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Conserved domains on  [gi|507053872|ref|WP_016124827|]
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DJ-1/PfpI family protein [Bacillus cereus]

Protein Classification

DJ-1/PfpI family protein( domain architecture ID 10123420)

DJ-1/PfpI family protein similar to Pseudomonas putida isonitrile hydratase, which catalyzes the hydration of cyclohexyl isocyanide to N-cyclohexylformamide and is involved in detoxification

EC:  4.2.1.-
Gene Ontology:  GO:0016829
PubMed:  15070401

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 3-192 2.27e-57

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: 178.89  E-value: 2.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVLKRAIEEGAPFTIEFVSsEQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGGwnhkaeh 82
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFLVS-ETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGG------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  83 GARKQAELGTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHY-RIADQGDVITARG 161
Cdd:cd03139   73 GTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDaRWVVDGNIWTSGG 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 507053872 162 VTSGVDLGLWITERFASPKIAAAVEYRMEYE 192
Cdd:cd03139  153 VSAGIDMALALVARLFGEELAQAVALLIEYD 183
 
Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 3-192 2.27e-57

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: 178.89  E-value: 2.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVLKRAIEEGAPFTIEFVSsEQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGGwnhkaeh 82
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFLVS-ETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGG------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  83 GARKQAELGTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHY-RIADQGDVITARG 161
Cdd:cd03139   73 GTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDaRWVVDGNIWTSGG 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 507053872 162 VTSGVDLGLWITERFASPKIAAAVEYRMEYE 192
Cdd:cd03139  153 VSAGIDMALALVARLFGEELAQAVALLIEYD 183
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 1-194 6.94e-29

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: 109.09  E-value: 6.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   1 MKIQIVLFDGFgELVSFA-PFEVLKRA--IEEGAPFTIEFVSsEQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGGwn 77
Cdd:COG4977    1 LRVAFLLLPGF-SLLDLAgPLEVFRLAnrLAGRPLYRWRLVS-LDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGL-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  78 hkaEHGARKQAELgtlTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEY--GAELLHYRIA-DQG 154
Cdd:COG4977   77 ---DPAAAADPAL---LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERfpDVRVDPDRLYvDDG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 507053872 155 DVITARGVTSGVDLGLWITERFASPKIAAAVEYRMEYERR 194
Cdd:COG4977  151 DILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPR 190
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-175 6.00e-22

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: 87.31  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872    1 MKIQIVLFDGFGELVSFAPFEVLKRAieeGAPFTiefVSSEQKQEVTTSFGVTV---KLYDFLRMDNrPDLLIVPGG-GW 76
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRA---GIKVT---VVSVDGGEVKGSRGVKVtvdASLDDVKPDD-YDALVLPGGrAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   77 NHKAehgaRKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHYRIADQGDV 156
Cdd:pfam01965  74 PERL----RDNEKLVEFVK---DFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNL 146

                         170
                  ....*....|....*....
gi 507053872  157 ITARGVTSGVDLGLWITER 175
Cdd:pfam01965 147 VTSRGPGDAPEFALEILEQ 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 2-177 1.76e-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: 62.43  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872    2 KIQIVLFDGFGELVSFAPFEVLKraiEEGAPFTIefvSSEQKQEVTTSFGVTVKL---YDFLRMDNRpDLLIVPGGgwnH 78
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLR---EAGHEVDT---VSKEAGTTVGKHGYSVTVdatIDEVNPEEY-DALVIPGG---R 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   79 KAEHgARKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHYRIA-DQGDVI 157
Cdd:TIGR01382  71 APEY-LRLNNKAVRLVR---EFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVvVDGNLV 146

                         170       180
                  ....*....|....*....|
gi 507053872  158 TARgvtSGVDLGLWITERFA 177
Cdd:TIGR01382 147 TSR---VPDDLPAFNREFLK 163
ftrA PRK09393
transcriptional activator FtrA; Provisional
 51-189 6.98e-11

