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 18404881  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRCVMSAHDFLGLE---------LTLNANFDDVTPENYDVIII 80
Cdd:cd03169   3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQtytekpghrFAVTADFDEVDPDDYDALVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881  81 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILaGGVKCTAFESIKPLIELSGGEWwqqpgiqsmfEI 160
Cdd:cd03169  83 PGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVL-KGRRCTAYPACKPEVELAGGTV----------VD 151

                       170       180
                ....*....|....*....|....*....
gi 18404881 161 TDCVKDGNFMSTVGWPTLGHGIKLLLESL 189
Cdd:cd03169 152 DGVVVDGNLVTAQAWPDHPAFLREFLKLL 180

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 18404881  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRCVMSAHDFLGLE---------LTLNANFDDVTPENYDVIII 80
Cdd:cd03169   3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQtytekpghrFAVTADFDEVDPDDYDALVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881  81 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILaGGVKCTAFESIKPLIELSGGEWwqqpgiqsmfEI 160
Cdd:cd03169  83 PGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVL-KGRRCTAYPACKPEVELAGGTV----------VD 151

                       170       180
                ....*....|....*....|....*....
gi 18404881 161 TDCVKDGNFMSTVGWPTLGHGIKLLLESL 189
Cdd:cd03169 152 DGVVVDGNLVTAQAWPDHPAFLREFLKLL 180

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881   203 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTpnKKKGEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYDCV 282
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTT---------------VGKHGYSVTVDATIDEVNPEEYDAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881   283 VVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEKGCVTDGK 362
Cdd:TIGR01382  65 VIPGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGN 144

                         170       180
                  ....*....|....*....|..
gi 18404881   363 VVTAASATDLPAFLFDLSTALG 384
Cdd:TIGR01382 145 LVTSRVPDDLPAFNREFLKLLG 166

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 18404881   7 KSALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNrnaGDRCVMSAHdflGLELTLNANFDDVTPENYDVIIIPGGRFT 86
Cdd:COG0693   3 KKVLILLTDGFEDEELTVPYDALREAGAEVDVASPE---GGPPVTSKH---GITVTADKTLDDVDPDDYDALVLPGGHGA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881  87 -ELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAgGVKCTAFESIKPLIELSGGEWWQQPgiqsmfeitdCVK 165
Cdd:COG0693  77 pDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLK-GRKVTSFPNIEDDLKNAGATYVDEE----------VVV 145

                       170       180
                ....*....|....*....|....*
gi 18404881 166 DGNFMSTVGWPTLGHGIKLLLESLG 190
Cdd:COG0693 146 DGNLITSRGPGDAPAFARALLELLA 170

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881    10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSpnRNAGDRCVMsahdfLGLELTLNANFDDVTPENYDVIIIPGGRFTELL 89
Cdd:TIGR01382   3 LVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTTVGK-----HGYSVTVDATIDEVNPEEYDALVIPGGRAPEYL 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881    90 SADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPLIELSGGEWWQQPGIqsmfeitdcVKDGNF 169
Cdd:TIGR01382  76 RLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGK-KLTSYPAIIDDVKNAGAEYVDIEVV---------VVDGNL 145

                  ..
gi 18404881   170 MS 171
Cdd:TIGR01382 146 VT 147

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 18404881  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRCVMSAHDFLGLE---------LTLNANFDDVTPENYDVIII 80
Cdd:cd03169   3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQtytekpghrFAVTADFDEVDPDDYDALVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881  81 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILaGGVKCTAFESIKPLIELSGGEWwqqpgiqsmfEI 160
Cdd:cd03169  83 PGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVL-KGRRCTAYPACKPEVELAGGTV----------VD 151

                       170       180
                ....*....|....*....|....*....
gi 18404881 161 TDCVKDGNFMSTVGWPTLGHGIKLLLESL 189
Cdd:cd03169 152 DGVVVDGNLVTAQAWPDHPAFLREFLKLL 180

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]

                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881   203 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTpnKKKGEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYDCV 282
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTT---------------VGKHGYSVTVDATIDEVNPEEYDAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881   283 VVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEKGCVTDGK 362
Cdd:TIGR01382  65 VIPGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGN 144

                         170       180
                  ....*....|....*....|..
gi 18404881   363 VVTAASATDLPAFLFDLSTALG 384
Cdd:TIGR01382 145 LVTSRVPDDLPAFNREFLKLLG 166

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881 203 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTPnKKKGEVCAtavydledgrqipaeKRGHN-FFVTASWDDICVDDYDC 281
Cdd:cd03134   2 VAILAADGFEDVELTYPLYRLREAGAEVVVAGP-EAGGEIQG---------------KHGYDtVTVDLTIADVDADDYDA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881 282 VVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVmEKGCVTDG 361
Cdd:cd03134  66 LVIPGGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWV-DEEVVVDG 144

