Atp2b1 [Sigmodon hispidus]
Protein Classification
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||
| ATPase-IIB_Ca super family | cl36924 | plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ... |
1-169 | 6.17e-86 | ||||
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. The actual alignment was detected with superfamily member TIGR01517: Pssm-ID: 273668 [Multi-domain] Cd Length: 956 Bit Score: 270.88 E-value: 6.17e-86
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| Name | Accession | Description | Interval | E-value | ||||
| ATPase-IIB_Ca | TIGR01517 | plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ... |
1-169 | 6.17e-86 | ||||
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: 270.88 E-value: 6.17e-86
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| Cation_ATPase_C | pfam00689 | Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, ... |
1-169 | 1.52e-30 | ||||
Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices. Pssm-ID: 376368 [Multi-domain] Cd Length: 175 Bit Score: 108.87 E-value: 1.52e-30
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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 ... |
1-42 | 9.95e-23 | ||||
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: 93.81 E-value: 9.95e-23
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
1-168 | 6.18e-19 | ||||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 82.85 E-value: 6.18e-19
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| Name | Accession | Description | Interval | E-value | ||||
| ATPase-IIB_Ca | TIGR01517 | plasma-membrane calcium-translocating P-type ATPase; This model describes the P-type ATPase ... |
1-169 | 6.17e-86 | ||||
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: 270.88 E-value: 6.17e-86
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| Cation_ATPase_C | pfam00689 | Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, ... |
1-169 | 1.52e-30 | ||||
Cation transporting ATPase, C-terminus; Members of this families are involved in Na+/K+, H+/K+, Ca++ and Mg++ transport. This family represents 5 transmembrane helices. Pssm-ID: 376368 [Multi-domain] Cd Length: 175 Bit Score: 108.87 E-value: 1.52e-30
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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 ... |
1-42 | 9.95e-23 | ||||
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: 93.81 E-value: 9.95e-23
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| MgtA | COG0474 | Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; |
1-168 | 6.18e-19 | ||||
Magnesium-transporting ATPase (P-type) [Inorganic ion transport and metabolism]; Pssm-ID: 440242 [Multi-domain] Cd Length: 874 Bit Score: 82.85 E-value: 6.18e-19
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| P-type_ATPase_cation | cd02080 | P-type cation-transporting ATPase similar to Exiguobacterium aurantiacum Mna, an Na(+)-ATPase, ... |
2-156 | 6.53e-11 | ||||
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: 59.58 E-value: 6.53e-11
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| P-type_ATPase_SPCA | cd02085 | golgi-associated secretory pathway Ca(2+) transport ATPases, similar to human ATPase secretory ... |
1-141 | 1.80e-10 | ||||
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: 58.57 E-value: 1.80e-10
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| DUF446 | pfam04287 | tRNA pseudouridine synthase C; This family is suggested to be the catalytic domain of tRNA ... |
141-167 | 3.54e-03 | ||||
tRNA pseudouridine synthase C; This family is suggested to be the catalytic domain of tRNA pseudouridine synthase C by association. The structure has been solved for one member, as PDB:2HGK, which by inference is designated in this way. Pssm-ID: 427841 Cd Length: 97 Bit Score: 35.21 E-value: 3.54e-03
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| YqcC | COG3098 | Uncharacterized conserved protein YqcC, DUF446 family [Function unknown]; |
141-167 | 6.02e-03 | ||||
Uncharacterized conserved protein YqcC, DUF446 family [Function unknown]; Pssm-ID: 442332 Cd Length: 109 Bit Score: 34.82 E-value: 6.02e-03
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| Blast search parameters | ||||
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