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Conserved domains on  [gi|389645642|ref|XP_003720453|]
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DJ-1/PfpI family protein [Pyricularia oryzae 70-15]

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 ...
 12-214 8.32e-44

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: 145.76  E-value: 8.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  12 MGVLL-EGVQISDIMG-IDLIGNLSRKyvsaaqglnpgiarflesAIDLEIFYLAETLAPTEVTPSFKYLPNVTYDDCPr 89
Cdd:cd03139    1 VGILLfPGVEVLDVIGpYEVFGRAPRL------------------AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPP- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  90 DLDLVLIGGNGF---ESQSEASKKFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTNRVAIEFGKQLYPGAEwQDKR 166
Cdd:cd03139   62 DLDVLLVPGGGGtraLVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVV-VDAR 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 389645642 167 WVVEdkvyegqgkGELWTGGAAGAGLDMVTEWCFQNFDKDFVNALSTY 214
Cdd:cd03139  141 WVVD---------GNIWTSGGVSAGIDMALALVARLFGEELAQAVALL 179
 
Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 12-214 8.32e-44

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: 145.76  E-value: 8.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  12 MGVLL-EGVQISDIMG-IDLIGNLSRKyvsaaqglnpgiarflesAIDLEIFYLAETLAPTEVTPSFKYLPNVTYDDCPr 89
Cdd:cd03139    1 VGILLfPGVEVLDVIGpYEVFGRAPRL------------------AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPP- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  90 DLDLVLIGGNGF---ESQSEASKKFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTNRVAIEFGKQLYPGAEwQDKR 166
Cdd:cd03139   62 DLDVLLVPGGGGtraLVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVV-VDAR 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 389645642 167 WVVEdkvyegqgkGELWTGGAAGAGLDMVTEWCFQNFDKDFVNALSTY 214
Cdd:cd03139  141 WVVD---------GNIWTSGGVSAGIDMALALVARLFGEELAQAVALL 179
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 14-194 3.12e-09

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: 56.32  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  14 VLLEGVQISDIMGidlignlsrkyvsAAQGLnpGIARFLESAIDLEIFYLAETLAPTEVTPSFKYLPNVTYDDCPRdLDL 93
Cdd:COG4977    6 LLLPGFSLLDLAG-------------PLEVF--RLANRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAA-ADT 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  94 VLI-GGNGFESQ-SEASKKFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTN-RVAIEFgKQLYPGAEWQDKRWVVE 170
Cdd:COG4977   70 LIVpGGLDPAAAaDPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHwEHADAF-AERFPDVRVDPDRLYVD 148

                        170       180
                 ....*....|....*....|....
gi 389645642 171 DkvyegqgkGELWTGGAAGAGLDM 194
Cdd:COG4977  149 D--------GDILTSAGGTAGIDL 164
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 57-182 5.42e-07

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: 48.02  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642   57 DLEIFYLAETLA-----PTEVTPS---------FKYLPNVTYDDC-PRDLD-LVLIGGNG---FESQSEASKKFIREAWP 117
Cdd:pfam01965  13 DIELIYPADVLRragikVTVVSVDggevkgsrgVKVTVDASLDDVkPDDYDaLVLPGGRAgpeRLRDNEKLVEFVKDFYE 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 389645642  118 KTRVWMTTCVGTLWLASAVDLTGLKVTTNRVAieFGKQLYPGAEWQDKRWVVEDKVYEGQGKGEL 182
Cdd:pfam01965  93 KGKPVAAICHGPQVLAAAGVLKGRKVTSHPAV--KDDLINAGATYVDKPVVVDGNLVTSRGPGDA 155
 
Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 12-214 8.32e-44

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: 145.76  E-value: 8.32e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  12 MGVLL-EGVQISDIMG-IDLIGNLSRKyvsaaqglnpgiarflesAIDLEIFYLAETLAPTEVTPSFKYLPNVTYDDCPr 89
Cdd:cd03139    1 VGILLfPGVEVLDVIGpYEVFGRAPRL------------------AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPP- 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  90 DLDLVLIGGNGF---ESQSEASKKFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTNRVAIEFGKQLYPGAEwQDKR 166
Cdd:cd03139   62 DLDVLLVPGGGGtraLVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVV-VDAR 140

