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Conserved domains on  [gi|984812023|gb|KWW53399|]
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cysteine protease [Bacillus cereus]

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
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 4-168 4.58e-79

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: 232.05  E-value: 4.58e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   4 KIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVHGKQGKSEVVIDKGIDNVSPENFDALFIPGGFSPDILRAD 83
Cdd:cd03134    1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  84 ERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDIPAFI 163
Cdd:cd03134   81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN-LITSRNPDDLPAFN 159


                 ....*
gi 984812023 164 EESLR 168
Cdd:cd03134  160 RAILK 164
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 4-168 4.58e-79

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: 232.05  E-value: 4.58e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   4 KIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVHGKQGKSEVVIDKGIDNVSPENFDALFIPGGFSPDILRAD 83
Cdd:cd03134    1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  84 ERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDIPAFI 163
Cdd:cd03134   81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN-LITSRNPDDLPAFN 159


                 ....*
gi 984812023 164 EESLR 168
Cdd:cd03134  160 RAILK 164
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-171 5.02e-71

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: 211.89  E-value: 5.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   1 MSKKIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVHGKQGKsEVVIDKGIDNVSPENFDALFIPGGF-SPDI 79
Cdd:COG0693    1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGI-TVTADKTLDDVDPDDYDALVLPGGHgAPDD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  80 LRADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDI 159
Cdd:COG0693   80 LREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGN-LITSRGPGDA 158

                        170
                 ....*....|..
gi 984812023 160 PAFIEESLRILR 171
Cdd:COG0693  159 PAFARALLELLA 170
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 4-170 1.25e-62

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: 190.32  E-value: 1.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023    4 KIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVhGKQGKSeVVIDKGIDNVSPENFDALFIPGGFSPDILRAD 83
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTV-GKHGYS-VTVDATIDEVNPEEYDALVIPGGRAPEYLRLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   84 ERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNQLVTSRQPEDIPAFI 163
Cdd:TIGR01382  79 NKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGNLVTSRVPDDLPAFN 158


                  ....*..
gi 984812023  164 EESLRIL 170
Cdd:TIGR01382 159 REFLKLL 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 3-168 4.81e-56

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: 173.60  E-value: 4.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023    3 KKIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGkTVHGKQGkSEVVIDKGIDNVSPENFDALFIPGGFS-PDILR 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGG-EVKGSRG-VKVTVDASLDDVKPDDYDALVLPGGRAgPERLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   82 ADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDIPA 161
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGN-LVTSRGPGDAPE 157


                  ....*..
gi 984812023  162 FIEESLR 168
Cdd:pfam01965 158 FALEILE 164
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-126 1.07e-06

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 47.06  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   1 MSKKIAILItdyFEDTE-YTEPAEAFKQKGyelttIEAEkgkTVHGKQGKSEVvidKGIDNvspenFDALFIPGGFSP-D 78
Cdd:PRK01175   2 ESIRVAVLR---MEGTNcEDETVKAFRRLG-----VEPE---YVHINDLAAER---KSVSD-----YDCLVIPGGFSAgD 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 984812023  79 ILRADERFVRFSKA--------FMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKS 126
Cdd:PRK01175  63 YIRAGAIFAARLKAvlrkdieeFIDEGYPIIGICNGFQVLVELGLLPGFDEIAEKP 118
 
Name Accession Description Interval E-value
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 4-168 4.58e-79

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: 232.05  E-value: 4.58e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   4 KIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVHGKQGKSEVVIDKGIDNVSPENFDALFIPGGFSPDILRAD 83
Cdd:cd03134    1 KVAILAADGFEDVELTYPLYRLREAGAEVVVAGPEAGGEIQGKHGYDTVTVDLTIADVDADDYDALVIPGGTNPDKLRRD 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  84 ERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDIPAFI 163
Cdd:cd03134   81 PDAVAFVRAFAEAGKPVAAICHGPWVLISAGVVRGRKLTSYPSIKDDLINAGANWVDEEVVVDGN-LITSRNPDDLPAFN 159


