RecName: Full=Transferrin; Flags: Precursor
Protein Classification
PBP2_transferrin domain-containing protein( domain architecture ID 13889953)
PBP2_transferrin domain-containing protein
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| TR_FER | smart00094 | Transferrin; |
23-359 | 6.17e-121 | ||||||
Transferrin; : Pssm-ID: 214514 Cd Length: 332 Bit Score: 363.55 E-value: 6.17e-121
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| TR_FER super family | cl30084 | Transferrin; |
371-677 | 4.24e-106 | ||||||
Transferrin; The actual alignment was detected with superfamily member smart00094: Pssm-ID: 214514 Cd Length: 332 Bit Score: 325.41 E-value: 4.24e-106
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| Name | Accession | Description | Interval | E-value | ||||||
| TR_FER | smart00094 | Transferrin; |
23-359 | 6.17e-121 | ||||||
Transferrin; Pssm-ID: 214514 Cd Length: 332 Bit Score: 363.55 E-value: 6.17e-121
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| TR_FER | smart00094 | Transferrin; |
371-677 | 4.24e-106 | ||||||
Transferrin; Pssm-ID: 214514 Cd Length: 332 Bit Score: 325.41 E-value: 4.24e-106
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| PBP2_transferrin | cd13529 | Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ... |
371-668 | 9.04e-81 | ||||||
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270247 Cd Length: 298 Bit Score: 258.49 E-value: 9.04e-81
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| PBP2_transferrin | cd13529 | Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ... |
22-359 | 6.60e-68 | ||||||
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270247 Cd Length: 298 Bit Score: 224.59 E-value: 6.60e-68
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| Transferrin | pfam00405 | Transferrin; |
371-611 | 6.93e-36 | ||||||
Transferrin; Pssm-ID: 395328 [Multi-domain] Cd Length: 328 Bit Score: 137.98 E-value: 6.93e-36
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| Transferrin | pfam00405 | Transferrin; |
49-290 | 6.56e-33 | ||||||
Transferrin; Pssm-ID: 395328 [Multi-domain] Cd Length: 328 Bit Score: 129.50 E-value: 6.56e-33
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| PhnD | COG3221 | ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ... |
106-157 | 1.34e-06 | ||||||
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 442454 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 1.34e-06
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| PhnD | COG3221 | ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ... |
431-517 | 2.91e-05 | ||||||
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 442454 [Multi-domain] Cd Length: 250 Bit Score: 46.07 E-value: 2.91e-05
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| 3A0109s03R | TIGR01098 | phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ... |
108-153 | 1.84e-04 | ||||||
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are a varied class of phosphorus-containing organic compound in which a direct C-P bond is found, rather than a C-O-P linkage of the phosphorus through an oxygen atom. They may be toxic but also may be used as sources of phosphorus and energy by various bacteria. Phosphonate utilization systems typically are encoded in 14 or more genes, including a three gene ABC transporter. This family includes the periplasmic binding protein component of ABC transporters for phosphonates as well as other, related binding components for closely related substances such as phosphate and phosphite. A number of members of this family are found in genomic contexts with components of selenium metabolic processes suggestive of a role in selenate or other selenium-compound transport. A subset of this model in which nearly all members exhibit genomic context with elements of phosphonate metabolism, particularly the C-P lyase system (GenProp0232) has been built (TIGR03431) as an equivalog. Nevertheless, there are members of this subfamily (TIGR01098) which show up sporadically on a phylogenetic tree that also show phosphonate context and are most likely competent to transport phosphonates. [Transport and binding proteins, Anions] Pssm-ID: 273442 [Multi-domain] Cd Length: 254 Bit Score: 43.88 E-value: 1.84e-04
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| Name | Accession | Description | Interval | E-value | ||||||
| TR_FER | smart00094 | Transferrin; |
23-359 | 6.17e-121 | ||||||
Transferrin; Pssm-ID: 214514 Cd Length: 332 Bit Score: 363.55 E-value: 6.17e-121
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| TR_FER | smart00094 | Transferrin; |
371-677 | 4.24e-106 | ||||||
Transferrin; Pssm-ID: 214514 Cd Length: 332 Bit Score: 325.41 E-value: 4.24e-106
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| PBP2_transferrin | cd13529 | Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ... |
371-668 | 9.04e-81 | ||||||
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270247 Cd Length: 298 Bit Score: 258.49 E-value: 9.04e-81
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| PBP2_transferrin | cd13529 | Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are ... |
22-359 | 6.60e-68 | ||||||
