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Conserved domains on  [gi|13124456|sp|Q9V1F8|]
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RecName: Full=Deglycase PYRAB04690; AltName: Full=Intracellular protease PYRAB04690

Protein Classification

type 1 glutamine amidotransferase domain-containing protein( domain architecture ID 10123305)

type 1 glutamine amidotransferase domain-containing protein similar to Pyrococcus furiosus deglycase PfpI that catalyzes the deglycation of the Maillard adducts formed between amino groups of proteins and reactive carbonyl groups of glyoxals (Probable)

CATH:  3.40.50.880
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
deglyc_PfpI NF040823
deglycase PfpI;
1-166 1.26e-121

deglycase PfpI;


:

Pssm-ID: 468763  Cd Length: 166  Bit Score: 339.55  E-value: 1.26e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNE 80
Cdd:NF040823   1 MKVLFLSADGFEDLELIYPLHRIKEEGHEVYIASFKKGKITGKHGYTVKVDLTFDEVDPDEFDALVLPGGRAPERVRLNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   81 KAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMRE 160
Cdd:NF040823  81 KAVAIAKKMFEDGKPVASICHGPQILISAGVLKGRKGTSYITIKDDLINAGAEWIDKEVVVDGNWVSSRHPGDLYAWMRE 160


                 ....*.
gi 13124456  161 FVKLLK 166
Cdd:NF040823 161 FVKLLK 166
 
Name Accession Description Interval E-value
deglyc_PfpI NF040823
deglycase PfpI;
1-166 1.26e-121

deglycase PfpI;


Pssm-ID: 468763  Cd Length: 166  Bit Score: 339.55  E-value: 1.26e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNE 80
Cdd:NF040823   1 MKVLFLSADGFEDLELIYPLHRIKEEGHEVYIASFKKGKITGKHGYTVKVDLTFDEVDPDEFDALVLPGGRAPERVRLNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   81 KAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMRE 160
Cdd:NF040823  81 KAVAIAKKMFEDGKPVASICHGPQILISAGVLKGRKGTSYITIKDDLINAGAEWIDKEVVVDGNWVSSRHPGDLYAWMRE 160


                 ....*.
gi 13124456  161 FVKLLK 166
Cdd:NF040823 161 FVKLLK 166
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 2-164 5.59e-95

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: 272.11  E-value: 5.59e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   2 RVLILSADQFEDVELIYPYHRLKEEGHEVLVASFK-RGVITGKHGY-TVNVDLAFEEVNPDEFDALVLPGGRAPERVRLN 79
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEaGGEIQGKHGYdTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  80 EKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMR 159
Cdd:cd03134  81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPAFNR 160


                ....*
gi 13124456 160 EFVKL 164
Cdd:cd03134 161 AILKA 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 3-166 2.92e-89

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: 257.73  E-value: 2.92e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456     3 VLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNEKA 82
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTVGKHGYSVTVDATIDEVNPEEYDALVIPGGRAPEYLRLNNKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    83 VEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAE-VVVDGNWVSSRVPGDLYAWMREF 161
Cdd:TIGR01382  82 VRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEvVVVDGNLVTSRVPDDLPAFNREF 161


                  ....*
gi 13124456   162 VKLLK 166
Cdd:TIGR01382 162 LKLLG 166
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-166 1.06e-82

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: 241.16  E-value: 1.06e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGV-ITGKHGYTVNVDLAFEEVNPDEFDALVLPGGR-APERVRL 78
Cdd:COG0693   3 KKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPpVTSKHGITVTADKTLDDVDPDDYDALVLPGGHgAPDDLRE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  79 NEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWM 158
Cdd:COG0693  83 DPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGNLITSRGPGDAPAFA 162


                ....*...
gi 13124456 159 REFVKLLK 166
Cdd:COG0693 163 RALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-164 2.12e-77

