guanylyl cyclase, partial [Toxoplasma gondii VAND]
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 ... |
1999-2384 | 9.91e-101 | |||||||
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 cd02073: Pssm-ID: 473868 [Multi-domain] Cd Length: 836 Bit Score: 346.08 E-value: 9.91e-101
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| HAD_like super family | cl21460 | Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ... |
149-508 | 2.98e-86 | |||||||
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 cd02073: Pssm-ID: 473868 [Multi-domain] Cd Length: 836 Bit Score: 303.32 E-value: 2.98e-86
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| HAD_like super family | cl21460 | Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ... |
1670-1771 | 1.28e-16 | |||||||
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 TIGR01652: Pssm-ID: 473868 [Multi-domain] Cd Length: 1057 Bit Score: 87.44 E-value: 1.28e-16
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| HAD_like super family | cl21460 | Haloacid Dehalogenase-like Hydrolases; The haloacid dehalogenase (HAD) superfamily includes ... |
785-832 | 2.01e-12 | |||||||
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 cd02073: Pssm-ID: 473868 [Multi-domain] Cd Length: 836 Bit Score: 73.36 E-value: 2.01e-12
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| Nucleotidyl_cyc_III super family | cl11967 | Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
2923-3041 | 1.21e-11 | |||||||
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways. The actual alignment was detected with superfamily member smart00044: Pssm-ID: 448371 Cd Length: 194 Bit Score: 66.13 E-value: 1.21e-11
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| PHA03307 super family | cl33723 | transcriptional regulator ICP4; Provisional |
1294-1544 | 1.39e-05 | |||||||
transcriptional regulator ICP4; Provisional The actual alignment was detected with superfamily member PHA03307: Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.94 E-value: 1.39e-05
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| Cse1 super family | cl38282 | Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the ... |
2707-2781 | 1.32e-03 | |||||||
Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha. This domain contains HEAT repeats. The actual alignment was detected with superfamily member pfam08506: Pssm-ID: 430038 [Multi-domain] Cd Length: 370 Bit Score: 43.83 E-value: 1.32e-03
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| MFS super family | cl28910 | Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse ... |
2779-2902 | 6.93e-03 | |||||||
Major Facilitator Superfamily; The Major Facilitator Superfamily (MFS) is a large and diverse group of secondary transporters that includes uniporters, symporters, and antiporters. MFS proteins facilitate the transport across cytoplasmic or internal membranes of a variety of substrates including ions, sugar phosphates, drugs, neurotransmitters, nucleosides, amino acids, and peptides. They do so using the electrochemical potential of the transported substrates. Uniporters transport a single substrate, while symporters and antiporters transport two substrates in the same or in opposite directions, respectively, across membranes. MFS proteins are typically 400 to 600 amino acids in length, and the majority contain 12 transmembrane alpha helices (TMs) connected by hydrophilic loops. The N- and C-terminal halves of these proteins display weak similarity and may be the result of a gene duplication/fusion event. Based on kinetic studies and the structures of a few bacterial superfamily members, GlpT (glycerol-3-phosphate transporter), LacY (lactose permease), and EmrD (multidrug transporter), MFS proteins are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Bacterial members function primarily for nutrient uptake, and as drug-efflux pumps to confer antibiotic resistance. Some MFS proteins have medical significance in humans such as the glucose transporter Glut4, which is impaired in type II diabetes, and glucose-6-phosphate transporter (G6PT), which causes glycogen storage disease when mutated. The actual alignment was detected with superfamily member cd06179: Pssm-ID: 475125 [Multi-domain] Cd Length: 518 Bit Score: 41.84 E-value: 6.93e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| P-type_ATPase_APLT_Dnf-like | cd02073 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
1999-2384 | 9.91e-101 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain] Cd Length: 836 Bit Score: 346.08 E-value: 9.91e-101
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
2010-2502 | 8.02e-89 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 315.86 E-value: 8.02e-89
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| P-type_ATPase_APLT_Dnf-like | cd02073 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
149-508 | 2.98e-86 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain] Cd Length: 836 Bit Score: 303.32 E-value: 2.98e-86
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
147-509 | 5.60e-78 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 283.12 E-value: 5.60e-78
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| PhoLip_ATPase_C | pfam16212 | Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ... |
2260-2503 | 2.22e-58 | ||||||||
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes. Pssm-ID: 465071 [Multi-domain] Cd Length: 250 Bit Score: 202.74 E-value: 2.22e-58
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
1998-2499 | 9.32e-51 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 198.97 E-value: 9.32e-51
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
132-430 | 5.78e-49 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 193.19 E-value: 5.78e-49
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| PhoLip_ATPase_N | pfam16209 | Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ... |
134-191 | 5.18e-20 | ||||||||
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes. Pssm-ID: 465069 [Multi-domain] Cd Length: 67 Bit Score: 85.99 E-value: 5.18e-20
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
1989-2244 | 1.37e-18 | ||||||||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 93.63 E-value: 1.37e-18
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
