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Conserved domains on  [gi|1738831168|emb|VAS52624|]
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AraC family transcriptional regulator [Klebsiella pneumoniae]

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 ...
 6-317 5.92e-128

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: 367.56  E-value: 5.92e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFG--DSVSEIKRFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVDRRP 83
Cdd:COG4977     3 VAFLLLPGFSLLDLAGPLEVFRlaNRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  84 PQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAAAL 163
Cdd:COG4977    83 DPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 164 DCCLYIIRQRFGSLAANQIARRMIVSPHREGGQAQFIAQPVPKNTRDARINCLLDYLQQHIAEPHSLDSLARVVAMSRRT 243
Cdd:COG4977   163 DLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRT 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738831168 244 LTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRRTFRRGA 317
Cdd:COG4977   243 LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
 
Name Accession Description Interval E-value
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 6-317 5.92e-128

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: 367.56  E-value: 5.92e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFG--DSVSEIKRFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVDRRP 83
Cdd:COG4977     3 VAFLLLPGFSLLDLAGPLEVFRlaNRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  84 PQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAAAL 163
Cdd:COG4977    83 DPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 164 DCCLYIIRQRFGSLAANQIARRMIVSPHREGGQAQFIAQPVPKNTRDARINCLLDYLQQHIAEPHSLDSLARVVAMSRRT 243
Cdd:COG4977   163 DLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRT 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738831168 244 LTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRRTFRRGA 317
Cdd:COG4977   243 LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
ftrA PRK09393
transcriptional activator FtrA; Provisional
 6-315 2.87e-111

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 325.38  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFGDSVSEIK----RFNlhICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVDR 81
Cdd:PRK09393   12 VVALAYDGLCTFEFGCAVEIFGLPRPELGvdwyRFA--VAAVEPGPLRAAGGITVVADGGLELLDRADTIVIPGWRGPDA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  82 RPPQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAA 161
Cdd:PRK09393   90 PVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 162 ALDCCLYIIRQRFGSLAANQIARRMIVSPHREGGQAQFIAQPVPKNTRDaRINCLLDYLQQHIAEPHSLDSLARVVAMSR 241
Cdd:PRK09393  170 GIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESD-RLGPLIDWMRAHLAEPHTVASLAARAAMSP 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738831168 242 RTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRRTFRR 315
Cdd:PRK09393  249 RTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR 322
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-188 3.38e-78

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: 236.24  E-value: 3.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFGDSVSEI--KRFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVD-RR 82
Cdd:cd03137     1 VAVLVFPGVSLLDLSGPAEVFGEANRALgpPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVPGGPDVDgRP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  83 PPQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAAA 162
Cdd:cd03137    81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160

                         170       180
                  ....*....|....*....|....*.
gi 1738831168 163 LDCCLYIIRQRFGSLAANQIARRMIV 188
Cdd:cd03137   161 IDLCLHLVREDLGAAVANRVARRLVV 186
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
227-310 9.25e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 87.22  E-value: 9.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  227 PHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1738831168  307 TEWR 310
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
233-311 8.66e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 84.56  E-value: 8.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 233 LARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLL-EAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRR 311
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 ...
 6-317 5.92e-128

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: 367.56  E-value: 5.92e-128
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFG--DSVSEIKRFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVDRRP 83
Cdd:COG4977     3 VAFLLLPGFSLLDLAGPLEVFRlaNRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  84 PQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAAAL 163
Cdd:COG4977    83 DPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGI 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 164 DCCLYIIRQRFGSLAANQIARRMIVSPHREGGQAQFIAQPVPKNTRDARINCLLDYLQQHIAEPHSLDSLARVVAMSRRT 243
Cdd:COG4977   163 DLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRT 242

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738831168 244 LTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRRTFRRGA 317
Cdd:COG4977   243 LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
ftrA PRK09393
transcriptional activator FtrA; Provisional
 6-315 2.87e-111

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 325.38  E-value: 2.87e-111
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFGDSVSEIK----RFNlhICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVDR 81
Cdd:PRK09393   12 VVALAYDGLCTFEFGCAVEIFGLPRPELGvdwyRFA--VAAVEPGPLRAAGGITVVADGGLELLDRADTIVIPGWRGPDA 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  82 RPPQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAA 161
Cdd:PRK09393   90 PVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAA 169

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 162 ALDCCLYIIRQRFGSLAANQIARRMIVSPHREGGQAQFIAQPVPKNTRDaRINCLLDYLQQHIAEPHSLDSLARVVAMSR 241
Cdd:PRK09393  170 GIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESD-RLGPLIDWMRAHLAEPHTVASLAARAAMSP 248

