MULTISPECIES: sulfate ABC transporter substrate-binding protein [Salmonella]
Protein Classification
sulfate ABC transporter substrate-binding protein( domain architecture ID 10793466)
sulfate ABC transporter substrate-binding protein serves as the initial receptor in the ABC transport of sulfate and thiosulfate
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||
| PRK10752 | PRK10752 | sulfate ABC transporter substrate-binding protein; |
1-329 | 0e+00 | ||||||
sulfate ABC transporter substrate-binding protein; : Pssm-ID: 182700 Cd Length: 329 Bit Score: 703.86 E-value: 0e+00
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK10752 | PRK10752 | sulfate ABC transporter substrate-binding protein; |
1-329 | 0e+00 | ||||||
sulfate ABC transporter substrate-binding protein; Pssm-ID: 182700 Cd Length: 329 Bit Score: 703.86 E-value: 0e+00
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| Sbp | COG1613 | ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ... |
1-329 | 0e+00 | ||||||
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441221 Cd Length: 340 Bit Score: 663.36 E-value: 0e+00
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| 3a0106s03 | TIGR00971 | sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ... |
12-326 | 0e+00 | ||||||
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein. [Transport and binding proteins, Anions] Pssm-ID: 130044 Cd Length: 315 Bit Score: 622.37 E-value: 0e+00
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| PBP2_CysP | cd01005 | Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ... |
20-326 | 0e+00 | ||||||
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins 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: 270226 Cd Length: 307 Bit Score: 563.86 E-value: 0e+00
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| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
41-280 | 3.52e-43 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 148.18 E-value: 3.52e-43
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| Name | Accession | Description | Interval | E-value | ||||||
| PRK10752 | PRK10752 | sulfate ABC transporter substrate-binding protein; |
1-329 | 0e+00 | ||||||
sulfate ABC transporter substrate-binding protein; Pssm-ID: 182700 Cd Length: 329 Bit Score: 703.86 E-value: 0e+00
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| Sbp | COG1613 | ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ... |
1-329 | 0e+00 | ||||||
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441221 Cd Length: 340 Bit Score: 663.36 E-value: 0e+00
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| 3a0106s03 | TIGR00971 | sulfate/thiosulfate-binding protein; This model describes binding proteins functionally ... |
12-326 | 0e+00 | ||||||
sulfate/thiosulfate-binding protein; This model describes binding proteins functionally associated with the sulfate ABC transporter. In the model bacterium E. coli, two different members work with the same transporter; mutation analysis says each enables the uptake of both sulfate and thiosulfate. In many species, a single binding protein is found, and may be referred to in general terms as a sulfate ABC transporter sulfate-binding protein. [Transport and binding proteins, Anions] Pssm-ID: 130044 Cd Length: 315 Bit Score: 622.37 E-value: 0e+00
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| PBP2_CysP | cd01005 | Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic ... |
20-326 | 0e+00 | ||||||
Substrate binding domain of an active sulfate transporter, a member of the type 2 periplasmic binding fold superfamily; This family contains sulfate binding domain of CysP proteins that serve as initial receptors in the ABC transport of sulfate and thiosulfate in eubacteria. After binding the ligand, CysP interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The CysP proteins 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: 270226 Cd Length: 307 Bit Score: 563.86 E-value: 0e+00
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| CysP | COG4150 | ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and ... |
1-329 | 1.60e-170 | ||||||
ABC-type sulfate transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 443321 Cd Length: 334 Bit Score: 476.72 E-value: 1.60e-170
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| PRK10852 | PRK10852 | thiosulfate ABC transporter substrate-binding protein CysP; |
2-326 | 9.66e-126 | ||||||
thiosulfate ABC transporter substrate-binding protein CysP; Pssm-ID: 236775 Cd Length: 338 Bit Score: 363.30 E-value: 9.66e-126
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| SBP_bac_11 | pfam13531 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
41-280 | 3.52e-43 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463911 [Multi-domain] Cd Length: 225 Bit Score: 148.18 E-value: 3.52e-43
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| ModA | COG0725 | ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion ... |
48-281 | 1.86e-16 | ||||||
ABC-type molybdate transport system, periplasmic Mo-binding protein ModA [Inorganic ion transport and metabolism]; ABC-type molybdate transport system, periplasmic Mo-binding protein ModA is part of the Pathway/BioSystem: Molybdopterin biosynthesis Pssm-ID: 440489 [Multi-domain] Cd Length: 253 Bit Score: 77.60 E-value: 1.86e-16
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| AfuA | COG1840 | ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; ... |
47-307 | 2.37e-14 | ||||||
ABC-type Fe3+ transport system, periplasmic component [Inorganic ion transport and metabolism]; Pssm-ID: 441445 [Multi-domain] Cd Length: 286 Bit Score: 72.28 E-value: 2.37e-14
