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Conserved domains on  [gi|446684800|ref|WP_000762146|]
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MULTISPECIES: peptidase E [Bacillus]

Protein Classification

peptidase E( domain architecture ID 10123553)

peptidase E is a serine hydrolase that hydrolyses only Asp-X dipeptides and one tripeptide Asp-Gly-Gly

CATH:  3.40.50.880
EC:  3.4.13.21
Gene Ontology:  GO:0016805|GO:0008236|GO:0006508|GO:0008233
MEROPS:  S51
PubMed:  10387030
SCOP:  3001405

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GAT1_Peptidase_E cd03146
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine ...
 2-213 3.05e-68

Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. 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 typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus PepE is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption.


:

Pssm-ID: 153240 [Multi-domain]  Cd Length: 212  Bit Score: 208.67  E-value: 3.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   2 KLAVIGGGDLQDSNHS-PINERLIELTNKQYPKVLFIPTASHDDESYIKLFLDTFEKQLHCEVQILRiiadTPSKYEIDE 80
Cdd:cd03146    1 KLLLTSGGGLGYLAHAlPAIDDLLLSLTKARPKVLFVPTASGDRDEYTARFYAAFESLRGVEVSHLH----LFDTEDPLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  81 MIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIRSDYEGSGYIES-NGWGIVNKRFC 159
Cdd:cd03146   77 ALLEADVIYVGGGNTFNLLAQWREHGLDAILKAALERGVVYIGWSAGSNCWFPSIGTTDSMPIELPPSfNGLGLLPFQIC 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446684800 160 PHYNQL---NRMNAFHSFLQNHQgNIEGIALEDNCALYITKESFEIIGEPEKAWEFY 213
Cdd:cd03146  157 PHYDSEdgeTREERFHEFLEAGP-TEPVIALDEGAALHVVGDGVADLLGEGAALVFD 212
 
Name Accession Description Interval E-value
GAT1_Peptidase_E cd03146
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine ...
 2-213 3.05e-68

Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. 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 typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus PepE is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption.


Pssm-ID: 153240 [Multi-domain]  Cd Length: 212  Bit Score: 208.67  E-value: 3.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   2 KLAVIGGGDLQDSNHS-PINERLIELTNKQYPKVLFIPTASHDDESYIKLFLDTFEKQLHCEVQILRiiadTPSKYEIDE 80
Cdd:cd03146    1 KLLLTSGGGLGYLAHAlPAIDDLLLSLTKARPKVLFVPTASGDRDEYTARFYAAFESLRGVEVSHLH----LFDTEDPLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  81 MIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIRSDYEGSGYIES-NGWGIVNKRFC 159
Cdd:cd03146   77 ALLEADVIYVGGGNTFNLLAQWREHGLDAILKAALERGVVYIGWSAGSNCWFPSIGTTDSMPIELPPSfNGLGLLPFQIC 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446684800 160 PHYNQL---NRMNAFHSFLQNHQgNIEGIALEDNCALYITKESFEIIGEPEKAWEFY 213
Cdd:cd03146  157 PHYDSEdgeTREERFHEFLEAGP-TEPVIALDEGAALHVVGDGVADLLGEGAALVFD 212
Peptidase_S51 pfam03575
Peptidase family S51;
3-203 2.21e-65

Peptidase family S51;


Pssm-ID: 397574 [Multi-domain]  Cd Length: 206  Bit Score: 201.37  E-value: 2.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800    3 LAVIGGGDLQDSNH-SPINERLIELTNKQYPKVLFIPTA--SHDDESYIKLFLDTFEKqLHCEVQILRIIADTPSkyEID 79
Cdd:pfam03575   1 LLLLSSSTFSGEPYlEHALPAILDFLGKANKRVLFIPTAsvSGDHDEYVEKVRKALEK-LGCEVDGLHLSTDPLA--EIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   80 EMIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIRSDYEGSGYIES---NGWGIVNK 156
Cdd:pfam03575  78 EKLLEADGIYVGGGNTFHLLKLLYETGLDKIIREAVQAGLPYIGWSAGANVAGPSIITTSYMDMPIVAPpsfEALGLVPF 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 446684800  157 RFCPHY---NQLNRMNAFHSFLQNHQGNIeGIALEDNCALYITKESFEII 203
Cdd:pfam03575 158 QINPHYlghNGETREERLAEFVESNPGTP-GIGLDEGTALHIEGDTARLI 206
PepE COG3340
Peptidase E [Amino acid transport and metabolism];
3-214 4.04e-58

