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Conserved domains on  [gi|2714137642|ref|WP_340834503|]
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DJ-1/PfpI family protein [Acinetobacter variabilis]

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 ...
4-169 7.11e-55

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 cd03134:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 165  Bit Score: 170.80  E-value: 7.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   4 RIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVHGQHGQSSVTIDRGIDHISIDDFDALLIPGGESPVSLANV 83
Cdd:cd03134     1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  84 MRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDLPIFI 163
Cdd:cd03134    81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN-LITSRNPDDLPAFN 159

                  ....*.
gi 2714137642 164 HECLDV 169
Cdd:cd03134   160 RAILKA 165
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
4-169 7.11e-55

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: 170.80  E-value: 7.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   4 RIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVHGQHGQSSVTIDRGIDHISIDDFDALLIPGGESPVSLANV 83
Cdd:cd03134     1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  84 MRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDLPIFI 163
Cdd:cd03134    81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN-LITSRNPDDLPAFN 159

                  ....*.
gi 2714137642 164 HECLDV 169
Cdd:cd03134   160 RAILKA 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
1-171 9.79e-43

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: 139.85  E-value: 9.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   1 MPKRIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVHGQHGQsSVTIDRGIDHISIDDFDALLIPGG-ESPVS 79
Cdd:COG0693     1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGI-TVTADKTLDDVDPDDYDALVLPGGhGAPDD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  80 LANVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDL 159
Cdd:COG0693    80 LREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGN-LITSRGPGDA 158
                         170
                  ....*....|..
gi 2714137642 160 PIFIHECLDVLK 171
Cdd:COG0693   159 PAFARALLELLA 170
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
5-171 9.36e-41

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 134.85  E-value: 9.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVhGQHGqSSVTIDRGIDHISIDDFDALLIPGGESPVSLANVM 84
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTV-GKHG-YSVTVDATIDEVNPEEYDALVIPGGRAPEYLRLNN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  85 RVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNQLISSRVPNDLPIFIH 164
Cdd:TIGR01382  80 KAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGNLVTSRVPDDLPAFNR 159

                  ....*..
gi 2714137642 165 ECLDVLK 171
Cdd:TIGR01382 160 EFLKLLG 166
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
3-171 1.59e-35

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: 121.59  E-value: 1.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   3 KRIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVhGQHGqSSVTIDRGIDHISIDDFDALLIPGGES-PVSLA 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGEVK-GSRG-VKVTVDASLDDVKPDDYDALVLPGGRAgPERLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  82 NVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDLPI 161
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGN-LVTSRGPGDAPE 157
                         170
                  ....*....|
gi 2714137642 162 FiheCLDVLK 171
Cdd:pfam01965 158 F---ALEILE 164
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
4-169 7.11e-55

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: 170.80  E-value: 7.11e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   4 RIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVHGQHGQSSVTIDRGIDHISIDDFDALLIPGGESPVSLANV 83
Cdd:cd03134     1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  84 MRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDLPIFI 163
Cdd:cd03134    81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN-LITSRNPDDLPAFN 159

                  ....*.
gi 2714137642 164 HECLDV 169
Cdd:cd03134   160 RAILKA 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
1-171 9.79e-43

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: 139.85  E-value: 9.79e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   1 MPKRIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVHGQHGQsSVTIDRGIDHISIDDFDALLIPGG-ESPVS 79
Cdd:COG0693     1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGI-TVTADKTLDDVDPDDYDALVLPGGhGAPDD 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  80 LANVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDL 159
Cdd:COG0693    80 LREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGN-LITSRGPGDA 158
                         170
                  ....*....|..
gi 2714137642 160 PIFIHECLDVLK 171
Cdd:COG0693   159 PAFARALLELLA 170
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
5-171 9.36e-41

intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has been solved to 2 Angstrom resolution. It is an ATP-independent intracellular protease that crystallizes as a hexameric ring. Cys-101 is proposed as the active site residue in a catalytic triad with the adjacent His-102 and a Glu residue from an adjacent monomer. A member of this family from Bacillus subtilis, GSP18, has been shown to be expressed in response to several forms of stress. A role in the degradation of small peptides has been suggested. A closely related family consists of the thiamine biosynthesis protein ThiJ and its homologs. [Protein fate, Degradation of proteins, peptides, and glycopeptides]