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: 227.52  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456     1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRA-PERVRLN 79
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAgPERLRDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    80 EKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMR 159
Cdd:pfam01965  81 EKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPEFAL 160


                  ....*
gi 13124456   160 EFVKL 164
Cdd:pfam01965 161 EILEQ 165
PRK11574 PRK11574
protein deglycase YajL;
32-152 1.23e-09

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 54.40  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   32 VASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGG-RAPERVRLNEKAVEIAKKMFSEGKPVASICHGPQ-ILISA 109
Cdd:PRK11574  37 VASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGiKGAECFRDSPLLVETVRQFHRSGRIVAAICAAPAtVLVPH 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 13124456  110 GVLRGRRGTSYPGIKDDMinAGVDWVDAEVVVDG--NWVSSRVPG 152
Cdd:PRK11574 117 DLFPIGNMTGFPTLKDKI--PAEQWQDKRVVWDArvNLLTSQGPG 159
 
Name Accession Description Interval E-value
deglyc_PfpI NF040823
deglycase PfpI;
1-166 1.26e-121

deglycase PfpI;


Pssm-ID: 468763  Cd Length: 166  Bit Score: 339.55  E-value: 1.26e-121
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNE 80
Cdd:NF040823   1 MKVLFLSADGFEDLELIYPLHRIKEEGHEVYIASFKKGKITGKHGYTVKVDLTFDEVDPDEFDALVLPGGRAPERVRLNE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   81 KAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMRE 160
Cdd:NF040823  81 KAVAIAKKMFEDGKPVASICHGPQILISAGVLKGRKGTSYITIKDDLINAGAEWIDKEVVVDGNWVSSRHPGDLYAWMRE 160


                 ....*.
gi 13124456  161 FVKLLK 166
Cdd:NF040823 161 FVKLLK 166
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 2-164 5.59e-95

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: 272.11  E-value: 5.59e-95
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   2 RVLILSADQFEDVELIYPYHRLKEEGHEVLVASFK-RGVITGKHGY-TVNVDLAFEEVNPDEFDALVLPGGRAPERVRLN 79
Cdd:cd03134   1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEaGGEIQGKHGYdTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  80 EKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMR 159
Cdd:cd03134  81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGNLITSRNPDDLPAFNR 160


                ....*
gi 13124456 160 EFVKL 164
Cdd:cd03134 161 AILKA 165
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 3-166 2.92e-89

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: 257.73  E-value: 2.92e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456     3 VLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRAPERVRLNEKA 82
Cdd:TIGR01382   2 LLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTVGKHGYSVTVDATIDEVNPEEYDALVIPGGRAPEYLRLNNKA 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    83 VEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAE-VVVDGNWVSSRVPGDLYAWMREF 161
Cdd:TIGR01382  82 VRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEvVVVDGNLVTSRVPDDLPAFNREF 161


                  ....*
gi 13124456   162 VKLLK 166
Cdd:TIGR01382 162 LKLLG 166
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-166 1.06e-82

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: 241.16  E-value: 1.06e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGV-ITGKHGYTVNVDLAFEEVNPDEFDALVLPGGR-APERVRL 78
Cdd:COG0693   3 KKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPpVTSKHGITVTADKTLDDVDPDDYDALVLPGGHgAPDDLRE 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  79 NEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWM 158
Cdd:COG0693  83 DPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGNLITSRGPGDAPAFA 162


                ....*...
gi 13124456 159 REFVKLLK 166
Cdd:COG0693 163 RALLELLA 170
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 1-164 2.12e-77

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: 227.52  E-value: 2.12e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456     1 MRVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRA-PERVRLN 79
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGGEVKGSRGVKVTVDASLDDVKPDDYDALVLPGGRAgPERLRDN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    80 EKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNWVSSRVPGDLYAWMR 159
Cdd:pfam01965  81 EKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGNLVTSRGPGDAPEFAL 160


                  ....*
gi 13124456   160 EFVKL 164
Cdd:pfam01965 161 EILEQ 165
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 2-165 1.90e-60

