 4.18e-04

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 39.14  E-value: 4.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015 228 LRHEDpIVVEFERFVRARLDEPFNVAFVAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALR 307
Cdd:PRK10219    1 MSHQK-IIQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMD 79


                  ....*...
gi 1042053015 308 VGYANAET 315
Cdd:PRK10219   80 LGYVSQQT 87
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 112-188 5.45e-04

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: 40.32  E-value: 5.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1042053015 112 SVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRATTSWFLGPEFRKRYPTVAldlDTMVVVDGNLVTAGAAFAH 188
Cdd:cd03169    96 KVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVV---DDGVVVDGNLVTAQAWPDH 169
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
255-312 6.40e-04

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 40.82  E-value: 6.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1042053015 255 VAQSLGTSRRTLERRVRAALNLTPLGFVQRLRIERARHLSATTDFTSAEIALRVGYAN 312
Cdd:PRK13503  193 LADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFGD 250
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 62-186 3.36e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 37.59  E-value: 3.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  62 KRRVTTTASMTLSVDHPLSE--SGEFDVVVVPAlGTLTAAATHDALqsrdarsviasLGRLDEATTR---IAAACTGVFA 136
Cdd:cd03140    36 GEPVTSIGGLRVVPDYSLDDlpPEDYDLLILPG-GDSWDNPEAPDL-----------AGLVRQALKQgkpVAAICGATLA 103

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1042053015 137 VAETGRMHHRRATTSwflGPEFRKRYPT----VALDLDTMVVVDGNLVTA-GAAF 186
Cdd:cd03140   104 LARAGLLNNRKHTSN---SLDFLKAHAPyyggAEYYDEPQAVSDGNLITAnGTAP 155
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 72-182 8.28e-03

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: 36.37  E-value: 8.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1042053015  72 TLSVDHPLSE--SGEFDVVVVPAlGTltaAAthDALqSRDARsVIASLGRLDEATTRIAAACTGVFAVAETGRMHHRRAT 149
Cdd:cd03134    48 TVTVDLTIADvdADDYDALVIPG-GT---NP--DKL-RRDPD-AVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLT 119

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1042053015 150 TswflgpefrkrYPTVALDL--------DTMVVVDGNLVTA 182
Cdd:cd03134   120 S-----------YPSIKDDLinaganwvDEEVVVDGNLITS 149
 
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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