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Conserved domains on  [gi|489955778|ref|WP_003859085|]
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MULTISPECIES: protein deglycase YajL [Enterobacter]

Protein Classification

DJ-1/PfpI family protein( domain architecture ID 10793591)

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
PRK11574 PRK11574
protein deglycase YajL;
1-196 1.27e-146

protein deglycase YajL;


:

Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 404.93  E-value: 1.27e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAE 80
Cdd:PRK11574   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  81 CFRDSPLLVETVRQFHLSGRIVAAICAAAGTVLVPHDIFPIGNMTGFPGLKDTIPEDQWVDKRVVWDPRVNLLTSQGPGT 160
Cdd:PRK11574  81 CFRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDARVNLLTSQGPGT 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489955778 161 AIDFGLKIIDLLVGREKAYEVASSLVMAAGIYNYYE 196
Cdd:PRK11574 161 AIDFALKIIDLLVGREKAHEVASQLVMAAGIYNYYE 196
 
Name Accession Description Interval E-value
PRK11574 PRK11574
protein deglycase YajL;
1-196 1.27e-146

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 404.93  E-value: 1.27e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAE 80
Cdd:PRK11574   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  81 CFRDSPLLVETVRQFHLSGRIVAAICAAAGTVLVPHDIFPIGNMTGFPGLKDTIPEDQWVDKRVVWDPRVNLLTSQGPGT 160
Cdd:PRK11574  81 CFRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDARVNLLTSQGPGT 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489955778 161 AIDFGLKIIDLLVGREKAYEVASSLVMAAGIYNYYE 196
Cdd:PRK11574 161 AIDFALKIIDLLVGREKAHEVASQLVMAAGIYNYYE 196
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 4-183 3.61e-75

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: 223.73  E-value: 3.61e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778    4 SALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAECFR 83
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   84 DSPLLVETVRQFHLSGRIVAAICAAAGTVLVPHDIFPiGNMTGFPGLKDTIPEDQW-VDKRVVWDprVNLLTSQGPGTAI 162
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLG-KKATCYPGFKEKLLNGNYsVNKTVVVD--GNLITSRGPGTAI 157

                         170       180
                  ....*....|....*....|.
gi 489955778  163 DFGLKIIDLLVGREKAYEVAS 183
Cdd:TIGR01383 158 EFALELVELLAGKEKAQEVAA 178
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 5-172 1.08e-58

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: 181.21  E-value: 1.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   5 ALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAECFRD 84
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASL--EKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  85 SPLLVETVRQFHLSGRIVAAICAAAgTVLVPHDIFPIGNMTGFPGLKDTIPEDQWVDKRVVWDprVNLLTSQGPGTAIDF 164
Cdd:cd03135   79 NEKLIKLLKEFNAKGKLIAAICAAP-AVLAKAGLLKGKKATCYPGFEDKLGGANYVDEPVVVD--GNIITSRGPGTAFEF 155


                 ....*...
gi 489955778 165 GLKIIDLL 172
Cdd:cd03135  156 ALKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 3-171 1.01e-55

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: 173.98  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778    3 ASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasdGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAECF 82
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSV---DGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   83 RDSPLLVETVRQFHLSGRIVAAICAAAgTVLVPHDIFPIGNMTGFPGLKDTI--PEDQWVDKRVVWDPrvNLLTSQGPGT 160
Cdd:pfam01965  78 RDNEKLVEFVKDFYEKGKPVAAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLinAGATYVDKPVVVDG--NLVTSRGPGD 154

                         170
                  ....*....|.
gi 489955778  161 AIDFGLKIIDL 171
Cdd:pfam01965 155 APEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-172 4.46e-51

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: 162.20  E-value: 4.46e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAE 80
Cdd:COG0693    1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASP--EGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  81 CFRDSPLLVETVRQFHLSGRIVAAICAAAGtVLVPHDIFPIGNMTGFPGLKDTIPED--QWVDKRVVWDprVNLLTSQGP 158
Cdd:COG0693   79 DLREDPDVVALVREFYEAGKPVAAICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAgaTYVDEEVVVD--GNLITSRGP 155