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: 185.16  E-value: 1.90e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   2 RVLILSADQFEDVELIYPYHRLKEEGHEVLVAS--FKRG--VITGKH------------GYTVNVDLAFEEVNPDEFDAL 65
Cdd:cd03169   1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVApgKKKGdtVVTAIHdfpgwqtytekpGHRFAVTADFDEVDPDDYDAL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  66 VLPGGRAPERVRLNEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVDWVDAEVVVDGNW 145
Cdd:cd03169  81 VIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDDGVVVDGNL 160

                       170       180
                ....*....|....*....|
gi 13124456 146 VSSRVPGDLYAWMREFVKLL 165
Cdd:cd03169 161 VTAQAWPDHPAFLREFLKLL 180
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 3-152 6.99e-35

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: 119.58  E-value: 6.99e-35
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   3 VLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRG-VITGKHGYTVNVDLAFEEVNPDEFDALVLPGGR-APERVRLNE 80
Cdd:cd03135   1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKlAVGSSHGIKVKADKTLSDVNLDDYDAIVIPGGLpGAQNLADNE 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 13124456  81 KAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVdwVDAEVVVDGNWVSSRVPG 152
Cdd:cd03135  81 KLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKLGGANY--VDEPVVVDGNIITSRGPG 150
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 2-166 2.39e-27

DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of proteins. PfpI, represented by a distinct model, is a putative intracellular cysteine protease. DJ-1 is described as an oncogene that acts cooperatively with H-Ras. Many members of the DJ-1 clade are annotated (apparently incorrectly) as ThiJ, a protein of thiamine biosynthesis. However, published reports of ThiJ activity and identification of a ThiJ/ThiD bifunctional protein describe an unrelated locus mapping near ThiM, rather than the DJ-1 homolog of E. coli. The ThiJ designation for this family may be spurious; the cited paper refers to a locus near thiD and thiM in E. coli, unlike the gene represented here. Current public annotation reflects ThiJ/ThiD bifunctional activity, apparently a property of ThiD and not of this locus. [Unknown function, General]


Pssm-ID: 213612 [Multi-domain]  Cd Length: 179  Bit Score: 100.85  E-value: 2.39e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456     2 RVLILSADQFEDVELIYPYHRLKEEGHEVLV--ASFKRG-VITGKHGYTVNVDLAFEEVNPDEFDALVLPGG-RAPERVR 77
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTVaiAGLNGKlAVKGSRGVKILADASLEDVDLEKFDVIVLPGGmPGAENLR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    78 LNEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINaGVDWVDAEVVVDGNWVSSRVPGDLYAW 157
Cdd:TIGR01383  81 NSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLN-GNYSVNKTVVVDGNLITSRGPGTAIEF 159


                  ....*....
gi 13124456   158 MREFVKLLK 166
Cdd:TIGR01383 160 ALELVELLA 168
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-107 1.70e-16

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: 71.09  E-value: 1.70e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   3 VLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGkhgytvnvdlafeEVNPDEFDALVLPGGRA-PERVRLNEK 81
Cdd:cd01653   1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVES-------------DVDLDDYDGLILPGGPGtPDDLARDEA 67

                        90       100
                ....*....|....*....|....*.
gi 13124456  82 AVEIAKKMFSEGKPVASICHGPQILI 107
Cdd:cd01653  68 LLALLREAAAAGKPILGICLGAQLLV 93
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 3-106 2.44e-14

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: 64.91  E-value: 2.44e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   3 VLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGkhgytvnvdlafeEVNPDEFDALVLPGGRA-PERVRLNEK 81
Cdd:cd03128   1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVES-------------DVDLDDYDGLILPGGPGtPDDLAWDEA 67

                        90       100
                ....*....|....*....|....*
gi 13124456  82 AVEIAKKMFSEGKPVASICHGPQIL 106
Cdd:cd03128  68 LLALLREAAAAGKPVLGICLGAQLL 92
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 14-144 5.93e-14

