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Conserved domains on  [gi|17531319|ref|NP_493696|]
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Glutathione-independent glyoxalase DJR-1.1 [Caenorhabditis elegans]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ThiJ super family cl28603
Putative intracellular protease/amidase [General function prediction only];
6-182 2.06e-74

Putative intracellular protease/amidase [General function prediction only];


The actual alignment was detected with superfamily member TIGR01383:

Pssm-ID: 333423  Cd Length: 179  Bit Score: 225.27  E-value: 2.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319     6 ALIILAAEGAEEMEVIITGDVLARGEIRVVY--AGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLA 83
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    84 ESLLVRDVLKSQVESGGLIGAICAAPIALLSHGVKAEL-VTSHPSVKEKLEKGgyKYSEDR-VVVSGKIITSRGPGTAFE 161
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKkATCYPGFKEKLLNG--NYSVNKtVVVDGNLITSRGPGTAIE 158
                         170       180
                  ....*....|....*....|.
gi 17531319   162 FALKIVELLEGKDKATSLIAP 182
Cdd:TIGR01383 159 FALELVELLAGKEKAQEVAAG 179
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
6-182 2.06e-74

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612  Cd Length: 179  Bit Score: 225.27  E-value: 2.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319     6 ALIILAAEGAEEMEVIITGDVLARGEIRVVY--AGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLA 83
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    84 ESLLVRDVLKSQVESGGLIGAICAAPIALLSHGVKAEL-VTSHPSVKEKLEKGgyKYSEDR-VVVSGKIITSRGPGTAFE 161
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKkATCYPGFKEKLLNG--NYSVNKtVVVDGNLITSRGPGTAIE 158
                         170       180
                  ....*....|....*....|.
gi 17531319   162 FALKIVELLEGKDKATSLIAP 182
Cdd:TIGR01383 159 FALELVELLAGKEKAQEVAAG 179
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
4-169 3.46e-62

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 280192  Cd Length: 165  Bit Score: 193.24  E-value: 3.46e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319     4 KSALIILAaEGAEEMEVIITGDVLARGEIRVVYAGLDGaEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLA 83
Cdd:pfam01965   1 KKVLVLLA-DGFEDIELIYPADVLRRAGIKVDVVSVDG-GEVKGKRGVKVTVDASLDDVKPADYDALVLPGGRAGPERLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    84 ESLLVRDVLKSQVESGGLIGAICAAPIALLSHGV-KAELVTSHPSVKEKLEKGGYKYSEDRVVVSGKIITSRGPGTAFEF 162
Cdd:pfam01965  79 DNEKVVEFVKEFYEKGKPVAAICHGPQVLAAAGVlKGRRVTSYPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPEF 158

                  ....*..
gi 17531319   163 ALKIVEL 169
Cdd:pfam01965 159 ALEILEQ 165
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
6-170 1.18e-60

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  Cd Length: 163  Bit Score: 189.30  E-value: 1.18e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   6 ALIILAaEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLAES 85
Cdd:cd03135   1 VLVILA-DGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  86 LLVRDVLKSQVESGGLIGAICAAPIALLSHGV-KAELVTSHPSVKEKLekGGYKYSEDRVVVSGKIITSRGPGTAFEFAL 164
Cdd:cd03135  80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLlKGKKATCYPGFEDKL--GGANYVDEPVVVDGNIITSRGPGTAFEFAL 157

                ....*.
gi 17531319 165 KIVELL 170
Cdd:cd03135 158 KIVEAL 163
PRK11574 PRK11574
oxidative-stress-resistance chaperone; Provisional
5-185 4.44e-33