1670-1771 | 1.28e-16 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 87.44 E-value: 1.28e-16
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
1682-1777 | 2.67e-13 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 76.48 E-value: 2.67e-13
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| P-type_ATPase_APLT_Dnf-like | cd02073 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
785-832 | 2.01e-12 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain] Cd Length: 836 Bit Score: 73.36 E-value: 2.01e-12
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| CYCc | smart00044 | Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ... |
2923-3041 | 1.21e-11 | ||||||||
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes. Pssm-ID: 214485 Cd Length: 194 Bit Score: 66.13 E-value: 1.21e-11
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| CHD | cd07302 | cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ... |
2963-3040 | 9.16e-11 | ||||||||
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide. Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 63.37 E-value: 9.16e-11
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
777-872 | 2.60e-10 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 66.64 E-value: 2.60e-10
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| Guanylate_cyc | pfam00211 | Adenylate and Guanylate cyclase catalytic domain; |
2956-3028 | 3.62e-07 | ||||||||
Adenylate and Guanylate cyclase catalytic domain; Pssm-ID: 425528 Cd Length: 183 Bit Score: 53.02 E-value: 3.62e-07
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1294-1544 | 1.39e-05 | ||||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.94 E-value: 1.39e-05
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| Cation_ATPase | pfam13246 | Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ... |
1685-1772 | 2.79e-05 | ||||||||
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases. Pssm-ID: 463817 [Multi-domain] Cd Length: 91 Bit Score: 44.90 E-value: 2.79e-05
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
792-827 | 2.34e-04 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 47.20 E-value: 2.34e-04
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
795-816 | 4.54e-04 | ||||||||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 45.87 E-value: 4.54e-04
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| Cse1 | pfam08506 | Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the ... |
2707-2781 | 1.32e-03 | ||||||||
Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha. This domain contains HEAT repeats. Pssm-ID: 430038 [Multi-domain] Cd Length: 370 Bit Score: 43.83 E-value: 1.32e-03
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| MFS_TRI12_like | cd06179 | Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; ... |
2779-2902 | 6.93e-03 | ||||||||
Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; This family includes Fusarium sporotrichioides trichothecene efflux pump (TRI12), which may play a role in F. sporotrichioides self-protection against trichothecenes. TRI12 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Pssm-ID: 340868 [Multi-domain] Cd Length: 518 Bit Score: 41.84 E-value: 6.93e-03
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| Name | Accession | Description | Interval | E-value | ||||||||
| P-type_ATPase_APLT_Dnf-like | cd02073 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
1999-2384 | 9.91e-101 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain] Cd Length: 836 Bit Score: 346.08 E-value: 9.91e-101
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
2010-2502 | 8.02e-89 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 315.86 E-value: 8.02e-89
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| P-type_ATPase_APLT_Dnf-like | cd02073 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
149-508 | 2.98e-86 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain] Cd Length: 836 Bit Score: 303.32 E-value: 2.98e-86
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
147-509 | 5.60e-78 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 283.12 E-value: 5.60e-78
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| P-type_ATPase_APLT | cd07536 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
2012-2383 | 1.51e-65 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319838 [Multi-domain] Cd Length: 805 Bit Score: 240.58 E-value: 1.51e-65
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| PhoLip_ATPase_C | pfam16212 | Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the ... |
2260-2503 | 2.22e-58 | ||||||||
Phospholipid-translocating P-type ATPase C-terminal; PhoLip_ATPase_C is found at the C-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes. Pssm-ID: 465071 [Multi-domain] Cd Length: 250 Bit Score: 202.74 E-value: 2.22e-58
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| P-type_ATPase_APLT_Neo1-like | cd07541 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ... |
2019-2384 | 5.13e-57 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. 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: 319841 [Multi-domain] Cd Length: 792 Bit Score: 214.58 E-value: 5.13e-57
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| P-type_ATPase_APLT | cd07536 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
150-518 | 2.39e-53 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319838 [Multi-domain] Cd Length: 805 Bit Score: 203.60 E-value: 2.39e-53
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
1998-2499 | 9.32e-51 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 198.97 E-value: 9.32e-51
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
132-430 | 5.78e-49 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 193.19 E-value: 5.78e-49
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| P-type_ATPase_APLT_Neo1-like | cd07541 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ... |
149-511 | 3.31e-38 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. 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: 319841 [Multi-domain] Cd Length: 792 Bit Score: 156.42 E-value: 3.31e-38
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| ATPase_P-type | TIGR01494 | ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ... |
1998-2297 | 1.08e-22 | ||||||||