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: 66.43  E-value: 5.93e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  14 VELIYPYHRLKEEGHEVLVASFKRGVIT----------GKHGYTVNVDLAF----------EEVNPDEFDALVLPGGRAP 73
Cdd:cd03141  23 EELAHPYDVFTEAGYEVDFASPKGGKVPldprsldaedDDDASVFDNDEEFkkklantkklSDVDPSDYDAIFIPGGHGP 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  74 ervrL-----NEKAVEIAKKMFSEGKPVASICHGPQILISAG------VLRGRRGTSYP-------GIKDDM-------- 127
Cdd:cd03141 103 ----MfdlpdNPDLQDLLREFYENGKVVAAVCHGPAALLNVKlsdgksLVAGKTVTGFTneeeeaaGLKKVVpflledel 178

                       170       180
                ....*....|....*....|..
gi 13124456 128 INAGVDWVDAE-----VVVDGN 144
Cdd:cd03141 179 KELGANYVKAEpwaefVVVDGR 200
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 26-165 2.01e-13

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: 64.16  E-value: 2.01e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  26 EGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGGRA---PErvrlNEKAVEIAKKMFSEGKPVASICHG 102
Cdd:cd03140  25 EGFEVRTVSPTGEPVTSIGGLRVVPDYSLDDLPPEDYDLLILPGGDSwdnPE----APDLAGLVRQALKQGKPVAAICGA 100

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124456 103 PQILISAGVLRGRRGTSYpgiKDDMINAGV-------DWVDAEVVVDGNWVSSrvPGDLY-AWMREFVKLL 165
Cdd:cd03140 101 TLALARAGLLNNRKHTSN---SLDFLKAHApyyggaeYYDEPQAVSDGNLITA--NGTAPvEFAAEILRAL 166
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 3-148 1.05e-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: 62.56  E-value: 1.05e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   3 VLILSADQFEDVELIYPY---HRLKEEGH--EVLVASFKRGVITGKHGYTVNVDLAFEEvnPDEFDALVLPGGrAPERVR 77
Cdd:cd03139   1 VGILLFPGVEVLDVIGPYevfGRAPRLAApfEVFLVSETGGPVSSRSGLTVLPDTSFAD--PPDLDVLLVPGG-GGTRAL 77

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 13124456  78 LNEKAVeIA--KKMFSEGKPVASICHGPQILISAGVLRGRRGTSYPGIKDDMINAGVD-WVDAEVVVDGNWVSS 148
Cdd:cd03139  78 VNDPAL-LDfiRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIvVVDARWVVDGNIWTS 150
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 29-148 2.36e-10

Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH domain [Transcription];


Pssm-ID: 444002 [Multi-domain]  Cd Length: 318  Bit Score: 57.47  E-value: 2.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  29 EVLVASFKRGVITGKHGYTVNVDLAFEEVnpDEFDALVLPGGRAPERvRLNEKAVEIAKKMFSEGKPVASICHGPQILIS 108
Cdd:COG4977  36 RWRLVSLDGGPVRSSSGLTVAPDHGLADL--AAADTLIVPGGLDPAA-AADPALLAWLRRAAARGARLASICTGAFLLAA 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 13124456 109 AGVLRGRRGTS-----------YPGIKddminagvdwVDAEV--VVDGNWVSS 148
Cdd:COG4977 113 AGLLDGRRATThwehadafaerFPDVR----------VDPDRlyVDDGDILTS 155
PRK11574 PRK11574
protein deglycase YajL;
32-152 1.23e-09