oxidative-stress-resistance chaperone; Provisional


Pssm-ID: 183210  Cd Length: 196  Bit Score: 119.11  E-value: 4.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    5 SALIILAAeGAEEMEVIITGDVLARGEIRVVYAGL--DGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTL 82
Cdd:PRK11574   4 SALVCLAP-GSEETEAVTTIDLLVRGGIKVTTASVasDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAECF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   83 AESLLVRDVLKSQVESGGLIGAICAAPIALLSHGVKAEL--VTSHPSVKEKLEKGgyKYSEDRVVVSGKI--ITSRGPGT 158
Cdd:PRK11574  83 RDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIgnMTGFPTLKDKIPAE--QWQDKRVVWDARVnlLTSQGPGT 160
                        170       180
                 ....*....|....*....|....*..
gi 17531319  159 AFEFALKIVELLEGKDKATSLIAPMLL 185
Cdd:PRK11574 161 AIDFALKIIDLLVGREKAHEVASQLVM 187
ThiJ COG0693
Putative intracellular protease/amidase [General function prediction only];
9-176 9.35e-28

Putative intracellular protease/amidase [General function prediction only];


Pssm-ID: 223765  Cd Length: 188  Bit Score: 104.92  E-value: 9.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   9 ILAAEGAEEMEVIITGDVLARG--EIRVVYAGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLAESL 86
Cdd:COG0693   7 ILLADGFEDLELIVPYDVLRRAgfEVDVASPEGKGKSVTSKRGGLVVADDKAFDDADAADYDALVIPGGDHGPEYLRPDP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  87 LVRDVLKSQVESGGLIGAICAAPIALLSHG--VKAELVTSHPSVKE----KLEKGGYKY-----SEDRVVVSGK-IITSR 154
Cdd:COG0693  87 DLLAFVRDFYANGKPVAAICHGPAVLAAAGllLKGRKATAFPDIEEdvknGDGKAGANYvdaplWTDEVVVDGNaLVTGR 166
                       170       180
                ....*....|....*....|..
gi 17531319 155 GPGTAFEFALKIVELLEGKDKA 176
Cdd:COG0693 167 NPASAPAFALELLKALGGAEKA 188
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
6-182 2.06e-74

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612  Cd Length: 179  Bit Score: 225.27  E-value: 2.06e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319     6 ALIILAAEGAEEMEVIITGDVLARGEIRVVY--AGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLA 83
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    84 ESLLVRDVLKSQVESGGLIGAICAAPIALLSHGVKAEL-VTSHPSVKEKLEKGgyKYSEDR-VVVSGKIITSRGPGTAFE 161
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKkATCYPGFKEKLLNG--NYSVNKtVVVDGNLITSRGPGTAIE 158
                         170       180
                  ....*....|....*....|.
gi 17531319   162 FALKIVELLEGKDKATSLIAP 182
Cdd:TIGR01383 159 FALELVELLAGKEKAQEVAAG 179
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
4-169 3.46e-62

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.


Pssm-ID: 280192  Cd Length: 165  Bit Score: 193.24  E-value: 3.46e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319     4 KSALIILAaEGAEEMEVIITGDVLARGEIRVVYAGLDGaEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLA 83
Cdd:pfam01965   1 KKVLVLLA-DGFEDIELIYPADVLRRAGIKVDVVSVDG-GEVKGKRGVKVTVDASLDDVKPADYDALVLPGGRAGPERLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    84 ESLLVRDVLKSQVESGGLIGAICAAPIALLSHGV-KAELVTSHPSVKEKLEKGGYKYSEDRVVVSGKIITSRGPGTAFEF 162
Cdd:pfam01965  79 DNEKVVEFVKEFYEKGKPVAAICHGPQVLAAAGVlKGRRVTSYPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPEF 158

                  ....*..
gi 17531319   163 ALKIVEL 169
Cdd:pfam01965 159 ALEILEQ 165
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
6-170 1.18e-60

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  Cd Length: 163  Bit Score: 189.30  E-value: 1.18e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   6 ALIILAaEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLAES 85
Cdd:cd03135   1 VLVILA-DGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLADN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  86 LLVRDVLKSQVESGGLIGAICAAPIALLSHGV-KAELVTSHPSVKEKLekGGYKYSEDRVVVSGKIITSRGPGTAFEFAL 164
Cdd:cd03135  80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLlKGKKATCYPGFEDKL--GGANYVDEPVVVDGNIITSRGPGTAFEFAL 157