                 ....*
gi 984812023 164 EESLR 168
Cdd:cd03134  160 RAILK 164
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-171 5.02e-71

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: 211.89  E-value: 5.02e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   1 MSKKIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVHGKQGKsEVVIDKGIDNVSPENFDALFIPGGF-SPDI 79
Cdd:COG0693    1 MMKKVLILLTDGFEDEELTVPYDALREAGAEVDVASPEGGPPVTSKHGI-TVTADKTLDDVDPDDYDALVLPGGHgAPDD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  80 LRADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDI 159
Cdd:COG0693   80 LREDPDVVALVREFYEAGKPVAAICHGPAVLAAAGLLKGRKVTSFPNIEDDLKNAGATYVDEEVVVDGN-LITSRGPGDA 158

                        170
                 ....*....|..
gi 984812023 160 PAFIEESLRILR 171
Cdd:COG0693  159 PAFARALLELLA 170
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 4-170 1.25e-62

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: 190.32  E-value: 1.25e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023    4 KIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVhGKQGKSeVVIDKGIDNVSPENFDALFIPGGFSPDILRAD 83
Cdd:TIGR01382   1 KLLVLTTDEFEDSELLYPLDRLREAGHEVDTVSKEAGTTV-GKHGYS-VTVDATIDEVNPEEYDALVIPGGRAPEYLRLN 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   84 ERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNQLVTSRQPEDIPAFI 163
Cdd:TIGR01382  79 NKAVRLVREFVEKGKPVAAICHGPQLLISAGVLRGKKLTSYPAIIDDVKNAGAEYVDIEVVVVDGNLVTSRVPDDLPAFN 158


                  ....*..
gi 984812023  164 EESLRIL 170
Cdd:TIGR01382 159 REFLKLL 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 3-168 4.81e-56

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: 173.60  E-value: 4.81e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023    3 KKIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGkTVHGKQGkSEVVIDKGIDNVSPENFDALFIPGGFS-PDILR 81
Cdd:pfam01965   1 KKVLVLLADGFEDIELIYPADVLRRAGIKVTVVSVDGG-EVKGSRG-VKVTVDASLDDVKPDDYDALVLPGGRAgPERLR 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   82 ADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNqLVTSRQPEDIPA 161
Cdd:pfam01965  79 DNEKLVEFVKDFYEKGKPVAAICHGPQVLAAAGVLKGRKVTSHPAVKDDLINAGATYVDKPVVVDGN-LVTSRGPGDAPE 157


                  ....*..
gi 984812023  162 FIEESLR 168
Cdd:pfam01965 158 FALEILE 164
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 4-170 7.96e-42

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: 138.16  E-value: 7.96e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   4 KIAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGK------TVHGKQGK---SE-----VVIDKGIDNVSPENFDAL 69
Cdd:cd03169    1 KILILTGDFVEDYEVMVPFQALQEVGHEVDVVAPGKKKgdtvvtAIHDFPGWqtyTEkpghrFAVTADFDEVDPDDYDAL 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  70 FIPGGFSPDILRADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNq 149
Cdd:cd03169   81 VIPGGRAPEYLRLDEKVLAIVRHFAEANKPVAAICHGPQILAAAGVLKGRRCTAYPACKPEVELAGGTVVDDGVVVDGN- 159

                        170       180
                 ....*....|....*....|.
gi 984812023 150 LVTSRQPEDIPAFIEESLRIL 170
Cdd:cd03169  160 LVTAQAWPDHPAFLREFLKLL 180
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 5-156 1.26e-26

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: 98.39  E-value: 1.26e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   5 IAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVHGKQGKSeVVIDKGIDNVSPENFDALFIPGGFS-PDILRAD 83
Cdd:cd03135    1 VLVILADGFEEIEAVTPVDVLRRAGIEVTTASLEKKLAVGSSHGIK-VKADKTLSDVNLDDYDAIVIPGGLPgAQNLADN 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984812023  84 ERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLknAGGNFHDKEVVVCQNqLVTSRQP 156
Cdd:cd03135   80 EKLIKLLKEFNAKGKLIAAICAAPAVLAKAGLLKGKKATCYPGFEDKL--GGANYVDEPVVVDGN-IITSRGP 149
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-114 7.67e-20