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1738831168 242 RTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRRTFRR 315
Cdd:PRK09393  249 RTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR 322
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-188 3.38e-78

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: 236.24  E-value: 3.38e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFGDSVSEI--KRFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVD-RR 82
Cdd:cd03137     1 VAVLVFPGVSLLDLSGPAEVFGEANRALgpPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVPGGPDVDgRP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  83 PPQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAAA 162
Cdd:cd03137    81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160

                         170       180
                  ....*....|....*....|....*.
gi 1738831168 163 LDCCLYIIRQRFGSLAANQIARRMIV 188
Cdd:cd03137   161 IDLCLHLVREDLGAAVANRVARRLVV 186
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 35-188 2.32e-35

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: 126.61  E-value: 2.32e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  35 RFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVP-YWGEVDRRPPQ---ALLDSLVRARDNGAEIVGLCLGAFV 110
Cdd:cd03138    37 PFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVPgLGGDPDELLLAdnpALIAWLRRQHANGATVAAACTGVFL 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738831168 111 LGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSAGTAAALDCCLYIIRQRFGSLAANQIARRMIV 188
Cdd:cd03138   117 LAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 6-188 3.64e-34

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: 123.08  E-value: 3.64e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSP--FHYAVPCMLFGDSVSEIKRFNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPYWGEVDRRP 83
Cdd:cd03136     1 FGFLLLPGFSLlaLASAIEPLRAANRLAGRELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGARRAV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  84 PQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLdINALYVDDQRIITSAGTAAAL 163
Cdd:cd03136    81 TPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEIDGDRLTCAGGTAAL 159

                         170       180
                  ....*....|....*....|....*
gi 1738831168 164 DCCLYIIRQRFGSLAANQIARRMIV 188
Cdd:cd03136   160 DLMLELIARDHGAALAARVAEQFLH 184
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-186 1.49e-30

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: 113.79  E-value: 1.49e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFGdSVSEIKR-FNLHICAERPGLLRARDGFALYATGDYAALEQADIVVVPyWGEVDRRPP 84
Cdd:cd03139     1 VGILLFPGVEVLDVIGPYEVFG-RAPRLAApFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVP-GGGGTRALV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  85 Q--ALLDsLVRARDNGAEIV-GLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQldINALYVDDQRIITSAGTAA 161
Cdd:cd03139    79 NdpALLD-FIRRQAARAKYVtSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVV--VDARWVVDGNIWTSGGVSA 155

                         170       180
                  ....*....|....*....|....*
gi 1738831168 162 ALDCCLYIIRQRFGSLAANQIARRM 186
Cdd:cd03139   156 GIDMALALVARLFGEELAQAVALLI 180
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
227-310 9.25e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 87.22  E-value: 9.25e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  227 PHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 1738831168  307 TEWR 310
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
78-315 3.27e-21

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 90.99  E-value: 3.27e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  78 EVDRRPPQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRFPQVQLDINALYVDDQRIITSA 157
Cdd:COG2207    11 LLLLALLLLLLLLLLLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 158 GTAAALDCCLYIIRQRFGSLAANQIARRMIVSPHREGGQAQFIAQPVPKNTRDARINCLLDY--------LQQHIAEPHS 229
Cdd:COG2207    91 LVGLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLllllllllLLLLLLLLLT 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 230 LDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEW 309
Cdd:COG2207   171 LEELARELGLSPRTLSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEY 250


                  ....*.
gi 1738831168 310 RRTFRR 315
Cdd:COG2207   251 RKRLRA 256
HTH_18 pfam12833
Helix-turn-helix domain;
233-311 8.66e-21

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 84.56  E-value: 8.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 233 LARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLL-EAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWRR 311
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERARRLLlEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 209-311 2.58e-15

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: 75.48  E-value: 2.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 209 RDARINCLLDYLQQHIAEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGdLPVEQVAEAVGY 288
Cdd:COG2169    82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTG-LSVTDAAYAAGF 160

                          90       100
                  ....*....|....*....|...
gi 1738831168 289 LSAVTWRQQFKARFGVSPTEWRR 311
Cdd:COG2169   161 GSLSRFYEAFKKLLGMTPSAYRR 183
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
201-311 3.24e-15

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 74.62  E-value: 3.24e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 201 AQPV-PKNTRDARINCLLDYLQQHIAEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPV 279
Cdd:PRK10572  172 AIPEsLHPPMDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPI 251