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 59.98  E-value: 6.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  51 GVTVKLYDFLRMDNRPDLLIVPGggWnhkaehgaRKQAEL--GTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKA 128
Cdd:PRK09393  61 GITVVADGGLELLDRADTIVIPG--W--------RGPDAPvpEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRA 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872 129 TMHYLAQDEMSEygaellHY---RI------ADQGDVITARGVTSGVDLGLWITERFASPKIAAAVEYRM 189
Cdd:PRK09393 131 TTHWRYAERLQA------RYpaiRVdpdvlyVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRL 194
 
Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 3-192 2.27e-57

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: 178.89  E-value: 2.27e-57
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVLKRAIEEGAPFTIEFVSsEQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGGwnhkaeh 82
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRLAAPFEVFLVS-ETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGG------- 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  83 GARKQAELGTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHY-RIADQGDVITARG 161
Cdd:cd03139   73 GTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDaRWVVDGNIWTSGG 152

                        170       180       190
                 ....*....|....*....|....*....|.
gi 507053872 162 VTSGVDLGLWITERFASPKIAAAVEYRMEYE 192
Cdd:cd03139  153 VSAGIDMALALVARLFGEELAQAVALLIEYD 183
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 3-186 3.06e-29

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: 107.35  E-value: 3.06e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVL-------KRAIEEGAPFTIEFVSSeQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGG 75
Cdd:cd03138    1 VTLLAYPGALASSLAGLLDLLraanrlaRRQQGGAPPFEVRLVSL-DGGPVLLAGGILILPDATLADVPAPDLVIVPGLG 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  76 WNHkAEHGARKQAELGTltkMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSE-YGAELLHY--RIAD 152
Cdd:cd03138   80 GDP-DELLLADNPALIA---WLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRrFPKVRLDPdrVVVT 155

                        170       180       190
                 ....*....|....*....|....*....|....
gi 507053872 153 QGDVITARGVTSGVDLGLWITERFASPKIAAAVE 186
Cdd:cd03138  156 DGNLITAGGAMAWADLALHLIERLAGPELAQLVA 189
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 1-194 6.94e-29

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: 109.09  E-value: 6.94e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   1 MKIQIVLFDGFgELVSFA-PFEVLKRA--IEEGAPFTIEFVSsEQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGGwn 77
Cdd:COG4977    1 LRVAFLLLPGF-SLLDLAgPLEVFRLAnrLAGRPLYRWRLVS-LDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGL-- 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  78 hkaEHGARKQAELgtlTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEY--GAELLHYRIA-DQG 154
Cdd:COG4977   77 ---DPAAAADPAL---LAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERfpDVRVDPDRLYvDDG 150

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 507053872 155 DVITARGVTSGVDLGLWITERFASPKIAAAVEYRMEYERR 194
Cdd:COG4977  151 DILTSAGGTAGIDLALHLVERDHGAELANAVARRLVVDPR 190
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 3-189 9.05e-25

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: 95.26  E-value: 9.05e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVLKRAIEE--GAPFTIEFVSSEQkQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGgwnhka 80
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRAlgPPAYELRVCSPEG-GPVRSSSGLSLVADAGLDALAAADTVIVPGG------ 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  81 eHGARKQAELGTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEygaelLHYRIA--------D 152
Cdd:cd03137   74 -PDVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLAR-----RFPAVRvdpdvlyvD 147

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 507053872 153 QGDVITARGVTSGVDLGLWITERFASPKIAAAVEYRM 189
Cdd:cd03137  148 DGNVWTSAGVTAGIDLCLHLVREDLGAAVANRVARRL 184
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-175 6.00e-22

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: 87.31  E-value: 6.00e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872    1 MKIQIVLFDGFGELVSFAPFEVLKRAieeGAPFTiefVSSEQKQEVTTSFGVTV---KLYDFLRMDNrPDLLIVPGG-GW 76
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRA---GIKVT---VVSVDGGEVKGSRGVKVtvdASLDDVKPDD-YDALVLPGGrAG 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   77 NHKAehgaRKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHYRIADQGDV 156
Cdd:pfam01965  74 PERL----RDNEKLVEFVK---DFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNL 146