Transferrin family of the type 2 periplasmic-binding protein superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helical and beta sheet domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270247 Cd Length: 298 Bit Score: 224.59 E-value: 6.60e-68
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| PBP2_transferrin_N | cd13618 | The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ... |
370-611 | 3.16e-38 | ||||||
The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270336 Cd Length: 324 Bit Score: 144.49 E-value: 3.16e-38
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| Transferrin | pfam00405 | Transferrin; |
371-611 | 6.93e-36 | ||||||
Transferrin; Pssm-ID: 395328 [Multi-domain] Cd Length: 328 Bit Score: 137.98 E-value: 6.93e-36
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| Transferrin | pfam00405 | Transferrin; |
49-290 | 6.56e-33 | ||||||
Transferrin; Pssm-ID: 395328 [Multi-domain] Cd Length: 328 Bit Score: 129.50 E-value: 6.56e-33
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| PBP2_transferrin_N | cd13618 | The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ... |
47-290 | 4.19e-27 | ||||||
The N-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270336 Cd Length: 324 Bit Score: 112.52 E-value: 4.19e-27
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| PBP2_transferrin_C | cd13617 | The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ... |
48-326 | 5.74e-25 | ||||||
The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270335 Cd Length: 331 Bit Score: 106.33 E-value: 5.74e-25
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| PBP2_transferrin_C | cd13617 | The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; ... |
371-611 | 3.40e-22 | ||||||
The C-lobe of transferrin, a member of the type 2 periplasmic binding protein fold superfamily; Transferrins are iron-binding blood plasma glycoproteins that regulate the level of free iron in biological fluids. Vertebrate transferrins are made of a single polypeptide chain with a molecular weight of about 80 kDa. The polypeptide is folded into two homologous lobes (the N-lobe and C-lobe), and each lobe is further subdivided into two similar alpha helices and beta sheets domains separated by a deep cleft that forms the binding site for ferric iron. Thus, the transferrin protein contains two homologous metal-binding sites with high affinities for ferric iron. The modern transferrin proteins are thought to be evolved from an ancestral gene coding for a protein of 40 kDa containing a single binding site by means of a gene duplication event. Vertebrate transferrins are found in a variety of bodily fluids, including serum transferrins, ovotransferrins, lactoferrins, and melanotransferrins. Transferrin-like proteins are also found in the circulatory fluid of certain invertebrates. The transferrins have the same structural fold as the type 2 periplasmic-binding proteins, many of which are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. Pssm-ID: 270335 Cd Length: 331 Bit Score: 98.24 E-value: 3.40e-22
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| Phosphonate-bd | pfam12974 | ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ... |
98-153 | 1.12e-07 | ||||||
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake. Pssm-ID: 432911 [Multi-domain] Cd Length: 243 Bit Score: 53.42 E-value: 1.12e-07
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| PhnD | COG3221 | ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ... |
106-157 | 1.34e-06 | ||||||
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 442454 [Multi-domain] Cd Length: 250 Bit Score: 50.30 E-value: 1.34e-06
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| Phosphonate-bd | pfam12974 | ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of ... |
403-517 | 1.98e-06 | ||||||
ABC transporter, phosphonate, periplasmic substrate-binding protein; This is a family of periplasmic proteins which are part of the transport system for alkylphosphonate uptake. Pssm-ID: 432911 [Multi-domain] Cd Length: 243 Bit Score: 49.57 E-value: 1.98e-06
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| PBP2_PhnD_like | cd01071 | Substrate binding domain of phosphonate uptake system-like, a member of the type 2 ... |
108-156 | 2.50e-05 | ||||||
Substrate binding domain of phosphonate uptake system-like, a member of the type 2 periplasmic-binding fold superfamily; This family includes alkylphosphonate binding domain PhnD. These domains are found in PhnD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. PhnD is the periplasmic binding component of an ABC-type phosphonate uptake system (PhnCDE) that recognizes and binds phosphonate. PhnD belongs to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. The PBP2 have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270232 [Multi-domain] Cd Length: 253 Bit Score: 46.49 E-value: 2.50e-05
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| PhnD | COG3221 | ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion ... |
431-517 | 2.91e-05 | ||||||
ABC-type phosphate/phosphonate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 442454 [Multi-domain] Cd Length: 250 Bit Score: 46.07 E-value: 2.91e-05
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| PBP2_PnhD_4 | cd13574 | Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ... |