Peptidase E [Amino acid transport and metabolism];


Pssm-ID: 442569 [Multi-domain]  Cd Length: 212  Bit Score: 183.09  E-value: 4.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   3 LAVIGGGDLQDSNHSPINERLIELTNKQYPKVLFIPTAS--HDDESYIKLFLDTFEKqLHCEVQILRIiaDTPSKYEIDE 80
Cdd:COG3340    1 LLLTSGGTFNGSEYEYLDEALLELLGKGRPKVLFIPTASvgGDHDAYTAKFYEAFSK-LGVKVSVLHL--FSPTFEDPVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  81 MIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFtSSIRSDYEGSGYIES-NGWGIVNKRFC 159
Cdd:COG3340   78 ALLEADVIFVGGGNTFNLLALWREHGLDDILREAVEAGTVYAGVSAGSNCWF-PTIRTTNDGPPPLRSfDGLGLVPFSIN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446684800 160 PHY----NQLNRMNAFHSFLQNHQgNIEGIALEDNCALYITKESFEIIGepEKAWEFYM 214
Cdd:COG3340  157 PHYddedMGETREPRIHEFLASNP-LPPVYALDDGTALHVRGGKLEVVG--EGAYRVFR 212
PRK05282 PRK05282
dipeptidase PepE;
33-137 6.09e-07

dipeptidase PepE;


Pssm-ID: 179990  Cd Length: 233  Bit Score: 48.72  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  33 KVLFIP----TASHDDesYIKLFLDTFEKqLHCEVQILRIIADtPSKyeideMIQSADLIYLGGGNYIQMITEWKEHKLD 108
Cdd:PRK05282  33 KAVFIPyagvTQSWDD--YTAKVAEALAP-LGIEVTGIHRVAD-PVA-----AIENAEAIFVGGGNTFQLLKQLYERGLL 103

                         90       100       110
                 ....*....|....*....|....*....|
gi 446684800 109 EKLLLALEQGTLIAGCSAGA-MCwfTSSIR 137
Cdd:PRK05282 104 APIREAVKNGTPYIGWSAGAnVA--GPTIR 131
 
Name Accession Description Interval E-value
GAT1_Peptidase_E cd03146
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine ...
 2-213 3.05e-68

Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. 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 typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus PepE is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption.


Pssm-ID: 153240 [Multi-domain]  Cd Length: 212  Bit Score: 208.67  E-value: 3.05e-68
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   2 KLAVIGGGDLQDSNHS-PINERLIELTNKQYPKVLFIPTASHDDESYIKLFLDTFEKQLHCEVQILRiiadTPSKYEIDE 80
Cdd:cd03146    1 KLLLTSGGGLGYLAHAlPAIDDLLLSLTKARPKVLFVPTASGDRDEYTARFYAAFESLRGVEVSHLH----LFDTEDPLD 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  81 MIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIRSDYEGSGYIES-NGWGIVNKRFC 159
Cdd:cd03146   77 ALLEADVIYVGGGNTFNLLAQWREHGLDAILKAALERGVVYIGWSAGSNCWFPSIGTTDSMPIELPPSfNGLGLLPFQIC 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 446684800 160 PHYNQL---NRMNAFHSFLQNHQgNIEGIALEDNCALYITKESFEIIGEPEKAWEFY 213
Cdd:cd03146  157 PHYDSEdgeTREERFHEFLEAGP-TEPVIALDEGAALHVVGDGVADLLGEGAALVFD 212
Peptidase_S51 pfam03575
Peptidase family S51;
3-203 2.21e-65

Peptidase family S51;


Pssm-ID: 397574 [Multi-domain]  Cd Length: 206  Bit Score: 201.37  E-value: 2.21e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800    3 LAVIGGGDLQDSNH-SPINERLIELTNKQYPKVLFIPTA--SHDDESYIKLFLDTFEKqLHCEVQILRIIADTPSkyEID 79
Cdd:pfam03575   1 LLLLSSSTFSGEPYlEHALPAILDFLGKANKRVLFIPTAsvSGDHDEYVEKVRKALEK-LGCEVDGLHLSTDPLA--EIE 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   80 EMIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIRSDYEGSGYIES---NGWGIVNK 156
Cdd:pfam03575  78 EKLLEADGIYVGGGNTFHLLKLLYETGLDKIIREAVQAGLPYIGWSAGANVAGPSIITTSYMDMPIVAPpsfEALGLVPF 157

