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Conserved domains on  [gi|754790681|ref|WP_042154279|]
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MULTISPECIES: DJ-1/PfpI family protein [Planktothrix]

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 ...
 6-192 2.14e-66

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: 202.00  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   6 VAILIFNGVQLLDFIGPFEVFSITSEIneDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREAL 85
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRL--AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGGGTRALV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  86 NQLQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPqtTVVDNQRFVDNGKIITAGGISAG 165
Cdd:cd03139   79 NDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGA--IVVVDARWVVDGNIWTSGGVSAG 156

                        170       180
                 ....*....|....*....|....*..
gi 754790681 166 IDMSLYVVAKLLGDSKALKTAQYMEYD 192
Cdd:cd03139  157 IDMALALVARLFGEELAQAVALLIEYD 183
 
Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-192 2.14e-66

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: 202.00  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   6 VAILIFNGVQLLDFIGPFEVFSITSEIneDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREAL 85
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRL--AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGGGTRALV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  86 NQLQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPqtTVVDNQRFVDNGKIITAGGISAG 165
Cdd:cd03139   79 NDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGA--IVVVDARWVVDGNIWTSGGVSAG 156

                        170       180
                 ....*....|....*....|....*..
gi 754790681 166 IDMSLYVVAKLLGDSKALKTAQYMEYD 192
Cdd:cd03139  157 IDMALALVARLFGEELAQAVALLIEYD 183
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 5-194 3.61e-45

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: 152.23  E-value: 3.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   5 NVAILIFNGVQLLDFIGPFEVFSITSEINEDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREA 84
Cdd:COG4977    2 RVAFLLLPGFSLLDLAGPLEVFRLANRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  85 LNQlQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDNQRFVDNGKIITAGGISA 164
Cdd:COG4977   82 ADP-ALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 754790681 165 GIDMSLYVVAKLLGDSKALKTAQYMEYDWK 194
Cdd:COG4977  161 GIDLALHLVERDHGAELANAVARRLVVDPR 190
ftrA PRK09393
transcriptional activator FtrA; Provisional
 104-187 3.45e-20

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 86.56  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681 104 ILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDNQRFVDNGKIITAGGISAGIDMSLYVVAKLLGDSKAL 183
Cdd:PRK09393 109 LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAAN 188


                 ....
gi 754790681 184 KTAQ 187
Cdd:PRK09393 189 RVAR 192
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 6-175 3.70e-11

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: 59.19  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681    6 VAILIFNGVQLLDFIGPFEVFSitseiNEDqpFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIP----GGIGT 81
Cdd:pfam01965   3 VLVLLADGFEDIELIYPADVLR-----RAG--IKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVlpggRAGPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   82 REALNQLqILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQamAPQTTVVDnQRFVDNGKIITAGG 161
Cdd:pfam01965  76 RLRDNEK-LVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLI--NAGATYVD-KPVVVDGNLVTSRG 151

                         170
                  ....*....|....
gi 754790681  162 ISAGIDMSLYVVAK 175
Cdd:pfam01965 152 PGDAPEFALEILEQ 165
 
Name Accession Description Interval E-value
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 6-192 2.14e-66

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: 202.00  E-value: 2.14e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   6 VAILIFNGVQLLDFIGPFEVFSITSEIneDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREAL 85
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFGRAPRL--AAPFEVFLVSETGGPVSSRSGLTVLPDTSFADPPDLDVLLVPGGGGTRALV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  86 NQLQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPqtTVVDNQRFVDNGKIITAGGISAG 165
Cdd:cd03139   79 NDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGA--IVVVDARWVVDGNIWTSGGVSAG 156

                        170       180
                 ....*....|....*....|....*..
gi 754790681 166 IDMSLYVVAKLLGDSKALKTAQYMEYD 192
Cdd:cd03139  157 IDMALALVARLFGEELAQAVALLIEYD 183
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-189 2.55e-45

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: 148.80  E-value: 2.55e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   6 VAILIFNGVQLLDFIGPFEVFSITSEINEDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREAL 85
Cdd:cd03137    1 VAVLVFPGVSLLDLSGPAEVFGEANRALGPPAYELRVCSPEGGPVRSSSGLSLVADAGLDALAAADTVIVPGGPDVDGRP 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  86 NQLQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDNQRFVDNGKIITAGGISAG 165
Cdd:cd03137   81 PPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRATTHWAYAEDLARRFPAVRVDPDVLYVDDGNVWTSAGVTAG 160

                        170       180
                 ....*....|....*....|....
gi 754790681 166 IDMSLYVVAKLLGDSKALKTAQYM 189
Cdd:cd03137  161 IDLCLHLVREDLGAAVANRVARRL 184
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 5-194 3.61e-45

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: 152.23  E-value: 3.61e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   5 NVAILIFNGVQLLDFIGPFEVFSITSEINEDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREA 84
Cdd:COG4977    2 RVAFLLLPGFSLLDLAGPLEVFRLANRLAGRPLYRWRLVSLDGGPVRSSSGLTVAPDHGLADLAAADTLIVPGGLDPAAA 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  85 LNQlQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDNQRFVDNGKIITAGGISA 164
Cdd:COG4977   82 ADP-ALLAWLRRAAARGARLASICTGAFLLAAAGLLDGRRATTHWEHADAFAERFPDVRVDPDRLYVDDGDILTSAGGTA 160

