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Conserved domains on  [gi|30687679|ref|NP_850303|]
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Class I glutamine amidotransferase-like superfamily protein [Arabidopsis thaliana]

Protein Classification

DJ-1/PfpI family protein( domain architecture ID 10123587)

DJ-1/PfpI family protein such as Arabidopsis thaliana DJ-1 homolog D, which shows glyoxalase I activity, catalyzing the conversion of hemimercaptal, formed from methylglyoxal and glutathione, to S-lactoylglutathione

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 211-392 6.93e-78

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: 238.32  E-value: 6.93e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 211 SVLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKGEVCATAVYDLEdGRQIPAEKRGHNFFVTASWDDICVDDYDC 290
Cdd:cd03169   1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFP-GWQTYTEKPGHRFAVTADFDEVDPDDYDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 291 VVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEkGCVTDG 370
Cdd:cd03169  80 LVIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDD-GVVVDG 158

                       170       180
                ....*....|....*....|..
gi 30687679 371 KVVTAASATDLPAFLFDLSTAL 392
Cdd:cd03169 159 NLVTAQAWPDHPAFLREFLKLL 180
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 10-198 4.26e-72

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: 223.29  E-value: 4.26e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRCVMSAHDFLGLELYTELVVDQLTLNANFDDVTPENYDVIII 89
Cdd:cd03169   3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDALVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  90 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILaGGVKCTAFESIKPLIELSGGEWwqqpgiqsmfEI 169
Cdd:cd03169  83 PGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVL-KGRRCTAYPACKPEVELAGGTV----------VD 151

                       170       180
                ....*....|....*....|....*....
gi 30687679 170 TDCVKDGNFMSTVGWPTLGHGIKLLLESL 198
Cdd:cd03169 152 DGVVVDGNLVTAQAWPDHPAFLREFLKLL 180
 
Name Accession Description Interval E-value
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 211-392 6.93e-78

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: 238.32  E-value: 6.93e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 211 SVLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKGEVCATAVYDLEdGRQIPAEKRGHNFFVTASWDDICVDDYDC 290
Cdd:cd03169   1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFP-GWQTYTEKPGHRFAVTADFDEVDPDDYDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 291 VVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEkGCVTDG 370
Cdd:cd03169  80 LVIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDD-GVVVDG 158

                       170       180
                ....*....|....*....|..
gi 30687679 371 KVVTAASATDLPAFLFDLSTAL 392
Cdd:cd03169 159 NLVTAQAWPDHPAFLREFLKLL 180
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 10-198 4.26e-72

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: 223.29  E-value: 4.26e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRCVMSAHDFLGLELYTELVVDQLTLNANFDDVTPENYDVIII 89
Cdd:cd03169   3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDALVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  90 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILaGGVKCTAFESIKPLIELSGGEWwqqpgiqsmfEI 169
Cdd:cd03169  83 PGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVL-KGRRCTAYPACKPEVELAGGTV----------VD 151

                       170       180
                ....*....|....*....|....*....
gi 30687679 170 TDCVKDGNFMSTVGWPTLGHGIKLLLESL 198
Cdd:cd03169 152 DGVVVDGNLVTAQAWPDHPAFLREFLKLL 180
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 210-391 2.07e-52

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: 172.06  E-value: 2.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   210 ASVLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKkkGEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYD 289
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDG--GEV---------------KGSRGVKVTVDASLDDVKPDDYD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   290 CVVVPGGRS-PELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVkVAGGEAVMEKGCVT 368
Cdd:pfam01965  64 ALVLPGGRAgPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDL-INAGATYVDKPVVV 142

                         170       180
                  ....*....|....*....|...
gi 30687679   369 DGKVVTAASATDLPAFLFDLSTA 391
Cdd:pfam01965 143 DGNLVTSRGPGDAPEFALEILEQ 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 212-393 3.73e-37

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: 132.54  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTpnKKKGEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYDCV 291
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTT---------------VGKHGYSVTVDATIDEVNPEEYDAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   292 VVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEKGCVTDGK 371
Cdd:TIGR01382  65 VIPGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGN 144

                         170       180
                  ....*....|....*....|..
gi 30687679   372 VVTAASATDLPAFLFDLSTALG 393
Cdd:TIGR01382 145 LVTSRVPDDLPAFNREFLKLLG 166
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 212-393 1.58e-35

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: 128.30  E-value: 1.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKgEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYDCV 291
Cdd:COG0693   5 VLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGP-PV---------------TSKHGITVTADKTLDDVDPDDYDAL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 292 VVPGGR-SPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEaVMEKGCVTDG 370
Cdd:COG0693  69 VLPGGHgAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGAT-YVDEEVVVDG 147