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: 79.95  E-value: 7.67e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   5 IAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVhgkqgksevvidkgiDNVSPENFDALFIPGGFS-PDILRAD 83
Cdd:cd01653    1 VAVLLFPGFEELELASPLDALREAGAEVDVVSPDGGPVE---------------SDVDLDDYDGLILPGGPGtPDDLARD 65

                         90       100       110
                 ....*....|....*....|....*....|..
gi 984812023  84 ERFVRFSKAFMDAEKPVFAICHGPQLLI-TAQ 114
Cdd:cd01653   66 EALLALLREAAAAGKPILGICLGAQLLVlGVQ 97
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 5-110 3.86e-18

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: 74.54  E-value: 3.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   5 IAILITDYFEDTEYTEPAEAFKQKGYELTTIEAEKGKTVhgkqgksevvidkgiDNVSPENFDALFIPGGFS-PDILRAD 83
Cdd:cd03128    1 VAVLLFGGSEELELASPLDALREAGAEVDVVSPDGGPVE---------------SDVDLDDYDGLILPGGPGtPDDLAWD 65

                         90       100
                 ....*....|....*....|....*..
gi 984812023  84 ERFVRFSKAFMDAEKPVFAICHGPQLL 110
Cdd:cd03128   66 EALLALLREAAAAGKPVLGICLGAQLL 92
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 16-170 1.29e-15

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: 71.05  E-value: 1.29e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  16 TEYTEPAEAFKQKGYELTtIEAEKGKTV----HGKQGKSEVVIDKG---------------IDNVSPENFDALFIPGGFS 76
Cdd:cd03141   23 EELAHPYDVFTEAGYEVD-FASPKGGKVpldpRSLDAEDDDDASVFdndeefkkklantkkLSDVDPSDYDAIFIPGGHG 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  77 P--DiLRADERFVRFSKAFMDAEKPVFAICHGPQLLITAQ------TLEGRDVTGY---------------KSIEVDLKN 133
Cdd:cd03141  102 PmfD-LPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKlsdgksLVAGKTVTGFtneeeeaaglkkvvpFLLEDELKE 180

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 984812023 134 AGGNFHDKEV----VVCQNQLVTSRQPEDIPAFIEESLRIL 170
Cdd:cd03141  181 LGANYVKAEPwaefVVVDGRLITGQNPASAAAVAEALVKAL 221
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 4-156 3.41e-15

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: 69.27  E-value: 3.41e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023    4 KIAILITDYFEDTEYTEPAEAFKQKGYELT--TIEAEKGKTVHGKQGKSeVVIDKGIDNVSPENFDALFIPGGF-SPDIL 80
Cdd:TIGR01383   1 KVLVPLAPGFEEMEAVITVDVLRRAGIKVTvaIAGLNGKLAVKGSRGVK-ILADASLEDVDLEKFDVIVLPGGMpGAENL 79

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 984812023   81 RADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNagGNFHDKEVVVCQNQLVTSRQP 156
Cdd:TIGR01383  80 RNSKLLLNILKSQESKGKLVAAICAAPAVLLAHGVLLGKKATCYPGFKEKLLN--GNYSVNKTVVVDGNLITSRGP 153
GuaA1 COG0518
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ...
 4-119 1.40e-09

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: 54.95  E-value: 1.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   4 KIAILITDYFEDtEYTEP-AEAFKQKGYELTTIEAEKGKTVHgkqgksevvidkgiDNVSPENFDALFIPGG----FSPD 78
Cdd:COG0518    1 KILILDHDPFGG-QYPGLiARRLREAGIELDVLRVYAGEILP--------------YDPDLEDPDGLILSGGpmsvYDED 65