36-154 | 7.25e-05 | ||||||
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270292 [Multi-domain] Cd Length: 250 Bit Score: 45.00 E-value: 7.25e-05
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| 3A0109s03R | TIGR01098 | phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are ... |
108-153 | 1.84e-04 | ||||||
phosphate/phosphite/phosphonate ABC transporter, periplasmic binding protein; Phosphonates are a varied class of phosphorus-containing organic compound in which a direct C-P bond is found, rather than a C-O-P linkage of the phosphorus through an oxygen atom. They may be toxic but also may be used as sources of phosphorus and energy by various bacteria. Phosphonate utilization systems typically are encoded in 14 or more genes, including a three gene ABC transporter. This family includes the periplasmic binding protein component of ABC transporters for phosphonates as well as other, related binding components for closely related substances such as phosphate and phosphite. A number of members of this family are found in genomic contexts with components of selenium metabolic processes suggestive of a role in selenate or other selenium-compound transport. A subset of this model in which nearly all members exhibit genomic context with elements of phosphonate metabolism, particularly the C-P lyase system (GenProp0232) has been built (TIGR03431) as an equivalog. Nevertheless, there are members of this subfamily (TIGR01098) which show up sporadically on a phylogenetic tree that also show phosphonate context and are most likely competent to transport phosphonates. [Transport and binding proteins, Anions] Pssm-ID: 273442 [Multi-domain] Cd Length: 254 Bit Score: 43.88 E-value: 1.84e-04
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| PBP2_PnhD_3 | cd13573 | Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ... |
103-157 | 1.83e-03 | ||||||
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270291 [Multi-domain] Cd Length: 253 Bit Score: 40.54 E-value: 1.83e-03
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| PBP2_PnhD_2 | cd13572 | Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ... |
99-156 | 2.85e-03 | ||||||
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding component of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270290 [Multi-domain] Cd Length: 249 Bit Score: 39.99 E-value: 2.85e-03
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| PBP2_PnhD_1 | cd13571 | Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains ... |
108-152 | 5.70e-03 | ||||||
Substrate binding domain of uncharacterized ABC-type phosphonate-like transporter; contains the type 2 periplasmic binding fold; This subfamily includes putative periplasmic binding components of an ABC transport system similar to alkylphosphonate binding domain PnhD. These domains are found in PnhD-like proteins that are predicted to function as initial receptors in hypophosphite, phosphonate, or phosphate ABC transport in archaea and eubacteria. They belong to the PBP2 superfamily of periplasmic binding proteins that differ in size and ligand specificity, but have similar tertiary structures consisting of two globular subdomains connected by a flexible hinge. They have been shown to bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. Pssm-ID: 270289 [Multi-domain] Cd Length: 253 Bit Score: 39.16 E-value: 5.70e-03
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| PBP2_BvgS_like_1 | cd13708 | Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is ... |
29-128 | 6.70e-03 | ||||||
Putative sensor domain similar to BvgS; the type 2 periplasmic binding protein domain; BvgS is composed of two periplasmic domains homologous to bacterial periplasmic-binding proteins (PBPs), a transmembrane region followed successively by a cytoplasmic PAS (Per/ARNT/SIM), a Histidine-kinase (HK), a receiver and a Histidine phosphotransfer (Hpt) domains. The sensor protein BvgS can autophosphorylate and phosphorylate the response regulator BvgA. The BvgAS phosphorelay controls the expression of virulence factors in response to certain environmental stimuli in Bordetella pertussis. Its close homologs, Escherichia coli EvgS and Klebsiella pneumoniae KvgS, appear to be involved in the transcriptional regulation of drug efflux pumps and in countering free radical stresses and sensing iron limiting conditions, respectively. The periplasmic sensor domain of BvgS belongs to the type 2 periplasmic-binding fold protein (PBP2) superfamily, whose members are involved in chemotaxis and uptake of nutrients and other small molecules from the extracellular space as a primary receptor. PBP2 typically comprises of two globular subdomains connected by a flexible hinge and bind their ligand in the cleft between these domains in a manner resembling a Venus flytrap. After binding their specific ligand with high affinity, they can interact with a cognate membrane transport complex comprised of two integral membrane domains and two receptor cytoplasmically-located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Pssm-ID: 270426 [Multi-domain] Cd Length: 220 Bit Score: 38.65 E-value: 6.70e-03
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