                        170       180       190
                 ....*....|....*....|....*....|
gi 754790681 165 GIDMSLYVVAKLLGDSKALKTAQYMEYDWK 194
Cdd:COG4977  161 GIDLALHLVERDHGAELANAVARRLVVDPR 190
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 6-192 9.43e-31

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: 111.58  E-value: 9.43e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   6 VAILIFNGVQLLDFIGPFEVFSITSEINEDQ-----PFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIG 80
Cdd:cd03138    1 VTLLAYPGALASSLAGLLDLLRAANRLARRQqggapPFEVRLVSLDGGPVLLAGGILILPDATLADVPAPDLVIVPGLGG 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  81 TREAL---NQLQILAWIqsKGYHAE--LILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDNQRFVDNGK 155
Cdd:cd03138   81 DPDELllaDNPALIAWL--RRQHANgaTVAAACTGVFLLAEAGLLDGRRATTHWWLAPQFRRRFPKVRLDPDRVVVTDGN 158

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 754790681 156 IITAGGISAGIDMSLYVVAKLLGDSKALKTAQYMEYD 192
Cdd:cd03138  159 LITAGGAMAWADLALHLIERLAGPELAQLVARFLLID 195
ftrA PRK09393
transcriptional activator FtrA; Provisional
 104-187 3.45e-20

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 86.56  E-value: 3.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681 104 ILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDNQRFVDNGKIITAGGISAGIDMSLYVVAKLLGDSKAL 183
Cdd:PRK09393 109 LCSICSGVFVLAAAGLLDGRRATTHWRYAERLQARYPAIRVDPDVLYVDEGQILTSAGSAAGIDLCLHLVRRDFGSEAAN 188


                 ....
gi 754790681 184 KTAQ 187
Cdd:PRK09393 189 RVAR 192
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 6-192 1.30e-18

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: 79.55  E-value: 1.30e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   6 VAILIFNGVQLLDFIGPFEVFSITSEINEDQPFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIPGGIGTREAL 85
Cdd:cd03136    1 FGFLLLPGFSLLALASAIEPLRAANRLAGRELYRWRVLSLDGAPVTSSNGLRVAPDAALEDAPPLDYLFVVGGLGARRAV 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681  86 NQlQILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMAPQTTVVDnQRFVDNGKIITAGGISAG 165
Cdd:cd03136   81 TP-ALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRATVHWEHLEAFAEAFPRVQVTR-DLFEIDGDRLTCAGGTAA 158

                        170       180
                 ....*....|....*....|....*..
gi 754790681 166 IDMSLYVVAKLLGDSKALKTAQYMEYD 192
Cdd:cd03136  159 LDLMLELIARDHGAALAARVAEQFLHD 185
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 6-175 3.70e-11

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: 59.19  E-value: 3.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681    6 VAILIFNGVQLLDFIGPFEVFSitseiNEDqpFNVFLVAETLNSVQCHYGLSFNPDCTLLDSPPPDIIIIP----GGIGT 81
Cdd:pfam01965   3 VLVLLADGFEDIELIYPADVLR-----RAG--IKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVlpggRAGPE 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 754790681   82 REALNQLqILAWIQSKGYHAELILSVCTGALLLAKVGLLDGLVATTHHQALDQLQamAPQTTVVDnQRFVDNGKIITAGG 161
Cdd:pfam01965  76 RLRDNEK-LVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLI--NAGATYVD-KPVVVDGNLVTSRG 151

                         170
                  ....*....|....
gi 754790681  162 ISAGIDMSLYVVAK 175
Cdd:pfam01965 152 PGDAPEFALEILEQ 165
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 103-176 1.29e-03

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: 38.16  E-value: 1.29e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754790681 103 LILSVCTGALLLAKVGLLDGLVATTHHQALDQLQAMApqTTVVDNQRFVDnGKIITAGGISAGIDMSLYVVAKL 176
Cdd:COG0693   99 PVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAG--ATYVDEEVVVD-GNLITSRGPGDAPAFARALLELL 169
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 103-176 3.43e-03

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: 36.76  E-value: 3.43e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 754790681 103 LILSVCTGALLLAKVGLLDGLVATTHHQALDQLQamapQTTVVDnQRFVDNGKIITAGGISAGIDMSLYVVAKL 176
Cdd:cd03135   95 LIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLG----GANYVD-EPVVVDGNIITSRGPGTAFEFALKIVEAL 163
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 107-164 9.61e-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: 35.66  E-value: 9.61e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 754790681 107 VCTGALLLAKVGLLDGLVATTHhqALDQLQAMAPQTT---VVDNQRFVDNGKIITAGGISA 164
Cdd:cd03140   97 ICGATLALARAGLLNNRKHTSN--SLDFLKAHAPYYGgaeYYDEPQAVSDGNLITANGTAP 155
 
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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