Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
50-407
0e+00
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK).
:
Pssm-ID: 153076 [Multi-domain] Cd Length: 357 Bit Score: 731.06 E-value: 0e+00
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
50-407
0e+00
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK).
Pssm-ID: 153076 [Multi-domain] Cd Length: 357 Bit Score: 731.06 E-value: 0e+00
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
187-401
6.08e-110
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.
Pssm-ID: 459716 Cd Length: 203 Bit Score: 321.41 E-value: 6.08e-110
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic ...
50-407
0e+00
Phosphagen (guanidino) kinases such as creatine kinase and similar enzymes; Eukaryotic creatine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CKs are found as tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial, cytosolic, and flagellar) isoforms. Mitochondrial and cytoplasmic CKs are dimeric or octameric, while the flagellar isoforms are trimers with three CD domains fused as a single protein chain. CKs are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK, one of the most studied members of this family, this model also represents other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK), and echinoderm arginine kinase (AK).
Pssm-ID: 153076 [Multi-domain] Cd Length: 357 Bit Score: 731.06 E-value: 0e+00
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are ...
57-400
8.31e-167
Phosphagen (guanidino) kinases mostly found in eukaryotes; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK).
Pssm-ID: 153078 [Multi-domain] Cd Length: 338 Bit Score: 471.38 E-value: 8.31e-167
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic ...
57-401
1.49e-123
Phosphagen (guanidino) kinases such as arginine kinase and similar enzymes; Eukaryotic arginine kinase-like phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphoarginine in the case of arginine kinase (AK), which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. Besides AK, one of the most studied members of this family, this model also represents a phosphagen kinase with different substrate specificity, hypotaurocyamine kinase (HTK).
Pssm-ID: 153079 [Multi-domain] Cd Length: 350 Bit Score: 362.02 E-value: 1.49e-123
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is ...
187-401
6.08e-110
ATP:guanido phosphotransferase, C-terminal catalytic domain; The substrate binding site is located in the cleft between N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain.
Pssm-ID: 459716 Cd Length: 203 Bit Score: 321.41 E-value: 6.08e-110
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that ...
160-400
1.96e-109
Phosphagen (guanidino) kinases; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, like phosphocreatine (PCr) in the case of creatine kinase (CK) or phosphoarginine in the case of arginine kinase, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. The substrate binding site is located in the cleft between the N and C-terminal domains, but most of the catalytic residues are found in the larger C-terminal domain. In higher eukaryotes, CK exists in tissue-specific (muscle, brain), as well as compartment-specific (mitochondrial and cytosolic) isoforms. They are either coupled to glycolysis (cytosolic form) or oxidative phosphorylation (mitochondrial form). Besides CK and AK, the most studied members of this family are also other phosphagen kinases with different substrate specificities, like glycocyamine kinase (GK), lombricine kinase (LK), taurocyamine kinase (TK) and hypotaurocyamine kinase (HTK). The majority of bacterial phosphagen kinases appear to lack the N-terminal domain and have not been functionally characterized.
Pssm-ID: 153075 Cd Length: 236 Bit Score: 321.85 E-value: 1.96e-109
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes ...
160-400
3.07e-36
Phosphagen (guanidino) kinases found in bacteria; Phosphagen (guanidino) kinases are enzymes that transphosphorylate a high energy phosphoguanidino compound, such as phosphocreatine (PCr) or phosphoarginine, which is used as an energy-storage and -transport metabolite, to ADP, thereby creating ATP. This subfamily is specific to bacteria and lacks an N-terminal domain, which otherwise forms part of the substrate binding site. Most of the catalytic residues are found in the larger C-terminal domain, however, which appears conserved in these bacterial proteins. Their functions have not been characterized.
Pssm-ID: 153077 Cd Length: 232 Bit Score: 132.63 E-value: 3.07e-36
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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