RecName: Full=CTP synthase; AltName: Full=Cytidine 5'-triphosphate synthase; AltName: Full=Cytidine triphosphate synthetase; Short=CTP synthetase; Short=CTPS; AltName: Full=UTP--ammonia ligase
Protein Classification
CTP synthase( domain architecture ID 11423441)
cytidine triphosphate (CTP) synthase catalyzes the conversion of UTP to CTP in the last committed step in pyrimidine nucleotide biosynthesis
List of domain hits
| Name | Accession | Description | Interval | E-value | ||||||||
| PyrG | COG0504 | CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
4-537 | 0e+00 | ||||||||
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis : Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 1090.05 E-value: 0e+00
|
||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||
| PyrG | COG0504 | CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
4-537 | 0e+00 | ||||||||
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 1090.05 E-value: 0e+00
|
||||||||||||
| pyrG | PRK05380 | CTP synthetase; Validated |
3-537 | 0e+00 | ||||||||
CTP synthetase; Validated Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1056.16 E-value: 0e+00
|
||||||||||||
| PyrG | TIGR00337 | CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
4-530 | 0e+00 | ||||||||
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 823.89 E-value: 0e+00
|
||||||||||||
| CTP_synth_N | pfam06418 | CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
5-269 | 0e+00 | ||||||||
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position. Pssm-ID: 461903 Cd Length: 265 Bit Score: 540.01 E-value: 0e+00
|
||||||||||||
| CTPS_N | cd03113 | N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
5-260 | 5.52e-168 | ||||||||
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product. Pssm-ID: 349767 Cd Length: 261 Bit Score: 475.82 E-value: 5.52e-168
|
||||||||||||
| Name | Accession | Description | Interval | E-value | ||||||||
| PyrG | COG0504 | CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase ... |
4-537 | 0e+00 | ||||||||
CTP synthase (UTP-ammonia lyase) [Nucleotide transport and metabolism]; CTP synthase (UTP-ammonia lyase) is part of the Pathway/BioSystem: Pyrimidine biosynthesis Pssm-ID: 440270 [Multi-domain] Cd Length: 535 Bit Score: 1090.05 E-value: 0e+00
|
||||||||||||
| pyrG | PRK05380 | CTP synthetase; Validated |
3-537 | 0e+00 | ||||||||
CTP synthetase; Validated Pssm-ID: 235437 [Multi-domain] Cd Length: 533 Bit Score: 1056.16 E-value: 0e+00
|
||||||||||||
| PyrG | TIGR00337 | CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. ... |
4-530 | 0e+00 | ||||||||
CTP synthase; CTP synthase is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. The enzyme catalyzes the reaction L-glutamine + H2O + UTP + ATP = CTP + phosphate + ADP + L-glutamate. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. This gene has been found circa 500 bp 5' upstream of enolase in both beta (Nitrosomonas europaea) and gamma (E.coli) subdivisions of proteobacterium (FEMS Microbiol Lett 1998 Aug 1;165(1):153-7). [Purines, pyrimidines, nucleosides, and nucleotides, Pyrimidine ribonucleotide biosynthesis] Pssm-ID: 273021 [Multi-domain] Cd Length: 525 Bit Score: 823.89 E-value: 0e+00
|
||||||||||||
| PLN02327 | PLN02327 | CTP synthase |
4-531 | 0e+00 | ||||||||
CTP synthase Pssm-ID: 215186 [Multi-domain] Cd Length: 557 Bit Score: 643.62 E-value: 0e+00
|
||||||||||||
| CTP_synth_N | pfam06418 | CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase ... |
5-269 | 0e+00 | ||||||||
CTP synthase N-terminus; This family consists of the N-terminal region of the CTP synthase protein (EC:6.3.4.2). This family is found in conjunction with pfam00117 located in the C-terminal region of the protein. CTP synthase catalyzes the synthesis of CTP from UTP by amination of the pyrimidine ring at the 4-position. Pssm-ID: 461903 Cd Length: 265 Bit Score: 540.01 E-value: 0e+00
|
||||||||||||
| CTPS_N | cd03113 | N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase ... |
5-260 | 5.52e-168 | ||||||||
N-terminal domain of cytidine 5'-triphosphate synthase; Cytidine 5'-triphosphate synthase (CTPS) is a two-domain protein, which consists of an N-terminal synthetase domain and C-terminal glutaminase domain. The enzymes hydrolyze the amide bond of glutamine to ammonia and glutamate at the glutaminase domains and transfer nascent ammonia to the acceptor substrate at the synthetase domain to form an aminated product. Pssm-ID: 349767 Cd Length: 261 Bit Score: 475.82 E-value: 5.52e-168
|
||||||||||||
| GATase1_CTP_Synthase | cd01746 | Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; ... |