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| Periplasmic_Binding_Protein_Type_2 | cd00648 | Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent ... |
29-245 | 3.57e-13 | ||||||
Type 2 periplasmic binding fold superfamily; This evolutionary model and hierarchy represent the ligand-binding domains found in solute binding proteins that serve as initial receptors in the transport, signal transduction and channel gating. The PBP2 proteins share the same architecture as periplasmic binding proteins type 1 (PBP1), but have a different topology. They are typically comprised 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. The origin of PBP module can be traced across the distant phyla, including eukaryotes, archebacteria, and prokaryotes. The majority of PBP2 proteins are involved in the uptake of a variety of soluble substrates such as phosphate, sulfate, polysaccharides, lysine/arginine/ornithine, and histidine. 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 cytoplasmically located ATPase domains. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. Besides transport proteins, the family includes ionotropic glutamate receptors and unorthodox sensor proteins involved in signal transduction. The substrate binding domain of the LysR transcriptional regulators and the oligopeptide-like transport systems also contain the type 2 periplasmic binding fold and thus they are significantly homologous to that of the PBP2; however, these two families are grouped into a separate hierarchy of the PBP2 superfamily due to the large number of protein sequences. Pssm-ID: 270214 [Multi-domain] Cd Length: 196 Bit Score: 67.21 E-value: 3.57e-13
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| PBP2_Fbp_like_2 | cd13547 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
75-281 | 3.53e-11 | ||||||
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins 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: 270265 [Multi-domain] Cd Length: 259 Bit Score: 62.63 E-value: 3.53e-11
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| PBP2_Fbp_like_1 | cd13544 | Substrate binding domain of a putative ferric iron transporter, a member of the type 2 ... |
131-311 | 6.33e-11 | ||||||
Substrate binding domain of a putative ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins 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: 270262 [Multi-domain] Cd Length: 292 Bit Score: 62.23 E-value: 6.33e-11
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| PBP2_ModA3_like | cd13517 | Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 ... |
48-279 | 7.90e-11 | ||||||
Substrate binding domain of molybdate binding protein-like (ModA3), a member of the type 2 periplasmic binding fold superfamily; This subfamily contains molybdate binding protein-like (ModA3) domain of an ABC-type transporter. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. ModA transporters import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arrangted around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. The ModA proteins 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: 270235 [Multi-domain] Cd Length: 223 Bit Score: 61.08 E-value: 7.90e-11
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| SBP_bac_6 | pfam13343 | Bacterial extracellular solute-binding protein; This family includes bacterial extracellular ... |
77-314 | 8.24e-08 | ||||||
Bacterial extracellular solute-binding protein; This family includes bacterial extracellular solute-binding proteins. Pssm-ID: 463852 [Multi-domain] Cd Length: 247 Bit Score: 52.36 E-value: 8.24e-08
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| PBP2_PEB3_AcfC | cd13519 | Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a ... |
77-276 | 9.66e-07 | ||||||
Ligand-binding domain of a glycoprotein adhesion and an accessory colonization factor, a member of the type 2 periplasmic binding fold superfamily; PEB3 is a glycoprotein adhesion from Campylobacter jejuni whose structure suggests a functional role in transport, and resembles PEB1a, an Asp/Glu transporter and an adhesin. The overall structure of PEB3 is a dimer and is similar to that of other type 2 periplasmic transport proteins such as the molybdate/tungstate, sulfate, and ferric iron transporters. PEB3 has high sequence identity to Paa, an Escherichia coli adhesin, and to AcfC, an accessory colonization factor from Vibrio cholera. Pssm-ID: 270237 [Multi-domain] Cd Length: 227 Bit Score: 48.85 E-value: 9.66e-07
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| PBP2_Fe3_thiamine_like | cd13518 | Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 ... |
114-279 | 2.39e-06 | ||||||
Substrate binding domain of iron and thiamine transporters-like, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. On the other hand, thiamin is an essential cofactor in all living systems. Thiamin diphosphate (ThDP)-dependent enzymes play an important role in carbohydrate and branched-chain amino acid metabolism. Most prokaryotes, plants, and fungi can synthesize thiamin, but it is not synthesized in vertebrates. These periplasmic domains have high affinities for their respective substrates and serve as the primary receptor for transport. After binding iron and thiamine with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The iron- and thiamine-binding proteins belong to the PBPI2 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: 270236 [Multi-domain] Cd Length: 260 Bit Score: 48.07 E-value: 2.39e-06
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| PBP2_Fbp_like_6 | cd13552 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
130-280 | 1.29e-05 | ||||||