                       170       180
                ....*....|....*....|...
gi 30687679 371 KVVTAASATDLPAFLFDLSTALG 393
Cdd:COG0693 148 NLITSRGPGDAPAFARALLELLA 170
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 7-199 1.49e-27

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: 107.11  E-value: 1.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   7 KSALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNrnaGDRCVMSAHDflglelytelvvDQLTLNANFDDVTPENYDV 86
Cdd:COG0693   3 KKVLILLTDGFEDEELTVPYDALREAGAEVDVASPE---GGPPVTSKHG------------ITVTADKTLDDVDPDDYDA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  87 IIIPGGRFT-ELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAgGVKCTAFESIKPLIELSGGEWWQQPgiqs 165
Cdd:COG0693  68 LVLPGGHGApDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLK-GRKVTSFPNIEDDLKNAGATYVDEE---- 142

                       170       180       190
                ....*....|....*....|....*....|....
gi 30687679 166 mfeitdCVKDGNFMSTVGWPTLGHGIKLLLESLG 199
Cdd:COG0693 143 ------VVVDGNLITSRGPGDAPAFARALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 7-187 3.42e-27

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: 105.80  E-value: 3.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679     7 KSALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNrnagDRCVMSAHDFlglelytelvvdQLTLNANFDDVTPENYDV 86
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVD----GGEVKGSRGV------------KVTVDASLDDVKPDDYDA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679    87 IIIPGGR-FTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPLIELSGGEWWQQPgiqs 165
Cdd:pfam01965  65 LVLPGGRaGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGR-KVTSHPAVKDDLINAGATYVDKP---- 139

                         170       180
                  ....*....|....*....|..
gi 30687679   166 mfeitdCVKDGNFMSTVGWPTL 187
Cdd:pfam01965 140 ------VVVDGNLVTSRGPGDA 155
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 10-180 4.75e-26

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: 102.88  E-value: 4.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679    10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSpnRNAGDRCVMSAHdflglelytelvvdQLTLNANFDDVTPENYDVIII 89
Cdd:TIGR01382   3 LVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTTVGKHGY--------------SVTVDATIDEVNPEEYDALVI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679    90 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPLIELSGGEWWQQPGIqsmfei 169
Cdd:TIGR01382  67 PGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGK-KLTSYPAIIDDVKNAGAEYVDIEVV------ 139

                         170
                  ....*....|.
gi 30687679   170 tdcVKDGNFMS 180
Cdd:TIGR01382 140 ---VVDGNLVT 147
 
Name Accession Description Interval E-value
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 211-392 6.93e-78

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: 238.32  E-value: 6.93e-78
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 211 SVLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKGEVCATAVYDLEdGRQIPAEKRGHNFFVTASWDDICVDDYDC 290
Cdd:cd03169   1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFP-GWQTYTEKPGHRFAVTADFDEVDPDDYDA 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 291 VVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEkGCVTDG 370
Cdd:cd03169  80 LVIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDD-GVVVDG 158

                       170       180
                ....*....|....*....|..
gi 30687679 371 KVVTAASATDLPAFLFDLSTAL 392
Cdd:cd03169 159 NLVTAQAWPDHPAFLREFLKLL 180
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 10-198 4.26e-72

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: 223.29  E-value: 4.26e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRCVMSAHDFLGLELYTELVVDQLTLNANFDDVTPENYDVIII 89
Cdd:cd03169   3 LILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKGDTVVTAIHDFPGWQTYTEKPGHRFAVTADFDEVDPDDYDALVI 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  90 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILaGGVKCTAFESIKPLIELSGGEWwqqpgiqsmfEI 169
Cdd:cd03169  83 PGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVL-KGRRCTAYPACKPEVELAGGTV----------VD 151

                       170       180
                ....*....|....*....|....*....
gi 30687679 170 TDCVKDGNFMSTVGWPTLGHGIKLLLESL 198
Cdd:cd03169 152 DGVVVDGNLVTAQAWPDHPAFLREFLKLL 180
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 210-391 2.07e-52

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: 172.06  E-value: 2.07e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   210 ASVLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKkkGEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYD 289
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDG--GEV---------------KGSRGVKVTVDASLDDVKPDDYD 63

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   290 CVVVPGGRS-PELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVkVAGGEAVMEKGCVT 368
Cdd:pfam01965  64 ALVLPGGRAgPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDL-INAGATYVDKPVVV 142

