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Conserved domains on  [gi|1679321070|ref|WP_138893206|]
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type 1 glutamine amidotransferase domain-containing protein [Mycobacterium sp. KBS0706]

Protein Classification

type 1 glutamine amidotransferase domain-containing protein( domain architecture ID 10123442)

type 1 glutamine amidotransferase (GATase1) domain-containing protein similar to Homo sapiens glutamine amidotransferase-like class 1 domain-containing protein 1 (GATD1)

CATH:  3.40.50.880
Gene Ontology:  GO:0019172
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 3-223 3.14e-107

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: 307.95  E-value: 3.14e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070   3 ILMVFTSHDVLGKTGRKTGFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPVDPKSDLPENQTpAMTRFKQDPQAQKDFAN 82
Cdd:cd03141     1 ILIVLTSADKLGGTGRPTGLWLEELAHPYDVFTEAGYEVDFASPKGGKVPLDPRSLDAEDDD-DASVFDNDEEFKKKLAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  83 TFFLKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVAYK-GEPIVKGKRVTGFTNT 161
Cdd:cd03141    80 TKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSdGKSLVAGKTVTGFTNE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1679321070 162 EEEEVQLTHVVPFLVEDELRRLGGIFKKVPNWQSFAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:cd03141   160 EEEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
 
Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 3-223 3.14e-107

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: 307.95  E-value: 3.14e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070   3 ILMVFTSHDVLGKTGRKTGFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPVDPKSDLPENQTpAMTRFKQDPQAQKDFAN 82
Cdd:cd03141     1 ILIVLTSADKLGGTGRPTGLWLEELAHPYDVFTEAGYEVDFASPKGGKVPLDPRSLDAEDDD-DASVFDNDEEFKKKLAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  83 TFFLKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVAYK-GEPIVKGKRVTGFTNT 161
Cdd:cd03141    80 TKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSdGKSLVAGKTVTGFTNE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1679321070 162 EEEEVQLTHVVPFLVEDELRRLGGIFKKVPNWQSFAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:cd03141   160 EEEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-224 1.07e-57

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: 180.68  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070   1 MKILMVFTShdvlgktgrktGFWLEEGAAPYFVFRDAGVSLTLASPKGGqPPVdpKSDLpenqtpamtrfkqdpqaQKDF 80
Cdd:COG0693     3 KKVLILLTD-----------GFEDEELTVPYDALREAGAEVDVASPEGG-PPV--TSKH-----------------GITV 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  81 ANTFFLKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVaykgePIVKGKRVTGFTN 160
Cdd:COG0693    52 TADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAA-----GLLKGRKVTSFPN 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1679321070 161 teeeevqlthvvpflVEDELRRLGGIFKkvpnwQSFAITDGRLITGQNPASSTAGAQHLLKLLS 224
Cdd:COG0693   127 ---------------IEDDLKNAGATYV-----DEEVVVDGNLITSRGPGDAPAFARALLELLA 170
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 20-223 3.58e-17

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: 75.92  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  20 TGFWLEEGAAPYFVFRDAGVSLTLASPKGGQppvdpKSDLPENQtpamtrFKQDPQAQkdfantfflkDMRSEGFDAVFY 99
Cdd:TIGR01382   8 DEFEDSELLYPLDRLREAGHEVDTVSKEAGT-----TVGKHGYS------VTVDATID----------EVNPEEYDALVI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 100 PGGHGPMWdLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVAykgepIVKGKRVTGFTNteeeevqlthvvpflVEDE 179
Cdd:TIGR01382  67 PGGRAPEY-LRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAG-----VLRGKKLTSYPA---------------IIDD 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1679321070 180 LRRLGGIFKKvpnwQSFAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:TIGR01382 126 VKNAGAEYVD----IEVVVVDGNLVTSRVPDDLPAFNREFLKLL 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 21-225 5.63e-17

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: 75.37  E-value: 5.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  21 GFWLEEGAAPYFVFRDAGVSLTLASPKGGqpPVDPKSDLpenqtpamtRFKQDPQaqkdfantffLKDMRSEGFDAVFYP 100
Cdd:pfam01965  10 GFEDIELIYPADVLRRAGIKVTVVSVDGG--EVKGSRGV---------KVTVDAS----------LDDVKPDDYDALVLP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 101 GGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRvaykgEPIVKGKRVTGFtnteeeevqlthvvpFLVEDEL 180
Cdd:pfam01965  69 GGRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAA-----AGVLKGRKVTSH---------------PAVKDDL 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1679321070 181 RRLGGIFKKVPnwqsfAITDGRLITGQNPassTAGAQHLLKLLSE 225
Cdd:pfam01965 129 INAGATYVDKP-----VVVDGNLVTSRGP---GDAPEFALEILEQ 165
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
86-142 3.35e-07

