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Conserved domains on  [gi|503993288|ref|WP_014227282|]
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MULTISPECIES: GlxA family transcriptional regulator [Klebsiella]

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 3.34e-125

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: 360.63  E-value: 3.34e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFG--DTVSETKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYWGAVNQRP 83
Cdd:COG4977    3 VAFLLLPGFSLLDLAGPLEVFRlaNRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAAAL 163
Cdd:COG4977   83 DPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 164 DCCLYLIRQRFGSLVANQIARRMIVPPHREGGQAQFIAQPVPKNTRDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRT 243
Cdd:COG4977  163 DLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRT 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993288 244 LTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRRTFRRGA 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 3.34e-125

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: 360.63  E-value: 3.34e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFG--DTVSETKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYWGAVNQRP 83
Cdd:COG4977    3 VAFLLLPGFSLLDLAGPLEVFRlaNRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAAAL 163
Cdd:COG4977   83 DPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 164 DCCLYLIRQRFGSLVANQIARRMIVPPHREGGQAQFIAQPVPKNTRDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRT 243
Cdd:COG4977  163 DLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRT 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993288 244 LTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRRTFRRGA 317
Cdd:COG4977  243 LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
ftrA PRK09393
transcriptional activator FtrA; Provisional
 6-315 6.19e-109

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 319.60  E-value: 6.19e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFGDTVSETK----RFNlhICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYWGAVNQ 81
Cdd:PRK09393  12 VVALAYDGLCTFEFGCAVEIFGLPRPELGvdwyRFA--VAAVEPGPLRAAGGITVVADGGLELLDRADTIVIPGWRGPDA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  82 RPSQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAA 161
Cdd:PRK09393  90 PVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 162 ALDCCLYLIRQRFGSLVANQIARRMIVPPHREGGQAQFIAQPVPKNTRDaRINGLLEYLQQHIREPHNLDSLAQVAAMSR 241
Cdd:PRK09393 170 GIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESD-RLGPLIDWMRAHLAEPHTVASLAARAAMSP 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993288 242 RTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRRTFRR 315
Cdd:PRK09393 249 RTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR 322
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-189 2.66e-76

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: 231.62  E-value: 2.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFGDTVSE--TKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYW-GAVNQR 82
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRAlgPPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVPGGpDVDGRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  83 PSQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAAA 162
Cdd:cd03137   81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160

                        170       180
                 ....*....|....*....|....*..
gi 503993288 163 LDCCLYLIRQRFGSLVANQIARRMIVP 189
Cdd:cd03137  161 IDLCLHLVREDLGAAVANRVARRLVVP 187
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
227-310 6.77e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 87.61  E-value: 6.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   227 PHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 503993288   307 AEWR 310
Cdd:smart00342  81 SEYR 84
HTH_18 pfam12833
Helix-turn-helix domain;
233-311 5.19e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 82.64  E-value: 5.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  233 LAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRS-QILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRR 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 3.34e-125

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: 360.63  E-value: 3.34e-125
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFG--DTVSETKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYWGAVNQRP 83
Cdd:COG4977    3 VAFLLLPGFSLLDLAGPLEVFRlaNRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAAA 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAAAL 163
Cdd:COG4977   83 DPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTAGI 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 164 DCCLYLIRQRFGSLVANQIARRMIVPPHREGGQAQFIAQPVPKNTRDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRT 243
Cdd:COG4977  163 DLALHLVERDHGAELANAVARRLVVDPRRPGGQAQFSPLLVPLGHRDPRLARAQAWMEANLEEPLSVDELARRAGMSPRT 242

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993288 244 LTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRRTFRRGA 317
Cdd:COG4977  243 LERRFRAATGTTPARYLQRLRLERARRLLETTDLSIEEIAAACGFGSASHFRRAFRRRFGVSPSAYRRRFRARA 316
ftrA PRK09393
transcriptional activator FtrA; Provisional
 6-315 6.19e-109