                ....*.
gi 17531319 165 KIVELL 170
Cdd:cd03135 158 KIVEAL 163
PRK11574 PRK11574
oxidative-stress-resistance chaperone; Provisional
5-185 4.44e-33

oxidative-stress-resistance chaperone; Provisional


Pssm-ID: 183210  Cd Length: 196  Bit Score: 119.11  E-value: 4.44e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    5 SALIILAAeGAEEMEVIITGDVLARGEIRVVYAGL--DGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTL 82
Cdd:PRK11574   4 SALVCLAP-GSEETEAVTTIDLLVRGGIKVTTASVasDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAECF 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   83 AESLLVRDVLKSQVESGGLIGAICAAPIALLSHGVKAEL--VTSHPSVKEKLEKGgyKYSEDRVVVSGKI--ITSRGPGT 158
Cdd:PRK11574  83 RDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIgnMTGFPTLKDKIPAE--QWQDKRVVWDARVnlLTSQGPGT 160
                        170       180
                 ....*....|....*....|....*..
gi 17531319  159 AFEFALKIVELLEGKDKATSLIAPMLL 185
Cdd:PRK11574 161 AIDFALKIIDLLVGREKAHEVASQLVM 187
ThiJ COG0693
Putative intracellular protease/amidase [General function prediction only];
9-176 9.35e-28

Putative intracellular protease/amidase [General function prediction only];


Pssm-ID: 223765  Cd Length: 188  Bit Score: 104.92  E-value: 9.35e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   9 ILAAEGAEEMEVIITGDVLARG--EIRVVYAGLDGAEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLAESL 86
Cdd:COG0693   7 ILLADGFEDLELIVPYDVLRRAgfEVDVASPEGKGKSVTSKRGGLVVADDKAFDDADAADYDALVIPGGDHGPEYLRPDP 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  87 LVRDVLKSQVESGGLIGAICAAPIALLSHG--VKAELVTSHPSVKE----KLEKGGYKY-----SEDRVVVSGK-IITSR 154
Cdd:COG0693  87 DLLAFVRDFYANGKPVAAICHGPAVLAAAGllLKGRKATAFPDIEEdvknGDGKAGANYvdaplWTDEVVVDGNaLVTGR 166
                       170       180
                ....*....|....*....|..
gi 17531319 155 GPGTAFEFALKIVELLEGKDKA 176
Cdd:COG0693 167 NPASAPAFALELLKALGGAEKA 188
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
8-169 1.53e-20

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  Cd Length: 165  Bit Score: 84.90  E-value: 1.53e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   8 IILAAEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKCARGAHIV-PDVKLEDVETEKFDIVILPGGqpgsnTLAESL 86
Cdd:cd03134   3 AILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVtVDLTIADVDADDYDALVIPGG-----TNPDKL 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  87 L----VRDVLKSQVESGGLIGAICAAPIALLSHG-VKAELVTSHPSVKEKLEKGGYKYSEDRVVVSGKIITSRGPGTAFE 161
Cdd:cd03134  78 RrdpdAVAFVRAFAEAGKPVAAICHGPWVLISAGvVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPA 157

                ....*...
gi 17531319 162 FALKIVEL 169
Cdd:cd03134 158 FNRAILKA 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
7-171 1.75e-17

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591  Cd Length: 166  Bit Score: 76.69  E-value: 1.75e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319     7 LIILAAEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKcARGAHIVPDVKLEDVETEKFDIVILPGGQpGSNTLAESL 86
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTVG-KHGYSVTVDATIDEVNPEEYDALVIPGGR-APEYLRLNN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319    87 LVRDVLKSQVESGGLIGAICAAPIALLSHGV-KAELVTSHPSVKEKLEKGGYKYSEDR-VVVSGKIITSRGPGTAFEFAL 164
Cdd:TIGR01382  80 KAVRLVREFVEKGKPVAAICHGPQLLISAGVlRGKKLTSYPAIIDDVKNAGAEYVDIEvVVVDGNLVTSRVPDDLPAFNR 159