                        170
                 ....*....|....
gi 489955778 159 GTAIDFGLKIIDLL 172
Cdd:COG0693  156 GDAPAFARALLELL 169
 
Name Accession Description Interval E-value
PRK11574 PRK11574
protein deglycase YajL;
1-196 1.27e-146

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 404.93  E-value: 1.27e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAE 80
Cdd:PRK11574   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGIKGAE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  81 CFRDSPLLVETVRQFHLSGRIVAAICAAAGTVLVPHDIFPIGNMTGFPGLKDTIPEDQWVDKRVVWDPRVNLLTSQGPGT 160
Cdd:PRK11574  81 CFRDSPLLVETVRQFHRSGRIVAAICAAPATVLVPHDLFPIGNMTGFPTLKDKIPAEQWQDKRVVWDARVNLLTSQGPGT 160

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 489955778 161 AIDFGLKIIDLLVGREKAYEVASSLVMAAGIYNYYE 196
Cdd:PRK11574 161 AIDFALKIIDLLVGREKAHEVASQLVMAAGIYNYYE 196
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 4-183 3.61e-75

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: 223.73  E-value: 3.61e-75
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778    4 SALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAECFR 83
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVAIAGLNGKLAVKGSRGVKILADASLEDVDLEKFDVIVLPGGMPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   84 DSPLLVETVRQFHLSGRIVAAICAAAGTVLVPHDIFPiGNMTGFPGLKDTIPEDQW-VDKRVVWDprVNLLTSQGPGTAI 162
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLG-KKATCYPGFKEKLLNGNYsVNKTVVVD--GNLITSRGPGTAI 157

                         170       180
                  ....*....|....*....|.
gi 489955778  163 DFGLKIIDLLVGREKAYEVAS 183
Cdd:TIGR01383 158 EFALELVELLAGKEKAQEVAA 178
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 5-172 1.08e-58

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: 181.21  E-value: 1.08e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   5 ALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAECFRD 84
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASL--EKKLAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLPGAQNLAD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  85 SPLLVETVRQFHLSGRIVAAICAAAgTVLVPHDIFPIGNMTGFPGLKDTIPEDQWVDKRVVWDprVNLLTSQGPGTAIDF 164
Cdd:cd03135   79 NEKLIKLLKEFNAKGKLIAAICAAP-AVLAKAGLLKGKKATCYPGFEDKLGGANYVDEPVVVD--GNIITSRGPGTAFEF 155


                 ....*...
gi 489955778 165 GLKIIDLL 172
Cdd:cd03135  156 ALKIVEAL 163
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 3-171 1.01e-55

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: 173.98  E-value: 1.01e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778    3 ASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasdGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAECF 82
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSV---DGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAGPERL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   83 RDSPLLVETVRQFHLSGRIVAAICAAAgTVLVPHDIFPIGNMTGFPGLKDTI--PEDQWVDKRVVWDPrvNLLTSQGPGT 160
Cdd:pfam01965  78 RDNEKLVEFVKDFYEKGKPVAAICHGP-QVLAAAGVLKGRKVTSHPAVKDDLinAGATYVDKPVVVDG--NLVTSRGPGD 154

                         170
                  ....*....|.
gi 489955778  161 AIDFGLKIIDL 171
Cdd:pfam01965 155 APEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-172 4.46e-51

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: 162.20  E-value: 4.46e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   1 MSASALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVasDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAE 80
Cdd:COG0693    1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASP--EGGPPVTSKHGITVTADKTLDDVDPDDYDALVLPGGHGAPD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  81 CFRDSPLLVETVRQFHLSGRIVAAICAAAGtVLVPHDIFPIGNMTGFPGLKDTIPED--QWVDKRVVWDprVNLLTSQGP 158
Cdd:COG0693   79 DLREDPDVVALVREFYEAGKPVAAICHGPA-VLAAAGLLKGRKVTSFPNIEDDLKNAgaTYVDEEVVVD--GNLITSRGP 155