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 319.60  E-value: 6.19e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFGDTVSETK----RFNlhICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYWGAVNQ 81
Cdd:PRK09393  12 VVALAYDGLCTFEFGCAVEIFGLPRPELGvdwyRFA--VAAVEPGPLRAAGGITVVADGGLELLDRADTIVIPGWRGPDA 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  82 RPSQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAA 161
Cdd:PRK09393  90 PVPEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAA 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 162 ALDCCLYLIRQRFGSLVANQIARRMIVPPHREGGQAQFIAQPVPKNTRDaRINGLLEYLQQHIREPHNLDSLAQVAAMSR 241
Cdd:PRK09393 170 GIDLCLHLVRRDFGSEAANRVARRLVVPPHRDGGQAQFVPRPVASRESD-RLGPLIDWMRAHLAEPHTVASLAARAAMSP 248

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 503993288 242 RTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRRTFRR 315
Cdd:PRK09393 249 RTFLRRFEAATGMTPAEWLLRERLARARDLLESSALSIDQIAERAGFGSEESLRHHFRRRAATSPAAYRKRFGR 322
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-189 2.66e-76

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: 231.62  E-value: 2.66e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFGDTVSE--TKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYW-GAVNQR 82
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRAlgPPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVPGGpDVDGRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  83 PSQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAAA 162
Cdd:cd03137   81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160

                        170       180
                 ....*....|....*....|....*..
gi 503993288 163 LDCCLYLIRQRFGSLVANQIARRMIVP 189
Cdd:cd03137  161 IDLCLHLVREDLGAAVANRVARRLVVP 187
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-188 9.00e-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: 125.07  E-value: 9.00e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGfsPFHYSVpcMLFGDTVS-----------ETKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVP 74
Cdd:cd03138    1 VTLLAYPG--ALASSL--AGLLDLLRaanrlarrqqgGAPPFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  75 -YWGAVNQRPSQ---PLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDD 150
Cdd:cd03138   77 gLGGDPDELLLAdnpALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTD 156

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 503993288 151 EGIITSAGTAAALDCCLYLIRQRFGSLVANQIARRMIV 188
Cdd:cd03138  157 GNLITAGGAMAWADLALHLIERLAGPELAQLVARFLLI 194
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 6-189 6.64e-33

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: 120.00  E-value: 6.64e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYS--VPCMLFGDTVSETKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPYWGAVNQRP 83
Cdd:cd03136    1 FGFLLLPGFSLLALAsaIEPLRAANRLAGRELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGARRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLdINALYVDDEGIITSAGTAAAL 163
Cdd:cd03136   81 TPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQV-TRDLFEIDGDRLTCAGGTAAL 159

                        170       180
                 ....*....|....*....|....*.
gi 503993288 164 DCCLYLIRQRFGSLVANQIARRMIVP 189
Cdd:cd03136  160 DLMLELIARDHGAALAARVAEQFLHD 185
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-186 1.54e-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: 1.54e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFGDTVSETKRFNLHICAERPGLLSARDGFALNASGDFSLLAQADIVVVPywGAVNQR--- 82
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVP--GGGGTRalv 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  83 PSQPLLDgLVRARNNGAQIV-GLCLGAFVLGYAGLLDDRRAATHWEFEqDFQRQFPqVRLDINALYVDDEGIITSAGTAA 161
Cdd:cd03139   79 NDPALLD-FIRRQAARAKYVtSVCTGALLLAAAGLLDGRRATTHWAAI-DWLKEFG-AIVVVDARWVVDGNIWTSGGVSA 155

                        170       180
                 ....*....|....*....|....*
gi 503993288 162 ALDCCLYLIRQRFGSLVANQIARRM 186
Cdd:cd03139  156 GIDMALALVARLFGEELAQAVALLI 180
HTH_ARAC smart00342
helix_turn_helix, arabinose operon control protein;
227-310 6.77e-22

helix_turn_helix, arabinose operon control protein;


Pssm-ID: 197666 [Multi-domain]  Cd Length: 84  Bit Score: 87.61  E-value: 6.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   227 PHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSP 306
Cdd:smart00342   1 PLTLEDLAEALGVSPRHLQRLFKKETGTTPKQYLRDRRLERARRLLRDTDLSVTEIALRVGFSSQSYFSRAFKKLFGVTP 80


                   ....
gi 503993288   307 AEWR 310
Cdd:smart00342  81 SEYR 84
AraC COG2207
AraC-type DNA-binding domain and AraC-containing proteins [Transcription];
84-315 8.26e-21