                         170       180
                  ....*....|....*....|...
gi 30687679   369 DGKVVTAASATDLPAFLFDLSTA 391
Cdd:pfam01965 143 DGNLVTSRGPGDAPEFALEILEQ 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 212-393 3.73e-37

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: 132.54  E-value: 3.73e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTpnKKKGEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYDCV 291
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTT---------------VGKHGYSVTVDATIDEVNPEEYDAL 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   292 VVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVMEKGCVTDGK 371
Cdd:TIGR01382  65 VIPGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGN 144

                         170       180
                  ....*....|....*....|..
gi 30687679   372 VVTAASATDLPAFLFDLSTALG 393
Cdd:TIGR01382 145 LVTSRVPDDLPAFNREFLKLLG 166
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 212-393 1.58e-35

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: 128.30  E-value: 1.58e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKgEVcatavydledgrqipAEKRGHNFFVTASWDDICVDDYDCV 291
Cdd:COG0693   5 VLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGP-PV---------------TSKHGITVTADKTLDDVDPDDYDAL 68

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 292 VVPGGR-SPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEaVMEKGCVTDG 370
Cdd:COG0693  69 VLPGGHgAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGAT-YVDEEVVVDG 147

                       170       180
                ....*....|....*....|...
gi 30687679 371 KVVTAASATDLPAFLFDLSTALG 393
Cdd:COG0693 148 NLITSRGPGDAPAFARALLELLA 170
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 212-384 7.45e-34

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: 123.81  E-value: 7.45e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTPnKKKGEVCAtavydledgrqipaeKRGHN-FFVTASWDDICVDDYDC 290
Cdd:cd03134   2 VAILAADGFEDVELTYPLYRLREAGAEVVVAGP-EAGGEIQG---------------KHGYDtVTVDLTIADVDADDYDA 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 291 VVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVMVKVAGGEAVmEKGCVTDG 370
Cdd:cd03134  66 LVIPGGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWV-DEEVVVDG 144

                       170
                ....*....|....
gi 30687679 371 KVVTAASATDLPAF 384
Cdd:cd03134 145 NLITSRNPDDLPAF 158
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 7-199 1.49e-27

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: 107.11  E-value: 1.49e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   7 KSALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNrnaGDRCVMSAHDflglelytelvvDQLTLNANFDDVTPENYDV 86
Cdd:COG0693   3 KKVLILLTDGFEDEELTVPYDALREAGAEVDVASPE---GGPPVTSKHG------------ITVTADKTLDDVDPDDYDA 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  87 IIIPGGRFT-ELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAgGVKCTAFESIKPLIELSGGEWWQQPgiqs 165
Cdd:COG0693  68 LVLPGGHGApDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLK-GRKVTSFPNIEDDLKNAGATYVDEE---- 142

                       170       180       190
                ....*....|....*....|....*....|....
gi 30687679 166 mfeitdCVKDGNFMSTVGWPTLGHGIKLLLESLG 199
Cdd:COG0693 143 ------VVVDGNLITSRGPGDAPAFARALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 7-187 3.42e-27

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: 105.80  E-value: 3.42e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679     7 KSALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNrnagDRCVMSAHDFlglelytelvvdQLTLNANFDDVTPENYDV 86
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVD----GGEVKGSRGV------------KVTVDASLDDVKPDDYDA 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679    87 IIIPGGR-FTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPLIELSGGEWWQQPgiqs 165
Cdd:pfam01965  65 LVLPGGRaGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGR-KVTSHPAVKDDLINAGATYVDKP---- 139

                         170       180
                  ....*....|....*....|..
gi 30687679   166 mfeitdCVKDGNFMSTVGWPTL 187
Cdd:pfam01965 140 ------VVVDGNLVTSRGPGDA 155
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 10-180 4.75e-26

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: 102.88  E-value: 4.75e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679    10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSpnRNAGDRCVMSAHdflglelytelvvdQLTLNANFDDVTPENYDVIII 89
Cdd:TIGR01382   3 LVLTTDEFEDSELLYPLDRLREAGHEVDTVS--KEAGTTVGKHGY--------------SVTVDATIDEVNPEEYDALVI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679    90 PGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPLIELSGGEWWQQPGIqsmfei 169
Cdd:TIGR01382  67 PGGRAPEYLRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGK-KLTSYPAIIDDVKNAGAEYVDIEVV------ 139

                         170
                  ....*....|.
gi 30687679   170 tdcVKDGNFMS 180
Cdd:TIGR01382 140 ---VVDGNLVT 147
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 9-180 7.77e-21