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins 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: 270270 [Multi-domain] Cd Length: 266 Bit Score: 45.91 E-value: 1.29e-05
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| YvgK | COG1910 | Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism]; |
118-153 | 4.65e-05 | ||||||
Periplasmic molybdate-binding protein/domain [Inorganic ion transport and metabolism]; Pssm-ID: 441514 [Multi-domain] Cd Length: 328 Bit Score: 44.61 E-value: 4.65e-05
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| PBP2_Fbp_like_3 | cd13549 | Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 ... |
68-281 | 8.15e-05 | ||||||
Substrate binding domain of an uncharacterized ferric iron transporter, a member of the type 2 periplasmic binding fold superfamily; The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. This periplasmic domain (Fbp) has high affinity for ferric iron and serves as the primary receptor for transport. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins 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: 270267 [Multi-domain] Cd Length: 263 Bit Score: 43.59 E-value: 8.15e-05
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| PBP_like | pfam12727 | PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It ... |
118-153 | 1.20e-04 | ||||||
PBP superfamily domain; This family belongs to the periplasmic binding domain superfamily. It is often associated with a helix-turn-helix domain. Pssm-ID: 463683 [Multi-domain] Cd Length: 192 Bit Score: 42.18 E-value: 1.20e-04
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| PotD | COG0687 | Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; |
87-310 | 1.95e-04 | ||||||
Spermidine/putrescine-binding periplasmic protein [Amino acid transport and metabolism]; Pssm-ID: 440451 [Multi-domain] Cd Length: 348 Bit Score: 42.59 E-value: 1.95e-04
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| PBP2_BitB | cd13546 | Substrate binding domain of a putative iron transporter BitB, a member of the type 2 ... |
117-281 | 2.88e-04 | ||||||
Substrate binding domain of a putative iron transporter BitB, a member of the type 2 periplasmic binding fold superfamily; The substrate domain of this group shows a high homology to the periplasmic component of ferric iron transporter (Fbp), but its biochemical characterization has not been performed. The periplasmic iron binding protein plays an essential role in the iron uptake pathway of Gram-negative pathogenic bacteria from the Pasteurellaceae and Neisseriaceae families and is critical for survival of these pathogens within the host. After binding iron with high affinity, Fbp interacts with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. The ferric iron-binding proteins 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: 270264 [Multi-domain] Cd Length: 258 Bit Score: 41.86 E-value: 2.88e-04
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| PBP2_ModA_like | cd00993 | Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein ... |
41-277 | 3.74e-04 | ||||||
Substrate binding domain of molybdate-binding proteins, the type 2 periplasmic binding protein fold; Molybdate binding domain ModA. Molybdate transport system is comprised of a periplasmic binding protein, an integral membrane protein, and an energizer protein. These three proteins are coded by modA, modB, and modC genes, respectively. ModA proteins serve as initial receptors in the ABC transport of molybdate mostly in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has revealed a binding site for molybdate and tungstate where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins 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: 270215 [Multi-domain] Cd Length: 225 Bit Score: 41.17 E-value: 3.74e-04
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| SBP_bac_1 | pfam01547 | Bacterial extracellular solute-binding protein; This family also includes the bacterial ... |
36-272 | 7.87e-03 | ||||||
Bacterial extracellular solute-binding protein; This family also includes the bacterial extracellular solute-binding protein family POTD/POTF. Pssm-ID: 460248 [Multi-domain] Cd Length: 294 Bit Score: 37.40 E-value: 7.87e-03
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| PBP2_AvModA | cd13539 | Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the ... |
48-273 | 9.53e-03 | ||||||
Substrate binding domain of ModA/WtpA from Azotobacter vinelandii and its closest homologs;the type 2 periplasmic binding protein fold; This subfamily contains domains found in ModA proteins that serve as initial receptors in the ABC transport of molybdate in eubacteria and archaea. Bacteria and archaea import molybdenum and tungsten from the environment in the form of the oxyanions molybdate (MoO(4) (2-)) and tungstate (WO(4) (2-)). After binding molybdate with high affinity, they interact with a cognate membrane transport complex comprised of two integral membrane domains and two cytoplasmically located ATPase. This interaction triggers the ligand translocation across the cytoplasmic membrane energized by ATP hydrolysis. In contrast to the structure of the two ModA homologs from Escherichia coli and Azotobacter vinelandii, where the oxygen atoms are tetrahedrally arranged around the metal center, the structure of Pyrococcus furiosus ModA/WtpA (PfModA) has shown that a binding site for molybdate and tungstate is where the central metal atom is in a hexacoordinate configuration. This octahedral geometry was rather unexpected. The ModA proteins 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: 270257 [Multi-domain] Cd Length: 226 Bit Score: 36.78 E-value: 9.53e-03
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