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 446684800  157 RFCPHY---NQLNRMNAFHSFLQNHQGNIeGIALEDNCALYITKESFEII 203
Cdd:pfam03575 158 QINPHYlghNGETREERLAEFVESNPGTP-GIGLDEGTALHIEGDTARLI 206
PepE COG3340
Peptidase E [Amino acid transport and metabolism];
3-214 4.04e-58

Peptidase E [Amino acid transport and metabolism];


Pssm-ID: 442569 [Multi-domain]  Cd Length: 212  Bit Score: 183.09  E-value: 4.04e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   3 LAVIGGGDLQDSNHSPINERLIELTNKQYPKVLFIPTAS--HDDESYIKLFLDTFEKqLHCEVQILRIiaDTPSKYEIDE 80
Cdd:COG3340    1 LLLTSGGTFNGSEYEYLDEALLELLGKGRPKVLFIPTASvgGDHDAYTAKFYEAFSK-LGVKVSVLHL--FSPTFEDPVE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  81 MIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFtSSIRSDYEGSGYIES-NGWGIVNKRFC 159
Cdd:COG3340   78 ALLEADVIFVGGGNTFNLLALWREHGLDDILREAVEAGTVYAGVSAGSNCWF-PTIRTTNDGPPPLRSfDGLGLVPFSIN 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 446684800 160 PHY----NQLNRMNAFHSFLQNHQgNIEGIALEDNCALYITKESFEIIGepEKAWEFYM 214
Cdd:COG3340  157 PHYddedMGETREPRIHEFLASNP-LPPVYALDDGTALHVRGGKLEVVG--EGAYRVFR 212
GAT1_Peptidase_E_like cd03129
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins; ...
 3-205 3.18e-56

Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins; Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins. This group contains proteins similar to the aspartyl dipeptidases Salmonella typhimurium peptidase E and Xenopus laevis peptidase E and, extracellular cyanophycinases from Pseudomonas anguilliseptica BI (CphE) and Synechocystis sp. PCC 6803 CphB. In bacteria peptidase E is believed to play a role in degrading peptides generated by intracellular protein breakdown or imported into the cell as nutrient sources. Peptidase E uniquely hydrolyses only Asp-X dipeptides (where X is any amino acid), and one tripeptide Asp-Gly-Gly. Cyanophycinases are intracellular exopeptidases which hydrolyze the polymer cyanophycin (multi L-arginyl-poly-L-aspartic acid) to the dipeptide beta-Asp-Arg. Peptidase E and cyanophycinases are thought to have a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow. Xenopus peptidase E is developmentally regulated in response to thyroid hormone and, it is thought to play a role in apoptosis during tail reabsorption.


Pssm-ID: 153223 [Multi-domain]  Cd Length: 210  Bit Score: 178.27  E-value: 3.18e-56
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   3 LAVIGGGDLQDSNHSPINERLIELTNKQYPKVLFIPTASHDDESYIKLFLDTFEKqLHCEVQILRIIaDTPSKYEIDEMI 82
Cdd:cd03129    1 LLLISGGGLDKAHARPILQDFLARAGGAGARVLFIPTASGDRDEYGEEYRAAFER-LGVEVVHLLLI-DTANDPDVVARL 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  83 QSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIR-SDYEGS-GYIESNGWGIVNKRFCP 160
Cdd:cd03129   79 LEADGIFVGGGNQLRLLSVLRETPLLDAILKRVARGVVIGGTSAGAAVMGETGIGtTPSEPEvTPPMAPGLGLLPGIIDP 158

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 446684800 161 HYNQLNRMNAFHSFLQNHQGnIEGIALEDNCALYITKES-FEIIGE 205
Cdd:cd03129  159 HFDSRGREGRLLELLAANPT-PLGIGIDEGTALVVDGDGkAEVIGE 203
GAT1_cyanophycinase cd03145
Type 1 glutamine amidotransferase (GATase1)-like domain found in cyanophycinase; Type 1 ...
 2-205 3.73e-16

Type 1 glutamine amidotransferase (GATase1)-like domain found in cyanophycinase; Type 1 glutamine amidotransferase (GATase1)-like domain found in cyanophycinase. This group contains proteins similar to the extracellular cyanophycinases from Pseudomonas anguilliseptica BI (CphE) and Synechocystis sp. PCC 6803 CphB. Cyanophycinases are intracellular exopeptidases which hydrolyze the polymer cyanophycin (multi L-arginyl-poly-L-aspartic acid) to the dipeptide beta-Asp-Arg. Cyanophycinase is believed to be a serine-type exopeptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad typical of GATase1 domains by having a Ser in place of the reactive Cys at the nucleophile elbow.