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: 88.37  E-value: 7.77e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   9 ALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDRcvmsahdflGLELYTELVVDqltlnANFDDVTPENYDVII 88
Cdd:cd03134   2 VAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQ---------GKHGYDTVTVD-----LTIADVDADDYDALV 67

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  89 IPGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAgGVKCTAFESIKPLIELSGGEWWQQpgiqsmfe 168
Cdd:cd03134  68 IPGGTNPDKLRRDPDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVR-GRKLTSYPSIKDDLINAGANWVDE-------- 138

                       170
                ....*....|..
gi 30687679 169 itDCVKDGNFMS 180
Cdd:cd03134 139 --EVVVDGNLIT 148
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 278-392 2.81e-13

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: 67.19  E-value: 2.81e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 278 ASWDDICVDDYDCVVVPGGRS-PELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKR--CASGKGMKVMVK 354
Cdd:cd03135  51 KTLSDVNLDDYDAIVIPGGLPgAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKatCYPGFEDKLGGA 130

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30687679 355 VAGGEAVmekgcVTDGKVVTAASatdlPAFLFDLSTAL 392
Cdd:cd03135 131 NYVDEPV-----VVDGNIITSRG----PGTAFEFALKI 159
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 266-379 5.29e-12

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: 64.10  E-value: 5.29e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 266 PAEKRGHNFFVTASWDDiCVDDYDCVVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCAS 345
Cdd:cd03139  42 PVSSRSGLTVLPDTSFA-DPPDLDVLLVPGGGGTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATT 120

                        90       100       110
                ....*....|....*....|....*....|....
gi 30687679 346 GKGMKVMVKVAGGEAVMEKGCVTDGKVVTAASAT 379
Cdd:cd03139 121 HWAAIDWLKEFGAIVVVDARWVVDGNIWTSGGVS 154
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 9-183 8.31e-11

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: 60.26  E-value: 8.31e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679   9 ALLLCGDYMEAYETIVPLYVLQSFGVSVHCVSpnrNAGDRCVMSAHDFLGLElytelvvdqltlNANFDDVTPENYDVII 88
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTAS---LEKKLAVGSSHGIKVKA------------DKTLSDVNLDDYDAIV 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  89 IPGGRF-TELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAGGvKCTAFESIKPliELSGGEWWQQPgiqsmf 167
Cdd:cd03135  66 IPGGLPgAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGK-KATCYPGFED--KLGGANYVDEP------ 136

                       170
                ....*....|....*.
gi 30687679 168 eitdCVKDGNFMSTVG 183
Cdd:cd03135 137 ----VVVDGNIITSRG 148
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 281-378 5.74e-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: 54.92  E-value: 5.74e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 281 DDICVDDYDCVVVPGGRS---PEllvmNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCAS-GKGMKVMVKVA 356
Cdd:cd03140  54 DDLPPEDYDLLILPGGDSwdnPE----APDLAGLVRQALKQGKPVAAICGATLALARAGLLNNRKHTSnSLDFLKAHAPY 129

                        90       100
                ....*....|....*....|....
gi 30687679 357 GGEA--VMEKGCVTDGKVVTAASA 378
Cdd:cd03140 130 YGGAeyYDEPQAVSDGNLITANGT 153
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 285-379 2.20e-06

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: 48.03  E-value: 2.20e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 285 VDDYDCVVVPG-GRSPELLVM--NEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCASGKGMKVM-------VK 354
Cdd:cd03138  67 VPAPDLVIVPGlGGDPDELLLadNPALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATTHWWLAPQfrrrfpkVR 146

                        90       100
                ....*....|....*....|....*
gi 30687679 355 VAGGEAVmekgcVTDGKVVTAASAT 379
Cdd:cd03138 147 LDPDRVV-----VTDGNLITAGGAM 166
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 260-344 6.09e-06

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: 47.84  E-value: 6.09e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 260 EDGRQIPAEkRGHNFFVTASWDDIcvDDYDCVVVPGGRSPELLVmNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLK 339
Cdd:COG4977  42 LDGGPVRSS-SGLTVAPDHGLADL--AAADTLIVPGGLDPAAAA-DPALLAWLRRAAARGARLASICTGAFLLAAAGLLD 117


                ....*
gi 30687679 340 GKRCA 344
Cdd:COG4977 118 GRRAT 122
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 212-336 8.05e-06