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 984812023  79 ILRADERfvRFSKAFMDAEKPVFAICHGPQLLitAQTLEGR 119
Cdd:COG0518   66 PWLEDEP--ALIREAFELGKPVLGICYGAQLL--AHALGGK 102
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 5-153 1.35e-08

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: 51.77  E-value: 1.35e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   5 IAILITDYFEDTEYTEPAEAF-----KQKGYELTTIeAEKGKTVHGKQGkSEVVIDKGIDNvsPENFDALFIPGGFSPDI 79
Cdd:cd03139    1 VGILLFPGVEVLDVIGPYEVFgraprLAAPFEVFLV-SETGGPVSSRSG-LTVLPDTSFAD--PPDLDVLLVPGGGGTRA 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984812023  80 LRADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKSIEVDLKNAGGNFHDKEVVVCQNQLVTS 153
Cdd:cd03139   77 LVNDPALLDFIRRQAARAKYVTSVCTGALLLAAAGLLDGRRATTHWAAIDWLKEFGAIVVVDARWVVDGNIWTS 150
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 5-152 1.82e-08

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: 51.07  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   5 IAILITDYFEDTEYT-EPAEAFKQKGYELTTIeAEKGKTVHGKQGKSeVVIDKGIDNVSPENFDALFIPGGFSPDILRAD 83
Cdd:cd03140    1 IAVFLTDEFADWEGAyLAALLNSYEGFEVRTV-SPTGEPVTSIGGLR-VVPDYSLDDLPPEDYDLLILPGGDSWDNPEAP 78

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984812023  84 ERFvRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVTGyKSIEvDLKN-----AGGNFHDKEVVVCQNQLVT 152
Cdd:cd03140   79 DLA-GLVRQALKQGKPVAAICGATLALARAGLLNNRKHTS-NSLD-FLKAhapyyGGAEYYDEPQAVSDGNLIT 149
PurL2 COG0047
Phosphoribosylformylglycinamidine (FGAM) synthase, glutamine amidotransferase domain ...
 61-122 9.37e-07

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


Pssm-ID: 439817 [Multi-domain]  Cd Length: 236  Bit Score: 46.98  E-value: 9.37e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 984812023  61 VSPENFDALFIPGGFS-PDILRADERFvRFS------KAFMDAEKPVFAICHGPQLLITAQTLEGRDVT 122
Cdd:COG0047   38 TDLDDFDGLVLPGGFSyGDYLRAGAIA-AFSpimdavREFARRGGLVLGICNGFQILTELGLLPGIWPA 105
PRK01175 PRK01175
phosphoribosylformylglycinamidine synthase I; Provisional
 1-126 1.07e-06

phosphoribosylformylglycinamidine synthase I; Provisional


Pssm-ID: 234913 [Multi-domain]  Cd Length: 261  Bit Score: 47.06  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   1 MSKKIAILItdyFEDTE-YTEPAEAFKQKGyelttIEAEkgkTVHGKQGKSEVvidKGIDNvspenFDALFIPGGFSP-D 78
Cdd:PRK01175   2 ESIRVAVLR---MEGTNcEDETVKAFRRLG-----VEPE---YVHINDLAAER---KSVSD-----YDCLVIPGGFSAgD 62

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 984812023  79 ILRADERFVRFSKA--------FMDAEKPVFAICHGPQLLITAQTLEGRDVTGYKS 126
Cdd:PRK01175  63 YIRAGAIFAARLKAvlrkdieeFIDEGYPIIGICNGFQVLVELGLLPGFDEIAEKP 118
GATase1_FGAR_AT cd01740
Type 1 glutamine amidotransferase (GATase1)-like domain found in Formylglycinamide ...
 61-110 6.30e-06

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: 44.53  E-value: 6.30e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 984812023  61 VSPENFDALFIPGGFS-PDILRA------DERFVRFSKAFMDAEKPVFAICHGPQLL 110
Cdd:cd01740   39 KDLDDYDGVVLPGGFSyGDYLRAgaiaaaSPLLMEEVKEFAERGGLVLGICNGFQIL 95
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
58-153 1.84e-05