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily. Pssm-ID: 273656 [Multi-domain] Cd Length: 545 Bit Score: 105.48 E-value: 1.08e-22
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| PhoLip_ATPase_N | pfam16209 | Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a ... |
134-191 | 5.18e-20 | ||||||||
Phospholipid-translocating ATPase N-terminal; PhoLip_ATPase_N is found at the N-terminus of a number of phospholipid-translocating ATPases. It is found in higher eukaryotes. Pssm-ID: 465069 [Multi-domain] Cd Length: 67 Bit Score: 85.99 E-value: 5.18e-20
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
1989-2244 | 1.37e-18 | ||||||||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 93.63 E-value: 1.37e-18
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| P-ATPase-V | TIGR01657 | P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade ... |
2009-2241 | 1.14e-17 | ||||||||
P-type ATPase of unknown pump specificity (type V); These P-type ATPases form a distinct clade but the substrate of their pumping activity has yet to be determined. This clade has been designated type V in. Pssm-ID: 273738 [Multi-domain] Cd Length: 1054 Bit Score: 90.89 E-value: 1.14e-17
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| P-type_ATPases | cd01431 | ATP-dependent membrane-bound cation and aminophospholipid transporters; The P-type ATPases, ... |
2017-2242 | 2.43e-17 | ||||||||
ATP-dependent membrane-bound cation and aminophospholipid transporters; 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319764 [Multi-domain] Cd Length: 319 Bit Score: 85.97 E-value: 2.43e-17
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
1670-1771 | 1.28e-16 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 87.44 E-value: 1.28e-16
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| P-type_ATPase_Ca_PMCA-like | cd02081 | animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related ... |
1989-2244 | 1.85e-15 | ||||||||
animal plasma membrane Ca2(+)-ATPases (PMCA), similar to human ATP2B1-4/PMCA1-4, and related Ca2(+)-ATPases including Saccharomyces cerevisiae vacuolar PMC1; Animal PMCAs function to export Ca(2+) from cells and play a role in regulating Ca(2+) signals following stimulus induction and in preventing calcium toxicity. Many PMCA pump variants exist due to alternative splicing of transcripts. PMCAs are regulated by the binding of calmodulin or by kinase-mediated phosphorylation. Saccharomyces cerevisiae vacuolar transporter Pmc1p facilitates the accumulation of Ca2+ into vacuoles. Pmc1p is not regulated by direct calmodulin binding but responds to the calmodulin/calcineurin-signaling pathway and is controlled by the transcription factor complex Tcn1p/Crz1p. Similarly, the expression of the gene for Dictyostelium discoideum Ca(2+)-ATPase PAT1, patA, is under the control of a calcineurin-dependent transcription factor. Plant vacuolar Ca(2+)-ATPases, are regulated by direct-calmodulin binding. Plant Ca(2+)-ATPases are present at various cellular locations including the plasma membrane, endoplasmic reticulum, chloroplast and vacuole. 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: 319776 [Multi-domain] Cd Length: 721 Bit Score: 83.02 E-value: 1.85e-15
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| ATPase_P-type | TIGR01494 | ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ... |
199-416 | 1.63e-14 | ||||||||
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily. Pssm-ID: 273656 [Multi-domain] Cd Length: 545 Bit Score: 79.67 E-value: 1.63e-14
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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 ... |
1988-2241 | 2.42e-13 | ||||||||
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: 76.11 E-value: 2.42e-13
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| P-type_ATPase_cation | cd07543 | P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 ... |
2014-2242 | 2.45e-13 | ||||||||
P-type cation-transporting ATPases, similar to human cation-transporting ATPase type 13A1 (ATP13A1) and Saccharomyces manganese-transporting ATPase 1 Spf1p; Saccharomyces Spf1p may mediate manganese transport into the endoplasmic reticulum (ER); one consequence of deletion of SPF1 is severe ER stress. This subfamily also includes Arabidopsis thaliana MIA (Male Gametogenesis Impaired Anthers) protein which is highly abundant in the endoplasmic reticulum and small vesicles of developing pollen grains and tapetum cells. The MIA gene functionally complements a mutant in the SPF1 from Saccharomyces cerevisiae. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. 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: 319843 [Multi-domain] Cd Length: 804 Bit Score: 76.27 E-value: 2.45e-13
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
1682-1777 | 2.67e-13 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 76.48 E-value: 2.67e-13
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| P-type_ATPase_cation | cd07542 | P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and ... |
2009-2240 | 1.04e-12 | ||||||||
P-type cation-transporting ATPases, similar to human ATPase type 13A2 (ATP13A2) protein and Saccharomyces cerevisiae Ypk9p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. This subfamily also includes zebrafish ATP13A2 a lysosome-specific transmembrane ATPase protein of unknown function which plays a crucial role during embryonic development, its deletion is lethal. 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: 319842 [Multi-domain] Cd Length: 760 Bit Score: 74.21 E-value: 1.04e-12
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| P-type_ATPase_APLT_Dnf-like | cd02073 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
785-832 | 2.01e-12 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, and human ATP8A2, -10D, -11B, -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. This subfamily includes mammalian flippases such as ATP11C which may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319770 [Multi-domain] Cd Length: 836 Bit Score: 73.36 E-value: 2.01e-12
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| CYCc | smart00044 | Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl ... |
2923-3041 | 1.21e-11 | ||||||||