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 389645642 167 WVVEdkvyegqgkGELWTGGAAGAGLDMVTEWCFQNFDKDFVNALSTY 214
Cdd:cd03139  141 WVVD---------GNIWTSGGVSAGIDMALALVARLFGEELAQAVALL 179
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 14-194 3.12e-09

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: 56.32  E-value: 3.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  14 VLLEGVQISDIMGidlignlsrkyvsAAQGLnpGIARFLESAIDLEIFYLAETLAPTEVTPSFKYLPNVTYDDCPRdLDL 93
Cdd:COG4977    6 LLLPGFSLLDLAG-------------PLEVF--RLANRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAA-ADT 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  94 VLI-GGNGFESQ-SEASKKFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTN-RVAIEFgKQLYPGAEWQDKRWVVE 170
Cdd:COG4977   70 LIVpGGLDPAAAaDPALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHwEHADAF-AERFPDVRVDPDRLYVD 148

                        170       180
                 ....*....|....*....|....
gi 389645642 171 DkvyegqgkGELWTGGAAGAGLDM 194
Cdd:COG4977  149 D--------GDILTSAGGTAGIDL 164
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 57-182 5.42e-07

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: 48.02  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642   57 DLEIFYLAETLA-----PTEVTPS---------FKYLPNVTYDDC-PRDLD-LVLIGGNG---FESQSEASKKFIREAWP 117
Cdd:pfam01965  13 DIELIYPADVLRragikVTVVSVDggevkgsrgVKVTVDASLDDVkPDDYDaLVLPGGRAgpeRLRDNEKLVEFVKDFYE 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 389645642  118 KTRVWMTTCVGTLWLASAVDLTGLKVTTNRVAieFGKQLYPGAEWQDKRWVVEDKVYEGQGKGEL 182
Cdd:pfam01965  93 KGKPVAAICHGPQVLAAAGVLKGRKVTSHPAV--KDDLINAGATYVDKPVVVDGNLVTSRGPGDA 155
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 14-195 6.83e-07

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: 48.41  E-value: 6.83e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  14 VLLEGVQISDIMGI-DLIGNLSRkyvsAAQGLNPGIARFlesaidlEIFYLAETLAPTEVTPSFKYLPNVTYDDCPrDLD 92
Cdd:cd03138    4 LAYPGALASSLAGLlDLLRAANR----LARRQQGGAPPF-------EVRLVSLDGGPVLLAGGILILPDATLADVP-APD 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  93 LVLIGGNGFESQSEASKKF------IREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTN-RVAIEFgKQLYPGAEWQDK 165
Cdd:cd03138   72 LVIVPGLGGDPDELLLADNpaliawLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHwWLAPQF-RRRFPKVRLDPD 150

                        170       180       190
                 ....*....|....*....|....*....|
gi 389645642 166 RWVVEDkvyegqgkGELWTGGAAGAGLDMV 195
Cdd:cd03138  151 RVVVTD--------GNLITAGGAMAWADLA 172
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 88-194 4.13e-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: 153231 [Multi-domain]  Cd Length: 187  Bit Score: 40.18  E-value: 4.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  88 PRDLDLVLI-GGNGFESQSEASK--KFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTN-RVAIEFgKQLYPGAEWQ 163
Cdd:cd03137   62 LAAADTVIVpGGPDVDGRPPPPAllAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHwAYAEDL-ARRFPAVRVD 140

                         90       100       110
                 ....*....|....*....|....*....|.
gi 389645642 164 DKRWVVEDkvyegqgkGELWTGGAAGAGLDM 194
Cdd:cd03137  141 PDVLYVDD--------GNVWTSAGVTAGIDL 163
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 76-172 2.62e-03

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: 37.59  E-value: 2.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 389645642  76 FKYLPNVTYDDCPR-DLD-LVLIGGNGFES-QSEASKKFIREAWPKTRVWMTTCVGTLWLASAVDLTGLKVTTNrvAIEF 152
Cdd:cd03140   45 LRVVPDYSLDDLPPeDYDlLILPGGDSWDNpEAPDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSN--SLDF 122

                         90       100
                 ....*....|....*....|...
gi 389645642 153 GKQ---LYPGAEWQDKRWVVEDK 172
Cdd:cd03140  123 LKAhapYYGGAEYYDEPQAVSDG 145
 
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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