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Conserved domains on  [gi|169154396|emb|CAQ13297|]
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es1 protein [Danio rerio]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

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
ElbB super family cl41965
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
37-268 1.31e-78

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


The actual alignment was detected with superfamily member COG3155:

Pssm-ID: 442389  Cd Length: 215  Bit Score: 236.60  E-value: 1.31e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  37 NIAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKMQPsSSDNRNMMMESARFSHGqgmmQMND 116
Cdd:COG3155    2 KVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARG----NIKP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 117 LSKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYER 195
Cdd:COG3155   77 LAELNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLGAgVKLTIGNDA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169154396 196 DessrwgrwpntnMVQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMWETDyhYHYIFDGIGNMVKHVMRMT 268
Cdd:COG3155  157 D------------TAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAAS--ISEAAEGIEKLVKKVLELA 215
 
Name Accession Description Interval E-value
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
37-268 1.31e-78

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 236.60  E-value: 1.31e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  37 NIAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKMQPsSSDNRNMMMESARFSHGqgmmQMND 116
Cdd:COG3155    2 KVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARG----NIKP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 117 LSKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYER 195
Cdd:COG3155   77 LAELNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLGAgVKLTIGNDA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169154396 196 DessrwgrwpntnMVQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMWETDyhYHYIFDGIGNMVKHVMRMT 268
Cdd:COG3155  157 D------------TAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAAS--ISEAAEGIEKLVKKVLELA 215
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 38-268 2.25e-78

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: 235.98  E-value: 2.25e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  38 IAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKmQPSSSDNRNMMMESARFSHGQgmmqMNDL 117
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLT-GEAEGESRNVLVESARIARGN----IKDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 118 SKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYERD 196
Cdd:cd03133   76 AKLKAADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILGEgVEVTIGNDAG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169154396 197 ESsrwgrwpntnmvQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMWETDyhYHYIFDGIGNMVKHVMRMT 268
Cdd:cd03133  156 TA------------AAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADS--IHEIADGIEKLVAKVLKLA 213
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
37-268 3.52e-70

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 215.42  E-value: 3.52e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  37 NIAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKMQPSSsDNRNMMMESARFSHGQgmmqMND 116
Cdd:PRK11780   3 KIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGE----IKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 117 LSKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYER 195
Cdd:PRK11780  78 LAEADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGAgVKLTIGNDE 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169154396 196 DESsrwgrwpntnmvQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMweTDYHYHYIFDGIGNMVKHVMRMT 268
Cdd:PRK11780 158 DTA------------AAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYM--LAQSIAEAASGIEKLVSRVLELA 216
 
Name Accession Description Interval E-value
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
37-268 1.31e-78

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 236.60  E-value: 1.31e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  37 NIAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKMQPsSSDNRNMMMESARFSHGqgmmQMND 116
Cdd:COG3155    2 KVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARG----NIKP 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 117 LSKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYER 195
Cdd:COG3155   77 LAELNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIGAICIAPALLAKLLGAgVKLTIGNDA 156

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169154396 196 DessrwgrwpntnMVQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMWETDyhYHYIFDGIGNMVKHVMRMT 268
Cdd:COG3155  157 D------------TAAAIEAMGGEHVECPVDEIVVDEENKVVTTPAYMLAAS--ISEAAEGIEKLVKKVLELA 215
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 38-268 2.25e-78

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: 235.98  E-value: 2.25e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  38 IAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKmQPSSSDNRNMMMESARFSHGQgmmqMNDL 117
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLT-GEAEGESRNVLVESARIARGN----IKDL 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 118 SKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYERD 196
Cdd:cd03133   76 AKLKAADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIGAICIAPALAAKILGEgVEVTIGNDAG 155

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 169154396 197 ESsrwgrwpntnmvQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMWETDyhYHYIFDGIGNMVKHVMRMT 268
Cdd:cd03133  156 TA------------AAIEKMGAEHVNCPVEEIVVDEKNKVVTTPAYMLADS--IHEIADGIEKLVAKVLKLA 213
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
37-268 3.52e-70

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 215.42  E-value: 3.52e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  37 NIAVVFSGCGWWDGTDIHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHMKMQPSSsDNRNMMMESARFSHGQgmmqMND 116
Cdd:PRK11780   3 KIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGE----IKD 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396 117 LSKLDANSFDAVIFPGGHGIVKNMSTFSKDGKDCKLNNDVERVLKDFHRARKPIGLSSMAPLLACRVLPS-LEVTMGYER 195
Cdd:PRK11780  78 LAEADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAMLPKILGAgVKLTIGNDE 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 169154396 196 DESsrwgrwpntnmvQAVKSMGARHNTREPYEAYVDEKNKVISTPTFMweTDYHYHYIFDGIGNMVKHVMRMT 268
Cdd:PRK11780 158 DTA------------AAIEKMGGEHVDCPVDDIVVDEENKVVTTPAYM--LAQSIAEAASGIEKLVSRVLELA 216
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 37-171 2.93e-06

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: 46.25  E-value: 2.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  37 NIAVVFSGcGWWDgtdiHEAAYTMYHLSRNGARFQIFAPNQQQMHVMDHM-KMQPSSSdnrnmmmesarfshgqgmmqmn 115
Cdd:COG0693    4 KVLILLTD-GFED----EELTVPYDALREAGAEVDVASPEGGPPVTSKHGiTVTADKT---------------------- 56

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 169154396 116 dLSKLDANSFDAVIFPGGHGivkNMSTFskdgkdcKLNNDVERVLKDFHRARKPIG 171
Cdd:COG0693   57 -LDDVDPDDYDALVLPGGHG---APDDL-------REDPDVVALVREFYEAGKPVA 101
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 46-171 3.34e-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: 43.70  E-value: 3.34e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  46 GWWDGtdihEAAYTMYHLSRNGARFQIFAPNQqqmhvmDHMKMQPSSSDnrnMMMESARFSHGQGMMQMNDL------SK 119
Cdd:cd03141   19 GLWLE----ELAHPYDVFTEAGYEVDFASPKG------GKVPLDPRSLD---AEDDDDASVFDNDEEFKKKLantkklSD 85

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 169154396 120 LDANSFDAVIFPGGHGIvknMSTFSKDGkdcklnnDVERVLKDFHRARKPIG 171
Cdd:cd03141   86 VDPSDYDAIFIPGGHGP---MFDLPDNP-------DLQDLLREFYENGKVVA 127
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 115-171 1.68e-03

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: 38.30  E-value: 1.68e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 169154396 115 NDLSKLDANSFDAVIFPGGHGIVKNMSTfskdgkdcklNNDVERVLKDFHRARKPIG 171
Cdd:cd03135   51 KTLSDVNLDDYDAIVIPGGLPGAQNLAD----------NEKLIKLLKEFNAKGKLIA 97
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 38-171 3.00e-03

Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153210 [Multi-domain]  Cd Length: 115  Bit Score: 36.81  E-value: 3.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 169154396  38 IAVVFSGCGWWDgtdihEAAYTMYHLSRNGARFQIFAPNQQQMHvmdhmkmqpsssdnrnmmmesarfshgqgmmqmndl 117
Cdd:cd01653    1 VAVLLFPGFEEL-----ELASPLDALREAGAEVDVVSPDGGPVE------------------------------------ 39

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 169154396 118 SKLDANSFDAVIFPGGHGIVKNMstfskdgkdcKLNNDVERVLKDFHRARKPIG 171
Cdd:cd01653   40 SDVDLDDYDGLILPGGPGTPDDL----------ARDEALLALLREAAAAGKPIL 83
 
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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