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Conserved domains on  [gi|2064413605|gb|KAG7391922|]
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hypothetical protein PHYPSEUDO_003128 [Phytophthora pseudosyringae]

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 ...
 3-181 8.29e-66

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: 199.47  E-value: 8.29e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   3 TALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPNNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLR 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  83 DSKEVVALLQKQKEGGKLYGAICAAPAVVLhSHGLLAPGAATSYPSFEPKMTGVGF-KHENVVVNGKCVTSQGPGTAMAM 161
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLL-AHGVLLGKKATCYPGFKEKLLNGNYsVNKTVVVDGNLITSRGPGTAIEF 159

                         170       180
                  ....*....|....*....|
gi 2064413605 162 GVKLVELLCGLEKAQSVAQG 181
Cdd:TIGR01383 160 ALELVELLAGKEKAQEVAAG 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 ...
 3-181 8.29e-66

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: 199.47  E-value: 8.29e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   3 TALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPNNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLR 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  83 DSKEVVALLQKQKEGGKLYGAICAAPAVVLhSHGLLAPGAATSYPSFEPKMTGVGF-KHENVVVNGKCVTSQGPGTAMAM 161
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLL-AHGVLLGKKATCYPGFKEKLLNGNYsVNKTVVVDGNLITSRGPGTAIEF 159

                         170       180
                  ....*....|....*....|
gi 2064413605 162 GVKLVELLCGLEKAQSVAQG 181
Cdd:TIGR01383 160 ALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 4-169 1.61e-63

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: 193.15  E-value: 1.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   4 ALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKpnNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLRD 83
Cdd:cd03135     1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKK--LAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLAD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  84 SKEVVALLQKQKEGGKLYGAICAAPAVVLHsHGLLAPGAATSYPSFEPKMTGVGFKHENVVVNGKCVTSQGPGTAMAMGV 163
Cdd:cd03135    79 NEKLIKLLKEFNAKGKLIAAICAAPAVLAK-AGLLKGKKATCYPGFEDKLGGANYVDEPVVVDGNIITSRGPGTAFEFAL 157


                  ....*.
gi 2064413605 164 KLVELL 169
Cdd:cd03135   158 KIVEAL 163
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-169 2.47e-50

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: 159.88  E-value: 2.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   1 MTTALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPnnIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEH 80
Cdd:COG0693     2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGP--PVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  81 LRDSKEVVALLQKQKEGGKLYGAICAAPAvVLHSHGLLAPGAATSYPSFEPKMTGVG--FKHENVVVNGKCVTSQGPGTA 158
Cdd:COG0693    80 LREDPDVVALVREFYEAGKPVAAICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAGatYVDEEVVVDGNLITSRGPGDA 158

                         170
                  ....*....|.
gi 2064413605 159 MAMGVKLVELL 169
Cdd:COG0693   159 PAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
3-186 2.04e-46

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 151.08  E-value: 2.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   3 TALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPNNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLR 82
Cdd:PRK11574    4 SALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAECFR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  83 DSKEVVALLQKQKEGGKLYGAICAAPAVVLHSHGLLAPGAATSYPSFEPKMTGVGFKHENVVVNGKC--VTSQGPGTAMA 160
Cdd:PRK11574   84 DSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDARVnlLTSQGPGTAID 163

                         170       180
                  ....*....|....*....|....*.
gi 2064413605 161 MGVKLVELLCGLEKAQSVAQGLLNTP 186
Cdd:PRK11574  164 FALKIIDLLVGREKAHEVASQLVMAA 189
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-168 2.74e-46

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: 149.71  E-value: 2.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   4 ALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPnniVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLRD 83
Cdd:pfam01965   3 VLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGE---VKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  84 SKEVVALLQKQKEGGKLYGAICAAPaVVLHSHGLLAPGAATSYPSFEPKMTGVGFKH--ENVVVNGKCVTSQGPGTAMAM 161
Cdd:pfam01965  80 NEKLVEFVKDFYEKGKPVAAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLINAGATYvdKPVVVDGNLVTSRGPGDAPEF 158