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 49.40  E-value: 3.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1679321070  86 LKDMRSEGFDAVFYPGGHGPMWDLVD----------NPDSIALIESFYNSGKPVAAVCHAPAVLHRV 142
Cdd:PRK11780   78 LAEADAEDFDALIVPGGFGAAKNLSNfavkgaectvNPDVKALVRAFHQAGKPIGFICIAPAMLPKI 144
 
Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 3-223 3.14e-107

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: 307.95  E-value: 3.14e-107
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070   3 ILMVFTSHDVLGKTGRKTGFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPVDPKSDLPENQTpAMTRFKQDPQAQKDFAN 82
Cdd:cd03141     1 ILIVLTSADKLGGTGRPTGLWLEELAHPYDVFTEAGYEVDFASPKGGKVPLDPRSLDAEDDD-DASVFDNDEEFKKKLAN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  83 TFFLKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVAYK-GEPIVKGKRVTGFTNT 161
Cdd:cd03141    80 TKKLSDVDPSDYDAIFIPGGHGPMFDLPDNPDLQDLLREFYENGKVVAAVCHGPAALLNVKLSdGKSLVAGKTVTGFTNE 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1679321070 162 EEEEVQLTHVVPFLVEDELRRLGGIFKKVPNWQSFAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:cd03141   160 EEEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 1-224 1.07e-57

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: 180.68  E-value: 1.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070   1 MKILMVFTShdvlgktgrktGFWLEEGAAPYFVFRDAGVSLTLASPKGGqPPVdpKSDLpenqtpamtrfkqdpqaQKDF 80
Cdd:COG0693     3 KKVLILLTD-----------GFEDEELTVPYDALREAGAEVDVASPEGG-PPV--TSKH-----------------GITV 51

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  81 ANTFFLKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVaykgePIVKGKRVTGFTN 160
Cdd:COG0693    52 TADKTLDDVDPDDYDALVLPGGHGAPDDLREDPDVVALVREFYEAGKPVAAICHGPAVLAAA-----GLLKGRKVTSFPN 126

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1679321070 161 teeeevqlthvvpflVEDELRRLGGIFKkvpnwQSFAITDGRLITGQNPASSTAGAQHLLKLLS 224
Cdd:COG0693   127 ---------------IEDDLKNAGATYV-----DEEVVVDGNLITSRGPGDAPAFARALLELLA 170
GATase1_Ydr533c_like cd03147
Type 1 glutamine amidotransferase (GATase1)-like domain found in Saccharomyces cerevisiae ...
 2-223 9.02e-36

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: 126.28  E-value: 9.02e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070   2 KILMVFTS-HDVLGKTGRKTGFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPvDPKSDLPenqtPAMTRFKQDPQAQKD- 79
Cdd:cd03147     1 KALIALTSyYGPFYPDGKNTGVFFSEALHPFNVFREAGFEVDFVSETGTFGF-DDHSLDP----DFLNGEDLEVFSNKDs 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  80 -----FANTFFLKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRV--AYKGEPIVKG 152
Cdd:cd03147    76 dfwkkLKNIKKADEVNPDDYGIFFVAGGHGTLFDFPHATNLQKIAQQIYANGGVVAAVCHGPAILANLkdPKTGKPLIKG 155

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1679321070 153 KRVTGFTNTEEEEVQLTHVVPFL----VEDELRRLGGIFKKVPN-WQSFAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:cd03147   156 KTVTGFTDKGEEIMGVMEILKKRnlesIEDIAERAGANFIRPPGpWDDFTVVDGRIVTGSNPASATSTAEAAIKAL 231
GATase1_PfpI_like cd03134
A type 1 glutamine amidotransferase (GATase1)-like domain found in PfpI from Pyrococcus ...
 30-209 1.53e-19

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: 82.21  E-value: 1.53e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  30 PYFVFRDAGVSLTLASPKGGQPpvdpksdlpenqtpaMTRFKQDPQAQKDFAntffLKDMRSEGFDAVFYPGGHGPmwDL 109
Cdd:cd03134    18 PLYRLREAGAEVVVAGPEAGGE---------------IQGKHGYDTVTVDLT----IADVDADDYDALVIPGGTNP--DK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 110 VD-NPDSIALIESFYNSGKPVAAVCHAPAVLhrVAYKgepIVKGKRVTGFtnteeeevqlthvvpFLVEDELRRLGGIFK 188
Cdd:cd03134    77 LRrDPDAVAFVRAFAEAGKPVAAICHGPWVL--ISAG---VVRGRKLTSY---------------PSIKDDLINAGANWV 136