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 54.40  E-value: 1.23e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   32 VASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGG-RAPERVRLNEKAVEIAKKMFSEGKPVASICHGPQ-ILISA 109
Cdd:PRK11574  37 VASDGNLEITCSRGVKLLADAPLVEVADGDFDVIVLPGGiKGAECFRDSPLLVETVRQFHRSGRIVAAICAAPAtVLVPH 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 13124456  110 GVLRGRRGTSYPGIKDDMinAGVDWVDAEVVVDG--NWVSSRVPG 152
Cdd:PRK11574 117 DLFPIGNMTGFPTLKDKI--PAEQWQDKRVVWDArvNLLTSQGPG 159
GATase1_AraC_1 cd03137
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 21-148 2.97e-09

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: 53.27  E-value: 2.97e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  21 HRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEvnPDEFDALVLPGGRAPERVRLNEKAVEIAKKMFSEGKPVASIC 100
Cdd:cd03137  26 RALGPPAYELRVCSPEGGPVRSSSGLSLVADAGLDA--LAAADTVIVPGGPDVDGRPPPPALLAALRRAAARGARVASVC 103

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 13124456 101 HGPQILISAGVLRGRRGTS-----------YPGIKddminagvdwVDAEV--VVDGNWVSS 148
Cdd:cd03137 104 TGAFVLAEAGLLDGRRATThwayaedlarrFPAVR----------VDPDVlyVDDGNVWTS 154
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 4-158 3.55e-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: 47.64  E-value: 3.55e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   4 LILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVnpDEFDALVLPG-GRAPER--VRLNE 80
Cdd:cd03138  14 LAGLLDLLRAANRLARRQQGGAPPFEVRLVSLDGGPVLLAGGILILPDATLADV--PAPDLVIVPGlGGDPDEllLADNP 91

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  81 KAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRGT-----------SYPGIKDDMinagvdwvDAEVVVDGNWVSSr 149
Cdd:cd03138  92 ALIAWLRRQHANGATVAAACTGVFLLAEAGLLDGRRATthwwlapqfrrRFPKVRLDP--------DRVVVTDGNLITA- 162


                ....*....
gi 13124456 150 vpGDLYAWM 158
Cdd:cd03138 163 --GGAMAWA 169
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 32-118 1.16e-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: 43.34  E-value: 1.16e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  32 VASFKRGVITGKHGYTVNVDLAFEevNPDEFDALVLPGGRAPER---VRLNEKAVEIAKKmfseGKPVASICHGPQILIS 108
Cdd:cd03136  37 VLSLDGAPVTSSNGLRVAPDAALE--DAPPLDYLFVVGGLGARRavtPALLAWLRRAARR----GVALGGIDTGAFLLAR 110

                        90
                ....*....|
gi 13124456 109 AGVLRGRRGT 118
Cdd:cd03136 111 AGLLDGRRAT 120
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
54-114 1.32e-05

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 43.57  E-value: 1.32e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 13124456   54 FEEVNPDEFDALVLPGG--------------RAPervrlnekAVEIAKKMFSEGKPVASICHGPQILISAGVLRG 114
Cdd:PRK03619  34 HKETDLDGVDAVVLPGGfsygdylrcgaiaaFSP--------IMKAVKEFAEKGKPVLGICNGFQILTEAGLLPG 100
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 51-115 1.74e-05

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


Pssm-ID: 153211 [Multi-domain]  Cd Length: 238  Bit Score: 43.37  E-value: 1.74e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 13124456  51 DLAFEEVNPDEFDALVLPGG-------RAPE----RVRLNEKAVEIAKKmfseGKPVASICHGPQILISAGVLRGR 115
Cdd:cd01740  33 DLLAGRKDLDDYDGVVLPGGfsygdylRAGAiaaaSPLLMEEVKEFAER----GGLVLGICNGFQILVELGLLPGA 104
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 14-106 3.08e-05

Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein; Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae Ydr533c protein. This group includes proteins similar to S. cerevisiae Ydr533c. Ydr533c is upregulated in response to various stress conditions along with the heat shock family. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with a typical GATase1domain, a reactive Cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. This Cys together with a different His and Glu residue form a different catalytic triad from the typical GATase1domain. Ydr533c protein is a homodimer.


