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Conserved domains on  [gi|1907294704|ref|WP_189909144|]
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type 1 glutamine amidotransferase domain-containing protein [Streptomyces albogriseolus]

Protein Classification

type 1 glutamine amidotransferase domain-containing protein( domain architecture ID 10123305)

type 1 glutamine amidotransferase domain-containing protein similar to Pyrococcus furiosus deglycase PfpI that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals (Probable)

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 2-174 1.19e-76

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: 226.27  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   2 RIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQS-GEVQAFHHLDkadTFPVQEVVGDTSADTFDGLVLPGGVaNPD 80
Cdd:cd03134     1 KVAILAA-DGFEDVELTYPLYRLREAGAEVVVAGPEAgGEIQGKHGYD---TVTVDLTIADVDADDYDALVIPGGT-NPD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCDHgsnkLVTSRK 160
Cdd:cd03134    76 KLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN----LITSRN 151

                         170
                  ....*....|....
gi 1907294704 161 PDDLKAFCETFLEV 174
Cdd:cd03134   152 PDDLPAFNRAILKA 165
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 2-174 1.19e-76

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: 226.27  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   2 RIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQS-GEVQAFHHLDkadTFPVQEVVGDTSADTFDGLVLPGGVaNPD 80
Cdd:cd03134     1 KVAILAA-DGFEDVELTYPLYRLREAGAEVVVAGPEAgGEIQGKHGYD---TVTVDLTIADVDADDYDALVIPGGT-NPD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCDHgsnkLVTSRK 160
Cdd:cd03134    76 KLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN----LITSRN 151

                         170
                  ....*....|....
gi 1907294704 161 PDDLKAFCETFLEV 174
Cdd:cd03134   152 PDDLPAFNRAILKA 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-176 3.25e-64

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: 194.94  E-value: 3.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   1 MRIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAfhhLDKADTFPVQEVVGDTSADTFDGLVLPGGVANPD 80
Cdd:COG0693     3 KKVLILLT-DGFEDEELTVPYDALREAGAEVDVASPEGGPPVT---SKHGITVTADKTLDDVDPDDYDALVLPGGHGAPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVkVCDhgsNKLVTSRK 160
Cdd:COG0693    79 DLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEV-VVD---GNLITSRG 154

                         170
                  ....*....|....*.
gi 1907294704 161 PDDLKAFCETFLEVFA 176
Cdd:COG0693   155 PGDAPAFARALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-173 8.44e-59

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: 180.92  E-value: 8.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   1 MRIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLdkadTFPVQEVVGDTSADTFDGLVLPGGVANPD 80
Cdd:pfam01965   1 KKVLVLLA-DGFEDIELIYPADVLRRAGIKVTVVSVDGGEVKGSRGV----KVTVDASLDDVKPDDYDALVLPGGRAGPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCdhgsNKLVTSRK 160
Cdd:pfam01965  76 RLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVD----GNLVTSRG 151

                         170
                  ....*....|...
gi 1907294704 161 PDDLKAFCETFLE 173
Cdd:pfam01965 152 PGDAPEFALEILE 164
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 3-173 1.44e-50

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 [Multi-domain]  Cd Length: 166  Bit Score: 160.28  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   3 IAFLTaPEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLdkadTFPVQEVVGDTSADTFDGLVLPGGVAnPDFL 82
Cdd:TIGR01382   2 LLVLT-TDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTVGKHGY----SVTVDATIDEVNPEEYDALVIPGGRA-PEYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  83 RMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCDhgsNKLVTSRKPD 162
Cdd:TIGR01382  76 RLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVD---GNLVTSRVPD 152

                         170
                  ....*....|.
gi 1907294704 163 DLKAFCETFLE 173
Cdd:TIGR01382 153 DLPAFNREFLK 163
PRK11574 PRK11574
protein deglycase YajL;
50-161 1.76e-07

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 49.01  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  50 ADTfPVQEVVGDTsadtFDGLVLPGGVANPDFLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEA-DVVRGRVLTSWPS 128
Cdd:PRK11574   55 ADA-PLVEVADGD----FDVIVLPGGIKGAECFRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPhDLFPIGNMTGFPT 129

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907294704 129 LRTDLgnAGATWVNEQVkVCDHGSNkLVTSRKP 161
Cdd:PRK11574  130 LKDKI--PAEQWQDKRV-VWDARVN-LLTSQGP 158
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 2-174 1.19e-76

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: 226.27  E-value: 1.19e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   2 RIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQS-GEVQAFHHLDkadTFPVQEVVGDTSADTFDGLVLPGGVaNPD 80
Cdd:cd03134     1 KVAILAA-DGFEDVELTYPLYRLREAGAEVVVAGPEAgGEIQGKHGYD---TVTVDLTIADVDADDYDALVIPGGT-NPD 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCDHgsnkLVTSRK 160
Cdd:cd03134    76 KLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN----LITSRN 151

                         170
                  ....*....|....
gi 1907294704 161 PDDLKAFCETFLEV 174
Cdd:cd03134   152 PDDLPAFNRAILKA 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-176 3.25e-64

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: 194.94  E-value: 3.25e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   1 MRIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAfhhLDKADTFPVQEVVGDTSADTFDGLVLPGGVANPD 80
Cdd:COG0693     3 KKVLILLT-DGFEDEELTVPYDALREAGAEVDVASPEGGPPVT---SKHGITVTADKTLDDVDPDDYDALVLPGGHGAPD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVkVCDhgsNKLVTSRK 160
Cdd:COG0693    79 DLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEV-VVD---GNLITSRG 154

                         170
                  ....*....|....*.
gi 1907294704 161 PDDLKAFCETFLEVFA 176
Cdd:COG0693   155 PGDAPAFARALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-173 8.44e-59

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: 180.92  E-value: 8.44e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   1 MRIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLdkadTFPVQEVVGDTSADTFDGLVLPGGVANPD 80
Cdd:pfam01965   1 KKVLVLLA-DGFEDIELIYPADVLRRAGIKVTVVSVDGGEVKGSRGV----KVTVDASLDDVKPDDYDALVLPGGRAGPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  81 FLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCdhgsNKLVTSRK 160
Cdd:pfam01965  76 RLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVD----GNLVTSRG 151

                         170
                  ....*....|...
gi 1907294704 161 PDDLKAFCETFLE 173
Cdd:pfam01965 152 PGDAPEFALEILE 164
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 3-173 1.44e-50

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 [Multi-domain]  Cd Length: 166  Bit Score: 160.28  E-value: 1.44e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   3 IAFLTaPEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLdkadTFPVQEVVGDTSADTFDGLVLPGGVAnPDFL 82
Cdd:TIGR01382   2 LLVLT-TDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTVGKHGY----SVTVDATIDEVNPEEYDALVIPGGRA-PEYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  83 RMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCDhgsNKLVTSRKPD 162
Cdd:TIGR01382  76 RLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVD---GNLVTSRVPD 152

                         170
                  ....*....|.
gi 1907294704 163 DLKAFCETFLE 173
Cdd:TIGR01382 153 DLPAFNREFLK 163
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 2-174 5.62e-37

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: 125.84  E-value: 5.62e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   2 RIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVS--TQSGE--VQAFHHLDKADT--------FPVQEVVGDTSADTFDG 69
Cdd:cd03169     1 KILILTG-DFVEDYEVMVPFQALQEVGHEVDVVApgKKKGDtvVTAIHDFPGWQTytekpghrFAVTADFDEVDPDDYDA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  70 LVLPGGVAnPDFLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGNAGATWVNEQVKVCD 149
Cdd:cd03169    80 LVIPGGRA-PEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDDGVVVDG 158

                         170       180
                  ....*....|....*....|....*
gi 1907294704 150 HgsnkLVTSRKPDDLKAFCETFLEV 174
Cdd:cd03169   159 N----LVTAQAWPDHPAFLREFLKL 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 9-175 2.06e-21

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: 85.30  E-value: 2.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   9 PEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHH--LDKADTfpvqeVVGDTSADTFDGLVLPGGVANPDFLRMDD 86
Cdd:cd03135     6 ADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHgiKVKADK-----TLSDVNLDDYDAIVIPGGLPGAQNLADNE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  87 KAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTSWPSLRTDLGnaGATWVNEQVKVcdhgSNKLVTSRKPDDLKA 166
Cdd:cd03135    81 KLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG--GANYVDEPVVV----DGNIITSRGPGTAFE 154