                         170       180
                  ....*....|....*....|.
gi 1679321070 189 KVPnwqsfAITDGRLITGQNP 209
Cdd:cd03134   137 DEE-----VVVDGNLITSRNP 152
GATase1_PfpI_1 cd03169
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 26-223 1.06e-17

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: 77.69  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  26 EGAAPYFVFRDAGVSLTLASP--KGGQPPVDPKSDLPENQTPaMTRFKQDPQAQKDFAntfflkDMRSEGFDAVFYPGGH 103
Cdd:cd03169    14 EVMVPFQALQEVGHEVDVVAPgkKKGDTVVTAIHDFPGWQTY-TEKPGHRFAVTADFD------EVDPDDYDALVIPGGR 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 104 GPMWdLVDNPDSIALIESFYNSGKPVAAVCHAPAVLhrvAYKGepIVKGKRVTGFtnteeeevqlthvvpFLVEDELRRL 183
Cdd:cd03169    87 APEY-LRLDEKVLAIVRHFAEANKPVAAICHGPQIL---AAAG--VLKGRRCTAY---------------PACKPEVELA 145

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1679321070 184 GGIFKKVPnwqsfAITDGRLITGQ----NPASstagAQHLLKLL 223
Cdd:cd03169   146 GGTVVDDG-----VVVDGNLVTAQawpdHPAF----LREFLKLL 180
GATase1_DJ-1 cd03135
Type 1 glutamine amidotransferase (GATase1)-like domain found in Human DJ-1; Type 1 glutamine ...
 21-223 1.92e-17

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: 76.44  E-value: 1.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  21 GFWLEEGAAPYFVFRDAGVSLTLASPkggqppvdpksdlpENQTPAMTRFKQDPQAQKDfantffLKDMRSEGFDAVFYP 100
Cdd:cd03135     8 GFEEIEAVTPVDVLRRAGIEVTTASL--------------EKKLAVGSSHGIKVKADKT------LSDVNLDDYDAIVIP 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 101 GGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLhrvAYKGepIVKGKRVTGFtnteeeevqlthvvPfLVEDEL 180
Cdd:cd03135    68 GGLPGAQNLADNEKLIKLLKEFNAKGKLIAAICAAPAVL---AKAG--LLKGKKATCY--------------P-GFEDKL 127

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1679321070 181 rrLGGIFKKVPnwqsfAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:cd03135   128 --GGANYVDEP-----VVVDGNIITSRGPGTAFEFALKIVEAL 163
PfpI TIGR01382
intracellular protease, PfpI family; The member of this family from Pyrococcus horikoshii has ...
 20-223 3.58e-17

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: 75.92  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  20 TGFWLEEGAAPYFVFRDAGVSLTLASPKGGQppvdpKSDLPENQtpamtrFKQDPQAQkdfantfflkDMRSEGFDAVFY 99
Cdd:TIGR01382   8 DEFEDSELLYPLDRLREAGHEVDTVSKEAGT-----TVGKHGYS------VTVDATID----------EVNPEEYDALVI 66

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 100 PGGHGPMWdLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVAykgepIVKGKRVTGFTNteeeevqlthvvpflVEDE 179
Cdd:TIGR01382  67 PGGRAPEY-LRLNNKAVRLVREFVEKGKPVAAICHGPQLLISAG-----VLRGKKLTSYPA---------------IIDD 125

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1679321070 180 LRRLGGIFKKvpnwQSFAITDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:TIGR01382 126 VKNAGAEYVD----IEVVVVDGNLVTSRVPDDLPAFNREFLKLL 165
DJ-1_PfpI pfam01965
DJ-1/PfpI family; The family includes the protease PfpI. This domain is also found in ...
 21-225 5.63e-17

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: 75.37  E-value: 5.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  21 GFWLEEGAAPYFVFRDAGVSLTLASPKGGqpPVDPKSDLpenqtpamtRFKQDPQaqkdfantffLKDMRSEGFDAVFYP 100
Cdd:pfam01965  10 GFEDIELIYPADVLRRAGIKVTVVSVDGG--EVKGSRGV---------KVTVDAS----------LDDVKPDDYDALVLP 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 101 GGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRvaykgEPIVKGKRVTGFtnteeeevqlthvvpFLVEDEL 180
Cdd:pfam01965  69 GGRAGPERLRDNEKLVEFVKDFYEKGKPVAAICHGPQVLAA-----AGVLKGRKVTSH---------------PAVKDDL 128