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 134.85  E-value: 9.36e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVhGQHGqSSVTIDRGIDHISIDDFDALLIPGGESPVSLANVM 84
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTV-GKHG-YSVTVDATIDEVNPEEYDALVIPGGRAPEYLRLNN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  85 RVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNQLISSRVPNDLPIFIH 164
Cdd:TIGR01382  80 KAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGNLVTSRVPDDLPAFNR 159

                  ....*..
gi 2714137642 165 ECLDVLK 171
Cdd:TIGR01382 160 EFLKLLG 166
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
3-171 1.59e-35

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: 121.59  E-value: 1.59e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   3 KRIAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVhGQHGqSSVTIDRGIDHISIDDFDALLIPGGES-PVSLA 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGEVK-GSRG-VKVTVDASLDDVKPDDYDALVLPGGRAgPERLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  82 NVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSRVPNDLPI 161
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGN-LVTSRGPGDAPE 157
                         170
                  ....*....|
gi 2714137642 162 FiheCLDVLK 171
Cdd:pfam01965 158 F---ALEILE 164
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
14-170 1.82e-23

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: 90.79  E-value: 1.82e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  14 EDLEYTEPVAALLAAEHSVcnielHA--------GKVVHGQHG----QSSV-------TIDRGIDHISIDDFDALLIPGG 74
Cdd:cd03169    11 EDYEVMVPFQALQEVGHEV-----DVvapgkkkgDTVVTAIHDfpgwQTYTekpghrfAVTADFDEVDPDDYDALVIPGG 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  75 ESPVSLANVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNqLISSR 154
Cdd:cd03169    86 RAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDDGVVVDGN-LVTAQ 164
                         170
                  ....*....|....*.
gi 2714137642 155 VPNDLPIFIHECLDVL 170
Cdd:cd03169   165 AWPDHPAFLREFLKLL 180
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
5-156 5.28e-22

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: 86.84  E-value: 5.28e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELHAGKVVHGQHGqSSVTIDRGIDHISIDDFDALLIPGG-ESPVSLANV 83
Cdd:cd03135     1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHG-IKVKADKTLSDVNLDDYDAIVIPGGlPGAQNLADN 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2714137642  84 MRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSirAHAPRVQHAGATYYDVELVNDNNqLISSRVP 156
Cdd:cd03135    80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATC--YPGFEDKLGGANYVDEPVVVDGN-IITSRGP 149
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
5-153 3.36e-11

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: 58.71  E-value: 3.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEHSVCNIELH----AGKVVHGQHGqSSVTIDRGIDHIsiDDFDALLIPGGESPVSL 80
Cdd:cd03139     1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFlvseTGGPVSSRSG-LTVLPDTSFADP--PDLDVLLVPGGGGTRAL 77
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2714137642  81 ANVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVQHAGATYYDVELVNDNNQLISS 153
Cdd:cd03139    78 VNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDARWVVDGNIWTS 150
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
51-152 1.18e-10

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: 153234 [Multi-domain]  Cd Length: 170  Bit Score: 56.85  E-value: 1.18e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642  51 SVTIDRGIDHISIDDFDALLIPGGESPVSLANvMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITS-----IR 125
Cdd:cd03140    46 RVVPDYSLDDLPPEDYDLLILPGGDSWDNPEA-PDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSnsldfLK 124
                          90       100
                  ....*....|....*....|....*...
gi 2714137642 126 AHAPrvQHAGATYYDVEL-VNDNNqLIS 152
Cdd:cd03140   125 AHAP--YYGGAEYYDEPQaVSDGN-LIT 149
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
4-156 2.61e-09