                  ....*....
gi 1907294704 167 FCETFLEVF 175
Cdd:cd03135   155 FALKIVEAL 163
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-113 2.70e-15

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: 68.39  E-value: 2.70e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   3 IAFLTAPeGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLDKadtfpvqevvgdtsadtFDGLVLPGGVANPDFL 82
Cdd:cd01653     1 VAVLLFP-GFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDD-----------------YDGLILPGGPGTPDDL 62

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1907294704  83 RMDDKAVAFVRNFFEQGRPVAAICHAPWTLI 113
Cdd:cd01653    63 ARDEALLALLREAAAAGKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-112 4.46e-14

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: 64.53  E-value: 4.46e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   3 IAFLTAPeGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLDKadtfpvqevvgdtsadtFDGLVLPGGVANPDFL 82
Cdd:cd03128     1 VAVLLFG-GSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLDD-----------------YDGLILPGGPGTPDDL 62

                          90       100       110
                  ....*....|....*....|....*....|
gi 1907294704  83 RMDDKAVAFVRNFFEQGRPVAAICHAPWTL 112
Cdd:cd03128    63 AWDEALLALLREAAAAGKPVLGICLGAQLL 92
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 34-161 1.29e-13

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 [Multi-domain]  Cd Length: 179  Bit Score: 65.42  E-value: 1.29e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  34 VSTQSGE-VQAFHHLD-KADTfpvqeVVGDTSADTFDGLVLPGGVANPDFLRMDDKAVAFVRNFFEQGRPVAAICHAPWT 111
Cdd:TIGR01383  34 AGLNGKLaVKGSRGVKiLADA-----SLEDVDLEKFDVIVLPGGMPGAENLRNSKLLLNILKSQESKGKLVAAICAAPAV 108

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907294704 112 LIEADVVRGRVLTSWPSLRTDLGNAGATwVNEQVKVcdhgSNKLVTSRKP 161
Cdd:TIGR01383 109 LLAHGVLLGKKATCYPGFKEKLLNGNYS-VNKTVVV----DGNLITSRGP 153
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 9-127 2.48e-11

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 [Multi-domain]  Cd Length: 221  Bit Score: 59.88  E-value: 2.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   9 PEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAFHHLDKADTFPVQEV----------------VGDTSADTFDGLVL 72
Cdd:cd03141    17 PTGLWLEELAHPYDVFTEAGYEVDFASPKGGKVPLDPRSLDAEDDDDASVfdndeefkkklantkkLSDVDPSDYDAIFI 96

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907294704  73 PGGVAnP--DFlrMDDKAV-AFVRNFFEQGRPVAAICHAPWTLIEAD------VVRGRVLTSWP 127
Cdd:cd03141    97 PGGHG-PmfDL--PDNPDLqDLLREFYENGKVVAAVCHGPAALLNVKlsdgksLVAGKTVTGFT 157
PRK11574 PRK11574
protein deglycase YajL;
50-161 1.76e-07

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 49.01  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  50 ADTfPVQEVVGDTsadtFDGLVLPGGVANPDFLRMDDKAVAFVRNFFEQGRPVAAICHAPWTLIEA-DVVRGRVLTSWPS 128
Cdd:PRK11574   55 ADA-PLVEVADGD----FDVIVLPGGIKGAECFRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPhDLFPIGNMTGFPT 129

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1907294704 129 LRTDLgnAGATWVNEQVkVCDHGSNkLVTSRKP 161
Cdd:PRK11574  130 LKDKI--PAEQWQDKRV-VWDARVN-LLTSQGP 158
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
63-109 6.23e-06

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 44.78  E-value: 6.23e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907294704  63 SADTFDGLVLPG--GVA---------------NPDFLRmddkavaFVRNFFEQGRPVAAICHAP 109
Cdd:PRK11780   82 DAEDFDALIVPGgfGAAknlsnfavkgaectvNPDVKA-------LVRAFHQAGKPIGFICIAP 138
katE PRK11249
hydroperoxidase II; Provisional
 2-105 3.95e-05

hydroperoxidase II; Provisional


Pssm-ID: 236886 [Multi-domain]  Cd Length: 752  Bit Score: 43.11  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   2 RIAFLTAPeGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAfhhlDKADTFPVQEVVGDTSADTFDGLVLPGGVANPDF 81
Cdd:PRK11249  599 KVAILLND-GVDAADLLAILKALKAKGVHAKLLYPRMGEVTA----DDGTVLPIAATFAGAPSLTFDAVIVPGGKANIAD 673