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 1679321070 181 RRLGGIFKKVPnwqsfAITDGRLITGQNPassTAGAQHLLKLLSE 225
Cdd:pfam01965 129 INAGATYVDKP-----VVVDGNLVTSRGP---GDAPEFALEILEQ 165
GATase1 cd01653
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 21-139 6.13e-13

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: 63.39  E-value: 6.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  21 GFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPVDPKSDlpenqtpamtrfkqdpqaqkdfantfflkdmrseGFDAVFYP 100
Cdd:cd01653     8 GFEELELASPLDALREAGAEVDVVSPDGGPVESDVDLD----------------------------------DYDGLILP 53

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1679321070 101 GGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVL 139
Cdd:cd01653    54 GGPGTPDDLARDEALLALLREAAAAGKPILGICLGAQLL 92
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 21-139 6.62e-13

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: 62.60  E-value: 6.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  21 GFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPVDPKSDlpenqtpamtrfkqdpqaqkdfantfflkdmrseGFDAVFYP 100
Cdd:cd03128     8 GSEELELASPLDALREAGAEVDVVSPDGGPVESDVDLD----------------------------------DYDGLILP 53

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1679321070 101 GGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVL 139
Cdd:cd03128    54 GGPGTPDDLAWDEALLALLREAAAAGKPVLGICLGAQLL 92
ThiJ_like pfam17124
ThiJ/PfpI family-like; This is a family of fungal and bacterial ThiJ/PfpI-like proteins.
 20-143 3.19e-12

ThiJ/PfpI family-like; This is a family of fungal and bacterial ThiJ/PfpI-like proteins.


Pssm-ID: 435734  Cd Length: 186  Bit Score: 63.16  E-value: 3.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  20 TGFWLEEGAAPYFVFRDAGVSLTLASPKGGQPPVDPKSdlpenQTPAMTRFKQDPQAQKD----------FANTfflKDM 89
Cdd:pfam17124   4 EGYDVTEVCIPWRYFTDHGFMVEFATPHGIVPQADQRL-----LSGWKGKLLGASKEAKDiysrmstleeFTNP---LSW 75

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1679321070  90 RSEGF-----DAVFYPGGHGPM-WDLVDNP-------DSIALIESFYNSGKPVAAVCHAPAVLHRVA 143
Cdd:pfam17124  76 SSEGFtltpyDLVLIPGGHDPGvRELVDSPrlhsllvPYLPLCKRIGSPSKVLGAICQGVLALSEAA 142
not_thiJ TIGR01383
DJ-1 family protein; This model represents the DJ-1 clade of the so-called ThiJ/PfpI family of ...
 86-223 3.19e-10

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: 57.33  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  86 LKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHrvaykGEPIVKGKRVTGFTNteeee 165
Cdd:TIGR01383  56 LEDVDLEKFDVIVLPGGMPGAENLRNSKLLLNILKSQESKGKLVAAICAAPAVLL-----AHGVLLGKKATCYPG----- 125

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1679321070 166 vqlthvvpflVEDELrrLGGIFKKVPNWQsfaiTDGRLITGQNPASSTAGAQHLLKLL 223
Cdd:TIGR01383 126 ----------FKEKL--LNGNYSVNKTVV----VDGNLITSRGPGTAIEFALELVELL 167
PRK11780 PRK11780
isoprenoid biosynthesis glyoxalase ElbB;
86-142 3.35e-07

isoprenoid biosynthesis glyoxalase ElbB;


Pssm-ID: 236980  Cd Length: 217  Bit Score: 49.40  E-value: 3.35e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1679321070  86 LKDMRSEGFDAVFYPGGHGPMWDLVD----------NPDSIALIESFYNSGKPVAAVCHAPAVLHRV 142
Cdd:PRK11780   78 LAEADAEDFDALIVPGGFGAAKNLSNfavkgaectvNPDVKALVRAFHQAGKPIGFICIAPAMLPKI 144
GATase1_PfpI_3 cd03140
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 84-223 4.33e-07

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: 48.37  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  84 FFLKDMRSEGFDAVFYPGGHgpMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRvaykgepivkgkrvTGFTNtee 163
Cdd:cd03140    51 YSLDDLPPEDYDLLILPGGD--SWDNPEAPDLAGLVRQALKQGKPVAAICGATLALAR--------------AGLLN--- 111