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1738831168 280 EQVAEAVGYLSAVTWRQQFKARFGVSPTEWRR 311
Cdd:PRK10572  252 ATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
210-310 6.31e-09

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 55.84  E-value: 6.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 210 DARINCLLDYLQQHIAEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYL 289
Cdd:PRK13503  170 DARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFG 249

                          90       100
                  ....*....|....*....|.
gi 1738831168 290 SAVTWRQQFKARFGVSPTEWR 310
Cdd:PRK13503  250 DSNHFSTLFRREFSWSPRDIR 270
PRK10219 PRK10219
superoxide response transcriptional regulator SoxS;
213-312 1.10e-08

superoxide response transcriptional regulator SoxS;


Pssm-ID: 182314 [Multi-domain]  Cd Length: 107  Bit Score: 52.23  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 213 INCLLDYLQQHIAEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAV 292
Cdd:PRK10219    7 IQTLIAWIDEHIDQPLNIDVVAKKSGYSKWYLQRMFRTVTHQTLGDYIRQRRLLLAAVELRTTERPIFDIAMDLGYVSQQ 86

                          90       100
                  ....*....|....*....|
gi 1738831168 293 TWRQQFKARFGVSPTEWRRT 312
Cdd:PRK10219   87 TFSRVFRRQFDRTPSDYRHR 106
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
173-310 3.36e-08

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 53.90  E-value: 3.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 173 RFGSLAANQiARRMIV-----SPHREG----------GQA-------QFIAQPVPKNTRDARINCLLDYLQQHIAEPHSL 230
Cdd:PRK13502  117 RLGSMGMNQ-ARQVINqleheSNGRDPlanemaellfGQLvmtlkrhRYATDDLPATSRETLLDKLITALANSLECPFAL 195

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 231 DSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPTEWR 310
Cdd:PRK13502  196 DAFCQQEQCSERVLRQQFRAQTGMTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
205-317 9.99e-07

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 49.79  E-value: 9.99e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 205 PKNTRDARINCLLDYLQQHiaEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDlPVEQVAE 284
Cdd:PRK15435   79 PQQHRLDKITHACRLLEQE--TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSIL 155

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1738831168 285 AVGYLSAVTWRQQFKARFGVSPtewrRTFRRGA 317
Cdd:PRK15435  156 NAGFPDSSSYYRKADETLGMTA----KQFRHGG 184
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 61-172 1.13e-06

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: 47.64  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  61 DYAALEQADIVVVP--YWGEVDRRPPQALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRfpq 138
Cdd:pfam01965  55 DDVKPDDYDALVLPggRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINA--- 131

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1738831168 139 vqldiNALYVD-----DQRIITSAGTAAALDCCLYIIRQ 172
Cdd:pfam01965 132 -----GATYVDkpvvvDGNLVTSRGPGDAPEFALEILEQ 165
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
212-317 1.93e-06

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 48.36  E-value: 1.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 212 RINCLLDYLQQHIAEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVG---- 287
Cdd:PRK13501  177 QLDLIMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGfeds 256

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1738831168 288 -YLSAVTWRQQfkarfGVSPTEWRRTFRRGA 317
Cdd:PRK13501  257 nYFSAVFTREA-----GMTPRDYRQRFIRSP 282
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 222-314 1.98e-06

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 48.49  E-value: 1.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 222 QHIAEPH-SLDSLARVVAMSRRTLTRHFARaTGMSITDWLTAERLRRSQTLLE--AGDLPVEQVAEAVGYLSAVTWRQQF 298
Cdd:PRK09685  208 QSIQEEIlRPEWIAGELGISVRSLYRLFAE-QGLVVAQYIRNRRLDRCADDLRpaADDEKITSIAYKWGFSDSSHFSTAF 286

                          90
                  ....*....|....*.
gi 1738831168 299 KARFGVSPTEWRRTFR 314
Cdd:PRK09685  287 KQRFGVSPGEYRRKFR 302
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 85-172 1.73e-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: 44.47  E-value: 1.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  85 QALLDSLVRARDNGAEIVGLCLGAFVLGYAGLLDGRRAATHWEFEQDFQrrfpqvqldiNALYVD-----DQRIITSAGT 159
Cdd:cd03135    80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG----------GANYVDepvvvDGNIITSRGP 149

                          90
                  ....*....|...
gi 1738831168 160 AAALDCCLYIIRQ 172
Cdd:cd03135   150 GTAFEFALKIVEA 162
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 220-261 5.23e-05