                  ....*..
gi 2064413605 162 GVKLVEL 168
Cdd:pfam01965 159 ALEILEQ 165
 
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 ...
 3-181 8.29e-66

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: 199.47  E-value: 8.29e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   3 TALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPNNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLR 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  83 DSKEVVALLQKQKEGGKLYGAICAAPAVVLhSHGLLAPGAATSYPSFEPKMTGVGF-KHENVVVNGKCVTSQGPGTAMAM 161
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLL-AHGVLLGKKATCYPGFKEKLLNGNYsVNKTVVVDGNLITSRGPGTAIEF 159

                         170       180
                  ....*....|....*....|
gi 2064413605 162 GVKLVELLCGLEKAQSVAQG 181
Cdd:TIGR01383 160 ALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 4-169 1.61e-63

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: 193.15  E-value: 1.61e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   4 ALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKpnNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLRD 83
Cdd:cd03135     1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKK--LAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLAD 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  84 SKEVVALLQKQKEGGKLYGAICAAPAVVLHsHGLLAPGAATSYPSFEPKMTGVGFKHENVVVNGKCVTSQGPGTAMAMGV 163
Cdd:cd03135    79 NEKLIKLLKEFNAKGKLIAAICAAPAVLAK-AGLLKGKKATCYPGFEDKLGGANYVDEPVVVDGNIITSRGPGTAFEFAL 157


                  ....*.
gi 2064413605 164 KLVELL 169
Cdd:cd03135   158 KIVEAL 163
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-169 2.47e-50

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: 159.88  E-value: 2.47e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   1 MTTALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPnnIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEH 80
Cdd:COG0693     2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGP--PVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPDD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  81 LRDSKEVVALLQKQKEGGKLYGAICAAPAvVLHSHGLLAPGAATSYPSFEPKMTGVG--FKHENVVVNGKCVTSQGPGTA 158
Cdd:COG0693    80 LREDPDVVALVREFYEAGKPVAAICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAGatYVDEEVVVDGNLITSRGPGDA 158

                         170
                  ....*....|.
gi 2064413605 159 MAMGVKLVELL 169
Cdd:COG0693   159 PAFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
3-186 2.04e-46

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 151.08  E-value: 2.04e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   3 TALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPNNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLR 82
Cdd:PRK11574    4 SALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAECFR 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  83 DSKEVVALLQKQKEGGKLYGAICAAPAVVLHSHGLLAPGAATSYPSFEPKMTGVGFKHENVVVNGKC--VTSQGPGTAMA 160
Cdd:PRK11574   84 DSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDARVnlLTSQGPGTAID 163

                         170       180
                  ....*....|....*....|....*.
gi 2064413605 161 MGVKLVELLCGLEKAQSVAQGLLNTP 186
Cdd:PRK11574  164 FALKIIDLLVGREKAHEVASQLVMAA 189
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 4-168 2.74e-46

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: 149.71  E-value: 2.74e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   4 ALIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPnniVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMPGAEHLRD 83
Cdd:pfam01965   3 VLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGE---VKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERLRD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  84 SKEVVALLQKQKEGGKLYGAICAAPaVVLHSHGLLAPGAATSYPSFEPKMTGVGFKH--ENVVVNGKCVTSQGPGTAMAM 161
Cdd:pfam01965  80 NEKLVEFVKDFYEKGKPVAAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLINAGATYvdKPVVVDGNLVTSRGPGDAPEF 158


                  ....*..
gi 2064413605 162 GVKLVEL 168
Cdd:pfam01965 159 ALEILEQ 165
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 3-156 3.27e-19

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: 79.90  E-value: 3.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   3 TALIPIADGSEEIEAITLADVLTRGGVEVTLATVGsKPNNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPGGMpGAEHLR 82
Cdd:cd03134     1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPE-AGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGT-NPDKLR 78

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2064413605  83 DSKEVVALLQKQKEGGKLYGAICAAPAvVLHSHGLLAPGAATSYPSFEPKMT--GVGFKHENVVVNGKCVTSQGPG 156
Cdd:cd03134    79 RDPDAVAFVRAFAEAGKPVAAICHGPW-VLISAGVVRGRKLTSYPSIKDDLInaGANWVDEEVVVDGNLITSRNPD 153
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-182 1.16e-13

