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Conserved domains on  [gi|1361458886|emb|SPI59365|]
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putative peptidase [Leuconostoc mesenteroides]

Protein Classification

type 1 glutamine amidotransferase family protein( domain architecture ID 73)

type 1 glutamine amidotransferase (GATase1) family protein

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
GAT_1 super family cl00020
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ...
 12-138 2.53e-30

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.


The actual alignment was detected with superfamily member pfam03575:

Pssm-ID: 469582 [Multi-domain]  Cd Length: 206  Bit Score: 108.16  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886  12 KIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGIEYNKIMDSPKVASylIDYSGLGITD 91
Cdd:pfam03575  79 KLLEADGIYVGGGNTFHLLKLLYETGLDKIIREAVQAGLPYIGWSAGANVAGPSIITTSYMDMPIVAP--PSFEALGLVP 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1361458886  92 FYTLPHYI---ERPFTKTVQETYNAYRKKlNLILINNHEAIIVTDTGYRV 138
Cdd:pfam03575 157 FQINPHYLghnGETREERLAEFVESNPGT-PGIGLDEGTALHIEGDTARL 205
 
Name Accession Description Interval E-value
Peptidase_S51 pfam03575
Peptidase family S51;
12-138 2.53e-30

Peptidase family S51;


Pssm-ID: 397574 [Multi-domain]  Cd Length: 206  Bit Score: 108.16  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886  12 KIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGIEYNKIMDSPKVASylIDYSGLGITD 91
Cdd:pfam03575  79 KLLEADGIYVGGGNTFHLLKLLYETGLDKIIREAVQAGLPYIGWSAGANVAGPSIITTSYMDMPIVAP--PSFEALGLVP 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1361458886  92 FYTLPHYI---ERPFTKTVQETYNAYRKKlNLILINNHEAIIVTDTGYRV 138
Cdd:pfam03575 157 FQINPHYLghnGETREERLAEFVESNPGT-PGIGLDEGTALHIEGDTARL 205
PepE COG3340
Peptidase E [Amino acid transport and metabolism];
13-138 1.18e-17

Peptidase E [Amino acid transport and metabolism];


Pssm-ID: 442569 [Multi-domain]  Cd Length: 212  Bit Score: 75.24  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886  13 IEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGieynkIMDSPKVASYLIDYSGLGITDF 92
Cdd:COG3340    79 LLEADVIFVGGGNTFNLLALWREHGLDDILREAVEAGTVYAGVSAGSNCWFPT-----IRTTNDGPPPLRSFDGLGLVPF 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1361458886  93 YTLPHYIERPFTKTVQETYNAYRKKLNL-----------ILINNHEAIIVTDTGYRV 138
Cdd:COG3340   154 SINPHYDDEDMGETREPRIHEFLASNPLppvyalddgtaLHVRGGKLEVVGEGAYRV 210
PRK05282 PRK05282
dipeptidase PepE;
13-59 1.45e-15

dipeptidase PepE;


Pssm-ID: 179990  Cd Length: 233  Bit Score: 70.29  E-value: 1.45e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1361458886  13 IEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGA 59
Cdd:PRK05282   77 IENAEAIFVGGGNTFQLLKQLYERGLLAPIREAVKNGTPYIGWSAGA 123
GAT1_Peptidase_E_like cd03129
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins; ...
 1-101 1.66e-15

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: 69.64  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886   1 MPNEDTDTVVHKIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGieynKIMDSPKVAS- 79
Cdd:cd03129    66 IDTANDPDVVARLLEADGIFVGGGNQLRLLSVLRETPLLDAILKRVARGVVIGGTSAGAAVMGET----GIGTTPSEPEv 141

                          90       100
                  ....*....|....*....|..
gi 1361458886  80 YLIDYSGLGITDFYTLPHYIER 101
Cdd:cd03129   142 TPPMAPGLGLLPGIIDPHFDSR 163
 
Name Accession Description Interval E-value
Peptidase_S51 pfam03575
Peptidase family S51;
12-138 2.53e-30