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: 44.51  E-value: 8.05e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKGEvcatavydledgrqipaekrghnffvtaswDDICVDDYDCV 291
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVE------------------------------SDVDLDDYDGL 50

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 30687679 292 VVPGGRS-PELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATG 336
Cdd:cd01653  51 ILPGGPGtPDDLARDEALLALLREAAAAGKPILGICLGAQLLVLGV 96
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 228-381 8.75e-06

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: 46.40  E-value: 8.75e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 228 PFRALQALGCKVDAVTPNKKKGEVCATAVyDLEDGRQIPAEKRGHNFFV----TASWDDICVDDYDCVVVPGGRSPEL-L 302
Cdd:cd03141  28 PYDVFTEAGYEVDFASPKGGKVPLDPRSL-DAEDDDDASVFDNDEEFKKklanTKKLSDVDPSDYDAIFIPGGHGPMFdL 106

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 303 VMNEKAVALVKSFAEKDKVFAAIGQG-KLLLAATG-----VLKGKRC---------ASGKGMKVM------VKVAGgeAV 361
Cdd:cd03141 107 PDNPDLQDLLREFYENGKVVAAVCHGpAALLNVKLsdgksLVAGKTVtgftneeeeAAGLKKVVPflledeLKELG--AN 184

                       170       180
                ....*....|....*....|....*....
gi 30687679 362 MEKG------CVTDGKVVTA---ASATDL 381
Cdd:cd03141 185 YVKAepwaefVVVDGRLITGqnpASAAAV 213
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-132 3.31e-05

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: 42.97  E-value: 3.31e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDrcvmsahdflglelytelvvdqltlnanfDDVTPENYDVIII 89
Cdd:cd01653   2 AVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVE-----------------------------SDVDLDDYDGLIL 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 30687679  90 PGGR-FTELLSADEKCVDLVARFAESKKLIFTSCH-SQVMLMAAG 132
Cdd:cd01653  53 PGGPgTPDDLARDEALLALLREAAAAGKPILGICLgAQLLVLGVQ 97
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 70-136 5.50e-05

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


Pssm-ID: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 43.69  E-value: 5.50e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 30687679  70 LTLNANFDDVTPENYDVIIIPGGRFTELLSADEKCVDLVARFAESKKLIFTSCHSQVMLMAAGILAG 136
Cdd:cd03139  49 LTVLPDTSFADPPDLDVLLVPGGGGTRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDG 115
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 260-344 9.68e-05

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: 42.96  E-value: 9.68e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 260 EDGRQIPAeKRGHNFFVTASWDDICvdDYDCVVVPGGRSPELLVMNEKAVALVKSfAEKDKVFAAIGQGKLLLAATGVLK 339
Cdd:cd03136  40 LDGAPVTS-SNGLRVAPDAALEDAP--PLDYLFVVGGLGARRAVTPALLAWLRRA-ARRGVALGGIDTGAFLLARAGLLD 115


                ....*
gi 30687679 340 GKRCA 344
Cdd:cd03136 116 GRRAT 120
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 212-328 1.12e-04

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: 40.65  E-value: 1.12e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679 212 VLFLIGDYVEDYGINVPFRALQALGCKVDAVTPNKKKGEvcatavydledgrqipaekrghnffvtaswDDICVDDYDCV 291
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVE------------------------------SDVDLDDYDGL 50

                        90       100       110
                ....*....|....*....|....*....|....*...
gi 30687679 292 VVPGGRS-PELLVMNEKAVALVKSFAEKDKVFAAIGQG 328
Cdd:cd03128  51 ILPGGPGtPDDLAWDEALLALLREAAAAGKPVLGICLG 88
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 286-344 1.79e-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: 42.10  E-value: 1.79e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 30687679 286 DDYDCVVVPGGRSPELLVMNEKAVALVKSFAEKDKVFAAIGQGKLLLAATGVLKGKRCA 344
Cdd:cd03137  63 AAADTVIVPGGPDVDGRPPPPALLAALRRAAARGARVASVCTGAFVLAEAGLLDGRRAT 121
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 10-128 5.97e-04

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: 38.72  E-value: 5.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 30687679  10 LLLCGDYMEAYETIVPLYVLQSFGVSVHCVSPNRNAGDrcvmsahdflglelytelvvdqltlnanfDDVTPENYDVIII 89
Cdd:cd03128   2 AVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVE-----------------------------SDVDLDDYDGLIL 52

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 30687679  90 PGGR-FTELLSADEKCVDLVARFAESKKLIFTSCHSQVML 128
Cdd:cd03128  53 PGGPgTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
 
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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