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


Pssm-ID: 441809 [Multi-domain]  Cd Length: 258  Bit Score: 89.84  E-value: 8.26e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQFPQVRLDINALYVDDEGIITSAGTAAAL 163
Cdd:COG2207   25 LLLILLLLALVLLLLLLALLLLLLLLLGLLGGLLLLLLLLLLLGLLLLLLLLLLGLLLLALLALLLLVGLLLLLLLLLLL 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 164 DCCLYLIRQRFGSLVANQIARRMIVPPHREGGQAQFIAQPVPKNTRDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRT 243
Cdd:COG2207  105 LLLLLLLLLLLLLLLLLLLLLLLLALLRALELLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLLTLEELARELGLSPRT 184

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 503993288 244 LTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRRTFRR 315
Cdd:COG2207  185 LSRLFKEETGTSPKQYLRELRLERAKRLLAETDLSISEIAYELGFSSQSHFSRAFKKRFGVTPSEYRKRLRA 256
HTH_18 pfam12833
Helix-turn-helix domain;
233-311 5.19e-20

Helix-turn-helix domain;


Pssm-ID: 432818 [Multi-domain]  Cd Length: 81  Bit Score: 82.64  E-value: 5.19e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  233 LAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRS-QILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWRR 311
Cdd:pfam12833   1 LAAALGMSPRTLSRLFKRELGLSPKEYLRRLRLERArRLLLEDTGLSVAEIALALGFSDASHFSRAFRRLFGLTPSEYRR 80
AdaA COG2169
Methylphosphotriester-DNA--protein-cysteine methyltransferase (N-terminal fragment of Ada), ...
 209-311 1.50e-14

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: 73.16  E-value: 1.50e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 209 RDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGdLPVGQVAEEVGY 288
Cdd:COG2169   82 RADLVARACRLIEAGAEDRPSLEDLAARLGLSPRHLRRLFKAHTGVTPKAYARARRLLRARQLLQTG-LSVTDAAYAAGF 160

                         90       100
                 ....*....|....*....|...
gi 503993288 289 RSAVTWRQQFKARFGVSPAEWRR 311
Cdd:COG2169  161 GSLSRFYEAFKKLLGMTPSAYRR 183
PRK10572 PRK10572
arabinose operon transcriptional regulator AraC;
201-311 1.12e-12

arabinose operon transcriptional regulator AraC;


Pssm-ID: 236717 [Multi-domain]  Cd Length: 290  Bit Score: 67.31  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 201 AQPV-PKNTRDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPV 279
Cdd:PRK10572 172 AIPEsLHPPMDPRVREACQYISDHLASEFDIESVAQHVCLSPSRLAHLFRQQLGISVLRWREDQRISRAKLLLQTTRMPI 251

                         90       100       110
                 ....*....|....*....|....*....|..
gi 503993288 280 GQVAEEVGYRSAVTWRQQFKARFGVSPAEWRR 311
Cdd:PRK10572 252 ATIGRNVGYDDQLYFSRVFKKCTGASPSEFRA 283
PRK13502 PRK13502
HTH-type transcriptional activator RhaR;
174-310 1.00e-09

HTH-type transcriptional activator RhaR;


Pssm-ID: 184093 [Multi-domain]  Cd Length: 282  Bit Score: 58.53  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 174 FGSLVanqiarrMIVPPHReggqaqFIAQPVPKNTRDARINGLLEYLQQHIREPHNLDSLAQVAAMSRRTLTRHFAKATG 253
Cdd:PRK13502 152 FGQLV-------MTLKRHR------YATDDLPATSRETLLDKLITALANSLECPFALDAFCQQEQCSERVLRQQFRAQTG 218

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 503993288 254 MGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPAEWR 310
Cdd:PRK13502 219 MTINQYLRQVRICHAQYLLQHSPLMISEISMQCGFEDSNYFSVVFTRETGMTPSQWR 275
PRK13503 PRK13503
HTH-type transcriptional activator RhaS;
210-310 2.31e-07

HTH-type transcriptional activator RhaS;


Pssm-ID: 184094 [Multi-domain]  Cd Length: 278  Bit Score: 51.22  E-value: 2.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 210 DARINGLLEYLQQHIREPHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYR 289
Cdd:PRK13503 170 DARLNQLLAWLEDHFAEEVNWEALADQFSLSLRTLHRQLKQQTGLTPQRYLNRLRLLKARHLLRHSDASVTDIAYRCGFG 249