                         170
                  ....*....|....*....
gi 507053872  157 ITARGVTSGVDLGLWITER 175
Cdd:pfam01965 147 VTSRGPGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-161 2.08e-18

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: 78.22  E-value: 2.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   1 MKIQIVLFDGF--GELVsfAPFEVLKRAieegaPFTIEFVSSEQKQEVTTSFGVTVKLY---------DFlrmdnrpDLL 69
Cdd:COG0693    3 KKVLILLTDGFedEELT--VPYDALREA-----GAEVDVASPEGGPPVTSKHGITVTADktlddvdpdDY-------DAL 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  70 IVPGGgwnhkaeHGA----RKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAEL 145
Cdd:COG0693   69 VLPGG-------HGApddlREDPDVVALVR---EFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATY 138

                        170
                 ....*....|....*..
gi 507053872 146 LHYR-IADqGDVITARG 161
Cdd:COG0693  139 VDEEvVVD-GNLITSRG 154
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 5-185 7.74e-16

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: 71.85  E-value: 7.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   5 IVLFDGFgELVSFAPF-EVLKRA--IEEGAPFTIEFVSsEQKQEVTTSFGVTVKLYDFLRMDNRPDLLIVPGGgWNHKAE 81
Cdd:cd03136    3 FLLLPGF-SLLALASAiEPLRAAnrLAGRELYRWRVLS-LDGAPVTSSNGLRVAPDAALEDAPPLDYLFVVGG-LGARRA 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  82 HGARKQAELGTLtkmisemHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEY--GAELLHYRIADQGDVITA 159
Cdd:cd03136   80 VTPALLAWLRRA-------ARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAfpRVQVTRDLFEIDGDRLTC 152

                        170       180
                 ....*....|....*....|....*.
gi 507053872 160 RGVTSGVDLGLWITERFASPKIAAAV 185
Cdd:cd03136  153 AGGTAALDLMLELIARDHGAALAARV 178
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 5-176 2.10e-15

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: 70.28  E-value: 2.10e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   5 IVLFDGFGELVSFAPFEVLKRAieegaPFTIEFVSSEQKQEVTTSFGVTVK----LYDFLRMDnrPDLLIVPGGGwnhka 80
Cdd:cd03135    3 VILADGFEEIEAVTPVDVLRRA-----GIEVTTASLEKKLAVGSSHGIKVKadktLSDVNLDD--YDAIVIPGGL----- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  81 eHGARKQAELGTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMS--EYGAELLHYriaDqGDVIT 158
Cdd:cd03135   71 -PGAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLGgaNYVDEPVVV---D-GNIIT 145

                        170
                 ....*....|....*...
gi 507053872 159 ARGVTSGVDLGLWITERF 176
Cdd:cd03135  146 SRGPGTAFEFALKIVEAL 163
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 5-161 8.75e-14

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: 66.09  E-value: 8.75e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   5 IVLFDGFGelvsFAPFEV--LKRAIEEGAPFTIEFVSSeQKQEVTTSFGVTVK---LYDFLRMDNrPDLLIVPGG-GWNH 78
Cdd:cd03140    1 IAVFLTDE----FADWEGayLAALLNSYEGFEVRTVSP-TGEPVTSIGGLRVVpdySLDDLPPED-YDLLILPGGdSWDN 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  79 KaEHGArkqaelgtLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHYRIADQ----G 154
Cdd:cd03140   75 P-EAPD--------LAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSNSLDFLKAHAPYYGGAEYYDEPQavsdG 145