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1679321070 164 eevQLTHVVpflveDELRRLGGIFKKVPNWQSF----AITDGRLITgqnpASSTAG---AQHLLKLL 223
Cdd:cd03140   112 ---NRKHTS-----NSLDFLKAHAPYYGGAEYYdepqAVSDGNLIT----ANGTAPvefAAEILRAL 166
GATase1_ES1 cd03133
Type 1 glutamine amidotransferase (GATase1)-like domain found in zebrafish ES1; Type 1 ...
 86-156 2.24e-06

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: 46.85  E-value: 2.24e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  86 LKDMRSEGFDAVFYPGGHGPMWDLVD----------NPDSIALIESFYNSGKPVAAVCHAPAVLHRVaykgepIVKGKRV 155
Cdd:cd03133    75 LAKLKAADFDALIFPGGFGAAKNLSDfavkgadctvNPEVERLVREFHQAGKPIGAICIAPALAAKI------LGEGVEV 148


                  .
gi 1679321070 156 T 156
Cdd:cd03133   149 T 149
GATase1_PfpI_2 cd03139
Type 1 glutamine amidotransferase (GATase1)-like domain found in a subgroup of proteins ...
 28-223 2.08e-05

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


Pssm-ID: 153233 [Multi-domain]  Cd Length: 183  Bit Score: 43.69  E-value: 2.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  28 AAPYFVF-----RDAGVSLTLASPKGGQPPVDPKSDLPENqtpamTRFKQDPQaqkdfantfflkdmrsegFDAVFYPGG 102
Cdd:cd03139    15 IGPYEVFgraprLAAPFEVFLVSETGGPVSSRSGLTVLPD-----TSFADPPD------------------LDVLLVPGG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070 103 HGpMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVaykGepIVKGKRVTgftnteeeevqlTHvvpFLVEDELRR 182
Cdd:cd03139    72 GG-TRALVNDPALLDFIRRQAARAKYVTSVCTGALLLAAA---G--LLDGRRAT------------TH---WAAIDWLKE 130

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1679321070 183 LGGIFKKVPNWqsfaITDGRLITGqnpASSTAG---AQHLLKLL 223
Cdd:cd03139   131 FGAIVVVDARW----VVDGNIWTS---GGVSAGidmALALVARL 167
PRK04155 PRK04155
protein deglycase HchA;
96-221 4.10e-05

protein deglycase HchA;


Pssm-ID: 235228 [Multi-domain]  Cd Length: 287  Bit Score: 43.45  E-value: 4.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  96 AVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLHRVAY-KGEPIVKGKRVTGFTNTEEEEVQ----LTH 170
Cdd:PRK04155  150 AVFIPGGHGALIGLPESEDVAAALQWALDNDRFIITLCHGPAALLAAGVdHGDNPLNGYSICAFPDALDKQTPeigyMPG 229

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1679321070 171 VVPFLVEDELRRLG------GIFKKVpnwqsfaITDGRLITGQNPASSTA----GAQHLLK 221
Cdd:PRK04155  230 HLTWLFGEELKKMGvnivndDITGRV-------HKDRKLLTGDSPLASNAlgklAAQELLA 283
GATase1_AraC_2 cd03138
AraC transcriptional regulators having a Type 1 glutamine amidotransferase (GATase1)-like ...
 91-236 1.34e-03

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: 38.40  E-value: 1.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1679321070  91 SEGFDAVFYPGGHGPM--WDLVDNPDSIALIESFYNSGKPVAAVCHAPAVLhrvAYKGepIVKGKRVTgftnteeeevql 168
Cdd:cd03138    67 VPAPDLVIVPGLGGDPdeLLLADNPALIAWLRRQHANGATVAAACTGVFLL---AEAG--LLDGRRAT------------ 129

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1679321070 169 THvvpFLVEDELRRLggiFKKV-PNWQSFAITDGRLITGqnpASSTAGAQHLLKLLSETTSATRASSAA 236
Cdd:cd03138   130 TH---WWLAPQFRRR---FPKVrLDPDRVVVTDGNLITA---GGAMAWADLALHLIERLAGPELAQLVA 189
PRK11574 PRK11574
protein deglycase YajL;
86-139 1.58e-03

protein deglycase YajL;


Pssm-ID: 183210 [Multi-domain]  Cd Length: 196  Bit Score: 38.22  E-value: 1.58e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1679321070  86 LKDMRSEGFDAVFYPGGHGPMWDLVDNPDSIALIESFYNSGKPVAAVCHAPAVL 139
Cdd:PRK11574   59 LVEVADGDFDVIVLPGGIKGAECFRDSPLLVETVRQFHRSGRIVAAICAAPATV 112
 
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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