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Conserved domains on  [gi|755523881|ref|XP_006536234|]
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glutamine amidotransferase-like class 1 domain-containing protein 1 isoform X1 [Mus musculus]

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 ...
 12-201 9.32e-53

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: 168.50  E-value: 9.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  12 CLLVASGASE--------GVSAQSFVHCF-TLASAAFNLQVATPGGK--AIDFVDVT-ESNARWVQDFRL----KAYASP 75
Cdd:cd03141    1 ILIVLTSADKlggtgrptGLWLEELAHPYdVFTEAGYEVDFASPKGGkvPLDPRSLDaEDDDDASVFDNDeefkKKLANT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  76 AKLESIDGARYHALLIPSCPGALTDLAS---------------KPICAIGHGVAALCCATNEDRSWVFQGYSLTGPSVYE 140
Cdd:cd03141   81 KKLSDVDPSDYDAIFIPGGHGPMFDLPDnpdlqdllrefyengKVVAAVCHGPAALLNVKLSDGKSLVAGKTVTGFTNEE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523881 141 LIRAPGFARLPLIVEDFVKDSGAGFSASEPDAVHVVLDRHLVTGQNANSTVPAVQNLLFLC 201
Cdd:cd03141  161 EEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
 
Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 12-201 9.32e-53

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: 168.50  E-value: 9.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  12 CLLVASGASE--------GVSAQSFVHCF-TLASAAFNLQVATPGGK--AIDFVDVT-ESNARWVQDFRL----KAYASP 75
Cdd:cd03141    1 ILIVLTSADKlggtgrptGLWLEELAHPYdVFTEAGYEVDFASPKGGkvPLDPRSLDaEDDDDASVFDNDeefkKKLANT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  76 AKLESIDGARYHALLIPSCPGALTDLAS---------------KPICAIGHGVAALCCATNEDRSWVFQGYSLTGPSVYE 140
Cdd:cd03141   81 KKLSDVDPSDYDAIFIPGGHGPMFDLPDnpdlqdllrefyengKVVAAVCHGPAALLNVKLSDGKSLVAGKTVTGFTNEE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523881 141 LIRAPGFARLPLIVEDFVKDSGAGFSASEPDAVHVVLDRHLVTGQNANSTVPAVQNLLFLC 201
Cdd:cd03141  161 EEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 34-198 6.49e-10

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: 55.88  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  34 LASAAFNLQVATPGGKAIdfvdVTESNARWVQdfrlkayaSPAKLESIDGARYHALLIPSCPGALTDL------------ 101
Cdd:COG0693   25 LREAGAEVDVASPEGGPP----VTSKHGITVT--------ADKTLDDVDPDDYDALVLPGGHGAPDDLredpdvvalvre 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881 102 ---ASKPICAIGHGVAALCcatnedRSWVFQGYSLTG-PSVyelirapgfarlplivEDFVKDSGAGFSASepdavHVVL 177
Cdd:COG0693   93 fyeAGKPVAAICHGPAVLA------AAGLLKGRKVTSfPNI----------------EDDLKNAGATYVDE-----EVVV 145

                        170       180
                 ....*....|....*....|.
gi 755523881 178 DRHLVTGQNANSTVPAVQNLL 198
Cdd:COG0693  146 DGNLITSRGPGDAPAFARALL 166
 
Name Accession Description Interval E-value
GATase1_Hsp31_like cd03141
Type 1 glutamine amidotransferase (GATase1)-like domain found in proteins similar to ...
 12-201 9.32e-53

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: 168.50  E-value: 9.32e-53
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  12 CLLVASGASE--------GVSAQSFVHCF-TLASAAFNLQVATPGGK--AIDFVDVT-ESNARWVQDFRL----KAYASP 75
Cdd:cd03141    1 ILIVLTSADKlggtgrptGLWLEELAHPYdVFTEAGYEVDFASPKGGkvPLDPRSLDaEDDDDASVFDNDeefkKKLANT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  76 AKLESIDGARYHALLIPSCPGALTDLAS---------------KPICAIGHGVAALCCATNEDRSWVFQGYSLTGPSVYE 140
Cdd:cd03141   81 KKLSDVDPSDYDAIFIPGGHGPMFDLPDnpdlqdllrefyengKVVAAVCHGPAALLNVKLSDGKSLVAGKTVTGFTNEE 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755523881 141 LIRAPGFARLPLIVEDFVKDSGAGFSASEPDAVHVVLDRHLVTGQNANSTVPAVQNLLFLC 201
Cdd:cd03141  161 EEAAGLKKVVPFLLEDELKELGANYVKAEPWAEFVVVDGRLITGQNPASAAAVAEALVKAL 221
YajL COG0693
Protein/nucleotide deglycase, PfpI/YajL/DJ-1 family (repair of methylglyoxal-glycated proteins ...
 34-198 6.49e-10

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: 55.88  E-value: 6.49e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881  34 LASAAFNLQVATPGGKAIdfvdVTESNARWVQdfrlkayaSPAKLESIDGARYHALLIPSCPGALTDL------------ 101
Cdd:COG0693   25 LREAGAEVDVASPEGGPP----VTSKHGITVT--------ADKTLDDVDPDDYDALVLPGGHGAPDDLredpdvvalvre 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755523881 102 ---ASKPICAIGHGVAALCcatnedRSWVFQGYSLTG-PSVyelirapgfarlplivEDFVKDSGAGFSASepdavHVVL 177
Cdd:COG0693   93 fyeAGKPVAAICHGPAVLA------AAGLLKGRKVTSfPNI----------------EDDLKNAGATYVDE-----EVVV 145

                        170       180
                 ....*....|....*....|.
gi 755523881 178 DRHLVTGQNANSTVPAVQNLL 198
Cdd:COG0693  146 DGNLITSRGPGDAPAFARALL 166
 
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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