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Conserved domains on  [gi|530360487|ref|XP_005263481|]
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Parkinson disease protein 7 isoform X1 [Homo sapiens]

Protein Classification

DJ-1/PfpI family protein( domain architecture ID 11492385)

DJ-1/PfpI family protein, similar to Escherichia coli YajL, a covalent chaperone that protects cells against protein sulfenylation

Graphical summary

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List of domain hits

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 ...
5-184 2.46e-81

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: 239.14  E-value: 2.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487    5 RALVILAKGAEEMETVIPVDVMRRAGIKVTV--AGLAGKDPVQCSRDVVICPDASLEDAKKEgPYDVVVLPGGNLGAQNL 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDVDLE-KFDVIVLPGGMPGAENL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   83 SESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENR-VEKDGLILTSRGPGTS 161
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNG---NYSVNKtVVVDGNLITSRGPGTA 156
                         170       180
                  ....*....|....*....|...
gi 530360487  162 FEFALAIVEALNGKEVAAQVKAP 184
Cdd:TIGR01383 157 IEFALELVELLAGKEKAQEVAAG 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 ...
5-184 2.46e-81

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: 239.14  E-value: 2.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487    5 RALVILAKGAEEMETVIPVDVMRRAGIKVTV--AGLAGKDPVQCSRDVVICPDASLEDAKKEgPYDVVVLPGGNLGAQNL 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDVDLE-KFDVIVLPGGMPGAENL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   83 SESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENR-VEKDGLILTSRGPGTS 161
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNG---NYSVNKtVVVDGNLITSRGPGTA 156
                         170       180
                  ....*....|....*....|...
gi 530360487  162 FEFALAIVEALNGKEVAAQVKAP 184
Cdd:TIGR01383 157 IEFALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
6-172 4.16e-69

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: 207.41  E-value: 4.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   6 ALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKkEGPYDVVVLPGGNLGAQNLSES 85
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVN-LDDYDAIVIPGGLPGAQNLADN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  86 AAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENRVEKDGLILTSRGPGTSFEFA 165
Cdd:cd03135   80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLGGA---NYVDEPVVVDGNIITSRGPGTAFEFA 156

                 ....*..
gi 530360487 166 LAIVEAL 172
Cdd:cd03135  157 LKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
4-171 1.93e-63

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: 193.24  E-value: 1.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487    4 KRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKdPVQCSRDVVICPDASLEDAKkEGPYDVVVLPGGNLGAQNLS 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGG-EVKGSRGVKVTVDASLDDVK-PDDYDALVLPGGRAGPERLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   84 ESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGhYTYSENRVEKDGLILTSRGPGTSFE 163
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAG-ATYVDKPVVVDGNLVTSRGPGDAPE 157

                  ....*...
gi 530360487  164 FALAIVEA 171
Cdd:pfam01965 158 FALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
3-172 2.09e-49

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: 157.57  E-value: 2.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   3 SKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGpYDVVVLPGGNLGAQNL 82
Cdd:COG0693    2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDD-YDALVLPGGHGAPDDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  83 SESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHyTYSENRVEKDGLILTSRGPGTSF 162
Cdd:COG0693   81 REDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGA-TYVDEEVVVDGNLITSRGPGDAP 159
                        170
                 ....*....|
gi 530360487 163 EFALAIVEAL 172
Cdd:COG0693  160 AFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
3-187 2.30e-35

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 122.58  E-value: 2.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   3 SKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLA--GKDPVQCSRDVVICPDASLEDAKkEGPYDVVVLPGGNLGAQ 80
Cdd:PRK11574   2 SASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVAsdGNLEITCSRGVKLLADAPLVEVA-DGDFDVIVLPGGIKGAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  81 NLSESAAVKEILKEQENRKGLIAAICAGP-TALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENRVEKDGLI--LTSRG 157
Cdd:PRK11574  81 CFRDSPLLVETVRQFHRSGRIVAAICAAPaTVLVPHDLFPIGNMTGFPTLKDKIPAE---QWQDKRVVWDARVnlLTSQG 157
                        170       180       190
                 ....*....|....*....|....*....|
gi 530360487 158 PGTSFEFALAIVEALNGKEVAAQVKAPLVL 187
Cdd:PRK11574 158 PGTAIDFALKIIDLLVGREKAHEVASQLVM 187
 