                  ....*..
gi 17531319   165 KIVELLE 171
Cdd:TIGR01382 160 EFLKLLG 166
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
34-171 3.48e-16

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  Cd Length: 170  Bit Score: 73.02  E-value: 3.48e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  34 VVYAGLDGaEPVKCARGAHIVPDVKLEDVETEKFDIVILPGGQPGSNTLAESL--LVRDVLKSQVesggLIGAICAAPIA 111
Cdd:cd03140  29 VRTVSPTG-EPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDNPEAPDLagLVRQALKQGK----PVAAICGATLA 103
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17531319 112 LLSHGVKAELvtSHPS-VKEKLEKGGYKYSED------RVVVSGKIITSrgPGTAF-EFALKIVELLE 171
Cdd:cd03140 104 LARAGLLNNR--KHTSnSLDFLKAHAPYYGGAeyydepQAVSDGNLITA--NGTAPvEFAAEILRALD 167
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
9-176 7.53e-13

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  Cd Length: 183  Bit Score: 63.33  E-value: 7.53e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   9 ILAAEGAEEMEVIITGDVLAR-----GEIRVVYAGLDGAePVKCARGAHIVPDVKLEDVEteKFDIVILPGGqPGSNTLA 83
Cdd:cd03139   3 ILLFPGVEVLDVIGPYEVFGRaprlaAPFEVFLVSETGG-PVSSRSGLTVLPDTSFADPP--DLDVLLVPGG-GGTRALV 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  84 ESLLVRDVLKSQVESGGLIGAIC------AApiALLSHGVKAelvTSHPSVKEKL-EKGGYKYSEDRVVVSGKIITSRGP 156
Cdd:cd03139  79 NDPALLDFIRRQAARAKYVTSVCtgalllAA--AGLLDGRRA---TTHWAAIDWLkEFGAIVVVDARWVVDGNIWTSGGV 153
                       170       180
                ....*....|....*....|
gi 17531319 157 GTAFEFALKIVELLEGKDKA 176
Cdd:cd03139 154 SAGIDMALALVARLFGEELA 173
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
57-170 7.20e-10

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.


Pssm-ID: 153235  Cd Length: 221  Bit Score: 55.64  E-value: 7.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  57 VKLEDVETEKFDIVILPGGQPGSNTLAESLLVRDVLKSQVESGGLIGAICAAPIALL-------SHGVKAELVTSHP--- 126
Cdd:cd03141  81 KKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLnvklsdgKSLVAGKTVTGFTnee 160
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17531319 127 ------------SVKEKLEKGGYKYSE-----DRVVVSGKIITSRGPGTAFEFALKIVELL 170
Cdd:cd03141 161 eeaaglkkvvpfLLEDELKELGANYVKaepwaEFVVVDGRLITGQNPASAAAVAEALVKAL 221
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
8-113 6.73e-09

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  Cd Length: 115  Bit Score: 51.45  E-value: 6.73e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   8 IILAAEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKcargahivpdvkleDVETEKFDIVILPGGQPGSNTLAESLL 87
Cdd:cd01653   2 AVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVES--------------DVDLDDYDGLILPGGPGTPDDLARDEA 67
                        90       100
                ....*....|....*....|....*.
gi 17531319  88 VRDVLKSQVESGGLIGAICAAPIALL 113
Cdd:cd01653  68 LLALLREAAAAGKPILGICLGAQLLV 93
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
38-168 5.65e-08