                       170
                ....*....|....
gi 18404881 362 KVVTAASATDLPAF 375
Cdd:cd03134 145 NLITSRNPDDLPAF 158

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 18404881     7 KSALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNrnaGDRCVMSahdfLGLELTLNANFDDVTPENYDVIIIPGGR-F 85
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVD---GGEVKGS----RGVKVTVDASLDDVKPDDYDALVLPGGRaG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881    86 TELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPLIELSGGEWWQQPgiqsmfeitdCVK 165
Cdd:pfam01965  74 PERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGR-KVTSHPAVKDDLINAGATYVDKP----------VVV 142

                         170
                  ....*....|...
gi 18404881   166 DGNFMSTVGWPTL 178
Cdd:pfam01965 143 DGNLVTSRGPGDA 155

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881   9 ALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRcvmsaHDFLGLELTLNANFDDVTPENYDVIIIPGGRFTEL 88
Cdd:cd03134   2 VAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQ-----GKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDK 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881  89 LSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAgGVKCTAFESIKPLIELSGGEWWQQpgiqsmfeitDCVKDGN 168
Cdd:cd03134  77 LRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVR-GRKLTSYPSIKDDLINAGANWVDE----------EVVVDGN 145

                ...
gi 18404881 169 FMS 171
Cdd:cd03134 146 LIT 148

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 18404881 257 PAEKRGHNFFVTASWDDiCVDDYDCVVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCAS 336
Cdd:cd03139  42 PVSSRSGLTVLPDTSFA-DPPDLDVLLVPGGGGTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATT 120

                        90       100       110
                ....*....|....*....|....*....|....
gi 18404881 337 GKGMKVMVKVAGGEAVMEKGCVTDGKVVTAASAT 370
Cdd:cd03139 121 HWAAIDWLKEFGAIVVVDARWVVDGNIWTSGGVS 154

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 18404881 272 DDICVDDYDCVVVPGGRS---PEllvmNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCAS-GKGMKVMVKVA 347
Cdd:cd03140  54 DDLPPEDYDLLILPGGDSwdnPE----APDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSnSLDFLKAHAPY 129

                        90       100
                ....*....|....*....|....
gi 18404881 348 GGEA--VMEKGCVTDGKVVTAASA 369
Cdd:cd03140 130 YGGAeyYDEPQAVSDGNLITANGT 153

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 18404881  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDrcvmsahdflgleltlnanfDDVTPENYDVIIIPGGR-FTEL 88
Cdd:cd01653   2 AVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVE--------------------SDVDLDDYDGLILPGGPgTPDD 61

                        90       100       110
                ....*....|....*....|....*....|....*.
gi 18404881  89 LSADEKCVDLVARFAESKKLIFTSCH-SQVMLMAAG 123
Cdd:cd01653  62 LARDEALLALLREAAAAGKPILGICLgAQLLVLGVQ 97

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881 251 EDGRQIPAEkRGHNFFVTASWDDIcvDDYDCVVVPGGRSPELLVmNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLK 330
Cdd:COG4977  42 LDGGPVRSS-SGLTVAPDHGLADL--AAADTLIVPGGLDPAAAA-DPALLAWLRRAAARGARLASICTGAFLLAAAGLLD 117

                ....*
gi 18404881 331 GKRCA 335
Cdd:COG4977 118 GRRAT 122

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.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881 219 PFRALQALGCKVDAVTPNKKKGEVCATAVyDLEDGRQIPAEKRGHNFFV----TASWDDICVDDYDCVVVPGGRSPEL-L 293
Cdd:cd03141  28 PYDVFTEAGYEVDFASPKGGKVPLDPRSL-DAEDDDDASVFDNDEEFKKklanTKKLSDVDPSDYDAIFIPGGHGPMFdL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18404881 294 VMNEKAVALVKSFAEKDKVFAAIGQG-KLLLAATG-----VLKGKRC---------ASGKGMKVM------VKVAGgeAV 352
Cdd:cd03141 107 PDNPDLQDLLREFYENGKVVAAVCHGpAALLNVKLsdgksLVAGKTVtgftneeeeAAGLKKVVPflledeLKELG--AN 184

                       170       180
                ....*....|....*....|....*....
gi 18404881 353 MEKG------CVTDGKVVTA---ASATDL 372
Cdd:cd03141 185 YVKAepwaefVVVDGRLITGqnpASAAAV 213

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 18404881 251 EDGRQIPAeKRGHNFFVTASWDDICvdDYDCVVVPGGRSPELLVMNEKAVALVKSfAEKDKVFAAIGQGKLLLAATGVLK 330
Cdd:cd03136  40 LDGAPVTS-SNGLRVAPDAALEDAP--PLDYLFVVGGLGARRAVTPALLAWLRRA-ARRGVALGGIDTGAFLLARAGLLD 115

                ....*
gi 18404881 331 GKRCA 335
Cdd:cd03136 116 GRRAT 120

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
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18404881 277 DDYDCVVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCA 335
Cdd:cd03137  63 AAADTVIVPGGPDVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRAT 121