Name Accession Description Interval E-value
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
5-184 2.46e-81

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: 239.14  E-value: 2.46e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487    5 RALVILAKGAEEMETVIPVDVMRRAGIKVTV--AGLAGKDPVQCSRDVVICPDASLEDAKKEgPYDVVVLPGGNLGAQNL 82
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKLAVKGSRGVKILADASLEDVDLE-KFDVIVLPGGMPGAENL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   83 SESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENR-VEKDGLILTSRGPGTS 161
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLNG---NYSVNKtVVVDGNLITSRGPGTA 156
                         170       180
                  ....*....|....*....|...
gi 530360487  162 FEFALAIVEALNGKEVAAQVKAP 184
Cdd:TIGR01383 157 IEFALELVELLAGKEKAQEVAAG 179
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
6-172 4.16e-69

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: 207.41  E-value: 4.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   6 ALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKkEGPYDVVVLPGGNLGAQNLSES 85
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIKVKADKTLSDVN-LDDYDAIVIPGGLPGAQNLADN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  86 AAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENRVEKDGLILTSRGPGTSFEFA 165
Cdd:cd03135   80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLGGA---NYVDEPVVVDGNIITSRGPGTAFEFA 156

                 ....*..
gi 530360487 166 LAIVEAL 172
Cdd:cd03135  157 LKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
4-171 1.93e-63

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: 193.24  E-value: 1.93e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487    4 KRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKdPVQCSRDVVICPDASLEDAKkEGPYDVVVLPGGNLGAQNLS 83
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGG-EVKGSRGVKVTVDASLDDVK-PDDYDALVLPGGRAGPERLR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   84 ESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGhYTYSENRVEKDGLILTSRGPGTSFE 163
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAG-ATYVDKPVVVDGNLVTSRGPGDAPE 157

                  ....*...
gi 530360487  164 FALAIVEA 171
Cdd:pfam01965 158 FALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
3-172 2.09e-49

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: 157.57  E-value: 2.09e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   3 SKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICPDASLEDAKKEGpYDVVVLPGGNLGAQNL 82
Cdd:COG0693    2 MKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGITVTADKTLDDVDPDD-YDALVLPGGHGAPDDL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  83 SESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMNGGHyTYSENRVEKDGLILTSRGPGTSF 162
Cdd:COG0693   81 REDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGA-TYVDEEVVVDGNLITSRGPGDAP 159
                        170
                 ....*....|
gi 530360487 163 EFALAIVEAL 172
Cdd:COG0693  160 AFARALLELL 169
PRK11574 PRK11574
protein deglycase YajL;
3-187 2.30e-35

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 122.58  E-value: 2.30e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   3 SKRALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLA--GKDPVQCSRDVVICPDASLEDAKkEGPYDVVVLPGGNLGAQ 80
Cdd:PRK11574   2 SASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVAsdGNLEITCSRGVKLLADAPLVEVA-DGDFDVIVLPGGIKGAE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  81 NLSESAAVKEILKEQENRKGLIAAICAGP-TALLAHEIGFGSKVTTHPLAKDKMMNGghyTYSENRVEKDGLI--LTSRG 157
Cdd:PRK11574  81 CFRDSPLLVETVRQFHRSGRIVAAICAAPaTVLVPHDLFPIGNMTGFPTLKDKIPAE---QWQDKRVVWDARVnlLTSQG 157
                        170       180       190
                 ....*....|....*....|....*....|
gi 530360487 158 PGTSFEFALAIVEALNGKEVAAQVKAPLVL 187
Cdd:PRK11574 158 PGTAIDFALKIIDLLVGREKAHEVASQLVM 187
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
5-171 1.57e-23