                         90       100
                 ....*....|....*....|.
gi 503993288 290 SAVTWRQQFKARFGVSPAEWR 310
Cdd:PRK13503 250 DSNHFSTLFRREFSWSPRDIR 270
PRK13501 PRK13501
HTH-type transcriptional activator RhaR;
216-317 2.37e-07

HTH-type transcriptional activator RhaR;


Pssm-ID: 184092 [Multi-domain]  Cd Length: 290  Bit Score: 51.44  E-value: 2.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 216 LLEYLQQHIREPHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWR 295
Cdd:PRK13501 181 IMSALQQSLGAYFDMADFCHKNQLVERSLKQLFRQQTGMSISHYLRQIRLCHAKCLLRGSEHRISDIAARCGFEDSNYFS 260

                         90       100
                 ....*....|....*....|..
gi 503993288 296 QQFKARFGVSPAEWRRTFRRGA 317
Cdd:PRK13501 261 AVFTREAGMTPRDYRQRFIRSP 282
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 6-172 3.31e-07

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: 49.09  E-value: 3.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFG------DTVSETKrfNLHICAERPGLLSARDGFALNASGDFsllaqaDIVVVP--YWG 77
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRragievTTASLEK--KLAVGSSHGIKVKADKTLSDVNLDDY------DAIVIPggLPG 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  78 AVNQRPSQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWEFEQDFQrqfpqvrldiNALYVD-----DEG 152
Cdd:cd03135   73 AQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG----------GANYVDepvvvDGN 142

                        170       180
                 ....*....|....*....|
gi 503993288 153 IITSAGTAAALDCCLYLIRQ 172
Cdd:cd03135  143 IITSRGPGTAFEFALKIVEA 162
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 6-172 6.13e-06

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: 45.86  E-value: 6.13e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFGDtvsetKRFNLHICAERPGL-LSARDGFALNASGDFS--LLAQADIVVVP--YWGAVN 80
Cdd:COG0693    5 VLILLTDGFEDEELTVPYDALRE-----AGAEVDVASPEGGPpVTSKHGITVTADKTLDdvDPDDYDALVLPggHGAPDD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  81 QRPSQPLLDgLVRARNNGAQIVG-LCLGAFVLGYAGLLDDRRAATHWEFEQDFQRQfpqvrldiNALYVD-----DEGII 154
Cdd:COG0693   80 LREDPDVVA-LVREFYEAGKPVAaICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNA--------GATYVDeevvvDGNLI 150

                        170
                 ....*....|....*...
gi 503993288 155 TSAGTAAALDCCLYLIRQ 172
Cdd:COG0693  151 TSRGPGDAPAFARALLEL 168
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 69-172 9.48e-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: 44.94  E-value: 9.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   69 DIVVVP--YWGAVNQRPSQPLLDGLVRARNNGAQIVGLCLGAFVLGYAGLLDDRRAATHWefeqdfqrqfpQVRLDINA- 145
Cdd:pfam01965  63 DALVLPggRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHP-----------AVKDDLINa 131

                          90       100       110
                  ....*....|....*....|....*....|....
gi 503993288  146 -------LYVDDEGIITSAGTAAALDCCLYLIRQ 172
Cdd:pfam01965 132 gatyvdkPVVVDGNLVTSRGPGDAPEFALEILEQ 165
PRK15435 PRK15435
bifunctional DNA-binding transcriptional regulator/O6-methylguanine-DNA methyltransferase Ada;
205-317 1.35e-05

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


Pssm-ID: 185333 [Multi-domain]  Cd Length: 353  Bit Score: 46.32  E-value: 1.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 205 PKNTRDARINGLLEYLQQHirEPHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWLAAERLRRSQILLEAGDlPVGQVAE 284
Cdd:PRK15435  79 PQQHRLDKITHACRLLEQE--TPVTLEALADQVAMSPFHLHRLFKATTGMTPKAWQQAWRARRLREALAKGE-SVTTSIL 155

                         90       100       110
                 ....*....|....*....|....*....|...
gi 503993288 285 EVGYRSAVTWRQQFKARFGVSPaewrRTFRRGA 317
Cdd:PRK15435 156 NAGFPDSSSYYRKADETLGMTA----KQFRHGG 184
PRK09685 PRK09685
DNA-binding transcriptional activator FeaR; Provisional
 222-314 2.57e-05

