MULTISPECIES: TrkA family potassium uptake protein [unclassified Campylobacter]
potassium channel family protein( domain architecture ID 11426271)
potassium channel family protein spans the cell membrane to form a conduction pathway or pore, through which selective ions such as potassium, sodium, and calcium translocate across cell membranes, similar to Trk system potassium uptake protein TrkA
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
8-199 | 3.40e-40 | ||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; : Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 139.05 E-value: 3.40e-40
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Name | Accession | Description | Interval | E-value | ||||
TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
8-199 | 3.40e-40 | ||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 139.05 E-value: 3.40e-40
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TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
8-121 | 4.07e-26 | ||||
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD. Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 97.21 E-value: 4.07e-26
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trkA | PRK09496 | Trk system potassium transporter TrkA; |
8-208 | 2.26e-13 | ||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 67.84 E-value: 2.26e-13
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NAD_bind_Leu_Phe_Val_DH | cd01075 | NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
5-45 | 3.82e-05 | ||||
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133444 Cd Length: 200 Bit Score: 42.96 E-value: 3.82e-05
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Name | Accession | Description | Interval | E-value | ||||
TrkA | COG0569 | Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion ... |
8-199 | 3.40e-40 | ||||
Trk/Ktr K+ transport system regulatory component TrkA/KtrA/KtrC, RCK domain [Inorganic ion transport and metabolism, Signal transduction mechanisms]; Pssm-ID: 440335 [Multi-domain] Cd Length: 296 Bit Score: 139.05 E-value: 3.40e-40
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TrkA_N | pfam02254 | TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include ... |
8-121 | 4.07e-26 | ||||
TrkA-N domain; This domain is found in a wide variety of proteins. These proteins include potassium channels, phosphoesterases, and various other transporters. This domain binds to NAD. Pssm-ID: 426679 [Multi-domain] Cd Length: 115 Bit Score: 97.21 E-value: 4.07e-26
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Kch | COG1226 | Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; |
8-130 | 1.10e-15 | ||||
Voltage-gated potassium channel Kch [Inorganic ion transport and metabolism]; Pssm-ID: 440839 [Multi-domain] Cd Length: 279 Bit Score: 73.61 E-value: 1.10e-15
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trkA | PRK09496 | Trk system potassium transporter TrkA; |
8-208 | 2.26e-13 | ||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 67.84 E-value: 2.26e-13
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trkA | PRK09496 | Trk system potassium transporter TrkA; |
8-121 | 1.12e-06 | ||||
Trk system potassium transporter TrkA; Pssm-ID: 236541 [Multi-domain] Cd Length: 453 Bit Score: 48.19 E-value: 1.12e-06
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PRK09599 | PRK09599 | NADP-dependent phosphogluconate dehydrogenase; |
7-45 | 7.03e-06 | ||||
NADP-dependent phosphogluconate dehydrogenase; Pssm-ID: 236582 [Multi-domain] Cd Length: 301 Bit Score: 45.51 E-value: 7.03e-06
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PRK03562 | PRK03562 | glutathione-regulated potassium-efflux system protein KefC; Provisional |
8-131 | 1.99e-05 | ||||
glutathione-regulated potassium-efflux system protein KefC; Provisional Pssm-ID: 235131 [Multi-domain] Cd Length: 621 Bit Score: 44.60 E-value: 1.99e-05
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NAD_bind_Leu_Phe_Val_DH | cd01075 | NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine ... |
5-45 | 3.82e-05 | ||||
