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Conserved domains on  [gi|1907156746|ref|XP_036020176|]
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Parkinson disease protein 7 homolog isoform X1 [Mus musculus]

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
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 51-128 8.93e-29

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.


The actual alignment was detected with superfamily member TIGR01383:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 179  Bit Score: 103.17  E-value: 8.93e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156746  51 ACPTALLAHEVGFGCKVTTHPLAKDKMMNGsHYSySESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAP 128
Cdd:TIGR01383 104 AAPAVLLAHGVLLGKKATCYPGFKEKLLNG-NYS-VNKTVVVDGNLITSRGPGTAIEFALELVELLAGKEKAQEVAAG 179
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 51-128 8.93e-29

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: 103.17  E-value: 8.93e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156746  51 ACPTALLAHEVGFGCKVTTHPLAKDKMMNGsHYSySESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAP 128
Cdd:TIGR01383 104 AAPAVLLAHGVLLGKKATCYPGFKEKLLNG-NYS-VNKTVVVDGNLITSRGPGTAIEFALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 51-116 2.58e-20

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: 81.06  E-value: 2.58e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156746  51 ACPTALLAHEVGFGCKVTTHPLAKDKMMNGShysYSESRVEKDGLILTSRGPGTSFEFALAIVEAL 116
Cdd:cd03135   101 AAPAVLAKAGLLKGKKATCYPGFEDKLGGAN---YVDEPVVVDGNIITSRGPGTAFEFALKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 53-115 4.79e-20

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: 80.38  E-value: 4.79e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156746  53 PTALLAHEVGFGCKVTTHPLAKDKMMNGsHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEA 115
Cdd:pfam01965 104 PQVLAAAGVLKGRKVTSHPAVKDDLINA-GATYVDKPVVVDGNLVTSRGPGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 53-116 4.02e-11

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: 57.04  E-value: 4.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156746  53 PTALLAHEVGFGCKVTTHPLAKDKMMN-GSHYSysESRVEKDGLILTSRGPGTSFEFALAIVEAL 116
Cdd:COG0693   107 PAVLAAAGLLKGRKVTSFPNIEDDLKNaGATYV--DEEVVVDGNLITSRGPGDAPAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
37-131 1.24e-08

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 50.93  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156746  37 REAFLRGEKEACSEACPTALLAHEVGFGC-KVTTHPLAKDKMmngSHYSYSESRVEKDGLI--LTSRGPGTSFEFALAIV 113
Cdd:PRK11574   93 RQFHRSGRIVAAICAAPATVLVPHDLFPIgNMTGFPTLKDKI---PAEQWQDKRVVWDARVnlLTSQGPGTAIDFALKII 169

                          90
                  ....*....|....*...
gi 1907156746 114 EALVGKDMANQVKAPLVL 131
Cdd:PRK11574  170 DLLVGREKAHEVASQLVM 187
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 51-128 8.93e-29

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: 103.17  E-value: 8.93e-29
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907156746  51 ACPTALLAHEVGFGCKVTTHPLAKDKMMNGsHYSySESRVEKDGLILTSRGPGTSFEFALAIVEALVGKDMANQVKAP 128
Cdd:TIGR01383 104 AAPAVLLAHGVLLGKKATCYPGFKEKLLNG-NYS-VNKTVVVDGNLITSRGPGTAIEFALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 51-116 2.58e-20

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: 81.06  E-value: 2.58e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907156746  51 ACPTALLAHEVGFGCKVTTHPLAKDKMMNGShysYSESRVEKDGLILTSRGPGTSFEFALAIVEAL 116
Cdd:cd03135   101 AAPAVLAKAGLLKGKKATCYPGFEDKLGGAN---YVDEPVVVDGNIITSRGPGTAFEFALKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 53-115 4.79e-20

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: 80.38  E-value: 4.79e-20
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907156746  53 PTALLAHEVGFGCKVTTHPLAKDKMMNGsHYSYSESRVEKDGLILTSRGPGTSFEFALAIVEA 115
Cdd:pfam01965 104 PQVLAAAGVLKGRKVTSHPAVKDDLINA-GATYVDKPVVVDGNLVTSRGPGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 53-116 4.02e-11

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: 57.04  E-value: 4.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907156746  53 PTALLAHEVGFGCKVTTHPLAKDKMMN-GSHYSysESRVEKDGLILTSRGPGTSFEFALAIVEAL 116
Cdd:COG0693   107 PAVLAAAGLLKGRKVTSFPNIEDDLKNaGATYV--DEEVVVDGNLITSRGPGDAPAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
37-131 1.24e-08

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 50.93  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907156746  37 REAFLRGEKEACSEACPTALLAHEVGFGC-KVTTHPLAKDKMmngSHYSYSESRVEKDGLI--LTSRGPGTSFEFALAIV 113
Cdd:PRK11574   93 RQFHRSGRIVAAICAAPATVLVPHDLFPIgNMTGFPTLKDKI---PAEQWQDKRVVWDARVnlLTSQGPGTAIDFALKII 169

                          90
                  ....*....|....*...
gi 1907156746 114 EALVGKDMANQVKAPLVL 131
Cdd:PRK11574  170 DLLVGREKAHEVASQLVM 187
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 52-125 8.27e-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: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 40.22  E-value: 8.27e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907156746  52 CPTALLAHEVGF--GCKVTTHPLAKDKM-MNGSHYSYSESRVEkDGLILTSRGPGTSFEFALAIVEALVGKDMANQV 125
Cdd:cd03139   101 CTGALLLAAAGLldGRRATTHWAAIDWLkEFGAIVVVDARWVV-DGNIWTSGGVSAGIDMALALVARLFGEELAQAV 176
 
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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