Adenylyl- / guanylyl cyclase, catalytic domain; Present in two copies in mammalian adenylyl cyclases. Eubacterial homologues are known. Two residues (Asn, Arg) are thought to be involved in catalysis. These cyclases have important roles in a diverse range of cellular processes. Pssm-ID: 214485 Cd Length: 194 Bit Score: 66.13 E-value: 1.21e-11
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| P-type_ATPase_cation | cd02082 | P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins ... |
2010-2242 | 4.17e-11 | ||||||||
P-type cation-transporting ATPases, similar to human ATPase type 13A1-A4 (ATP13A1-A4) proteins and Saccharomyces cerevisiae Ypk9p and Spf1p; Saccharomyces cerevisiae Yph9p localizes to the yeast vacuole and may play a role in sequestering heavy metal ions, its deletion confers sensitivity for growth for cadmium, manganese, nickel or selenium. Saccharomyces 1 Spf1p may mediate manganese transport into the endoplasmic reticulum. Human ATP13A2 (PARK9/CLN12) is a lysosomal transporter with zinc as the possible substrate. Mutation in the ATP13A2 gene has been linked to Parkinson's disease and Kufor-Rakeb syndrome, and to neuronal ceroid lipofuscinoses. ATP13A3/AFURS1 is a candidate gene for oculo auriculo vertebral spectrum (OAVS), being one of nine genes included in a 3q29 microduplication in a patient with OAVS. Mutation in the human ATP13A4 may be involved in a speech-language disorder. The expression of ATP13A1 has been followed during mouse development, ATP13A1 transcript expression showed an increase as development progressed, with the highest expression at the peak of neurogenesis. 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: 319777 [Multi-domain] Cd Length: 786 Bit Score: 69.16 E-value: 4.17e-11
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| CHD | cd07302 | cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also ... |
2963-3040 | 9.16e-11 | ||||||||
cyclase homology domain; Catalytic domains of the mononucleotidyl cyclases (MNC's), also called cyclase homology domains (CHDs), are part of the class III nucleotidyl cyclases. This class includes eukaryotic and prokaryotic adenylate cyclases (AC's) and guanylate cyclases (GC's). They seem to share a common catalytic mechanism in their requirement for two magnesium ions to bind the polyphosphate moiety of the nucleotide. Pssm-ID: 143636 [Multi-domain] Cd Length: 177 Bit Score: 63.37 E-value: 9.16e-11
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| P-type_ATPase | cd07538 | uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ... |
2046-2244 | 9.95e-11 | ||||||||
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319839 [Multi-domain] Cd Length: 653 Bit Score: 67.47 E-value: 9.95e-11
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| P-type_ATPase_SERCA | cd02083 | sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; ... |
2019-2241 | 1.43e-10 | ||||||||
sarco/endoplasmic reticulum Ca(2+)-ATPase (SERCA), similar to mammalian ATP2A1-3/SERCA1-3; SERCA is a transmembrane (Ca2+)-ATPase and a major regulator of Ca(2+) homeostasis and contractility in cardiac and skeletal muscle. It re-sequesters cytoplasmic Ca(2+) to the sarco/endoplasmic reticulum store, thereby also terminating Ca(2+)-induced signaling such as in muscle contraction. Three genes (ATP2A1-3/SERCA1-3) encode SERCA pumps in mammals, further isoforms exist due to alternative splicing of transcripts. The activity of SERCA is regulated by two small membrane proteins called phospholamban and sarcolipin. 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: 319778 [Multi-domain] Cd Length: 979 Bit Score: 67.32 E-value: 1.43e-10
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| ATPase-Plipid | TIGR01652 | phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase ... |
777-872 | 2.60e-10 | ||||||||
phospholipid-translocating P-type ATPase, flippase; This model describes the P-type ATPase responsible for transporting phospholipids from one leaflet of bilayer membranes to the other. These ATPases are found only in eukaryotes. Pssm-ID: 273734 [Multi-domain] Cd Length: 1057 Bit Score: 66.64 E-value: 2.60e-10
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| P-type_ATPase_Na_ENA | cd02086 | fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces ... |
1989-2242 | 2.88e-10 | ||||||||
fungal-type Na(+)-ATPase, similar to the plasma membrane sodium transporters Saccharomyces cerevisiae Ena1p, Ena2p and Ustilago maydis Ena1, and the endoplasmic reticulum sodium transporter Ustilago maydis Ena2; Fungal-type Na(+)-ATPase (also called ENA ATPases). This subfamily includes the Saccharomyces cerevisiae plasma membrane transporters: Na(+)/Li(+)-exporting ATPase Ena1p which may also extrudes K(+), and Na(+)-exporting P-type ATPase Ena2p. It also includes Ustilago maydis plasma membrane Ena1, an K(+)/Na(+)-ATPase whose chief role is to pump Na(+) and K(+) out of the cytoplasm, especially at high pH values, and endoplasmic reticulum Ena2 ATPase which mediates Na(+) or K(+) fluxes in the ER or in other endomembranes. 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: 319780 [Multi-domain] Cd Length: 920 Bit Score: 66.32 E-value: 2.88e-10
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| P-type_ATPase_cation | cd02080 | P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ... |
1989-2244 | 6.47e-10 | ||||||||
P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, and Synechocystis sp. PCC 6803 PMA1, a putative Ca(2+)-ATPase; This subfamily includes the P-type Na(+)-ATPase of an alkaliphilic bacterium Exiguobacterium aurantiacum Mna and cyanobacterium Synechocystis sp. PCC 6803 PMA1, a cation-transporting ATPase which may translocate calcium. 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: 319775 [Multi-domain] Cd Length: 819 Bit Score: 64.98 E-value: 6.47e-10
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| P-type_ATPase | cd07539 | uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase ... |
1989-2242 | 1.02e-09 | ||||||||
uncharacterized subfamily of P-type ATPase transporters; This subfamily contains P-type ATPase transporters of unknown function. 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd2+, and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319840 [Multi-domain] Cd Length: 634 Bit Score: 64.36 E-value: 1.02e-09