NAD(P) binding domain of leucine dehydrogenase, phenylalanine dehydrogenase, and valine dehydrogenase; Amino acid dehydrogenase (DH) is a widely distributed family of enzymes that catalyzes the oxidative deamination of an amino acid to its keto acid and ammonia with concomitant reduction of NADP+. For example, leucine DH catalyzes the reversible oxidative deamination of L-leucine and several other straight or branched chain amino acids to the corresponding 2-oxoacid derivative. Amino acid DH -like NAD(P)-binding domains are members of the Rossmann fold superfamily and include glutamate, leucine, and phenylalanine DHs, methylene tetrahydrofolate DH, methylene-tetrahydromethanopterin DH, methylene-tetrahydropholate DH/cyclohydrolase, Shikimate DH-like proteins, malate oxidoreductases, and glutamyl tRNA reductase. Amino acid DHs catalyze the deamination of amino acids to keto acids with NAD(P)+ as a cofactor. The NAD(P)-binding Rossmann fold superfamily includes a wide variety of protein families including NAD(P)- binding domains of alcohol DHs, tyrosine-dependent oxidoreductases, glyceraldehyde-3-phosphate DH, lactate/malate DHs, formate/glycerate DHs, siroheme synthases, 6-phosphogluconate DH, amino acid DHs, repressor rex, NAD-binding potassium channel domain, CoA-binding, and ornithine cyclodeaminase-like domains. These domains have an alpha-beta-alpha configuration. NAD binding involves numerous hydrogen and van der Waals contacts. Pssm-ID: 133444 Cd Length: 200 Bit Score: 42.96 E-value: 3.82e-05
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ProC | COG0345 | Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; ... |
7-75 | 1.02e-04 | ||||
Pyrroline-5-carboxylate reductase [Amino acid transport and metabolism]; Pyrroline-5-carboxylate reductase is part of the Pathway/BioSystem: Proline biosynthesis Pssm-ID: 440114 [Multi-domain] Cd Length: 267 Bit Score: 41.97 E-value: 1.02e-04
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NAD_binding_2 | pfam03446 | NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of ... |
5-76 | 1.10e-04 | ||||
NAD binding domain of 6-phosphogluconate dehydrogenase; The NAD binding domain of 6-phosphogluconate dehydrogenase adopts a Rossmann fold. Pssm-ID: 427298 [Multi-domain] Cd Length: 159 Bit Score: 40.92 E-value: 1.10e-04
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COG2085 | COG2085 | Predicted dinucleotide-binding enzyme [General function prediction only]; |
6-75 | 1.85e-04 | ||||
Predicted dinucleotide-binding enzyme [General function prediction only]; Pssm-ID: 441688 [Multi-domain] Cd Length: 205 Bit Score: 40.92 E-value: 1.85e-04
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MmsB | COG2084 | 3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport ... |
3-74 | 2.40e-04 | ||||
3-hydroxyisobutyrate dehydrogenase or related beta-hydroxyacid dehydrogenase [Lipid transport and metabolism]; Pssm-ID: 441687 [Multi-domain] Cd Length: 285 Bit Score: 40.87 E-value: 2.40e-04
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PLN02256 | PLN02256 | arogenate dehydrogenase |
7-88 | 7.04e-04 | ||||
arogenate dehydrogenase Pssm-ID: 215144 [Multi-domain] Cd Length: 304 Bit Score: 39.65 E-value: 7.04e-04
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PRK10669 | PRK10669 | putative cation:proton antiport protein; Provisional |
8-137 | 9.61e-04 | ||||
putative cation:proton antiport protein; Provisional Pssm-ID: 182633 [Multi-domain] Cd Length: 558 Bit Score: 39.70 E-value: 9.61e-04
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WecC | COG0677 | UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; |
7-73 | 1.04e-03 | ||||
UDP-N-acetyl-D-mannosaminuronate dehydrogenase [Cell wall/membrane/envelope biogenesis]; Pssm-ID: 440441 [Multi-domain] Cd Length: 413 Bit Score: 39.27 E-value: 1.04e-03
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PRK08293 | PRK08293 | 3-hydroxyacyl-CoA dehydrogenase; |
1-105 | 1.34e-03 | ||||
3-hydroxyacyl-CoA dehydrogenase; Pssm-ID: 181359 [Multi-domain] Cd Length: 287 Bit Score: 38.77 E-value: 1.34e-03
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garR | PRK11559 | tartronate semialdehyde reductase; Provisional |
7-72 | 1.96e-03 | ||||