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: 39.83  E-value: 5.23e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1738831168 220 LQQHIAEPHSLDSLARVVAMSRRTLTRHFARATGMSITDWLT 261
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYRH 42
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 6-172 7.34e-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: 42.40  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFGDsvseiKRFNLHICAERPGL-LRARDGFALYATGDYAAL--EQADIVVVP--YWGEVD 80
Cdd:COG0693     5 VLILLTDGFEDEELTVPYDALRE-----AGAEVDVASPEGGPpVTSKHGITVTADKTLDDVdpDDYDALVLPggHGAPDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  81 -RRPPQALldSLVRARDNGAEIVG-LCLGAFVLGYAGLLDGRRAATHWEFEQDFQRRfpqvqldiNALYVD-----DQRI 153
Cdd:COG0693    80 lREDPDVV--ALVREFYEAGKPVAaICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNA--------GATYVDeevvvDGNL 149

                         170
                  ....*....|....*....
gi 1738831168 154 ITSAGTAAALDCCLYIIRQ 172
Cdd:COG0693   150 ITSRGPGDAPAFARALLEL 168
PRK09978 PRK09978
DNA-binding transcriptional regulator GadX; Provisional
 220-310 3.15e-04

DNA-binding transcriptional regulator GadX; Provisional


Pssm-ID: 137624 [Multi-domain]  Cd Length: 274  Bit Score: 41.83  E-value: 3.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168 220 LQQHIAEPHSLDSLARVVAMSRRTLTRHFaRATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFK 299
Cdd:PRK09978  151 INNNIAHEWTLARIASELLMSPSLLKKKL-REEETSYSQLLTECRMQRALQLIVIHGFSIKRVAVSCGYHSVSYFIYVFR 229

                          90
                  ....*....|.
gi 1738831168 300 ARFGVSPTEWR 310
Cdd:PRK09978  230 NYYGMTPTEYQ 240
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 276-311 3.26e-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: 37.52  E-value: 3.26e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1738831168 276 DLPVEQVAEAVGYlSAVTWRQQFKARFGVSPTEWRR 311
Cdd:pfam00165   8 NLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 230-307 6.73e-04

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 40.75  E-value: 6.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1738831168 230 LDSLARVVAMSRRTLTRHFArATGMSITDWLTAERLRRSQTLLEAGDLPVEQVAEAVGYLSAVTWRQQFKARFGVSPT 307
Cdd:PRK15185  225 LTDVADHIFMSTSTLKRKLA-EEGTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPS 301
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-111 1.16e-03

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 37.96  E-value: 1.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFgdsvsEIKRFNLHICAERPGLLRARdgfalyatgdyAALEQADIVVVP--YWGEVDRRP 83
Cdd:cd01653     1 VAVLLFPGFEELELASPLDAL-----REAGAEVDVVSPDGGPVESD-----------VDLDDYDGLILPggPGTPDDLAR 64

                          90       100
                  ....*....|....*....|....*...
gi 1738831168  84 PQALLDSLVRARDNGAEIVGLCLGAFVL 111
Cdd:cd01653    65 DEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-111 2.93e-03

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 36.41  E-value: 2.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168   6 VAIVAVEGFSPFHYAVPCMLFgdsvsEIKRFNLHICAERPGLLRARdgfalyatgdyAALEQADIVVVPYWGEV--DRRP 83
Cdd:cd03128     1 VAVLLFGGSEELELASPLDAL-----REAGAEVDVVSPDGGPVESD-----------VDLDDYDGLILPGGPGTpdDLAW 64

                          90       100
                  ....*....|....*....|....*...
gi 1738831168  84 PQALLDSLVRARDNGAEIVGLCLGAFVL 111
Cdd:cd03128    65 DEALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 57-172 9.04e-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: 36.43  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1738831168  57 YATGDYAaLEQADIVVVP---YWGEVDrrPPQALldSLVR-ARDNGAEIVGLCLGAFVLGYAGLLDGRR----------- 121
Cdd:cd03140    51 YSLDDLP-PEDYDLLILPggdSWDNPE--APDLA--GLVRqALKQGKPVAAICGATLALARAGLLNNRKhtsnsldflka 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1738831168 122 ---AATHWEFEQDfqrrfPQVqldinalyVDDQRIITSAGTaAALDCCLYIIRQ 172
Cdd:cd03140   126 hapYYGGAEYYDE-----PQA--------VSDGNLITANGT-APVEFAAEILRA 165
 
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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