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Conserved domains on  [gi|999809129|ref|NP_001307312|]
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glutamine amidotransferase-like class 1 domain-containing protein 3, mitochondrial isoform 3 precursor [Homo sapiens]

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];
43-174 1.35e-81

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


The actual alignment was detected with superfamily member COG3155:

Pssm-ID: 442389  Cd Length: 215  Bit Score: 243.53  E-value: 1.35e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPsEGESRNVLTESARIARGKITDLAN 122
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 999809129 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:COG3155   80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIG 131
 
Name Accession Description Interval E-value
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
43-174 1.35e-81

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 243.53  E-value: 1.35e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPsEGESRNVLTESARIARGKITDLAN 122
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 999809129 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:COG3155   80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIG 131
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 45-174 2.01e-81

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: 242.91  E-value: 2.01e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  45 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLS 124
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 999809129 125 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:cd03133   80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIG 129
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
43-174 1.50e-78

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 235.84  E-value: 1.50e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPSEgESRNVLTESARIARGKITDLAN 122
Cdd:PRK11780   2 KKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 999809129 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIG 132
 
Name Accession Description Interval E-value
ElbB COG3155
Glyoxalase ElbB, DJ-1 superfamily [Defense mechanisms];
43-174 1.35e-81

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


Pssm-ID: 442389  Cd Length: 215  Bit Score: 243.53  E-value: 1.35e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPsEGESRNVLTESARIARGKITDLAN 122
Cdd:COG3155    1 KKVAVILSGCGVYDGSEIHEAVLTLLALDRAGAEYQCFAPDIEQHHVINHLTGEE-MGEKRNVLVESARIARGNIKPLAE 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 999809129 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:COG3155   80 LNAEDFDALILPGGFGAAKNLSDFAFKGADCTVNPDVLRLVRAFHEAGKPIG 131
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 45-174 2.01e-81

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: 242.91  E-value: 2.01e-81
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  45 VALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQpSEGESRNVLTESARIARGKITDLANLS 124
Cdd:cd03133    1 VAVVLSGCGVYDGSEIHEAVLTLLALDRAGAEVQCFAPDIEQMHVVNHLTGE-AEGESRNVLVESARIARGNIKDLAKLK 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 999809129 125 AANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:cd03133   80 AADFDALIFPGGFGAAKNLSDFAVKGADCTVNPEVERLVREFHQAGKPIG 129
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
43-174 1.50e-78

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 235.84  E-value: 1.50e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  43 ARVALVLSGCGVYDGTEIHEASAILVHLSRGGAEVQIFAPDVPQMHVIDHTKGQPSEgESRNVLTESARIARGKITDLAN 122
Cdd:PRK11780   2 KKIAVILSGCGVYDGSEIHEAVLTLLALDRAGAEAVCFAPDIPQLHVINHLTGEEMG-ETRNVLVESARIARGEIKDLAE 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 999809129 123 LSAANHDAAIFPGGFGAAKNLSTFAVDGKDCKVNKEVERVLKEFHQAGKPIG 174
Cdd:PRK11780  81 ADAEDFDALIVPGGFGAAKNLSNFAVKGAECTVNPDVKALVRAFHQAGKPIG 132
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 42-174 6.43e-10

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: 56.65  E-value: 6.43e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  42 AARVALVLSgcgvyDGTEIHEASAILVHLSRGGAEVQIFAPDvpqmhvidhtKGQPSEGESRNVLTESAriargkitDLA 121
Cdd:COG0693    2 MKKVLILLT-----DGFEDEELTVPYDALREAGAEVDVASPE----------GGPPVTSKHGITVTADK--------TLD 58

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 999809129 122 NLSAANHDAAIFPGGFGAAKNLstfavdgkdcKVNKEVERVLKEFHQAGKPIG 174
Cdd:COG0693   59 DVDPDDYDALVLPGGHGAPDDL----------REDPDVVALVREFYEAGKPVA 101
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 54-174 6.19e-05

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: 42.16  E-value: 6.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 999809129  54 VYDGTEIHEASAILVHLSRGGAEVQIFApdvpqmhvidhTKGQPSEGESRNVltesariargKITDLANLSAANH---DA 130
Cdd:cd03135    5 LADGFEEIEAVTPVDVLRRAGIEVTTAS-----------LEKKLAVGSSHGI----------KVKADKTLSDVNLddyDA 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 999809129 131 AIFPGGFGAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIG 174
Cdd:cd03135   64 IVIPGGLPGAQNLAD----------NEKLIKLLKEFNAKGKLIA 97
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 120-174 6.35e-03

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: 36.37  E-value: 6.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 999809129 120 LANLSAANHDAAIFPGGFgAAKNLSTfavdgkdckvNKEVERVLKEFHQAGKPIG 174
Cdd:cd03134   55 IADVDADDYDALVIPGGT-NPDKLRR----------DPDAVAFVRAFAEAGKPVA 98
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 120-174 8.69e-03

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: 36.38  E-value: 8.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 999809129 120 LANLSAANHDAAIFPGGFGAaknLSTFAVdgkdckvNKEVERVLKEFHQAGKPIG 174
Cdd:cd03141   83 LSDVDPSDYDAIFIPGGHGP---MFDLPD-------NPDLQDLLREFYENGKVVA 127
 
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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