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Conserved domains on  [gi|924355407|ref|WP_053488458|]
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MULTISPECIES: type 1 glutamine amidotransferase family protein [Priestia]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 10123441)

type 1 glutamine amidotransferase (GATase1) family protein similar to Bacillus subtilis proteases YoaZ and YdeA

CATH:  3.40.50.880
EC:  3.2.-.-
Gene Ontology:  GO:0019172|GO:0008233
MEROPS:  C56
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-181 5.19e-77

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: 228.64  E-value: 5.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   6 VYIYVFNTMSDWEYGYLIAELNSGRyfrqglaPLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGNTWS 85
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLNSYE-------GFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  86 EEIHQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVCPNYKGEKLYEVGPVVSDNNMITASGV 165
Cdd:cd03140   74 NPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQAVSDGNLITANGT 153

                        170
                 ....*....|....*.
gi 924355407 166 APLEFARDVLKKLDVF 181
Cdd:cd03140  154 APVEFAAEILRALDVF 169
 
Name Accession Description Interval E-value
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-181 5.19e-77

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: 228.64  E-value: 5.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   6 VYIYVFNTMSDWEYGYLIAELNSGRyfrqglaPLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGNTWS 85
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLNSYE-------GFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  86 EEIHQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVCPNYKGEKLYEVGPVVSDNNMITASGV 165
Cdd:cd03140   74 NPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQAVSDGNLITANGT 153

                        170
                 ....*....|....*.
gi 924355407 166 APLEFARDVLKKLDVF 181
Cdd:cd03140  154 APVEFAAEILRALDVF 169
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-177 7.96e-42

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: 138.93  E-value: 7.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407    4 KKVYIYVFNTMSDWEYGYLIAELNSgryfrqglAPLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGNT 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRR--------AGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   84 WSEEIHQP--ILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVCPNYKgeklYEVGPVVSDNNMIT 161
Cdd:pfam01965  73 GPERLRDNekLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGAT----YVDKPVVVDGNLVT 148

                         170
                  ....*....|....*..
gi 924355407  162 ASGV-APLEFARDVLKK 177
Cdd:pfam01965 149 SRGPgDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 4-178 3.93e-29

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: 106.34  E-value: 3.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   4 KKVYIYVFNTMSDWEYGYLIAELNSGRYfrqglaplKVMTVGVNKEI-IKTMGGLSIQPDISLDECTLLDKDLLILPGGN 82
Cdd:COG0693    3 KKVLILLTDGFEDEELTVPYDALREAGA--------EVDVASPEGGPpVTSKHGITVTADKTLDDVDPDDYDALVLPGGH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  83 TWSEEI--HQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVcpNYKGEklYEVGPVVSDNNMI 160
Cdd:COG0693   75 GAPDDLreDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLK--NAGAT--YVDEEVVVDGNLI 150

                        170
                 ....*....|....*....
gi 924355407 161 TASGVAPL-EFARDVLKKL 178
Cdd:COG0693  151 TSRGPGDApAFARALLELL 169
 
Name Accession Description Interval E-value
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-181 5.19e-77

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: 228.64  E-value: 5.19e-77
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   6 VYIYVFNTMSDWEYGYLIAELNSGRyfrqglaPLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGNTWS 85
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLNSYE-------GFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWD 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  86 EEIHQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVCPNYKGEKLYEVGPVVSDNNMITASGV 165
Cdd:cd03140   74 NPEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQAVSDGNLITANGT 153

                        170
                 ....*....|....*.
gi 924355407 166 APLEFARDVLKKLDVF 181
Cdd:cd03140  154 APVEFAAEILRALDVF 169
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-177 7.96e-42

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: 138.93  E-value: 7.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407    4 KKVYIYVFNTMSDWEYGYLIAELNSgryfrqglAPLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGNT 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRR--------AGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   84 WSEEIHQP--ILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVCPNYKgeklYEVGPVVSDNNMIT 161
Cdd:pfam01965  73 GPERLRDNekLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGAT----YVDKPVVVDGNLVT 148

                         170
                  ....*....|....*..
gi 924355407  162 ASGV-APLEFARDVLKK 177
Cdd:pfam01965 149 SRGPgDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 4-178 3.93e-29

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: 106.34  E-value: 3.93e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   4 KKVYIYVFNTMSDWEYGYLIAELNSGRYfrqglaplKVMTVGVNKEI-IKTMGGLSIQPDISLDECTLLDKDLLILPGGN 82
Cdd:COG0693    3 KKVLILLTDGFEDEELTVPYDALREAGA--------EVDVASPEGGPpVTSKHGITVTADKTLDDVDPDDYDALVLPGGH 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  83 TWSEEI--HQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTLNNLEYTKMVcpNYKGEklYEVGPVVSDNNMI 160
Cdd:COG0693   75 GAPDDLreDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLK--NAGAT--YVDEEVVVDGNLI 150

                        170
                 ....*....|....*....
gi 924355407 161 TASGVAPL-EFARDVLKKL 178
Cdd:COG0693  151 TSRGPGDApAFARALLELL 169
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 39-178 1.73e-17