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| ATPase-IIB_Ca | TIGR01517 | plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ... |
1989-2243 | 2.03e-08 | ||||||||
plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase responsible for translocating calcium ions across the plasma membrane of eukaryotes, out of the cell. In some organisms, this type of pump may also be found in vacuolar membranes. In humans and mice, at least, there are multiple isoforms of the PMCA pump with overlapping but not redundant functions. Accordingly, there are no human diseases linked to PMCA defects, although alterations of PMCA function do elicit physiological effects. The calcium P-type ATPases have been characterized as Type IIB based on a phylogenetic analysis which distinguishes this group from the Type IIA SERCA calcium pump. A separate analysis divides Type IIA into sub-types (SERCA and PMR1) which are represented by two corresponding models (TIGR01116 and TIGR01522). This model is well separated from those. Pssm-ID: 273668 [Multi-domain] Cd Length: 956 Bit Score: 60.18 E-value: 2.03e-08
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| ATPase_P-type | TIGR01494 | ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large ... |
748-828 | 3.65e-08 | ||||||||
ATPase, P-type (transporting), HAD superfamily, subfamily IC; The P-type ATPases are a large family of trans-membrane transporters acting on charged substances. The distinguishing feature of the family is the formation of a phosphorylated intermediate (aspartyl-phosphate) during the course of the reaction. Another common name for these enzymes is the E1-E2 ATPases based on the two isolable conformations: E1 (unphosphorylated) and E2 (phosphorylated). Generally, P-type ATPases consist of only a single subunit encompassing the ATPase and ion translocation pathway, however, in the case of the potassium (TIGR01497) and sodium/potassium (TIGR01106) varieties, these functions are split between two subunits. Additional small regulatory or stabilizing subunits may also exist in some forms. P-type ATPases are nearly ubiquitous in life and are found in numerous copies in higher organisms (at least 45 in Arabidopsis thaliana, for instance). Phylogenetic analyses have revealed that the P-type ATPase subfamily is divided up into groups based on substrate specificities and this is represented in the various subfamily and equivalog models that have been made: IA (K+) TIGR01497, IB (heavy metals) TIGR01525, IIA1 (SERCA-type Ca++) TIGR01116, IIA2 (PMR1-type Ca++) TIGR01522, IIB (PMCA-type Ca++) TIGR01517, IIC (Na+/K+, H+/K+ antiporters) TIGR01106, IID (fungal-type Na+ and K+) TIGR01523, IIIA (H+) TIGR01647, IIIB (Mg++) TIGR01524, IV (phospholipid, flippase) TIGR01652 and V (unknown specificity) TIGR01657. The crystal structure of one calcium-pumping ATPase and an analysis of the fold of the catalytic domain of the P-type ATPases have been published. These reveal that the catalytic core of these enzymes is a haloacid dehalogenase(HAD)-type aspartate-nucleophile hydrolase. The location of the ATP-binding loop in between the first and second HAD conserved catalytic motifs defines these enzymes as members of subfamily I of the HAD superfamily (see also TIGR01493, TIGR01509, TIGR01549, TIGR01544 and TIGR01545). Based on these classifications, the P-type ATPase _superfamily_ corresponds to the IC subfamily of the HAD superfamily. Pssm-ID: 273656 [Multi-domain] Cd Length: 545 Bit Score: 58.87 E-value: 3.65e-08
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| ATPase-IID_K-Na | TIGR01523 | potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium ... |
1989-2242 | 9.99e-08 | ||||||||
potassium and/or sodium efflux P-type ATPase, fungal-type; Initially described as a calcium efflux ATPase, more recent work has shown that the S. pombe CTA3 gene is in fact a potassium ion efflux pump. This model describes the clade of fungal P-type ATPases responsible for potassium and sodium efflux. The degree to which these pumps show preference for sodium or potassium varies. This group of ATPases has been classified by phylogentic analysis as type IID. The Leishmania sequence (GP|3192903), which falls between trusted and noise in this model, may very well turn out to be an active potassium pump. Pssm-ID: 130586 [Multi-domain] Cd Length: 1053 Bit Score: 58.10 E-value: 9.99e-08
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| P-type_ATPase_SPCA | cd02085 | golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ... |
1988-2242 | 1.02e-07 | ||||||||
golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory pathway Ca(2+) transporting 1/hSPCA1 and Saccharomyces cerevisiae Ca(2+)/Mn(2+)-transporting P-type ATPase, Pmr1p; SPCAs are Ca(2+) pumps important for the golgi-associated secretion pathway, in addition some function as Mn(2+) pumps in Mn(2+) detoxification. Saccharomyces cerevisiae Pmr1p is a high affinity Ca(2+)/Mn(2+) ATPase which transports Ca(2+) and Mn(2+) from the cytoplasm into the Golgi. Pmr1p also contributes to Cd(2+) detoxification. This subfamily includes human SPCA1 and SPCA2, encoded by the ATP2C1 and ATP2C2 genes; autosomal dominant Hailey-Hailey disease is caused by mutations in the human ATP2C1 gene. It also includes Strongylocentrotus purpuratus testis secretory pathway calcium transporting ATPase SPCA which plays an important role in fertilization. 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: 319779 [Multi-domain] Cd Length: 804 Bit Score: 57.79 E-value: 1.02e-07
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| P-type_ATPase_APLT | cd07536 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, ... |
787-828 | 1.67e-07 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Dnf1-3p, Drs2p, Neo1p, and human ATP8A2, -9B, -10D, -11B, and -11C; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. Yeast Dnf1 and Dnf2 mediate the transport of phosphatidylethanolamine, phosphatidylserine, and phosphatidylcholine from the outer to the inner leaflet of the plasma membrane. Mammalian ATP11C may selectively transports PS and PE from the outer leaflet of the plasma membrane to the inner leaflet. The yeast Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Human putative ATPase phospholipid transporting 9B, ATP9B, localizes to the trans-golgi network in a CDC50 protein-independent manner. It also includes Arabidopsis phospholipid flippases including ALA1, and Caenorhabditis elegans flippases, including TAT-1, the latter has been shown to facilitate the inward transport of phosphatidylserine. 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: 319838 [Multi-domain] Cd Length: 805 Bit Score: 57.23 E-value: 1.67e-07