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: 91.07  E-value: 1.57e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   5 RALVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVIC-PDASLEDAKKEgPYDVVVLPGGnLGAQNLS 83
Cdd:cd03134    1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVtVDLTIADVDAD-DYDALVIPGG-TNPDKLR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  84 ESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHPLAKDKMMN-GGHYTYSEnrVEKDGLILTSRGPGTSF 162
Cdd:cd03134   79 RDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINaGANWVDEE--VVVDGNLITSRNPDDLP 156

                 ....*....
gi 530360487 163 EFALAIVEA 171
Cdd:cd03134  157 AFNRAILKA 165
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
4-181 2.06e-15

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: 72.50  E-value: 2.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   4 KRALVILAKGAEEMETVIPVDVMRRA-------GIKVTVAGLAGkDPVQCSRDVVICPDASLEDAkkeGPYDVVVLPGGn 76
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFRLAnrlagrpLYRWRLVSLDG-GPVRSSSGLTVAPDHGLADL---AAADTLIVPGG- 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  77 lGAQNLSESAAVKEILKEQENRKGLIAAICAGptALLAHEIGF--GSKVTTHPLAKDKMMNgghyTYSENRVE------K 148
Cdd:COG4977   76 -LDPAAAADPALLAWLRRAAARGARLASICTG--AFLLAAAGLldGRRATTHWEHADAFAE----RFPDVRVDpdrlyvD 148
                        170       180       190
                 ....*....|....*....|....*....|...
gi 530360487 149 DGLILTSRGPGTSFEFALAIVEALNGKEVAAQV 181
Cdd:COG4977  149 DGDILTSAGGTAGIDLALHLVERDHGAELANAV 181
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
8-181 3.80e-15

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: 69.88  E-value: 3.80e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   8 VILAKGAEEMETVIPVDVMRRA-----GIKVTVAGLAGkDPVQCSRDVVICPDASLEDAkkeGPYDVVVLPGGnLGAQNL 82
Cdd:cd03139    3 ILLFPGVEVLDVIGPYEVFGRAprlaaPFEVFLVSETG-GPVSSRSGLTVLPDTSFADP---PDLDVLLVPGG-GGTRAL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  83 SESAAVKEILKEQENRKGLIAAICAGptALLAHEIGF--GSKVTTHPLAKDKM-MNGGHYTYSENRVEkDGLILTSRGPG 159
Cdd:cd03139   78 VNDPALLDFIRRQAARAKYVTSVCTG--ALLLAAAGLldGRRATTHWAAIDWLkEFGAIVVVDARWVV-DGNIWTSGGVS 154
                        170       180
                 ....*....|....*....|..
gi 530360487 160 TSFEFALAIVEALNGKEVAAQV 181
Cdd:cd03139  155 AGIDMALALVARLFGEELAQAV 176
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
7-113 5.53e-12

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: 59.92  E-value: 5.53e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   7 LVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVqcsrdvvicPDASLEDakkegpYDVVVLPGGNLGAQNLSESA 86
Cdd:cd01653    2 AVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVE---------SDVDLDD------YDGLILPGGPGTPDDLARDE 66
                         90       100
                 ....*....|....*....|....*..
gi 530360487  87 AVKEILKEQENRKGLIAAICAGPTALL 113
Cdd:cd01653   67 ALLALLREAAAAGKPILGICLGAQLLV 93
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
23-181 1.77e-11