                        170
                 ....*....|....
gi 489955778 159 GTAIDFGLKIIDLL 172
Cdd:COG0693  156 GDAPAFARALLELL 169
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 5-171 6.18e-17

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: 74.12  E-value: 6.18e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   5 ALVCLAPGSEETEAVTTIDLLVRGGIKVTTASVASDGSlaITCSRGVKIL-ADAPLVQVADGDYDIIVLPGGLkGAECFR 83
Cdd:cd03134    2 VAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGE--IQGKHGYDTVtVDLTIADVDADDYDALVIPGGT-NPDKLR 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  84 DSPLLVETVRQFHLSGRIVAAICaAAGTVLVPHDIFPIGNMTGFPGLKDtipeD------QWVDKRVVWDPrvNLLTSQG 157
Cdd:cd03134   79 RDPDAVAFVRAFAEAGKPVAAIC-HGPWVLISAGVVRGRKLTSYPSIKD----DlinagaNWVDEEVVVDG--NLITSRN 151

                        170
                 ....*....|....
gi 489955778 158 PGTAIDFGLKIIDL 171
Cdd:cd03134  152 PDDLPAFNRAILKA 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 6-172 3.25e-12

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


Pssm-ID: 273591 [Multi-domain]  Cd Length: 166  Bit Score: 61.66  E-value: 3.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778    6 LVCLAP-GSEETEAVTTIDLLVRGGIKVTTASvASDGSlaITCSRGVKILADAPLVQVADGDYDIIVLPGGlKGAECFRD 84
Cdd:TIGR01382   2 LLVLTTdEFEDSELLYPLDRLREAGHEVDTVS-KEAGT--TVGKHGYSVTVDATIDEVNPEEYDALVIPGG-RAPEYLRL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   85 SPLLVETVRQFHLSGRIVAAICAAAgTVLVPHDIFPIGNMTGFPGLKDTIPE--DQWVDKRVVWDPRvNLLTSQGPGTAI 162
Cdd:TIGR01382  78 NNKAVRLVREFVEKGKPVAAICHGP-QLLISAGVLRGKKLTSYPAIIDDVKNagAEYVDIEVVVVDG-NLVTSRVPDDLP 155

                         170
                  ....*....|
gi 489955778  163 DFGLKIIDLL 172
Cdd:TIGR01382 156 AFNREFLKLL 165
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 36-187 5.62e-10

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: 57.47  E-value: 5.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  36 SVASDGSLAITCSRGVKILADAPLVQVADgdYDIIVLPGGLKGAEcfRDSPLLVETVRQFHLSGRIVAAIC------AAA 109
Cdd:COG4977   38 RLVSLDGGPVRSSSGLTVAPDHGLADLAA--ADTLIVPGGLDPAA--AADPALLAWLRRAAARGARLASICtgafllAAA 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778 110 G-------TVlvpH----DIFpignMTGFPGLkdtipedQWVDKRVVWDPRvNLLTSQGPGTAIDFGLKIIDLLVGREKA 178
Cdd:COG4977  114 GlldgrraTT---HwehaDAF----AERFPDV-------RVDPDRLYVDDG-DILTSAGGTAGIDLALHLVERDHGAELA 178


                 ....*....
gi 489955778 179 YEVASSLVM 187
Cdd:COG4977  179 NAVARRLVV 187
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 5-172 5.46e-09

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: 52.99  E-value: 5.46e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   5 ALVCLAPGSEETEAVTTIDLLVRG-GIKVTTASVASDgslAITCSRGVKILADAPLVQVADGDYDIIVLPGGLKGAEcfR 83
Cdd:cd03140    1 IAVFLTDEFADWEGAYLAALLNSYeGFEVRTVSPTGE---PVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSWDN--P 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  84 DSPLLVETVRQFHLSGRIVAAICAA------AGtVL--VPHdifpIGNMTGFpgLKDTIP----EDQWVDKRVVWDPrvN 151
Cdd:cd03140   76 EAPDLAGLVRQALKQGKPVAAICGAtlalarAG-LLnnRKH----TSNSLDF--LKAHAPyyggAEYYDEPQAVSDG--N 146