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| Guanylate_cyc | pfam00211 | Adenylate and Guanylate cyclase catalytic domain; |
2956-3028 | 3.62e-07 | ||||||||
Adenylate and Guanylate cyclase catalytic domain; Pssm-ID: 425528 Cd Length: 183 Bit Score: 53.02 E-value: 3.62e-07
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| P-type_ATPase_Cu-like | cd02094 | P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A ... |
2064-2242 | 1.29e-06 | ||||||||
P-type heavy metal-transporting ATPase, similar to human copper-transporting ATPases, ATP7A and ATP7B; The mammalian copper-transporting P-type ATPases, ATP7A and ATP7B are key molecules required for the regulation and maintenance of copper homeostasis. Menkes and Wilson diseases are caused by mutation in ATP7A and ATP7B respectively. This subfamily includes other copper-transporting ATPases such as: Bacillus subtilis CopA , Archeaoglobus fulgidus CopA, and Saccharomyces cerevisiae Ccc2p. This subclass of P-type ATPase is also referred to as CPx-type ATPases because their amino acid sequences contain a characteristic CPC or CPH motif associated with a stretch of hydrophobic amino acids and N-terminal ion-binding sequences. 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: 319783 [Multi-domain] Cd Length: 647 Bit Score: 54.02 E-value: 1.29e-06
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| HAD_PSP | cd07500 | phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces ... |
2198-2243 | 1.24e-05 | ||||||||
phosphoserine phosphatase (PSP), similar to Methanococcus Jannaschii PSP and Saccharomyces cerevisiae SER2p; This family includes Methanococcus jannaschii PSP, and Saccharomyces cerevisiae phosphoserine phosphatase SER2p, EC 3.1.3.3, which participates in a pathway whereby serine and glycine are synthesized from the glycolytic intermediate 3-phosphoglycerate; phosphoserine phosphatase catalyzes the hydrolysis of phospho-L-serine to L-serine and inorganic phosphate, the third reaction in this pathway. This family belongs to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319803 [Multi-domain] Cd Length: 180 Bit Score: 48.31 E-value: 1.24e-05
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1294-1544 | 1.39e-05 | ||||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.94 E-value: 1.39e-05
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| PRK07764 | PRK07764 | DNA polymerase III subunits gamma and tau; Validated |
1307-1536 | 1.47e-05 | ||||||||
DNA polymerase III subunits gamma and tau; Validated Pssm-ID: 236090 [Multi-domain] Cd Length: 824 Bit Score: 50.75 E-value: 1.47e-05
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| ZntA | COG2217 | Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; |
2055-2242 | 1.80e-05 | ||||||||
Cation-transporting P-type ATPase [Inorganic ion transport and metabolism]; Pssm-ID: 441819 [Multi-domain] Cd Length: 717 Bit Score: 50.53 E-value: 1.80e-05
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1336-1679 | 1.99e-05 | ||||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 50.55 E-value: 1.99e-05
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| Cof | COG0561 | Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport ... |
2193-2241 | 2.49e-05 | ||||||||
Hydroxymethylpyrimidine pyrophosphatase and other HAD family phosphatases [Coenzyme transport and metabolism, General function prediction only]; Pssm-ID: 440327 [Multi-domain] Cd Length: 192 Bit Score: 47.82 E-value: 2.49e-05
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| Cation_ATPase | pfam13246 | Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including ... |
1685-1772 | 2.79e-05 | ||||||||
Cation transport ATPase (P-type); This domain is found in cation transport ATPases, including phospholipid-transporting ATPases, calcium-transporting ATPases, and sodium-potassium ATPases. Pssm-ID: 463817 [Multi-domain] Cd Length: 91 Bit Score: 44.90 E-value: 2.79e-05
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| YedP | COG3769 | Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and ... |
2203-2245 | 3.00e-05 | ||||||||
Mannosyl-3-phosphoglycerate phosphatase YedP/MpgP, HAD superfamily [Carbohydrate transport and metabolism]; Pssm-ID: 442983 [Multi-domain] Cd Length: 268 Bit Score: 48.67 E-value: 3.00e-05
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1309-1516 | 3.34e-05 | ||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 49.94 E-value: 3.34e-05
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| PRK00192 | PRK00192 | mannosyl-3-phosphoglycerate phosphatase; Reviewed |
2203-2244 | 5.06e-05 | ||||||||
mannosyl-3-phosphoglycerate phosphatase; Reviewed Pssm-ID: 234684 [Multi-domain] Cd Length: 273 Bit Score: 48.01 E-value: 5.06e-05
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| Nucleotidyl_cyc_III | cd07556 | Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse ... |
2964-3026 | 7.38e-05 | ||||||||
Class III nucleotidyl cyclases; Class III nucleotidyl cyclases are the largest, most diverse group of nucleotidyl cyclases (NC's) containing prokaryotic and eukaryotic proteins. They can be divided into two major groups; the mononucleotidyl cyclases (MNC's) and the diguanylate cyclases (DGC's). The MNC's, which include the adenylate cyclases (AC's) and the guanylate cyclases (GC's), have a conserved cyclase homology domain (CHD), while the DGC's have a conserved GGDEF domain, named after a conserved motif within this subgroup. Their products, cyclic guanylyl and adenylyl nucleotides, are second messengers that play important roles in eukaryotic signal transduction and prokaryotic sensory pathways. Pssm-ID: 143637 [Multi-domain] Cd Length: 133 Bit Score: 45.04 E-value: 7.38e-05
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| COG4087 | COG4087 | Soluble P-type ATPase [General function prediction only]; |
2189-2245 | 1.04e-04 | ||||||||
