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Conserved domains on  [gi|20070420|ref|NP_613067|]
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glutamine amidotransferase-like class 1 domain-containing protein 3, mitochondrial isoform 1 precursor [Mus musculus]

Protein Classification

type 1 glutamine amidotransferase( domain architecture ID 10123302)

type 1 glutamine amidotransferase-like protein belonging to ES1 family is involved in the hydrolysis of ammonia from glutamine and the transfer of the amino group to an acceptor substrate

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 43-264 8.04e-121

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: 343.45  E-value: 8.04e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  43 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEpSERESRNVLAESARIARGKITSLAQLN 122
Cdd:cd03133   1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 123 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeggk 201
Cdd:cd03133  80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILgEGVEVTIGND------ 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070420 202 wpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELT 264
Cdd:cd03133 154 ---AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
 
Name Accession Description Interval E-value
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 43-264 8.04e-121

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: 343.45  E-value: 8.04e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  43 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEpSERESRNVLAESARIARGKITSLAQLN 122
Cdd:cd03133   1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 123 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeggk 201
Cdd:cd03133  80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILgEGVEVTIGND------ 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070420 202 wpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELT 264
Cdd:cd03133 154 ---AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
41-264 2.59e-113

Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];


Pssm-ID: 442389  Cd Length: 215  Bit Score: 324.43  E-value: 2.59e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  41 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEPSErESRNVLAESARIARGKITSLAQ 120
Cdd:COG3155   1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEEMG-EKRNVLVESARIARGNIKPLAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 121 LNAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeg 199
Cdd:COG3155  80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLgAGVKLTIGND---- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20070420 200 gkwpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELT 264
Cdd:COG3155 156 -----ADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKKVLELA 215
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
41-265 2.43e-109

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 314.42  E-value: 2.43e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420   41 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEPSErESRNVLAESARIARGKITSLAQ 120
Cdd:PRK11780   2 KKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  121 LNAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeg 199
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILgAGVKLTIGND---- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20070420  200 gkwpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELTG 265
Cdd:PRK11780 157 -----EDTAAAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVSRVLELAE 217
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 116-191 1.18e-04

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: 41.47  E-value: 1.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20070420   116 TSLAQLNAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHGAKKPIGLCCIAPVL--AAKVIKGVEVT 191
Cdd:pfam01965  52 ASLDDVKPDDYDALVLPGGRAGPERLRD----------NEKLVEFVKDFYEKGKPVAAICHGPQVlaAAGVLKGRKVT 119
 
Name Accession Description Interval E-value
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 43-264 8.04e-121

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: 343.45  E-value: 8.04e-121
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  43 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEpSERESRNVLAESARIARGKITSLAQLN 122
Cdd:cd03133   1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 123 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeggk 201
Cdd:cd03133  80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILgEGVEVTIGND------ 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 20070420 202 wpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELT 264
Cdd:cd03133 154 ---AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
41-264 2.59e-113

Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];


Pssm-ID: 442389  Cd Length: 215  Bit Score: 324.43  E-value: 2.59e-113
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  41 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEPSErESRNVLAESARIARGKITSLAQ 120
Cdd:COG3155   1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEEMG-EKRNVLVESARIARGNIKPLAE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 121 LNAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeg 199
Cdd:COG3155  80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLgAGVKLTIGND---- 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 20070420 200 gkwpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELT 264
Cdd:COG3155 156 -----ADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKKVLELA 215
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
41-265 2.43e-109

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 314.42  E-value: 2.43e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420   41 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGEPSErESRNVLAESARIARGKITSLAQ 120
Cdd:PRK11780   2 KKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  121 LNAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHGAKKPIGLCCIAPVLAAKVI-KGVEVTVGHEqeeg 199
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILgAGVKLTIGND---- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 20070420  200 gkwpyAGTAEAIKALGAKHCVKGVTEAHVDQKNKVVTTPAFMCETALHHIHDGIGAMVKNVLELTG 265
Cdd:PRK11780 157 -----EDTAAAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVSRVLELAE 217
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 40-241 1.59e-13