                        170       180
                 ....*....|....*....|..
gi 489955778 152 LLTSqgPGTA-IDFGLKIIDLL 172
Cdd:cd03140  147 LITA--NGTApVEFAAEILRAL 166
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-109 2.71e-08

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: 49.90  E-value: 2.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   6 LVCLAPGSEETEAVTTIDLLVRGGIKVTTASVAsdgslaitcsrgvkilADAPLVQVADGDYDIIVLPGGLKGAECFRDS 85
Cdd:cd01653    2 AVLLFPGFEELELASPLDALREAGAEVDVVSPD----------------GGPVESDVDLDDYDGLILPGGPGTPDDLARD 65

                         90       100
                 ....*....|....*....|....
gi 489955778  86 PLLVETVRQFHLSGRIVAAICAAA 109
Cdd:cd01653   66 EALLALLREAAAAGKPILGICLGA 89
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 27-182 7.44e-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: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 50.23  E-value: 7.44e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  27 RGGIKVTTASVASDGSlAITCSRGVKILADAPLVQVadGDYDIIVLPGGLKGAECFRDSPLLvETVRQFHLSGRIVAAIC 106
Cdd:cd03139   26 RLAAPFEVFLVSETGG-PVSSRSGLTVLPDTSFADP--PDLDVLLVPGGGGTRALVNDPALL-DFIRRQAARAKYVTSVC 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778 107 ------AAAG-------TvlvphdifpiGNMTGFPGLKDTIPEDQwVDKRVVWDPrvNLLTSQGPGTAIDFGLKIIDLLV 173
Cdd:cd03139  102 tgalllAAAGlldgrraT----------THWAAIDWLKEFGAIVV-VDARWVVDG--NIWTSGGVSAGIDMALALVARLF 168


                 ....*....
gi 489955778 174 GREKAYEVA 182
Cdd:cd03139  169 GEELAQAVA 177
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 27-157 1.07e-07

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: 49.57  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  27 RGGIKVTTASVASDGSLAITCSRGVKILADAPLVQVADGDYDIIVLPGGlKGAECFRDSPLLVETVRQFHLSGRIVAAIC 106
Cdd:cd03169   37 KKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDALVIPGG-RAPEYLRLDEKVLAIVRHFAEANKPVAAIC 115

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 489955778 107 AAAgTVLVPHDIFPIGNMTGFPGLKdtiPE-----DQWVDKRVVWDprVNLLTSQG 157
Cdd:cd03169  116 HGP-QILAAAGVLKGRRCTAYPACK---PEvelagGTVVDDGVVVD--GNLVTAQA 165
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 57-172 2.40e-07

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: 49.09  E-value: 2.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  57 APLVQVADGDYDIIVLPGGlKGA-ECFRDSPLLVETVRQFHLSGRIVAAIC-AAAGTVLVPHD----IFPIGNMTGFP-- 128
Cdd:cd03141   81 KKLSDVDPSDYDAIFIPGG-HGPmFDLPDNPDLQDLLREFYENGKVVAAVChGPAALLNVKLSdgksLVAGKTVTGFTne 159

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955778 129 -----GLKDTIP---EDQWVD------KRVVWDPRV----NLLTSQGPGTAIDFGLKIIDLL 172
Cdd:cd03141  160 eeeaaGLKKVVPfllEDELKElganyvKAEPWAEFVvvdgRLITGQNPASAAAVAEALVKAL 221
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 36-186 2.79e-07

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: 48.35  E-value: 2.79e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  36 SVASDGSLAITCSRGVKILADAPLVQVADGDYdIIVLPGGlkGAECFRDSPLLVeTVRQFHLSGRIVAAIC------AAA 109
Cdd:cd03136   36 RVLSLDGAPVTSSNGLRVAPDAALEDAPPLDY-LFVVGGL--GARRAVTPALLA-WLRRAARRGVALGGIDtgafllARA 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778 110 G-------TVLVPHdifpignmtgFPGLKDTIPEDQWVDKRVVWDPRVnlLTSQGPGTAIDFGLKIIDLLVGREKAYEVA 182
Cdd:cd03136  112 GlldgrraTVHWEH----------LEAFAEAFPRVQVTRDLFEIDGDR--LTCAGGTAALDLMLELIARDHGAALAARVA 179