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  Cd Length: 185  Bit Score: 49.89  E-value: 5.65e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  38 GLDGAePVKCARGAHIVPDVKLEDVetEKFDIVILPGGQPGSNTLAESLLvrDVLKSQVESGGLIGAICAAPIALLSHGV 117
Cdd:cd03136  39 SLDGA-PVTSSNGLRVAPDAALEDA--PPLDYLFVVGGLGARRAVTPALL--AWLRRAARRGVALGGIDTGAFLLARAGL 113
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 17531319 118 -KAELVTSH----PSVKEKLEkgGYKYSEDRVVVSGKIITSRGPGTAFEFALKIVE 168
Cdd:cd03136 114 lDGRRATVHwehlEAFAEAFP--RVQVTRDLFEIDGDRLTCAGGTAALDLMLELIA 167
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
8-112 1.19e-07

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  Cd Length: 92  Bit Score: 47.58  E-value: 1.19e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   8 IILAAEGAEEMEVIITGDVLARGEIRVVYAGLDGAEPVKcargahivpdvkleDVETEKFDIVILPGGQPGSNTLAESLL 87
Cdd:cd03128   2 AVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVES--------------DVDLDDYDGLILPGGPGTPDDLAWDEA 67
                        90       100
                ....*....|....*....|....*
gi 17531319  88 VRDVLKSQVESGGLIGAICAAPIAL 112
Cdd:cd03128  68 LLALLREAAAAGKPVLGICLGAQLL 92
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
49-155 1.77e-07

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  Cd Length: 180  Bit Score: 48.41  E-value: 1.77e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  49 RGAHIVPDVKLEDVETEKFDIVILPGGQ-PGSNTLAESL--LVRDVlksqVESGGLIGAICAAPIALLSHGV-KAELVTS 124
Cdd:cd03169  59 PGHRFAVTADFDEVDPDDYDALVIPGGRaPEYLRLDEKVlaIVRHF----AEANKPVAAICHGPQILAAAGVlKGRRCTA 134
                        90       100       110
                ....*....|....*....|....*....|.
gi 17531319 125 HPSVKEKLEKGGYKYSEDRVVVSGKIITSRG 155
Cdd:cd03169 135 YPACKPEVELAGGTVVDDGVVVDGNLVTAQA 165
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
31-176 2.33e-07

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  Cd Length: 195  Bit Score: 48.41  E-value: 2.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  31 EIRVVyaGLDGaEPVKCARGAHIVPDVKLEDVETekFDIVILPG--GQPGSNTLAESLLVRDVLKSQVESGGLIGAICAA 108
Cdd:cd03138  39 EVRLV--SLDG-GPVLLAGGILILPDATLADVPA--PDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVAAACTG 113
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319 109 PIAL----LSHGVKA--------ELVTSHPSVKEKLEKggykysedRVVVSGKIITSRGPGTAFEFALKIVELLEGKDKA 176
Cdd:cd03138 114 VFLLaeagLLDGRRAtthwwlapQFRRRFPKVRLDPDR--------VVVTDGNLITAGGAMAWADLALHLIERLAGPELA 185
GlxA COG4977
Transcriptional regulator GlxA family, contains an amidase domain and an AraC-type DNA-binding ...
9-172 9.01e-05

Transcriptional regulator GlxA family, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 227311  Cd Length: 328  Bit Score: 41.87  E-value: 9.01e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319   9 ILAAEGAEEMEVIiTGDVLARGEIRVVYAGLDGaEPVKCARGAHIVPDVKLEDveTEKFDIVILPGGQPGSNTLAESLLV 88
Cdd:COG4977  23 LMAFASAVEPLRA-ANRLAGRSLYVWSIVSADG-GPVRSSSGLSIAPDGGLEA--APPIDILPVCGGLGPERPVNAPALL 98
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17531319  89 RdVLKSQVESGGLIGAICAAPIALLSHGV------------KAELVTSHPSVKEklekggykySEDRVVVSGKIITSRGP 156
Cdd:COG4977  99 A-WLRRAARRGARLGGLCTGAFVLAEAGLldgrratthwehAEDFQERFPDVRV---------TDRLFVIDGDRITCAGG 168
                       170
                ....*....|....*.
gi 17531319 157 GTAFEFALKIVELLEG 172
Cdd:COG4977 169 TAAIDLMLALIRRDFG 184
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.16
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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