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: 66.67  E-value: 1.59e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  40 GARVALVLSgcgvyDGTEIHEASAILVHLSRGGAEVQIFAPdvpqmhvidhtKGEPSERESRNVLAESARiargkitSLA 119
Cdd:COG0693   2 MKKVLILLT-----DGFEDEELTVPYDALREAGAEVDVASP-----------EGGPPVTSKHGITVTADK-------TLD 58

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 120 QLNAANHDAAIFPGGFGAAKNLstfavdgkdcKVNKEVERVLKEFHGAKKPIGLCCIAPVL--AAKVIKGVEVTVgheqe 197
Cdd:COG0693  59 DVDPDDYDALVLPGGHGAPDDL----------REDPDVVALVREFYEAGKPVAAICHGPAVlaAAGLLKGRKVTS----- 123

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|.
gi 20070420 198 eggkwpYAGTAEAIKALGAKHcvkgVTE-AHVDqkNKVVT------TPAFM 241
Cdd:COG0693 124 ------FPNIEDDLKNAGATY----VDEeVVVD--GNLITsrgpgdAPAFA 162
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 116-201 4.17e-08

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: 51.40  E-value: 4.17e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 116 TSLAQLNAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHGAKKPIGLCCIAP--VLAAKVIKGVEVTV- 192
Cdd:cd03135  51 KTLSDVNLDDYDAIVIPGGLPGAQNLAD----------NEKLIKLLKEFNAKGKLIAAICAAPavLAKAGLLKGKKATCy 120

                        90
                ....*....|
gi 20070420 193 -GHEQEEGGK 201
Cdd:cd03135 121 pGFEDKLGGA 130
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 43-218 1.42e-06

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: 47.94  E-value: 1.42e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420  43 VALVLSGCGVYDGTEIH------EASAILVHLSRGGAEVQIFAP---DVPqmhvIDHT--KGEPSERESRNVLAESARIA 111
Cdd:cd03141   1 ILIVLTSADKLGGTGRPtglwleELAHPYDVFTEAGYEVDFASPkggKVP----LDPRslDAEDDDDASVFDNDEEFKKK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 112 RGKITSLAQLNAANHDAAIFPGGFGAaknLSTFAVdgkdckvNKEVERVLKEFHGAKKPIGLCCIAPV--LAAK------ 183
Cdd:cd03141  77 LANTKKLSDVDPSDYDAIFIPGGHGP---MFDLPD-------NPDLQDLLREFYENGKVVAAVCHGPAalLNVKlsdgks 146

                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 20070420 184 VIKGVEVTVGHEQEE-----GGKWPYaGTAEAIKALGAKH 218
Cdd:cd03141 147 LVAGKTVTGFTNEEEeaaglKKVVPF-LLEDELKELGANY 185
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 116-191 1.08e-05

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: 44.46  E-value: 1.08e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20070420 116 TSLAQLNAANHDAAIFPGGFgAAKNLSTfavdgkdckvNKEVERVLKEFHGAKKPIGLCCIAP-VLA-AKVIKGVEVT 191
Cdd:cd03134  53 LTIADVDADDYDALVIPGGT-NPDKLRR----------DPDAVAFVRAFAEAGKPVAAICHGPwVLIsAGVVRGRKLT 119
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 116-191 1.18e-04

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: 41.47  E-value: 1.18e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 20070420   116 TSLAQLNAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHGAKKPIGLCCIAPVL--AAKVIKGVEVT 191
Cdd:pfam01965  52 ASLDDVKPDDYDALVLPGGRAGPERLRD----------NEKLVEFVKDFYEKGKPVAAICHGPQVlaAAGVLKGRKVT 119
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 117-242 4.00e-04

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: 40.32  E-value: 4.00e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20070420 117 SLAQLNAANHDAAIFPGGfGAAKNLSTfavdgkdckvNKEVERVLKEFHGAKKPIGLCCIAPVL--AAKVIKGVEVTVgh 194
Cdd:cd03169  68 DFDEVDPDDYDALVIPGG-RAPEYLRL----------DEKVLAIVRHFAEANKPVAAICHGPQIlaAAGVLKGRRCTA-- 134

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 20070420 195 eqeeggkwpYAGTAEAIKALGAKHcvkGVTEAHVDqkNKVVTTPAFMC 242
Cdd:cd03169 135 ---------YPACKPEVELAGGTV---VDDGVVVD--GNLVTAQAWPD 168
 
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.
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