MULTISPECIES: cation-transporting P-type ATPase [Enterobacterales]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||
| HAD_like super family | cl21460 | Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ... |
11-64 | 1.89e-14 | ||
Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes carbon and phosphorus hydrolases such as 2-haloalkonoate dehalogenase, epoxide hydrolase, phosphoserine phosphatase, phosphomannomutase, phosphoglycolate phosphatase, P-type ATPase, among others. These proteins catalyze nucleophilic substitution reactions at phosphorus or carbon centers, using a conserved Asp carboxylate in covalent catalysis. All members possess a conserve alpha/beta core domain, and many also possess a small cap domain, with varying folds and functions. The actual alignment was detected with superfamily member cd02076: Pssm-ID: 473868 [Multi-domain] Cd Length: 781 Bit Score: 66.48 E-value: 1.89e-14
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| Name | Accession | Description | Interval | E-value | ||
| P-type_ATPase_H | cd02076 | plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ... |
11-64 | 1.89e-14 | ||
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases; This subfamily includes eukaryotic plasma membrane H(+)-ATPase which transports H(+) from the cytosol to the extracellular space, thus energizing the plasma membrane for the uptake of ions and nutrients, and is expressed in plants and fungi. This H(+)-ATPase consists of four domains: a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. This subfamily also includes the putative P-type H(+)-ATPase, MJ1226p of the anaerobic hyperthermophilic archaea Methanococcus jannaschii. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319771 [Multi-domain] Cd Length: 781 Bit Score: 66.48 E-value: 1.89e-14
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
10-69 | 8.14e-11 | ||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 56.27 E-value: 8.14e-11
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| Cation_ATPase_N | pfam00690 | Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, ... |
1-58 | 2.63e-09 | ||
Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. Pssm-ID: 459907 [Multi-domain] Cd Length: 68 Bit Score: 48.33 E-value: 2.63e-09
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| Cation_ATPase_N | smart00831 | Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region ... |
2-62 | 7.98e-08 | ||
Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+, Na+, Ca2+, Na+/K+, and H+/K+. In the H+/K+- and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases. Pssm-ID: 214842 [Multi-domain] Cd Length: 75 Bit Score: 44.88 E-value: 7.98e-08
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| Name | Accession | Description | Interval | E-value | ||
| P-type_ATPase_H | cd02076 | plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+) ... |
11-64 | 1.89e-14 | ||
plant and fungal plasma membrane H(+)-ATPases, and related bacterial and archaeal putative H(+)-ATPases; This subfamily includes eukaryotic plasma membrane H(+)-ATPase which transports H(+) from the cytosol to the extracellular space, thus energizing the plasma membrane for the uptake of ions and nutrients, and is expressed in plants and fungi. This H(+)-ATPase consists of four domains: a transmembrane domain and three cytosolic domains: nucleotide-binding domain, phosphorylation domain and actuator domain, and belongs to the P-type ATPase type III subfamily. This subfamily also includes the putative P-type H(+)-ATPase, MJ1226p of the anaerobic hyperthermophilic archaea Methanococcus jannaschii. The P-type ATPases, are a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319771 [Multi-domain] Cd Length: 781 Bit Score: 66.48 E-value: 1.89e-14
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
10-69 | 8.14e-11 | ||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 56.27 E-value: 8.14e-11
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| Cation_ATPase_N | pfam00690 | Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, ... |
1-58 | 2.63e-09 | ||
Cation transporter/ATPase, N-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. Pssm-ID: 459907 [Multi-domain] Cd Length: 68 Bit Score: 48.33 E-value: 2.63e-09
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| Cation_ATPase_N | smart00831 | Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region ... |
2-62 | 7.98e-08 | ||
Cation transporter/ATPase, N-terminus; This entry represents the conserved N-terminal region found in several classes of cation-transporting P-type ATPases, including those that transport H+, Na+, Ca2+, Na+/K+, and H+/K+. In the H+/K+- and Na+/K+-exchange P-ATPases, this domain is found in the catalytic alpha chain. In gastric H+/K+-ATPases, this domain undergoes reversible sequential phosphorylation inducing conformational changes that may be important for regulating the function of these ATPases. Pssm-ID: 214842 [Multi-domain] Cd Length: 75 Bit Score: 44.88 E-value: 7.98e-08
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| P-type_ATPase_Ca_prok | cd02089 | prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL ... |
11-67 | 1.98e-06 | ||
prokaryotic P-type Ca(2+)-ATPase similar to Synechococcus elongatus sp. strain PCC 7942 PacL and Listeria monocytogenes LMCA1; Ca(2+) transport ATPase is a plasma membrane protein which pumps Ca(2+) ion out of the cytoplasm. This prokaryotic subfamily includes the Ca(2+)-ATPase Synechococcus elongatus PacL, Listeria monocytogenes Ca(2+)-ATPase 1 (LMCA1) which has a low Ca(2+) affinity and a high pH optimum (pH about 9) and may remove Ca(2+) from the microorganism in environmental conditions when e.g. stressed by high Ca(2+) and alkaline pH, and the Bacillus subtilis putative P-type Ca(2+)-transport ATPase encoded by the yloB gene, which is expressed during sporulation. This subfamily belongs to the P-type ATPases, a large family of integral membrane transporters that are of critical importance in all kingdoms of life. They generate and maintain (electro-) chemical gradients across cellular membranes, by translocating cations, heavy metals and lipids, and are distinguished from other main classes of transport ATPases (F- , V- , and ABC- type) by the formation of a phosphorylated (P-) intermediate state in the catalytic cycle. Pssm-ID: 319781 [Multi-domain] Cd Length: 674 Bit Score: 43.76 E-value: 1.98e-06
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| VHS_ENTH_ANTH | cd00197 | VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a ... |
27-76 | 7.99e-03 | ||
VHS, ENTH and ANTH domain superfamily; This superfamily is composed of proteins containing a VHS, CID, ENTH, or ANTH domain. The VHS domain is present in Vps27 (Vacuolar Protein Sorting), Hrs (Hepatocyte growth factor-regulated tyrosine kinase substrate) and STAM (Signal Transducing Adaptor Molecule). It is located at the N-termini of proteins involved in intracellular membrane trafficking. The CTD-Interacting Domain (CID) is present in several RNA-processing factors and binds tightly to the carboxy-terminal domain (CTD) of RNA polymerase II (RNAP II or Pol II). The epsin N-terminal homology (ENTH) domain is an evolutionarily conserved protein module found primarily in proteins that participate in clathrin-mediated endocytosis. A set of proteins previously designated as harboring an ENTH domain in fact contains a highly similar, yet unique module referred to as an AP180 N-Terminal Homology (ANTH) domain. VHS, ENTH, and ANTH domains are structurally similar and are composed of a superhelix of eight alpha helices. ENTH and ANTH (E/ANTH) domains bind both inositol phospholipids and proteins and contribute to the nucleation and formation of clathrin coats on membranes. ENTH domains also function in the development of membrane curvature through lipid remodeling during the formation of clathrin-coated vesicles. E/ANTH domain-bearing proteins have recently been shown to function with adaptor protein-1 and GGA adaptors at the Trans-Golgi Network, which suggests that E/ANTH domains are universal components of the machinery for clathrin-mediated membrane budding. Pssm-ID: 340764 Cd Length: 115 Bit Score: 32.78 E-value: 7.99e-03
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