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 43.24  E-value: 1.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  58 IDNVSPENFDALFIPGGF-----------SPDILRADERFVRFSKAFMDAEKPVFAICHGPQLLitAQTLE-------GR 119
Cdd:PRK11780  78 LAEADAEDFDALIVPGGFgaaknlsnfavKGAECTVNPDVKALVRAFHQAGKPIGFICIAPAML--PKILGagvkltiGN 155

                         90       100       110
                 ....*....|....*....|....*....|....*...
gi 984812023 120 DVTGYKSIEvdlkNAGGNFHD---KEVVV-CQNQLVTS 153
Cdd:PRK11780 156 DEDTAAAIE----KMGGEHVDcpvDDIVVdEENKVVTT 189
PRK03619 PRK03619
phosphoribosylformylglycinamidine synthase subunit PurQ;
62-143 2.05e-05

phosphoribosylformylglycinamidine synthase subunit PurQ;


Pssm-ID: 235140 [Multi-domain]  Cd Length: 219  Bit Score: 43.18  E-value: 2.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  62 SPENFDALFIPGGFS-PDILR----AderfvRFS------KAFMDAEKPVFAICHGPQLLITAQTLEGrdvtgyksieVD 130
Cdd:PRK03619  38 DLDGVDAVVLPGGFSyGDYLRcgaiA-----AFSpimkavKEFAEKGKPVLGICNGFQILTEAGLLPG----------AL 102

                         90
                 ....*....|...
gi 984812023 131 LKNAGGNFHDKEV 143
Cdd:PRK03619 103 TRNASLKFICRDV 115
COG3442 COG3442
Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction ...
 51-118 4.98e-05

Glutamine amidotransferase related to the GATase domain of CobQ [General function prediction only];


Pssm-ID: 442666 [Multi-domain]  Cd Length: 241  Bit Score: 42.09  E-value: 4.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  51 EVV-IDKGiDNVSPENFDALFIPGG-------FSPDILRADERFvrfsKAFMDAEKPVFAICHGPQLL----ITA--QTL 116
Cdd:COG3442   36 EVVeVNPG-DDLPFDDVDIVFIGGGqdreqeiVADDLLRIKDAL----RAAIEDGVPVLAICGGYQLLghyyETAdgERI 110


                 ..
gi 984812023 117 EG 118
Cdd:COG3442  111 PG 112
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 58-110 5.76e-05

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: 41.84  E-value: 5.76e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984812023  58 IDNVSPENFDALFIPGGF-----------SPDILRADERFVRFSKAFMDAEKPVFAICHGPQLL 110
Cdd:cd03133   75 LAKLKAADFDALIFPGGFgaaknlsdfavKGADCTVNPEVERLVREFHQAGKPIGAICIAPALA 138
GATase1_1 cd01741
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ...
 4-119 9.93e-05

Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: 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. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase.


Pssm-ID: 153212 [Multi-domain]  Cd Length: 188  Bit Score: 40.69  E-value: 9.93e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   4 KIAILITDYFEDTEYTEpaEAFKQKGYELTTIEaekgktvhgkqgksEVVIDKGIDNVSPENFDALFIPGGFSpDILRAD 83
Cdd:cd01741    1 RILILQHDTPEGPGLFE--DLLREAGAETIEID--------------VVDVYAGELLPDLDDYDGLVILGGPM-SVDEDD 63

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 984812023  84 ERFV----RFSKAFMDAEKPVFAICHGPQLLitAQTLEGR 119
Cdd:cd01741   64 YPWLkklkELIRQALAAGKPVLGICLGHQLL--ARALGGK 101
GlxA COG4977
Transcriptional regulator GlxA, contains an amidase domain and an AraC-type DNA-binding HTH ...
 3-122 1.22e-04