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: 59.91  E-value: 1.77e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  23 VDVMR-------RAGIKVTVAGLAGkDPVQCSRDVVICPDASLEDAkkeGPYDVVVLPGGNLGAQnlSESAAVKEILKEQ 95
Cdd:cd03136   18 IEPLRaanrlagRELYRWRVLSLDG-APVTSSNGLRVAPDAALEDA---PPLDYLFVVGGLGARR--AVTPALLAWLRRA 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  96 ENRKGLIAAICAGpTALLAhEIGF--GSKVTTHPLAKDKMM-NGGHYTYSENRVEKDGLILTSRGPGTSFEFALAIVEAL 172
Cdd:cd03136   92 ARRGVALGGIDTG-AFLLA-RAGLldGRRATVHWEHLEAFAeAFPRVQVTRDLFEIDGDRLTCAGGTAALDLMLELIARD 169

                 ....*....
gi 530360487 173 NGKEVAAQV 181
Cdd:cd03136  170 HGAALAARV 178
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
7-112 2.58e-10

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: 54.90  E-value: 2.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   7 LVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVqcsrdvvicPDASLEDakkegpYDVVVLPGGNLGAQNLSESA 86
Cdd:cd03128    2 AVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVE---------SDVDLDD------YDGLILPGGPGTPDDLAWDE 66
                         90       100
                 ....*....|....*....|....*.
gi 530360487  87 AVKEILKEQENRKGLIAAICAGPTAL 112
Cdd:cd03128   67 ALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
8-187 1.43e-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: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 54.81  E-value: 1.43e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   8 VILAKGAEEMETVIPVDVMRRAGIK-------VTVAGLAGkDPVQCSRDVVICPDASLEDAkkeGPYDVVVLPGGNlGAQ 80
Cdd:cd03137    3 VLVFPGVSLLDLSGPAEVFGEANRAlgppayeLRVCSPEG-GPVRSSSGLSLVADAGLDAL---AAADTVIVPGGP-DVD 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  81 NLSESAAVKEILKEQENRKGLIAAICAGptALLAHEIGF--GSKVTTH-----PLAKDkmmngghytYSENRVE------ 147
Cdd:cd03137   78 GRPPPPALLAALRRAAARGARVASVCTG--AFVLAEAGLldGRRATTHwayaeDLARR---------FPAVRVDpdvlyv 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530360487 148 KDGLILTSRGPGTSFEFALAIVEALNGKEVAAQVKAPLVL 187
Cdd:cd03137  147 DDGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVARRLVV 186
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
26-181 1.80e-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: 54.57  E-value: 1.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  26 MRRAGIKVTVAGLAGKdPVQCSRDVVICPDASLEDAkkeGPYDVVVLPG--GNLGAQNLSESAAVKEILKEQENRKGLIA 103
Cdd:cd03138   33 GGAPPFEVRLVSLDGG-PVLLAGGILILPDATLADV---PAPDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487 104 AICAGpTALLAhEIGF--GSKVTTH-----------PLAKDKMmngghytysENRVEKDGLILTSRGPGTSFEFALAIVE 170
Cdd:cd03138  109 AACTG-VFLLA-EAGLldGRRATTHwwlapqfrrrfPKVRLDP---------DRVVVTDGNLITAGGAMAWADLALHLIE 177
                        170
                 ....*....|.
gi 530360487 171 ALNGKEVAAQV 181
Cdd:cd03138  178 RLAGPELAQLV 188
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
13-172 2.10e-09

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: 54.87  E-value: 2.10e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  13 GAEEMETVIPVDVMRRAGIKVTVAGLAGK----DPVqcSRDVVICPDASLEDAKKEG----------------PYDVVVL 72
Cdd:cd03141   19 GLWLEELAHPYDVFTEAGYEVDFASPKGGkvplDPR--SLDAEDDDDASVFDNDEEFkkklantkklsdvdpsDYDAIFI 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  73 PGGnLGA-QNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS------KVTTHPLAKDKMM----------- 134
Cdd:cd03141   97 PGG-HGPmFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSDGKslvagkTVTGFTNEEEEAAglkkvvpflle 175
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 530360487 135 -----NGGHYTYSEN---RVEKDGLILTSRGPGTSFEFALAIVEAL 172
Cdd:cd03141  176 delkeLGANYVKAEPwaeFVVVDGRLITGQNPASAAAVAEALVKAL 221
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
41-173 2.72e-08