                 ....*..
gi 507053872 155 DVITARG 161
Cdd:cd03140  146 NLITANG 152
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 2-177 1.76e-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: 62.43  E-value: 1.76e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872    2 KIQIVLFDGFGELVSFAPFEVLKraiEEGAPFTIefvSSEQKQEVTTSFGVTVKL---YDFLRMDNRpDLLIVPGGgwnH 78
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLR---EAGHEVDT---VSKEAGTTVGKHGYSVTVdatIDEVNPEEY-DALVIPGG---R 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   79 KAEHgARKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHYRIA-DQGDVI 157
Cdd:TIGR01382  71 APEY-LRLNNKAVRLVR---EFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVvVDGNLV 146

                         170       180
                  ....*....|....*....|
gi 507053872  158 TARgvtSGVDLGLWITERFA 177
Cdd:TIGR01382 147 TSR---VPDDLPAFNREFLK 163
ftrA PRK09393
transcriptional activator FtrA; Provisional
 51-189 6.98e-11

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 59.98  E-value: 6.98e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  51 GVTVKLYDFLRMDNRPDLLIVPGggWnhkaehgaRKQAEL--GTLTKMISEMHNAGTIVAGVCTGGMLLAASGILNGRKA 128
Cdd:PRK09393  61 GITVVADGGLELLDRADTIVIPG--W--------RGPDAPvpEPLLEALRAAHARGARLCSICSGVFVLAAAGLLDGRRA 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872 129 TMHYLAQDEMSEygaellHY---RI------ADQGDVITARGVTSGVDLGLWITERFASPKIAAAVEYRM 189
Cdd:PRK09393 131 TTHWRYAERLQA------RYpaiRVdpdvlyVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAANRVARRL 194
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 2-160 3.74e-10

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: 56.01  E-value: 3.74e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   2 KIQIVLFDGFGELVSFAPFEVLKraiEEGApfTIEFVSSEQKQEVTTSFGVT----------VKLYDFlrmdnrpDLLIV 71
Cdd:cd03134    1 KVAILAADGFEDVELTYPLYRLR---EAGA--EVVVAGPEAGGEIQGKHGYDtvtvdltiadVDADDY-------DALVI 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  72 PGGgWNhkAEHgARKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELLHYRIA 151
Cdd:cd03134   69 PGG-TN--PDK-LRRDPDAVAFVR---AFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVV 141


                 ....*....
gi 507053872 152 DQGDVITAR 160
Cdd:cd03134  142 VDGNLITSR 150
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-117 8.88e-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: 48.75  E-value: 8.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVLKRAieegaPFTIEFVSSEQKQEVTtsfgvtvklydfLRMDNRPDLLIVPGGGWNHKAEH 82
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREA-----GAEVDVVSPDGGPVES------------DVDLDDYDGLILPGGPGTPDDLA 63

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 507053872  83 GARKQAELgtltkmISEMHNAGTIVAGVCTGGMLL 117
Cdd:cd01653   64 RDEALLAL------LREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-117 2.08e-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: 47.20  E-value: 2.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872   3 IQIVLFDGFGELVSFAPFEVLKRAieegaPFTIEFVSSEQKQEVTtsfgvtvklydfLRMDNRPDLLIVPGGGWNHKAEH 82
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREA-----GAEVDVVSPDGGPVES------------DVDLDDYDGLILPGGPGTPDDLA 63

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 507053872  83 GARKQAELgtltkmISEMHNAGTIVAGVCTGGMLL 117
Cdd:cd03128   64 WDEALLAL------LREAAAAGKPVLGICLGAQLL 92
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 67-161 5.11e-04

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: 39.17  E-value: 5.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 507053872  67 DLLIVPGGgwnhKAEHGARKQAELGTLTKmisEMHNAGTIVAGVCTGGMLLAASGILNGRKATMHYLAQDEMSEYGAELL 146
Cdd:cd03169   78 DALVIPGG----RAPEYLRLDEKVLAIVR---HFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVV 150

                         90
                 ....*....|....*
gi 507053872 147 HYRIADQGDVITARG 161
Cdd:cd03169  151 DDGVVVDGNLVTAQA 165
 
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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