Pssm-ID: 153241 [Multi-domain]  Cd Length: 231  Bit Score: 42.70  E-value: 3.08e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  14 VELIYPYHRLKEEGHEVLVASfkrgvITGKHGYTV-----------------NVDLAF----------EEVNPDEFDALV 66
Cdd:cd03147  25 SEALHPFNVFREAGFEVDFVS-----ETGTFGFDDhsldpdflngedlevfsNKDSDFwkklknikkaDEVNPDDYGIFF 99

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 13124456  67 LPGGRA-----PERVRLNEkaveIAKKMFSEGKPVASICHGPQIL 106
Cdd:cd03147 100 VAGGHGtlfdfPHATNLQK----IAQQIYANGGVVAAVCHGPAIL 140
GATase pfam00117
Glutamine amidotransferase class-I;
21-106 8.13e-05

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 41.07  E-value: 8.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456    21 HRLKEEGHEVLVasfkrgvitgkhgytVNVDLAFEEVNPDEFDALVLPGGraPERVRLNEKAVEIAKKMFSEGKPVASIC 100
Cdd:pfam00117  15 RALRELGVEVTV---------------VPNDTPAEEILEENPDGIILSGG--PGSPGAAGGAIEAIREARELKIPILGIC 77


                  ....*.
gi 13124456   101 HGPQIL 106
Cdd:pfam00117  78 LGHQLL 83
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
21-106 1.10e-04

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 40.92  E-value: 1.10e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   21 HRLKEEGHE---VLV--ASFKRGVITgkhgytvnvDLAfeEVNPDEFDALVLPGG-----------RAPERVRLNEKAVE 84
Cdd:PRK11780  51 HLTGEEMGEtrnVLVesARIARGEIK---------DLA--EADAEDFDALIVPGGfgaaknlsnfaVKGAECTVNPDVKA 119

                         90       100
                 ....*....|....*....|..
gi 13124456   85 IAKKMFSEGKPVASICHGPQIL 106
Cdd:PRK11780 120 LVRAFHQAGKPIGFICIAPAML 141
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 2-106 2.34e-04

GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis


Pssm-ID: 440284 [Multi-domain]  Cd Length: 225  Bit Score: 39.93  E-value: 2.34e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   2 RVLILSADQFED--VELIYPyhRLKEEGHEVLVASFKRGvitgkhgytvnvDLAFEEVNPDEFDALVLPGGR--APERVR 77
Cdd:COG0518   1 KILILDHDPFGGqyPGLIAR--RLREAGIELDVLRVYAG------------EILPYDPDLEDPDGLILSGGPmsVYDEDP 66

                        90       100
                ....*....|....*....|....*....
gi 13124456  78 LNEKAVEIAKKMFSEGKPVASICHGPQIL 106
Cdd:COG0518  67 WLEDEPALIREAFELGKPVLGICYGAQLL 95
ftrA PRK09393
transcriptional activator FtrA; Provisional
 32-137 3.17e-04

transcriptional activator FtrA; Provisional


Pssm-ID: 181818 [Multi-domain]  Cd Length: 322  Bit Score: 39.95  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   32 VASFKRGVITGKHGYTVNVDLAFEEVnpDEFDALVLPGGRAPErVRLNEKAVEIAKKMFSEGKPVASICHGPQILISAGV 111
Cdd:PRK09393  48 VAAVEPGPLRAAGGITVVADGGLELL--DRADTIVIPGWRGPD-APVPEPLLEALRAAHARGARLCSICSGVFVLAAAGL 124

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 13124456  112 LRGRRGTS-----------YPGIkddMINAGVDWVDA 137
Cdd:PRK09393 125 LDGRRATThwryaerlqarYPAI---RVDPDVLYVDE 158
GATase1_CPSase cd01744
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ...
 43-106 3.62e-04

Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I.