                          90       100
                  ....*....|....*....|....
gi 1907294704  82 LRMDDKAVAFVRNFFEQGRPVAAI 105
Cdd:PRK11249  674 LADNGDARYYLLEAYKHLKPIALA 697
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 59-125 7.87e-05

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: 41.05  E-value: 7.87e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907294704  59 VGDTSADTFDGLVLPGGVA--NPDflrmDDKAVAFVRNFFEQGRPVAAICHAPWTLIEADVVRGRVLTS 125
Cdd:cd03140    53 LDDLPPEDYDLLILPGGDSwdNPE----APDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTS 117
GATase1_catalase cd03132
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ...
 2-105 1.05e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.


Pssm-ID: 153226  Cd Length: 142  Bit Score: 40.32  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704   2 RIAFLTApEGVEQVELTEPWKAAEQAGHEPVLVSTQSGEVQAfhhlDKADTFPVQEVVGDTSADTFDGLVLPGGVANPDF 81
Cdd:cd03132     3 KVGILVA-DGVDAAELSALKAALKAAGANVKVVAPTLGGVVD----SDGKTLEVDQTYAGAPSVLFDAVVVPGGAEAAFA 77

                          90       100
                  ....*....|....*....|....
gi 1907294704  82 LRMDDKAVAFVRNFFEQGRPVAAI 105
Cdd:cd03132    78 LAPSGRALHFVTEAFKHGKPIGAV 101
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 22-106 1.60e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 40.68  E-value: 1.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  22 KAAEQAGHEPVLVstqsgevqafHHLDKADtfpvqevvGDTSADTFDGLVLPGGVANPDFLR------MDDKAVAFVRNF 95
Cdd:cd01740    17 YAFELAGFEAEDV----------WHNDLLA--------GRKDLDDYDGVVLPGGFSYGDYLRagaiaaASPLLMEEVKEF 78

                          90
                  ....*....|.
gi 1907294704  96 FEQGRPVAAIC 106
Cdd:cd01740    79 AERGGLVLGIC 89
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 61-109 1.36e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. This group includes, proteins similar to ES1, Escherichia coli enhancing lycopene biosynthesis protein 2, Azospirillum brasilense iaaC and, human HES1. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Zebrafish ES1 is expressed specifically in adult photoreceptor cells and appears to be a cytoplasmic protein. A. brasilense iaaC is involved in controlling IAA biosynthesis.


Pssm-ID: 153227  Cd Length: 213  Bit Score: 37.99  E-value: 1.36e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907294704  61 DTSADTFDGLVLPGG--VA--NPDF------LRMDDKAVAFVRNFFEQGRPVAAICHAP 109
Cdd:cd03133    77 KLKAADFDALIFPGGfgAAknLSDFavkgadCTVNPEVERLVREFHQAGKPIGAICIAP 135
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 39-114 3.40e-03

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 37.05  E-value: 3.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907294704  39 GEVQAFHHLDKADtfpvqevvGDTSADTFDGLVLPGGVANPDFLRMDD------KAVAF--VRNFFEQGRPVAAICHAPW 110
Cdd:PRK01175   29 VEPEYVHINDLAA--------ERKSVSDYDCLVIPGGFSAGDYIRAGAifaarlKAVLRkdIEEFIDEGYPIIGICNGFQ 100


                  ....
gi 1907294704 111 TLIE 114
Cdd:PRK01175  101 VLVE 104
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 61-107 6.85e-03

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 36.08  E-value: 6.85e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1907294704  61 DTSADTFDGLVLPGGVANP-DFLRMDDKAVAFVRNFFEQGRPVAAICH 107
Cdd:COG0518    43 DPDLEDPDGLILSGGPMSVyDEDPWLEDEPALIREAFELGKPVLGICY 90
 
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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