Soluble P-type ATPase [General function prediction only]; Pssm-ID: 443263 [Multi-domain] Cd Length: 156 Bit Score: 45.15 E-value: 1.04e-04
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| HAD-SF-IIB | TIGR01484 | HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid ... |
2079-2242 | 1.12e-04 | ||||||||
HAD-superfamily hydrolase, subfamily IIB; This subfamily falls within the Haloacid Dehalogenase (HAD) superfamily of aspartate-nucleophile hydrolases. The Class II subfamilies are characterized by a domain that is located between the second and third conserved catalytic motifs of the superfamily domain. The IIB subfamily is distinguished from the IIA subfamily (TIGR01460) by homology and the predicted secondary structure of this domain by PSI-PRED. The IIB subfamily's Class II domain has the following predicted structure: Helix-Sheet-Sheet-(Helix or Sheet)-Helix-Sheet-(variable)-Helix-Sheet-Sheet. The IIB subfamily consists of Trehalose-6-phosphatase (TIGR00685), plant and cyanobacterial Sucrose-phosphatase and a closely related group of bacterial and archaeal sequences, eukaryotic phosphomannomutase (pfam03332), a large subfamily ("Cof-like hydrolases", TIGR00099) containing many closely related bacterial sequences, a hypothetical equivalog containing the E. coli YedP protein, as well as two small clusters containing OMNI|TC0379 and OMNI|SA2196 whose relationship to the other groups is unclear. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 273651 [Multi-domain] Cd Length: 207 Bit Score: 45.83 E-value: 1.12e-04
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| P-type_ATPase | cd02609 | uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized ... |
1984-2242 | 1.67e-04 | ||||||||
uncharacterized subfamily of P-type ATPase transporter, similar to uncharacterized Streptococcus pneumoniae exported protein 7, Exp7; This subfamily contains P-type ATPase transporters of unknown function, similar to Streptococcus pneumoniae Exp7. 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. They 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. A general characteristic of P-type ATPases is a bundle of transmembrane helices which make up the transport path, and three domains on the cytoplasmic side of the membrane. Members include pumps that transport various light metal ions, such as H(+), Na(+), K(+), Ca(2+), and Mg(2+), pumps that transport indispensable trace elements, such as Zn(2+) and Cu(2+), pumps that remove toxic heavy metal ions, such as Cd(2+), and pumps such as aminophospholipid translocases which transport phosphatidylserine and phosphatidylethanolamine. Pssm-ID: 319795 [Multi-domain] Cd Length: 661 Bit Score: 47.28 E-value: 1.67e-04
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1290-1526 | 1.98e-04 | ||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 47.63 E-value: 1.98e-04
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| PLN03190 | PLN03190 | aminophospholipid translocase; Provisional |
792-827 | 2.34e-04 | ||||||||
aminophospholipid translocase; Provisional Pssm-ID: 215623 [Multi-domain] Cd Length: 1178 Bit Score: 47.20 E-value: 2.34e-04
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
795-816 | 4.54e-04 | ||||||||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 45.87 E-value: 4.54e-04
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| PHA03247 | PHA03247 | large tegument protein UL36; Provisional |
1324-1544 | 6.23e-04 | ||||||||
large tegument protein UL36; Provisional Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 6.23e-04
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| PRK14959 | PRK14959 | DNA polymerase III subunits gamma and tau; Provisional |
1384-1537 | 9.62e-04 | ||||||||
DNA polymerase III subunits gamma and tau; Provisional Pssm-ID: 184923 [Multi-domain] Cd Length: 624 Bit Score: 44.67 E-value: 9.62e-04
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| Cse1 | pfam08506 | Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the ... |
2707-2781 | 1.32e-03 | ||||||||
Cse1; This domain is present in Cse1 nuclear export receptor proteins. Cse1 mediates the nuclear export of importin alpha. This domain contains HEAT repeats. Pssm-ID: 430038 [Multi-domain] Cd Length: 370 Bit Score: 43.83 E-value: 1.32e-03
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| Hydrolase | pfam00702 | haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha ... |
2058-2237 | 1.45e-03 | ||||||||
haloacid dehalogenase-like hydrolase; This family is structurally different from the alpha/beta hydrolase family (pfam00561). This family includes L-2-haloacid dehalogenase, epoxide hydrolases and phosphatases. The structure of the family consists of two domains. One is an inserted four helix bundle, which is the least well conserved region of the alignment, between residues 16 and 96 of Swiss:P24069. The rest of the fold is composed of the core alpha/beta domain. Those members with the characteriztic DxD triad at the N-terminus are probably phosphatidylglycerolphosphate (PGP) phosphatases involved in cardiolipin biosynthesis in the mitochondria. Pssm-ID: 459910 [Multi-domain] Cd Length: 191 Bit Score: 42.57 E-value: 1.45e-03
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| P-type_ATPase_APLT_Neo1-like | cd07541 | Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human ... |
785-817 | 1.54e-03 | ||||||||
Aminophospholipid translocases (APLTs), similar to Saccharomyces cerevisiae Neo1p and human putative APLT, ATP9B; Aminophospholipid translocases (APLTs), also known as type 4 P-type ATPases, act as a flippases, and translocate specific phospholipids from the exoplasmic leaflet to the cytoplasmic leaflet of biological membranes. The yeast Neo1 gene is an essential gene; Neo1p localizes to the endoplasmic reticulum and the Golgi complex and plays a role in membrane trafficking within the endomembrane system. Also included in this sub family is human putative ATPase phospholipid transporting 9B, ATP9B, which localizes to the trans-golgi network in a CDC50 protein-independent manner. Levels of ATP9B, along with levels of other ATPase genes, may contribute to expressivity of and atypical presentations of Hailey-Hailey disease (HHD), and the ATP9B gene has recently been identified as a putative Alzheimer's disease loci. 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: 319841 [Multi-domain] Cd Length: 792 Bit Score: 44.32 E-value: 1.54e-03