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: 65.64  E-value: 1.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   6 IPIADGSEEIEAITLADVLT---RGGVEVTLATVGSKPNNIVTmSRGVKVQGDVAIEACVgkSFDLVVIPGGMPGAEHLR 82
Cdd:cd03139     3 ILLFPGVEVLDVIGPYEVFGrapRLAAPFEVFLVSETGGPVSS-RSGLTVLPDTSFADPP--DLDVLLVPGGGGTRALVN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  83 DsKEVVALLQKQKEGGKLYGAICAApAVVLHSHGLLAPGAATSYPSFEPKMTGVG---FKHENVVVNGKCVTSQGPGTAM 159
Cdd:cd03139    80 D-PALLDFIRRQAARAKYVTSVCTG-ALLLAAAGLLDGRRATTHWAAIDWLKEFGaivVVDARWVVDGNIWTSGGVSAGI 157

                         170       180
                  ....*....|....*....|...
gi 2064413605 160 AMGVKLVELLCGLEKAQSVAQGL 182
Cdd:cd03139   158 DMALALVARLFGEELAQAVALLI 180
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 15-183 3.00e-12

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


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 63.64  E-value: 3.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  15 IEAITLA-DVLTRGGVEVTLATVGSKPnniVTMSRGVKVQGDVAIEACvgKSFDLVVIPGGMpgAEHLRDSKEVVALLQK 93
Cdd:COG4977    20 LEVFRLAnRLAGRPLYRWRLVSLDGGP---VRSSSGLTVAPDHGLADL--AAADTLIVPGGL--DPAAAADPALLAWLRR 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  94 QKEGGKLYGAICAApAVVLHSHGLL-----------APGAATSYPSFEPkmtgvgfkHENV--VVNGKCVTSQGPGTAMA 160
Cdd:COG4977    93 AAARGARLASICTG-AFLLAAAGLLdgrratthwehADAFAERFPDVRV--------DPDRlyVDDGDILTSAGGTAGID 163

                         170       180
                  ....*....|....*....|...
gi 2064413605 161 MGVKLVELLCGLEKAQSVAQGLL 183
Cdd:COG4977   164 LALHLVERDHGAELANAVARRLV 186
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 26-158 7.14e-12

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: 60.70  E-value: 7.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  26 RGGVEVTLATVGSKPNNIVTMSrGVKVQGDVAIEACVGKSFDLVVIPGGMpgAEHLRDSKEVVALLQKQKEGGKLYGAIC 105
Cdd:cd03140    22 NSYEGFEVRTVSPTGEPVTSIG-GLRVVPDYSLDDLPPEDYDLLILPGGD--SWDNPEAPDLAGLVRQALKQGKPVAAIC 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2064413605 106 AAPaVVLHSHGLLAPGAATSYPSFEPKMTGVGFKHEN------VVVNGKCVTSqgPGTA 158
Cdd:cd03140    99 GAT-LALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEyydepqAVSDGNLITA--NGTA 154
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-116 8.66e-10

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: 53.76  E-value: 8.66e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   5 LIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPnnivtmsrgvkVQGDVAIEAcvgksFDLVVIPGGMPGAEHLRDS 84
Cdd:cd01653     2 AVLLFPGFEELELASPLDALREAGAEVDVVSPDGGP-----------VESDVDLDD-----YDGLILPGGPGTPDDLARD 65

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2064413605  85 KEVVALLQKQKEGGKLYGAICAAPAVVLHSHG 116
Cdd:cd01653    66 EALLALLREAAAAGKPILGICLGAQLLVLGVQ 97
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 44-183 9.48e-10

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.


Pssm-ID: 153230 [Multi-domain]  Cd Length: 185  Bit Score: 55.28  E-value: 9.48e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  44 VTMSRGVKVQGDVAIEAcvGKSFDLVVIPGGMPGaeHLRDSKEVVALLQKQKEGGKLYGAICAApAVVLHSHGLLAPGAA 123
Cdd:cd03136    45 VTSSNGLRVAPDAALED--APPLDYLFVVGGLGA--RRAVTPALLAWLRRAARRGVALGGIDTG-AFLLARAGLLDGRRA 119

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064413605 124 T----SYPSFEPKMTGVGFKHENVVVNGKCVTSQGPGTAMAMGVKLVELLCGLEKAQSVAQGLL 183
Cdd:cd03136   120 TvhweHLEAFAEAFPRVQVTRDLFEIDGDRLTCAGGTAALDLMLELIARDHGAALAARVAEQFL 183
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-110 4.68e-09