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: 53.47  E-value: 2.61e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   4 RIAVLVTNNFEDLEYTEPVAALLAAEHSV--CNIELHAGKVVHGQHGqSSVTIDRGIDHISIDDFDALLIPGG-ESPVSL 80
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVtvAIAGLNGKLAVKGSRG-VKILADASLEDVDLEKFDVIVLPGGmPGAENL 79
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2714137642  81 ANVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITSIRAHAPRVqhAGATYYDVELVNDNNQLISSRVP 156
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKL--LNGNYSVNKTVVVDGNLITSRGP 153
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
5-110 4.40e-09

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: 51.83  E-value: 4.40e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEHSVcnielhagKVVHGQHGQSSVTIDrgidhisIDDFDALLIPGGESPVS-LANV 83
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALREAGAEV--------DVVSPDGGPVESDVD-------LDDYDGLILPGGPGTPDdLARD 65
                          90       100
                  ....*....|....*....|....*..
gi 2714137642  84 MRVLHFIQAFNEAKKTIFSLCDASLLL 110
Cdd:cd01653    66 EALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
5-110 5.20e-08

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.


Pssm-ID: 153222 [Multi-domain]  Cd Length: 92  Bit Score: 48.35  E-value: 5.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEHSVcnielhagKVVHGQHGQSSVTIDrgidhisIDDFDALLIPGGESPVS-LANV 83
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALREAGAEV--------DVVSPDGGPVESDVD-------LDDYDGLILPGGPGTPDdLAWD 65
                          90       100
                  ....*....|....*....|....*..
gi 2714137642  84 MRVLHFIQAFNEAKKTIFSLCDASLLL 110
Cdd:cd03128    66 EALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
5-132 1.87e-05

AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like domain. AraC regulators are defined by a AraC-type helix-turn-helix DNA binding domain at their C-terminal. AraC family transcriptional regulators are widespread among bacteria and are involved in regulating diverse and important biological functions, including carbon metabolism, stress responses and virulence in different microorganisms. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with typical GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 42.87  E-value: 1.87e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2714137642   5 IAVLVTNNFEDLEYTEPVAALLAAEH---------SVCNIElhaGKVVHGQHGqssVTIDRGIDHISIDDFDALLIPGGE 75
Cdd:cd03137     1 VAVLVFPGVSLLDLSGPAEVFGEANRalgppayelRVCSPE---GGPVRSSSG---LSLVADAGLDALAAADTVIVPGGP 74
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2714137642  76 SPVSLANVMRVLHFIQAFNEAKKTIFSLCDASLLLSEADVLKNRIITS-------IRAHAPRVQ 132
Cdd:cd03137    75 DVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATThwayaedLARRFPAVR 138
GATase1_PB cd01749
Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine ...
57-111 6.11e-03

Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis; Glutamine Amidotransferase (GATase_I) involved in pyridoxine biosynthesis. Glutamine amidotransferase (GATase) activity involves the removal of the ammonia group from a glutamate molecule and its subsequent transfer to a specific substrate, thus creating a new carbon-nitrogen group on the substrate. This group contains proteins like Bacillus subtilus YaaE and Plasmodium falciparum Pdx2 which are members of the triad glutamine aminotransferase family and function in a pathway for the biosynthesis of vitamin B6.


Pssm-ID: 153220 [Multi-domain]  Cd Length: 183  Bit Score: 35.58  E-value: 6.11e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2714137642  57 GIDHISI------DDFDALLIPGGESPVsLANVMR---VLHFIQAFNEAKKTIFSLCDASLLLS 111
Cdd:cd01749    21 GVEVIEVrtpedlEGIDGLIIPGGESTT-IGKLLRrtgLLDPLREFIRAGKPVFGTCAGLILLA 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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