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: 41.30  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023   3 KKIAILITDYFEDTEYTEPAEAF-------KQKGYELTTIeAEKGKTVHGKQGkSEVVIDKGIDnvSPENFDALFIPGGF 75
Cdd:COG4977    1 LRVAFLLLPGFSLLDLAGPLEVFrlanrlaGRPLYRWRLV-SLDGGPVRSSSG-LTVAPDHGLA--DLAAADTLIVPGGL 76

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 984812023  76 SPDiLRADERFVRFSKAFMDAEKPVFAICHGPQLLitAQT--LEGRDVT 122
Cdd:COG4977   77 DPA-AAADPALLAWLRRAAARGARLASICTGAFLL--AAAglLDGRRAT 122
GATase pfam00117
Glutamine amidotransferase class-I;
49-110 1.23e-03

Glutamine amidotransferase class-I;


Pssm-ID: 395067 [Multi-domain]  Cd Length: 188  Bit Score: 37.60  E-value: 1.23e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 984812023   49 KSEVV-IDKGIDNVSPENFDALFIPGGF-SPDilrADERFVRFSKAFMDAEKPVFAICHGPQLL 110
Cdd:pfam00117  23 EVTVVpNDTPAEEILEENPDGIILSGGPgSPG---AAGGAIEAIREARELKIPILGICLGHQLL 83
GATase1_CobQ cd01750
Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type ...
 62-110 1.91e-03

Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ); Type 1 glutamine amidotransferase (GATase1) domain found in Cobyric Acid Synthase (CobQ). CobQ plays a role in cobalamin biosythesis. CobQ catalyses amidations at positions B, D, E, and G on adenosylcobyrinic A,C-diamide in the biosynthesis of cobalamin. CobQ belongs to the triad family of amidotransferases. Two of the three residues of the catalytic triad that are involved in glutamine binding, hydrolysis and transfer of the resulting ammonia to the acceptor substrate in other triad aminodotransferases are conserved in CobQ.


Pssm-ID: 153221 [Multi-domain]  Cd Length: 194  Bit Score: 37.23  E-value: 1.91e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 984812023  62 SPENFDALFIPGG--FSPDILRADER-FVRFSKAFMDAEKPVFAICHGPQLL 110
Cdd:cd01750   34 GLGDADLIILPGSkdTIQDLAWLRKRgLAEAIKNYARAGGPVLGICGGYQML 85
GATase1_AraC_ArgR_like cd03136
AraC transcriptional regulators having an N-terminal Type 1 glutamine amidotransferase ...
 63-122 2.96e-03

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: 36.79  E-value: 2.96e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 984812023  63 PENFDALFIPGGFSPDiLRADERFVRFSKAFMDAEKPVFAICHGPQLLITAQTLEGRDVT 122
Cdd:cd03136   62 APPLDYLFVVGGLGAR-RAVTPALLAWLRRAARRGVALGGIDTGAFLLARAGLLDGRRAT 120
GATase1_catalase cd03132
Type 1 glutamine amidotransferase (GATase1)-like domain found in at the C-terminal of several ...
 2-74 6.57e-03

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: 35.32  E-value: 6.57e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 984812023   2 SKKIAILITDYFEDTEYTEPAEAFKQKGYELTTIeAEKGKTVHGKQGKSEVViDKGIDNVSPENFDALFIPGG 74
Cdd:cd03132    1 GRKVGILVADGVDAAELSALKAALKAAGANVKVV-APTLGGVVDSDGKTLEV-DQTYAGAPSVLFDAVVVPGG 71
GATase_3 pfam07685
CobB/CobQ-like glutamine amidotransferase domain;
63-110 8.35e-03

CobB/CobQ-like glutamine amidotransferase domain;


Pssm-ID: 429595 [Multi-domain]  Cd Length: 189  Bit Score: 35.29  E-value: 8.35e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 984812023   63 PENFDALFIPGGFS---PDILRADERFVRFSKAFMDAEKPVFAICHGPQLL 110
Cdd:pfam07685  40 GPDADLIILPGGKPtiqDLALLRNSGMDEAIKEAAEDGGPVLGICGGYQML 90
 
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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