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: 51.07  E-value: 2.72e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  41 KDPVQCSRDVVICPDASLEDAKKEgPYDVVVLPGGNLGAQNlsESAAVKEILKEQENRKGLIAAICAGPTALLAHeiGF- 119
Cdd:cd03140   36 GEPVTSIGGLRVVPDYSLDDLPPE-DYDLLILPGGDSWDNP--EAPDLAGLVRQALKQGKPVAAICGATLALARA--GLl 110
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487 120 -GSKVTTHPLAKDKMM----NGGHYtYSENRVEKDGLILTSrgPGTSF-EFALAIVEALN 173
Cdd:cd03140  111 nNRKHTSNSLDFLKAHapyyGGAEY-YDEPQAVSDGNLITA--NGTAPvEFAAEILRALD 167
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
7-157 6.37e-05

Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus; Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins similar to PfpI from Pyrococcus furiosus. PfpI is an ATP-independent intracellular proteases which may hydrolyze small peptides to provide a nutritional source. Only Cys of the catalytic triad typical of GATase1 domains is conserved in this group. This Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow.


Pssm-ID: 153243 [Multi-domain]  Cd Length: 180  Bit Score: 41.48  E-value: 6.37e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   7 LVILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGKDPVQCSRDVVICP---------------DASLEDAKKEgPYDVVV 71
Cdd:cd03169    3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPgwqtytekpghrfavTADFDEVDPD-DYDALV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  72 LPGGNlGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGSKVTTHP-LAKDKMMNGGhyTYSENRVEKDG 150
Cdd:cd03169   82 IPGGR-APEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPaCKPEVELAGG--TVVDDGVVVDG 158

                 ....*..
gi 530360487 151 LILTSRG 157
Cdd:cd03169  159 NLVTAQA 165
PRK04155 PRK04155
protein deglycase HchA;
18-135 3.53e-04

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 39.98  E-value: 3.53e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487  18 ETVIPVDVMRRAGIKVTVAGLAG----------------------------KDPVQCSrDVVicpdASLEDAkkEGPYDV 69
Cdd:PRK04155  78 ETLLPMYHLHKAGFEFDVATLSGnpvkfeywamphedeavmgfyekykskfKQPKKLA-DVV----ANLLAP--DSDYAA 150
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530360487  70 VVLPGGNlGAQN-LSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGFGS------KVTTHPLAKDKMMN 135
Cdd:PRK04155 151 VFIPGGH-GALIgLPESEDVAAALQWALDNDRFIITLCHGPAALLAAGVDHGDnplngySICAFPDALDKQTP 222
GATase1_EcHsp31_like cd03148
Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 ...
9-135 3.72e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31); Type 1 glutamine amidotransferase (GATase1)-like domain found in Escherichia coli Hsp31 protein (EcHsp31). This group includes proteins similar to EcHsp31. EcHsp31 has chaperone activity. 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 GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. 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. EcHsp31 is a homodimer.


Pssm-ID: 153242 [Multi-domain]  Cd Length: 232  Bit Score: 36.77  E-value: 3.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530360487   9 ILAKGAEEMETVIPVDVMRRAGIKVTVAGLAGkDPVQC------SRDVVICP-----DASLEDAKK-----------EGP 66
Cdd:cd03148   18 LFSTGNHPVEMLLPLYHLHAAGFDFDVATLSG-LPVKFeywampHEDEAVMPffekhKSKLRNPKKladvvaslnadDSE 96
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530360487  67 YDVVVLPGGNLGAQNLSESAAVKEILKEQENRKGLIAAICAGPTALLAHEIGF------GSKVTTHPLAKDKMMN 135
Cdd:cd03148   97 YAAVFIPGGHGALIGIPESQDVAAALQWAIKNDRFVITLCHGPAAFLAARHGGgknpleGYSVCVFPDSLDEGAN 171
 
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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