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: 51.43  E-value: 4.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605   5 LIPIADGSEEIEAITLADVLTRGGVEVTLATVGSKPnnivtmsrgvkVQGDVAIEAcvgksFDLVVIPGGMPGAEHLRDS 84
Cdd:cd03128     2 AVLLFGGSEELELASPLDALREAGAEVDVVSPDGGP-----------VESDVDLDD-----YDGLILPGGPGTPDDLAWD 65

                          90       100
                  ....*....|....*....|....*.
gi 2064413605  85 KEVVALLQKQKEGGKLYGAICAAPAV 110
Cdd:cd03128    66 EALLALLREAAAAGKPVLGICLGAQL 91
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 49-183 7.20e-09

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: 153232 [Multi-domain]  Cd Length: 195  Bit Score: 53.03  E-value: 7.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  49 GVKVQGDVAIEAcvGKSFDLVVIPG--GMPGAEHLRDSKEVVALLQKQKEGGKLYGAICAApAVVLHSHGLLAPGAATS- 125
Cdd:cd03138    55 GILILPDATLAD--VPAPDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVAAACTG-VFLLAEAGLLDGRRATTh 131

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2064413605 126 ---YPSFE---PKMTGVGFKHenVVVNGKCVTSQGPGTAMAMGVKLVELLCGLEKAQSVAQGLL 183
Cdd:cd03138   132 wwlAPQFRrrfPKVRLDPDRV--VVTDGNLITAGGAMAWADLALHLIERLAGPELAQLVARFLL 193
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 30-180 3.13e-06

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: 45.57  E-value: 3.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  30 EVTLATVGSKPnniVTMSRGVKVQGDVAIEAcvGKSFDLVVIPGGmPGAEHLRDSKEVVALLQKQKEGGKLYGAICAApA 109
Cdd:cd03137    34 ELRVCSPEGGP---VRSSSGLSLVADAGLDA--LAAADTVIVPGG-PDVDGRPPPPALLAALRRAAARGARVASVCTG-A 106

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2064413605 110 VVLHSHGLLAPGAATSYPSFEPKMTGvgfKHENV--------VVNGKCVTSQGPGTAMAMGVKLVELLCGLEKAQSVAQ 180
Cdd:cd03137   107 FVLAEAGLLDGRRATTHWAYAEDLAR---RFPAVrvdpdvlyVDDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVAR 182
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 11-169 2.06e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to Escherichia coli Hsp31 protein (EcHsp31). This group includes EcHsp31 and Saccharomyces cerevisiae Ydr533c protein. EcHsp31 has chaperone activity. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. EcHsp31 coordinates a metal ion using a 2-His-1-carboxylate motif present in various ions that use iron as a cofactor such as Carboxypeptidase A. The catalytic triad typical of GATase1 domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1 domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For EcHsp31, this Cys together with a different His and, an Asp (rather than a Glu) residue form a different catalytic triad from the typical GATase1 domain. For Ydr533c a catalytic triad forms from the conserved Cys together with a different His and Glu from that of the typical GATase1domain. Ydr533c protein and EcHsp31 are homodimers.


Pssm-ID: 153235 [Multi-domain]  Cd Length: 221  Bit Score: 40.62  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  11 GSEEIEAITLADVLTRGGVEVTLATV-GSKP----------------NNIVTMSRGVKVQGDVAIEACVGKSFDLVVIPG 73
Cdd:cd03141    19 GLWLEELAHPYDVFTEAGYEVDFASPkGGKVpldprsldaeddddasVFDNDEEFKKKLANTKKLSDVDPSDYDAIFIPG 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2064413605  74 GmPGAEH-LRDSKEVVALLQKQKEGGKLYGAICAAPAVVLHSHglLAPGAA-------TSYPSFEPKMTGV--------- 136
Cdd:cd03141    99 G-HGPMFdLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVK--LSDGKSlvagktvTGFTNEEEEAAGLkkvvpflle 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2064413605 137 ------GFKH-------ENVVVNGKCVTSQGPGTAMAMGVKLVELL 169
Cdd:cd03141   176 delkelGANYvkaepwaEFVVVDGRLITGQNPASAAAVAEALVKAL 221
 
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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