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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLRNLP----DAEVRFVWHEPGPVTADSGVLmVGATHTFDETPSPDVVLVPGGPGSSAAAR 78
Cdd:cd03139     1 VGILLFPGVEVLDVIGPYEVFGRAPrlaaPFEVFLVSETGGPVSSRSGLT-VLPDTSFADPPDLDVLLVPGGGGTRALVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  79 DERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSALKMCGVTAVSDERIVRaDDKVITAAGVSAGID 158
Cdd:cd03139    80 DPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDARWVV-DGNIWTSGGVSAGID 158

                         170       180
                  ....*....|....*....|....*
gi 1583645910 159 LGMWLAGQIAGEAKAKAIQLLIEYD 183
Cdd:cd03139   159 MALALVARLFGEELAQAVALLIEYD 183

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLRNLP----DAEVRFVWHEPGPVTADSGVLmVGATHTFDETPSPDVVLVPGGPGSSAAAR 78
Cdd:cd03139     1 VGILLFPGVEVLDVIGPYEVFGRAPrlaaPFEVFLVSETGGPVSSRSGLT-VLPDTSFADPPDLDVLLVPGGGGTRALVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  79 DERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSALKMCGVTAVSDERIVRaDDKVITAAGVSAGID 158
Cdd:cd03139    80 DPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDARWVV-DGNIWTSGGVSAGID 158

                         170       180
                  ....*....|....*....|....*
gi 1583645910 159 LGMWLAGQIAGEAKAKAIQLLIEYD 183
Cdd:cd03139   159 MALALVARLFGEELAQAVALLIEYD 183

DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in transcriptional regulators.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   1 MQIAVVLYPTFTALDFIGPYEVLRNLpDAEVRFVWHEPGPVTADSGVLMVgATHTFDE--TPSPDVVLVPGG-PGSSAAA 77
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRA-GIKVTVVSVDGGEVKGSRGVKVT-VDASLDDvkPDDYDALVLPGGrAGPERLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  78 RDERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSALKMCGVTaVSDERIVRaDDKVITAAGVSAGI 157
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGAT-YVDKPVVV-DGNLVTSRGPGDAP 156

                  ...
gi 1583645910 158 DLG 160
Cdd:pfam01965 157 EFA 159

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLRNLP----DAEVRFVWHEPGPVTADSGVLmVGATHTFDETPSPDVVLVPGGPGSSAAAR 78
Cdd:cd03139     1 VGILLFPGVEVLDVIGPYEVFGRAPrlaaPFEVFLVSETGGPVSSRSGLT-VLPDTSFADPPDLDVLLVPGGGGTRALVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  79 DERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSALKMCGVTAVSDERIVRaDDKVITAAGVSAGID 158
Cdd:cd03139    80 DPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDARWVV-DGNIWTSGGVSAGID 158

                         170       180
                  ....*....|....*....|....*
gi 1583645910 159 LGMWLAGQIAGEAKAKAIQLLIEYD 183
Cdd:cd03139   159 MALALVARLFGEELAQAVALLIEYD 183

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLR------NLPDAEVRFVWHEPGPVTADSGvLMVGATHTFDETPSPDVVLVPGGPGSSAA 76
Cdd:cd03137     1 VAVLVFPGVSLLDLSGPAEVFGeanralGPPAYELRVCSPEGGPVRSSSG-LSLVADAGLDALAAADTVIVPGGPDVDGR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  77 ARDERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSAL-KMCGVTAVSDERIVRADDKVITAAGVSA 155
Cdd:cd03137    80 PPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLaRRFPAVRVDPDVLYVDDGNVWTSAGVTA 159

                         170       180
                  ....*....|....*....|.
gi 1583645910 156 GIDLGMWLAGQIAGEAKAKAI 176
Cdd:cd03137   160 GIDLCLHLVREDLGAAVANRV 180

AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain; A subgroup of AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to the Pseudomonas aeruginosa ArgR regulator. ArgR functions in the control of expression of certain genes of arginine biosynthesis and catabolism. 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 some sequences in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLR--NLPDAEVRFVWH----EPGPVTADSGVLmVGATHTFDETPSPDVVLVPGGPGSSAA 76
Cdd:cd03136     1 FGFLLLPGFSLLALASAIEPLRaaNRLAGRELYRWRvlslDGAPVTSSNGLR-VAPDAALEDAPPLDYLFVVGGLGARRA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  77 ArDERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSALK--MCGVTaVSDERIVRaDDKVITAAGVS 154
Cdd:cd03136    80 V-TPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAeaFPRVQ-VTRDLFEI-DGDRLTCAGGT 156

                         170       180
                  ....*....|....*....|..
gi 1583645910 155 AGIDLGMWLAGQIAGEAKAKAI 176
Cdd:cd03136   157 AALDLMLELIARDHGAALAARV 178

Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins and nucleic acids) [Defense mechanisms];

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   1 MQIAVVLYPTFTALDFIGPYEVLRNLpDAEVRFVWHEPG-PVTADSGVLMVgATHTFDETpSP---DVVLVPGGPGSSAA 76
Cdd:COG0693     3 KKVLILLTDGFEDEELTVPYDALREA-GAEVDVASPEGGpPVTSKHGITVT-ADKTLDDV-DPddyDALVLPGGHGAPDD 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1583645910  77 -ARDERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSALKMCGVTaVSDERIVRaDDKVITAAG 152
Cdd:COG0693    80 lREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGAT-YVDEEVVV-DGNLITSRG 154

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLRNLpDAEVRFVWHEPGPVTADSGVLMVGATHTFDETPSP--DVVLVPGG-PGSSAAARD 79
Cdd:cd03135     1 VLVILADGFEEIEAVTPVDVLRRA-GIEVTTASLEKKLAVGSSHGIKVKADKTLSDVNLDdyDAIVIPGGlPGAQNLADN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910  80 ERVLAWLRAVHPTANWVASVCSGSMVLAAAGLLDGKRATSHWGALSalKMCGVTaVSDERIVRaDDKVITAAGVSAGIDL 159
Cdd:cd03135    80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFED--KLGGAN-YVDEPVVV-DGNIITSRGPGTAFEF 155

                  .
gi 1583645910 160 G 160
Cdd:cd03135   156 A 156

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLRNLPdAEVRFVWHEPGPVTADsgvlmvgathtfDETPSPDVVLVPGGPGSS-AAARDER 81
Cdd:cd01653     1 VAVLLFPGFEELELASPLDALREAG-AEVDVVSPDGGPVESD------------VDLDDYDGLILPGGPGTPdDLARDEA 67

                          90       100
                  ....*....|....*....|....*
gi 1583645910  82 VLAWLRAVHPTANWVASVCSGSMVL 106
Cdd:cd01653    68 LLALLREAAAAGKPILGICLGAQLL 92

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.

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1583645910   3 IAVVLYPTFTALDFIGPYEVLRNLPdAEVRFVWHEPGPVTADsgvlmvgathtfDETPSPDVVLVPGGPGSS-AAARDER 81
Cdd:cd03128     1 VAVLLFGGSEELELASPLDALREAG-AEVDVVSPDGGPVESD------------VDLDDYDGLILPGGPGTPdDLAWDEA 67

                          90       100
                  ....*....|....*....|....*
gi 1583645910  82 VLAWLRAVHPTANWVASVCSGSMVL 106
Cdd:cd03128    68 LLALLREAAAAGKPVLGICLGAQLL 92