ATP-grasp domain-containing protein may be related to carbamoyl phosphate synthetase and predicted to be involved in the biosynthesis of a ribonucleoside involved in stress response
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase ...
1-215
4.01e-144
Carbamoyl-phosphate synthase L chain, ATP binding domain; Carbamoyl-phosphate synthase catalyzes the ATP-dependent synthesis of carbamyl-phosphate from glutamine or ammonia and bicarbonate. This important enzyme initiates both the urea cycle and the biosynthesis of arginine and/or pyrimidines. The carbamoyl-phosphate synthase (CPS) enzyme in prokaryotes is a heterodimer of a small and large chain. The small chain promotes the hydrolysis of glutamine to ammonia, which is used by the large chain to synthesize carbamoyl phosphate. See pfam00988. The small chain has a GATase domain in the carboxyl terminus. See pfam00117. The ATP binding domain (this one) has an ATP-grasp fold.
The actual alignment was detected with superfamily member PLN02941:
Pssm-ID: 473076 [Multi-domain] Cd Length: 328 Bit Score: 405.11 E-value: 4.01e-144
Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several ...
11-209
1.11e-117
Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several inositol 1, 3, 4-trisphosphate 5/6-kinase proteins. Inositol 1,3,4-trisphosphate is at a branch point in inositol phosphate metabolism. It is dephosphorylated by specific phosphatases to either inositol 3,4-bisphosphate or inositol 1,3-bisphosphate. Alternatively, it is phosphorylated to inositol 1,3,4,6-tetrakisphosphate or inositol 1,3,4,5-tetrakisphosphate by inositol trisphosphate 5/6-kinase. This entry represents the ATP-grasp domain.
Pssm-ID: 368606 Cd Length: 201 Bit Score: 333.27 E-value: 1.11e-117
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
17-193
4.54e-09
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 55.33 E-value: 4.54e-09
Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several ...
11-209
1.11e-117
Inositol 1,3,4-trisphosphate 5/6-kinase ATP-grasp domain; This family consists of several inositol 1, 3, 4-trisphosphate 5/6-kinase proteins. Inositol 1,3,4-trisphosphate is at a branch point in inositol phosphate metabolism. It is dephosphorylated by specific phosphatases to either inositol 3,4-bisphosphate or inositol 1,3-bisphosphate. Alternatively, it is phosphorylated to inositol 1,3,4,6-tetrakisphosphate or inositol 1,3,4,5-tetrakisphosphate by inositol trisphosphate 5/6-kinase. This entry represents the ATP-grasp domain.
Pssm-ID: 368606 Cd Length: 201 Bit Score: 333.27 E-value: 1.11e-117
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport ...
17-193
4.54e-09
Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily [Amino acid transport and metabolism, Coenzyme transport and metabolism, Translation, ribosomal structure and biogenesis, Secondary metabolites biosynthesis, transport and catabolism]; Glutathione synthase, LysX or RimK-type ligase, ATP-grasp superfamily is part of the Pathway/BioSystem: Lysine biosynthesis
Pssm-ID: 439959 [Multi-domain] Cd Length: 289 Bit Score: 55.33 E-value: 4.54e-09
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.
of the residues that compose this conserved feature have been mapped to the query sequence.
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