tartronate semialdehyde reductase; Provisional Pssm-ID: 183197 [Multi-domain] Cd Length: 296 Bit Score: 38.11 E-value: 1.96e-03
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PRK09186 | PRK09186 | flagellin modification protein A; Provisional |
10-45 | 2.10e-03 | ||||
flagellin modification protein A; Provisional Pssm-ID: 236399 [Multi-domain] Cd Length: 256 Bit Score: 38.05 E-value: 2.10e-03
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PRK05808 | PRK05808 | 3-hydroxybutyryl-CoA dehydrogenase; Validated |
1-105 | 3.92e-03 | ||||
3-hydroxybutyryl-CoA dehydrogenase; Validated Pssm-ID: 180269 [Multi-domain] Cd Length: 282 Bit Score: 37.25 E-value: 3.92e-03
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SDR_a4 | cd05266 | atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member ... |
7-75 | 6.00e-03 | ||||
atypical (a) SDRs, subgroup 4; Atypical SDRs in this subgroup are poorly defined, one member is identified as a putative NAD-dependent epimerase/dehydratase. Atypical SDRs are distinct from classical SDRs. Members of this subgroup have a glycine-rich NAD(P)-binding motif that is related to, but is different from, the archetypical SDRs, GXGXXG. This subgroup also lacks most of the characteristic active site residues of the SDRs; however, the upstream Ser is present at the usual place, and some potential catalytic residues are present in place of the usual YXXXK active site motif. Atypical SDRs generally lack the catalytic residues characteristic of the SDRs, and their glycine-rich NAD(P)-binding motif is often different from the forms normally seen in classical or extended SDRs. Atypical SDRs include biliverdin IX beta reductase (BVR-B,aka flavin reductase), NMRa (a negative transcriptional regulator of various fungi), progesterone 5-beta-reductase like proteins, phenylcoumaran benzylic ether and pinoresinol-lariciresinol reductases, phenylpropene synthases, eugenol synthase, triphenylmethane reductase, isoflavone reductases, and others. SDRs are a functionally diverse family of oxidoreductases that have a single domain with a structurally conserved Rossmann fold, an NAD(P)(H)-binding region, and a structurally diverse C-terminal region. Sequence identity between different SDR enzymes is typically in the 15-30% range; they catalyze a wide range of activities including the metabolism of steroids, cofactors, carbohydrates, lipids, aromatic compounds, and amino acids, and act in redox sensing. Classical SDRs have an TGXXX[AG]XG cofactor binding motif and a YXXXK active site motif, with the Tyr residue of the active site motif serving as a critical catalytic residue (Tyr-151, human 15-hydroxyprostaglandin dehydrogenase numbering). In addition to the Tyr and Lys, there is often an upstream Ser and/or an Asn, contributing to the active site; while substrate binding is in the C-terminal region, which determines specificity. The standard reaction mechanism is a 4-pro-S hydride transfer and proton relay involving the conserved Tyr and Lys, a water molecule stabilized by Asn, and nicotinamide. In addition to the Rossmann fold core region typical of all SDRs, extended SDRs have a less conserved C-terminal extension of approximately 100 amino acids, and typically have a TGXXGXXG cofactor binding motif. Complex (multidomain) SDRs such as ketoreductase domains of fatty acid synthase have a GGXGXXG NAD(P)-binding motif and an altered active site motif (YXXXN). Fungal type ketoacyl reductases have a TGXXXGX(1-2)G NAD(P)-binding motif. Pssm-ID: 187576 [Multi-domain] Cd Length: 251 Bit Score: 36.53 E-value: 6.00e-03
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MurD | COG0771 | UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; ... |
1-74 | 8.12e-03 | ||||
UDP-N-acetylmuramoylalanine-D-glutamate ligase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylmuramoylalanine-D-glutamate ligase is part of the Pathway/BioSystem: Mureine biosynthesis Pssm-ID: 440534 [Multi-domain] Cd Length: 445 Bit Score: 36.60 E-value: 8.12e-03
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Blast search parameters | ||||
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