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1291-1546 | 1.86e-03 | ||||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 44.01 E-value: 1.86e-03
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| P-type_ATPase_HM | cd02079 | P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) ... |
2066-2244 | 1.90e-03 | ||||||||
P-type heavy metal-transporting ATPase; Heavy metal-transporting ATPases (Type IB ATPases) transport heavy metal ions (Cu(+), Cu(2+), Zn(2+), Cd(2+), Co(2+), etc.) across biological membranes. These ATPases include mammalian copper-transporting ATPases, ATP7A and ATP7B, Bacillus subtilis CadA which transports cadmium, zinc and cobalt out of the cell, Bacillus subtilis ZosA/PfeT which transports copper, and perhaps also zinc and ferrous iron, Archaeoglobus fulgidus CopA and CopB, Staphylococcus aureus plasmid pI258 CadA, a cadmium-efflux ATPase, and Escherichia coli ZntA which is selective for Pb(2+), Zn(2+), and Cd(2+). The characteristic N-terminal heavy metal associated (HMA) domain of this group is essential for the binding of metal ions. This family 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: 319774 [Multi-domain] Cd Length: 617 Bit Score: 43.74 E-value: 1.90e-03
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| HAD_HPP | cd07517 | phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate ... |
2168-2241 | 3.16e-03 | ||||||||
phosphatase, similar to Bacteroides thetaiotaomicron VPI-5482 BT4131 hexose phosphate phosphatase; belongs to the haloacid dehalogenase-like superfamily; Bacteroides thetaiotaomicron VPI-5482 BT4131 is a phosphatase with preference for hexose phosphates. In addition this family includes uncharacterized Bacillus subtilis YkrA, a putative phosphatase and uncharacterized Streptococcus pyogenes MGAS10394 a putative bifunctional phosphatase/peptidyl-prolyl cis-trans isomerase. Members of this family belong to the haloacid dehalogenase-like (HAD) hydrolases, a large superfamily of diverse enzymes that catalyze carbon or phosphoryl group transfer reactions on a range of substrates, using an active site aspartate in nucleophilic catalysis. Members of this superfamily include 2-L-haloalkanoic acid dehalogenase, azetidine hydrolase, phosphonoacetaldehyde hydrolase, phosphoserine phosphatase, phosphomannomutase, P-type ATPases and many others. HAD hydrolases are found in all three kingdoms of life, and most genomes are predicted to contain multiple HAD-like proteins. Members possess a highly conserved alpha/beta core domain, and many also possess a small cap domain, the fold and function of which is variable. HAD hydrolases are sometimes referred to as belonging to the DDDD superfamily of phosphohydrolases. Pssm-ID: 319819 [Multi-domain] Cd Length: 213 Bit Score: 41.82 E-value: 3.16e-03
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| Cof-subfamily | TIGR00099 | Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of ... |
2203-2242 | 3.20e-03 | ||||||||
Cof subfamily of IIB subfamily of haloacid dehalogenase superfamily; This subfamily of sequences falls within the Class-IIB subfamily (TIGR01484) of the Haloacid Dehalogenase superfamily of aspartate-nucleophile hydrolases. The use of the name "Cof" as an identifier here is arbitrary and refers to the E. coli Cof protein. This subfamily is notable for the large number of recent paralogs in many species. Listeria, for instance, has 12, Clostridium, Lactococcus and Streptococcus pneumoniae have 8 each, Enterococcus and Salmonella have 7 each, and Bacillus subtilus, Mycoplasma, Staphylococcus and E. coli have 6 each. This high degree of gene duplication is limited to the gamma proteobacteria and low-GC gram positive lineages. The profusion of genes in this subfamily is not coupled with a high degree of divergence, so it is impossible to determine an accurate phylogeny at the equivalog level. Considering the relationship of this subfamily to the other known members of the HAD-IIB subfamily (TIGR01484), sucrose and trehalose phosphatases and phosphomannomutase, it seems a reasonable hypothesis that these enzymes act on phosphorylated sugars. Possibly the diversification of genes in this subfamily represents the diverse sugars and polysaccharides that various bacteria find in their biological niches. The members of this subfamily are restricted almost exclusively to bacteria (one sequences from S. pombe scores above trusted, while another is between trusted and noise). It is notable that no archaea are found in this group, the closest relations to the archaea found here being two Deinococcus sequences. [Unknown function, Enzymes of unknown specificity] Pssm-ID: 272905 [Multi-domain] Cd Length: 256 Bit Score: 42.26 E-value: 3.20e-03
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| SerB | COG0560 | Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is ... |
1990-2245 | 3.85e-03 | ||||||||
Phosphoserine phosphatase [Amino acid transport and metabolism]; Phosphoserine phosphatase is part of the Pathway/BioSystem: Serine biosynthesis Pssm-ID: 440326 [Multi-domain] Cd Length: 221 Bit Score: 41.36 E-value: 3.85e-03
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| PHA03307 | PHA03307 | transcriptional regulator ICP4; Provisional |
1294-1550 | 4.42e-03 | ||||||||
transcriptional regulator ICP4; Provisional Pssm-ID: 223039 [Multi-domain] Cd Length: 1352 Bit Score: 42.85 E-value: 4.42e-03
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| MFS_TRI12_like | cd06179 | Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; ... |
2779-2902 | 6.93e-03 | ||||||||
Fungal trichothecene efflux pump (TRI12) of the Major Facilitator Superfamily of transporters; This family includes Fusarium sporotrichioides trichothecene efflux pump (TRI12), which may play a role in F. sporotrichioides self-protection against trichothecenes. TRI12 belongs to the Major Facilitator Superfamily (MFS) of membrane transport proteins, which are thought to function through a single substrate binding site, alternating-access mechanism involving a rocker-switch type of movement. Pssm-ID: 340868 [Multi-domain] Cd Length: 518 Bit Score: 41.84 E-value: 6.93e-03
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