DNA-binding transcriptional activator FeaR; Provisional


Pssm-ID: 236612 [Multi-domain]  Cd Length: 302  Bit Score: 45.02  E-value: 2.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288 222 QHIREPH-NLDSLAQVAAMSRRTLTRHFAKaTGMGIADWLAAERLRRSqilleAGDL---PVGQVAEEVGYRSAVT---- 293
Cdd:PRK09685 208 QSIQEEIlRPEWIAGELGISVRSLYRLFAE-QGLVVAQYIRNRRLDRC-----ADDLrpaADDEKITSIAYKWGFSdssh 281

                         90       100
                 ....*....|....*....|.
gi 503993288 294 WRQQFKARFGVSPAEWRRTFR 314
Cdd:PRK09685 282 FSTAFKQRFGVSPGEYRRKFR 302
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 276-311 4.69e-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: 37.13  E-value: 4.69e-04
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 503993288  276 DLPVGQVAEEVGYrSAVTWRQQFKARFGVSPAEWRR 311
Cdd:pfam00165   8 NLTIADIADELGF-SRSYFSRLFKKYTGVTPSQYRH 42
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-111 1.45e-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: 1.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFgdtvsETKRFNLHICAERPGLLSARDgfalnasgdfsLLAQADIVVVP--YWGAVNQRP 83
Cdd:cd01653    1 VAVLLFPGFEELELASPLDAL-----REAGAEVDVVSPDGGPVESDV-----------DLDDYDGLILPggPGTPDDLAR 64

                         90       100
                 ....*....|....*....|....*...
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVL 111
Cdd:cd01653   65 DEALLALLREAAAAGKPILGICLGAQLL 92
HTH_AraC pfam00165
Bacterial regulatory helix-turn-helix proteins, AraC family; In the absence of arabinose, the ...
 220-260 2.43e-03

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: 35.21  E-value: 2.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 503993288  220 LQQHIREPHNLDSLAQVAAMSRRTLTRHFAKATGMGIADWL 260
Cdd:pfam00165   1 LRENLSTNLTIADIADELGFSRSYFSRLFKKYTGVTPSQYR 41
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 61-161 3.05e-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: 37.97  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288  61 DFSL----LAQADIVVVP---YWgavnQRPSQPLLDGLVR-ARNNGAQIVGLCLGAFVLGYAGLLDDRRaatH----WEF 128
Cdd:cd03140   50 DYSLddlpPEDYDLLILPggdSW----DNPEAPDLAGLVRqALKQGKPVAAICGATLALARAGLLNNRK---HtsnsLDF 122

                         90       100       110
                 ....*....|....*....|....*....|...
gi 503993288 129 EQDFQRQFPQVRLDINALYVDDEGIITSAGTAA 161
Cdd:cd03140  123 LKAHAPYYGGAEYYDEPQAVSDGNLITANGTAP 155
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-111 4.42e-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: 36.02  E-value: 4.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993288   6 VAIVAVDGFSPFHYSVPCMLFgdtvsETKRFNLHICAERPGLLSArdgfalnasgdFSLLAQADIVVVPYWGAV--NQRP 83
Cdd:cd03128    1 VAVLLFGGSEELELASPLDAL-----REAGAEVDVVSPDGGPVES-----------DVDLDDYDGLILPGGPGTpdDLAW 64

                         90       100
                 ....*....|....*....|....*...
gi 503993288  84 SQPLLDGLVRARNNGAQIVGLCLGAFVL 111
Cdd:cd03128   65 DEALLALLREAAAAGKPVLGICLGAQLL 92
PRK15185 PRK15185
transcriptional regulator HilD; Provisional
 230-307 6.83e-03

transcriptional regulator HilD; Provisional


Pssm-ID: 185107 [Multi-domain]  Cd Length: 309  Bit Score: 37.67  E-value: 6.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 503993288 230 LDSLAQVAAMSRRTLTRHFAKAtGMGIADWLAAERLRRSQILLEAGDLPVGQVAEEVGYRSAVTWRQQFKARFGVSPA 307
Cdd:PRK15185 225 LTDVADHIFMSTSTLKRKLAEE-GTSFSDIYLSARMNQAAKLLRIGNHNVNAVALKCGYDSTSYFIQCFKKYFKTTPS 301
 
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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