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: 76.05  E-value: 1.73e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  39 LKVMTVGVN-KEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGNTWSEEI--HQPILKKVGEVLELGTIVAAICGATDA 115
Cdd:cd03135   26 IEVTTASLEkKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLadNEKLIKLLKEFNAKGKLIAAICAAPAV 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924355407 116 LANSGYLDSRKHTLNNLEYTKMVCPNYKGEklyevgPVVSDNNMITASGVA-PLEFARDVLKKL 178
Cdd:cd03135  106 LAKAGLLKGKKATCYPGFEDKLGGANYVDE------PVVVDGNIITSRGPGtAFEFALKIVEAL 163
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 37-165 9.86e-10

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: 55.63  E-value: 9.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  37 APLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDkdLLILPGG-NTWSEEIHQPILKKVGEVLELGTIVAAICGATDA 115
Cdd:cd03139   29 APFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLD--VLLVPGGgGTRALVNDPALLDFIRRQAARAKYVTSVCTGALL 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 924355407 116 LANSGYLDSRKHTLN--NLEYTKMVCPNYKGEKLyevgpVVSDNNMITASGV 165
Cdd:cd03139  107 LAAAGLLDGRRATTHwaAIDWLKEFGAIVVVDAR-----WVVDGNIWTSGGV 153
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 22-128 9.94e-09

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: 53.03  E-value: 9.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  22 LIAELNSGRYfRQGLAPLKVMTVGVNKEIIKTMGGLSIQPDISLDEctLLDKDLLILPGGNTWSEEI----HQPILKKVG 97
Cdd:cd03138   22 RAANRLARRQ-QGGAPPFEVRLVSLDGGPVLLAGGILILPDATLAD--VPAPDLVIVPGLGGDPDELlladNPALIAWLR 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 924355407  98 EVLELGTIVAAICGATDALANSGYLDSRKHT 128
Cdd:cd03138   99 RQHANGATVAAACTGVFLLAEAGLLDGRRAT 129
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 34-126 2.08e-07

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: 50.16  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  34 QGLAPLKVMTVGVNKEIIKTMGGLSIQPDISLDECTLLDkdLLILPGGNTWSEEIHQPILKKVGEVLELGTIVAAICGAT 113
Cdd:COG4977   30 AGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAAD--TLIVPGGLDPAAAADPALLAWLRRAAARGARLASICTGA 107

                         90
                 ....*....|...
gi 924355407 114 DALANSGYLDSRK 126
Cdd:COG4977  108 FLLAAAGLLDGRR 120
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 41-177 5.07e-07

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: 47.54  E-value: 5.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  41 VMTVGVNKEIIKTMGGLSIQPDISLDECTLLDKDLLILPGGntWSEE---IHQPILKKVGEVLELGTIVAAICGATDALA 117
Cdd:cd03134   31 VAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGG--TNPDklrRDPDAVAFVRAFAEAGKPVAAICHGPWVLI 108

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 924355407 118 NSGYLDSRKHTlnnleytkmvcpNYKGEK--------LYEVGPVVSDNNMITASGVAPLE-FARDVLKK 177
Cdd:cd03134  109 SAGVVRGRKLT------------SYPSIKddlinagaNWVDEEVVVDGNLITSRNPDDLPaFNRAILKA 165
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 33-128 2.65e-06

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: 45.95  E-value: 2.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  33 RQGLAPLKVMTVGVNKEIIKTMGGLSIQPDISLDecTLLDKDLLILPGGNT-WSEEIHQPILKKVGEVLELGTIVAAICG 111
Cdd:cd03137   27 ALGPPAYELRVCSPEGGPVRSSSGLSLVADAGLD--ALAAADTVIVPGGPDvDGRPPPPALLAALRRAAARGARVASVCT 104

                         90
                 ....*....|....*..
gi 924355407 112 ATDALANSGYLDSRKHT 128
Cdd:cd03137  105 GAFVLAEAGLLDGRRAT 121
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 56-178 1.32e-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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 38.01  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407  56 GLSIQPDISLDECTLLDKDLLILPGGNTwSEEI--HQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTlnNLE 133
Cdd:cd03169   60 GHRFAVTADFDEVDPDDYDALVIPGGRA-PEYLrlDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCT--AYP 136

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 924355407 134 YTKMVCPNYKGEklYEVGPVVSDNNMITASGVAPL-EFARDVLKKL 178
Cdd:cd03169  137 ACKPEVELAGGT--VVDDGVVVDGNLVTAQAWPDHpAFLREFLKLL 180
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-116 5.14e-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: 35.65  E-value: 5.14e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 924355407   6 VYIYVFNTMSDWEYGYLIAELNSgryfrqglAPLKVMTVGVNKEIIKTmgglsiqpDISLDECtlldkDLLILPGG--NT 83
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALRE--------AGAEVDVVSPDGGPVES--------DVDLDDY-----DGLILPGGpgTP 59

                         90       100       110
                 ....*....|....*....|....*....|...
gi 924355407  84 WSEEIHQPILKKVGEVLELGTIVAAICGATDAL 116
Cdd:cd01653   60 DDLARDEALLALLREAAAAGKPILGICLGAQLL 92
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 56-129 7.52e-03

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: 36.02  E-value: 7.52e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 924355407  56 GLSIQPDISLDECTLLDkdLLILPGGNTWSEEIHQPILKKVGEVLELGTIVAAICGATDALANSGYLDSRKHTL 129
Cdd:cd03136   50 GLRVAPDAALEDAPPLD--YLFVVGGLGARRAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATV 121
 
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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