Pssm-ID: 153215 [Multi-domain]  Cd Length: 178  Bit Score: 39.02  E-value: 3.62e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  43 KHGYTVNV---DLAFEEVNPDEFDALVL---PGGraPERVrlnEKAVEIAKKMFSEGKPVASICHGPQIL 106
Cdd:cd01744  18 KRGCEVTVvpyNTDAEEILKLDPDGIFLsngPGD--PALL---DEAIKTVRKLLGKKIPIFGICLGHQLL 82
GATase1_catalase cd03132
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ...
 2-117 9.19e-04

Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases; Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several large catalases. Catalase catalyzes the dismutation of hydrogen peroxide (H2O2) to water and oxygen. This group includes the large catalases: Neurospora crassa Catalase-1 and Catalase-3 and, Escherichia coli HP-II. This GATase1-like domain has an essential role in HP-II catalase activity. However, it lacks enzymatic activity and the catalytic triad typical of GATase1 domains. Catalase-1 and -3 are homotetrameric, HP-II is homohexameric. It has been proposed that this domain may facilitate the folding and oligomerization process. The interface between this GATase1-like domain of HP-II and the core of the subunit forms part of a channel which provides access to the deeply buried catalase active sites of HPII. Catalase-1 is associated with non-growing cells; Catalase-3 is associated with growing conditions. HP-II is produced in stationary phase. Catalase-1 is induced by ethanol and heat shock. Catalase-3 is induced under stress conditions such a hydrogen peroxide, paraquat, cadmium, heat shock, uric acid and nitrate treatment.


Pssm-ID: 153226  Cd Length: 142  Bit Score: 37.63  E-value: 9.19e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456   2 RVLILSADQFEDVELIYPYHRLKEEGHEVLVASFKRGVITGKHGYTVNVDLAFEEVNPDEFDALVLPGG-RAPERVRLNE 80
Cdd:cd03132   3 KVGILVADGVDAAELSALKAALKAAGANVKVVAPTLGGVVDSDGKTLEVDQTYAGAPSVLFDAVVVPGGaEAAFALAPSG 82

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 13124456  81 KAVEIAKKMFSEGKPVASICHGPQILISAGVLRGRRG 117
Cdd:cd03132  83 RALHFVTEAFKHGKPIGAVGEGSDLLEAAGIPLEDPG 119
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 51-114 5.34e-03

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 36.28  E-value: 5.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 13124456   51 DLAFEEVNPDEFDALVLPGG-------RAPE--RVRLNEKAVEIAKKMFSEGKPVASICHGPQILISAGVLRG 114
Cdd:PRK01175  38 DLAAERKSVSDYDCLVIPGGfsagdyiRAGAifAARLKAVLRKDIEEFIDEGYPIIGICNGFQVLVELGLLPG 110
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 30-106 8.48e-03

Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1. This group includes, proteins similar to ES1, Escherichia coli enhancing lycopene biosynthesis protein 2, Azospirillum brasilense iaaC and, human HES1. The catalytic triad typical of GATase1domains is not conserved in this GATase1-like domain. However, in common with GATase1domains a reactive cys residue is found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. Zebrafish ES1 is expressed specifically in adult photoreceptor cells and appears to be a cytoplasmic protein. A. brasilense iaaC is involved in controlling IAA biosynthesis.


Pssm-ID: 153227  Cd Length: 213  Bit Score: 35.29  E-value: 8.48e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 13124456  30 VLVASFK--RGVITgkhgytvnvDLAfeEVNPDEFDALVLPGG-----------RAPERVRLNEKAVEIAKKMFSEGKPV 96
Cdd:cd03133  60 VLVESARiaRGNIK---------DLA--KLKAADFDALIFPGGfgaaknlsdfaVKGADCTVNPEVERLVREFHQAGKPI 128

                        90
                ....*....|
gi 13124456  97 ASICHGPQIL 106
Cdd:cd03133 129 GAICIAPALA 138
 
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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