                 ....
gi 489955778 183 SSLV 186
Cdd:cd03136  180 EQFL 183
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 6-109 3.13e-07

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: 46.42  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778   6 LVCLAPGSEETEAVTTIDLLVRGGIKVTTASVAsdgslaitcsrgvkilADAPLVQVADGDYDIIVLPGGLKGAECFRDS 85
Cdd:cd03128    2 AVLLFGGSEELELASPLDALREAGAEVDVVSPD----------------GGPVESDVDLDDYDGLILPGGPGTPDDLAWD 65

                         90       100
                 ....*....|....*....|....
gi 489955778  86 PLLVETVRQFHLSGRIVAAICAAA 109
Cdd:cd03128   66 EALLALLREAAAAGKPVLGICLGA 89
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 36-188 3.71e-05

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


Pssm-ID: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 42.49  E-value: 3.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  36 SVASDGSLAITCSRGVKILADAPLVqvADGDYDIIVLPGGlKGAECFRDSPLLVETVRQFHLSGRIVAAIC------AAA 109
Cdd:cd03137   36 RVCSPEGGPVRSSSGLSLVADAGLD--ALAAADTVIVPGG-PDVDGRPPPPALLAALRRAAARGARVASVCtgafvlAEA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778 110 GtVLvphdifpignmTG----------------FPGLKdtipedqwVDKRV--VWDPRVnlLTSQGPGTAIDFGLKIIDL 171
Cdd:cd03137  113 G-LL-----------DGrratthwayaedlarrFPAVR--------VDPDVlyVDDGNV--WTSAGVTAGIDLCLHLVRE 170

                        170
                 ....*....|....*..
gi 489955778 172 LVGREKAYEVASSLVMA 188
Cdd:cd03137  171 DLGAAVANRVARRLVVP 187
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 66-106 5.32e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase; Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ribonucleotide amidotransferase (FGAR-AT). FGAR-AT catalyzes the ATP-dependent conversion of formylglycinamide ribonucleotide (FGAR) and glutamine to formylglycinamidine ribonucleotide (FGAM), ADP, Pi, and glutamate in the fourth step of the purine biosynthetic pathway. FGAR-AT is a glutamine amidotransferase. Glutamine amidotransferase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. FGAR-AT belongs to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 39.52  E-value: 5.32e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 489955778  66 DYDIIVLPGG------LKGAECFRDSPLLVETVRQFHLSGRIVAAIC 106
Cdd:cd01740   43 DYDGVVLPGGfsygdyLRAGAIAAASPLLMEEVKEFAERGGLVLGIC 89
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 37-182 7.18e-04

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: 38.78  E-value: 7.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778  37 VASDGSlAITCSRGVKILADAPLVQVadGDYDIIVLPG--GLKGAECFRDSPLLVETVRQFHLSGRIVAAIC------AA 108
Cdd:cd03138   43 VSLDGG-PVLLAGGILILPDATLADV--PAPDLVIVPGlgGDPDELLLADNPALIAWLRRQHANGATVAAACtgvfllAE 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489955778 109 AGTvlvphdifpignMTG---------FPGLKDTIPEDQWVDKRVVWDPRvNLLTSQGPGTAIDFGLKIIDLLVGREKAY 179
Cdd:cd03138  120 AGL------------LDGrratthwwlAPQFRRRFPKVRLDPDRVVVTDG-NLITAGGAMAWADLALHLIERLAGPELAQ 186


                 ...
gi 489955778 180 EVA 182
Cdd:cd03138  187 LVA 189
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
58-108 3.14e-03

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 37.07  E-value: 3.14e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489955778  58 PLVQVADGDYDIIVLPGG-----------LKGAECFRDsPLLVETVRQFHLSGRIVAAICAA 108
Cdd:PRK11780  77 DLAEADAEDFDALIVPGGfgaaknlsnfaVKGAECTVN-PDVKALVRAFHQAGKPIGFICIA 137
 
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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