Pssm-ID: 153239  Cd Length: 217  Bit Score: 74.25  E-value: 3.73e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   2 KLAVIGGGDLQDSNhSPINERLIELTNKQYPKVLFIPTASHDDESYIKLFLDTFEKQLHCEVQILRII----ADTPskyE 77
Cdd:cd03145    1 KLVLIGGAEDKYDN-RAILQRFVARAGGAGARIVVIPAASEEPAEVGEEYRDVFERLGAREVEVLVIDsreaANDP---E 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  78 IDEMIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAM----CWFTSS-IRSDYEGSGYIESNGWG 152
Cdd:cd03145   77 VVARLRDADGIFFTGGDQLRITSALGGTPLLDALRKVYRGGVVIGGTSAGAAvmsdTMIAGGgAGEAPRESEVDMAPGLG 156

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 446684800 153 IVNKR-FCPHYNQLNRMNAFHSFLQNHQGNIeGIALEDNCALYITKE-SFEIIGE 205
Cdd:cd03145  157 FVPNViIDQHFSQRGRLGRLLTAVARNPAAL-GIGIDENTALVVDPDgRAEVIGE 210
CphB COG4242
Cyanophycinase and related exopeptidases [Secondary metabolites biosynthesis, transport and ...
 2-205 4.87e-16

Cyanophycinase and related exopeptidases [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 443384  Cd Length: 276  Bit Score: 74.91  E-value: 4.87e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800   2 KLAVIGGGDLQDsnhsPINERLIELTNKQYPKVLFIPTASHDDESYIKLFLDTFEKqLHCE-VQILRII----ADTPSKY 76
Cdd:COG4242   17 ALLIIGGGEDKD----EILRRFVELAGGKDARIVVIPTASSEPEEVGERYRRAFER-LGAKsVEVLDIDsredANDPEVV 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  77 EIdemIQSADLIYLGGGNYIQMITEWKEHKLDEKLLLALEQGTLIAGCSAGAMCWFTSSIRSDYEGSGYIESN-----GW 151
Cdd:COG4242   92 ER---LREATGVFFTGGDQLRLTDLLGGTPLLEAIRDRYARGGVIAGTSAGAAIMSETMIAGGTSGEALRKGNvdlapGL 168

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 446684800 152 GIVNKR-FCPHYNQLNRMNAFHSFLQNHQGNIeGIALEDNCALYITKE-SFEIIGE 205
Cdd:COG4242  169 GFLPGViIDQHFAQRGRLGRLLSAVARNPDLL-GIGIDEDTAIVVDPDgTAEVIGS 223
PRK05282 PRK05282
dipeptidase PepE;
33-137 6.09e-07

dipeptidase PepE;


Pssm-ID: 179990  Cd Length: 233  Bit Score: 48.72  E-value: 6.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  33 KVLFIP----TASHDDesYIKLFLDTFEKqLHCEVQILRIIADtPSKyeideMIQSADLIYLGGGNYIQMITEWKEHKLD 108
Cdd:PRK05282  33 KAVFIPyagvTQSWDD--YTAKVAEALAP-LGIEVTGIHRVAD-PVA-----AIENAEAIFVGGGNTFQLLKQLYERGLL 103

                         90       100       110
                 ....*....|....*....|....*....|
gi 446684800 109 EKLLLALEQGTLIAGCSAGA-MCwfTSSIR 137
Cdd:PRK05282 104 APIREAVKNGTPYIGWSAGAnVA--GPTIR 131
GAT_1 cd03128
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 34-130 2.89e-03

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: 36.02  E-value: 2.89e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446684800  34 VLFIPTASHDDESYIkLFLDTFEKqLHCEVQILRIIADTPskyEIDEMIQSADLIYLGGGNYIQMITEWKEHKLDEkLLL 113
Cdd:cd03128    1 VAVLLFGGSEELELA-SPLDALRE-AGAEVDVVSPDGGPV---ESDVDLDDYDGLILPGGPGTPDDLAWDEALLAL-LRE 74

                         90
                 ....*....|....*..
gi 446684800 114 ALEQGTLIAGCSAGAMC 130
Cdd:cd03128   75 AAAAGKPVLGICLGAQL 91
 
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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