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Conserved domains on  [gi|999809125|ref|NP_004640|]
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glutamine amidotransferase-like class 1 domain-containing protein 3, mitochondrial isoform 1 precursor [Homo sapiens]

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 ...
 45-266 9.12e-123

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: 348.46  E-value: 9.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  45 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLS 124
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 125 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggk 203
Cdd:cd03133   80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILgEGVEVTIGND------ 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 999809125 204 wpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELT 266
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 ...
 45-266 9.12e-123

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: 348.46  E-value: 9.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  45 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLS 124
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 125 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggk 203
Cdd:cd03133   80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILgEGVEVTIGND------ 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 999809125 204 wpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELT 266
Cdd:cd03133  154 ---AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
43-266 4.57e-113

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 324.04  E-value: 4.57e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPsEGESRNVLTESARIARGKITDLAN 122
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeg 201
Cdd:COG3155   80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLgAGVKLTIGND---- 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 999809125 202 gkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELT 266
Cdd:COG3155  156 -----ADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKKVLELA 215
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
43-267 2.20e-109

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 314.80  E-value: 2.20e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPSEgESRNVLTESARIARGKITDLAN 122
Cdd:PRK11780   2 KKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVLR-GVEVTVGHEqeeg 201
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGaGVKLTIGND---- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 999809125 202 gkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELTG 267
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 ...
 120-193 8.69e-05

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: 41.86  E-value: 8.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 999809125  120 LANLSAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVT 193
Cdd:pfam01965  54 LDDVKPDDYDALVLPGGRAGPERLRD----------NEKLVEFVKDFYEKGKPVAAICHGPQVlaAAGVLKGRKVT 119
 
Name Accession Description Interval E-value
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 45-266 9.12e-123

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: 348.46  E-value: 9.12e-123
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  45 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLS 124
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 125 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeggk 203
Cdd:cd03133   80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILgEGVEVTIGND------ 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 999809125 204 wpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELT 266
Cdd:cd03133  154 ---AGTAAAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADSIHEIADGIEKLVAKVLKLA 213
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
43-266 4.57e-113

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 324.04  E-value: 4.57e-113
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPsEGESRNVLTESARIARGKITDLAN 122
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAE 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVL-RGVEVTVGHEqeeg 201
Cdd:COG3155   80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLgAGVKLTIGND---- 155

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 999809125 202 gkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELT 266
Cdd:COG3155  156 -----ADTAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAASISEAAEGIEKLVKKVLELA 215
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
43-267 2.20e-109

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 314.80  E-value: 2.20e-109
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPSEgESRNVLTESARIARGKITDLAN 122
Cdd:PRK11780   2 KKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIGLCCIAPVLAAKVLR-GVEVTVGHEqeeg 201
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGaGVKLTIGND---- 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 999809125 202 gkwpyAGTAEAIKALGAKHCVKEVVEAHVDQKNKVVTTPAFMCETALHYIHDGIGAMVRKVLELTG 267
Cdd:PRK11780 157 -----EDTAAAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYMLAQSIAEAASGIEKLVSRVLELAE 217
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 42-243 4.28e-15

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: 70.90  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  42 AARVALVLSgcgvyDGTEIHEASAILVHLSRGGAEVQIFAPDvpqmhvidhtKGQPSEGESRNVLTESAriargkitDLA 121
Cdd:COG0693    2 MKKVLILLT-----DGFEDEELTVPYDALREAGAEVDVASPE----------GGPPVTSKHGITVTADK--------TLD 58

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 122 NLSAANHDAAIFPGGFGAAKNLstfavdgkdcKVNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVTVgheqe 199
Cdd:COG0693   59 DVDPDDYDALVLPGGHGAPDDL----------REDPDVVALVREFYEAGKPVAAICHGPAVlaAAGLLKGRKVTS----- 123

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 999809125 200 eggkwpYAGTAEAIKALGAKHCVKEVVeahVDqkNKVVT------TPAFM 243
Cdd:COG0693  124 ------FPNIEDDLKNAGATYVDEEVV---VD--GNLITsrgpgdAPAFA 162
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 54-238 2.32e-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: 52.17  E-value: 2.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125  54 VYDGTEIHEASAILVHLSRGGAEVQIFApdvpqmhvidhTKGQPSEGESRNVltesariargKITDLANLSAANH---DA 130
Cdd:cd03135    5 LADGFEEIEAVTPVDVLRRAGIEVTTAS-----------LEKKLAVGSSHGI----------KVKADKTLSDVNLddyDA 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 131 AIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAP--VLAAKVLRGVEVTVGHEQEEggkwpyag 208
Cdd:cd03135   64 IVIPGGLPGAQNLAD----------NEKLIKLLKEFNAKGKLIAAICAAPavLAKAGLLKGKKATCYPGFED-------- 125

                        170       180       190
                 ....*....|....*....|....*....|
gi 999809125 209 taeaiKALGAKHCVKEVVeahVDqkNKVVT 238
Cdd:cd03135  126 -----KLGGANYVDEPVV---VD--GNIIT 145
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 120-243 3.61e-06

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: 46.00  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 120 LANLSAANHDAAIFPGGFgAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAP-VLA-AKVLRGVEVTvghe 197
Cdd:cd03134   55 IADVDADDYDALVIPGGT-NPDKLRR----------DPDAVAFVRAFAEAGKPVAAICHGPwVLIsAGVVRGRKLT---- 119

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 999809125 198 qeeggkwPYAGTAEAIKALGAKHCVKEVVeahVDqkNKVVTT------PAFM 243
Cdd:cd03134  120 -------SYPSIKDDLINAGANWVDEEVV---VD--GNLITSrnpddlPAFN 159
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 120-230 1.13e-05

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: 45.24  E-value: 1.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 120 LANLSAANHDAAIFPGGFGAaknLSTFAVdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPV--LAAK------VLRGVE 191
Cdd:cd03141   83 LSDVDPSDYDAIFIPGGHGP---MFDLPD-------NPDLQDLLREFYENGKVVAAVCHGPAalLNVKlsdgksLVAGKT 152

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 999809125 192 VTVGHEQEE-----GGKWPYaGTAEAIKALGAKHCVKEVVEAHV 230
Cdd:cd03141  153 VTGFTNEEEeaaglKKVVPF-LLEDELKELGANYVKAEPWAEFV 195
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 119-244 3.32e-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: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 43.41  E-value: 3.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809125 119 DLANLSAANHDAAIFPGGfGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVTVgh 196
Cdd:cd03169   68 DFDEVDPDDYDALVIPGG-RAPEYLRL----------DEKVLAIVRHFAEANKPVAAICHGPQIlaAAGVLKGRRCTA-- 134

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 999809125 197 eqeeggkwpYAGTAEAIKALGAkhcvkEVVEAHVDQKNKVVTTPAFMC 244
Cdd:cd03169  135 ---------YPACKPEVELAGG-----TVVDDGVVVDGNLVTAQAWPD 168
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 120-193 8.69e-05

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: 41.86  E-value: 8.69e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 999809125  120 LANLSAANHDAAIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIGLCCIAPVL--AAKVLRGVEVT 193
Cdd:pfam01965  54 LDDVKPDDYDALVLPGGRAGPERLRD----------NEKLVEFVKDFYEKGKPVAAICHGPQVlaAAGVLKGRKVT 119
 
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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