Peptidase family S51;


Pssm-ID: 397574 [Multi-domain]  Cd Length: 206  Bit Score: 108.16  E-value: 2.53e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886  12 KIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGIEYNKIMDSPKVASylIDYSGLGITD 91
Cdd:pfam03575  79 KLLEADGIYVGGGNTFHLLKLLYETGLDKIIREAVQAGLPYIGWSAGANVAGPSIITTSYMDMPIVAP--PSFEALGLVP 156

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1361458886  92 FYTLPHYI---ERPFTKTVQETYNAYRKKlNLILINNHEAIIVTDTGYRV 138
Cdd:pfam03575 157 FQINPHYLghnGETREERLAEFVESNPGT-PGIGLDEGTALHIEGDTARL 205
PepE COG3340
Peptidase E [Amino acid transport and metabolism];
13-138 1.18e-17

Peptidase E [Amino acid transport and metabolism];


Pssm-ID: 442569 [Multi-domain]  Cd Length: 212  Bit Score: 75.24  E-value: 1.18e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886  13 IEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGieynkIMDSPKVASYLIDYSGLGITDF 92
Cdd:COG3340    79 LLEADVIFVGGGNTFNLLALWREHGLDDILREAVEAGTVYAGVSAGSNCWFPT-----IRTTNDGPPPLRSFDGLGLVPF 153

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1361458886  93 YTLPHYIERPFTKTVQETYNAYRKKLNL-----------ILINNHEAIIVTDTGYRV 138
Cdd:COG3340   154 SINPHYDDEDMGETREPRIHEFLASNPLppvyalddgtaLHVRGGKLEVVGEGAYRV 210
PRK05282 PRK05282
dipeptidase PepE;
13-59 1.45e-15

dipeptidase PepE;


Pssm-ID: 179990  Cd Length: 233  Bit Score: 70.29  E-value: 1.45e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1361458886  13 IEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGA 59
Cdd:PRK05282   77 IENAEAIFVGGGNTFQLLKQLYERGLLAPIREAVKNGTPYIGWSAGA 123
GAT1_Peptidase_E_like cd03129
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E_like proteins; ...
 1-101 1.66e-15

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: 69.64  E-value: 1.66e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886   1 MPNEDTDTVVHKIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGieynKIMDSPKVAS- 79
Cdd:cd03129    66 IDTANDPDVVARLLEADGIFVGGGNQLRLLSVLRETPLLDAILKRVARGVVIGGTSAGAAVMGET----GIGTTPSEPEv 141

                          90       100
                  ....*....|....*....|..
gi 1361458886  80 YLIDYSGLGITDFYTLPHYIER 101
Cdd:cd03129   142 TPPMAPGLGLLPGIIDPHFDSR 163
GAT1_Peptidase_E cd03146
Type 1 glutamine amidotransferase (GATase1)-like domain found in peptidase E; Type 1 glutamine ...
 5-100 2.50e-15

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: 69.23  E-value: 2.50e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1361458886   5 DTDTVVHKIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGAISLAPGIEYNKIMDSpkvaSYLIDY 84
Cdd:cd03146    70 DTEDPLDALLEADVIYVGGGNTFNLLAQWREHGLDAILKAALERGVVYIGWSAGSNCWFPSIGTTDSMPI----ELPPSF 145

                          90
                  ....*....|....*.
gi 1361458886  85 SGLGITDFYTLPHYIE 100
Cdd:cd03146   146 NGLGLLPFQICPHYDS 161
GAT1_cyanophycinase cd03145
Type 1 glutamine amidotransferase (GATase1)-like domain found in cyanophycinase; Type 1 ...
 5-59 4.29e-04

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: 38.42  E-value: 4.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1361458886   5 DTDTVVHKIEQAEILFITGGNTFYLLQKLKRKNLLPLLTEKIKNGTPYIGESPGA 59
Cdd:cd03145    73 NDPEVVARLRDADGIFFTGGDQLRITSALGGTPLLDALRKVYRGGVVIGGTSAGA 127
 
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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