294-528 | 1.28e-141 | ||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase; Type 1 glutamine amidotransferase (GATase1) domain found in Cytidine Triphosphate Synthetase (CTP). CTP is involved in pyrimidine ribonucleotide/ribonucleoside metabolism. CTPs produce CTP from UTP and glutamine and regulate intracellular CTP levels through interactions with four ribonucleotide triphosphates. The enzyme exists as a dimer of identical chains that aggregates as a tetramer. CTP is derived form UTP in three separate steps involving two active sites. In one active site, the UTP O4 oxygen is activated by Mg-ATP-dependent phosphorylation, followed by displacement of the resulting 4-phosphate moiety by ammonia. At a separate site, ammonia is generated via rate limiting glutamine hydrolysis (glutaminase) activity. A gated channel that spans between the glutamine hydrolysis and amidoligase active sites provides a path for ammonia diffusion. CTPs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153217 [Multi-domain] Cd Length: 235 Bit Score: 407.71 E-value: 1.28e-141
|
||||||||||||
| PRK06186 | PRK06186 | hypothetical protein; Validated |
293-532 | 1.00e-42 | ||||||||
hypothetical protein; Validated Pssm-ID: 180452 [Multi-domain] Cd Length: 229 Bit Score: 152.04 E-value: 1.00e-42
|
||||||||||||
| GATase | pfam00117 | Glutamine amidotransferase class-I; |
307-530 | 3.42e-38 | ||||||||
Glutamine amidotransferase class-I; Pssm-ID: 395067 [Multi-domain] Cd Length: 188 Bit Score: 138.52 E-value: 3.42e-38
|
||||||||||||
| PuuD | COG2071 | Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains ... |
338-531 | 2.21e-18 | ||||||||
Gamma-glutamyl-gamma-aminobutyrate hydrolase PuuD (putrescine degradation), contains GATase1-like domain [Amino acid transport and metabolism]; Pssm-ID: 441674 [Multi-domain] Cd Length: 231 Bit Score: 84.45 E-value: 2.21e-18
|
||||||||||||
| GATase1 | cd01653 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
296-392 | 1.38e-11 | ||||||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group includes proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA. and, the A4 beta-galactosidase middle domain. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153210 [Multi-domain] Cd Length: 115 Bit Score: 61.46 E-value: 1.38e-11
|
||||||||||||
| Peptidase_C26 | pfam07722 | Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze ... |
370-512 | 3.16e-11 | ||||||||
Peptidase C26; These peptidases have gamma-glutamyl hydrolase activity; that is they catalyze the cleavage of the gamma-glutamyl bond in poly-gamma-glutamyl substrates. They are structurally related to pfam00117, but contain extensions in four loops and at the C terminus. Pssm-ID: 429620 [Multi-domain] Cd Length: 219 Bit Score: 63.04 E-value: 3.16e-11
|
||||||||||||
| GAT_1 | cd03128 | Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase ... |
296-389 | 5.02e-11 | ||||||||
Type 1 glutamine amidotransferase (GATase1)-like domain; Type 1 glutamine amidotransferase (GATase1)-like domain. This group contains proteins similar to Class I glutamine amidotransferases, the intracellular PH1704 from Pyrococcus horikoshii, the C-terminal of the large catalase: Escherichia coli HP-II, Sinorhizobium meliloti Rm1021 ThuA, the A4 beta-galactosidase middle domain and peptidase E. The majority of proteins in this group have a reactive Cys found in the sharp turn between a beta strand and an alpha helix termed the nucleophile elbow. For Class I glutamine amidotransferases proteins which transfer ammonia from the amide side chain of glutamine to an acceptor substrate, this Cys forms a Cys-His-Glu catalytic triad in the active site. Glutamine amidotransferases activity can be found in a range of biosynthetic enzymes included in this cd: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase, anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase (CPSase), cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. For Pyrococcus horikoshii PH1704, the Cys of the nucleophile elbow together with a different His and, a Glu from an adjacent monomer form a catalytic triad different from the typical GATase1 triad. Peptidase E is believed to be a serine peptidase having a Ser-His-Glu catalytic triad which differs from the Cys-His-Glu catalytic triad of typical GATase1 domains, by having a Ser in place of the reactive Cys at the nucleophile elbow. The E. coli HP-II C-terminal domain, S. meliloti Rm1021 ThuA and the A4 beta-galactosidase middle domain lack the catalytic triad typical GATaseI domains. GATase1-like domains can occur either as single polypeptides, as in Class I glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Peptidase E has a circular permutation in the common core of a typical GTAse1 domain. Pssm-ID: 153222 [Multi-domain] Cd Length: 92 Bit Score: 59.14 E-value: 5.02e-11
|
||||||||||||
| GATase1_2 | cd01745 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
293-513 | 6.04e-11 | ||||||||
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153216 [Multi-domain] Cd Length: 189 Bit Score: 61.44 E-value: 6.04e-11
|
||||||||||||
| GATase1_CPSase | cd01744 | Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This ... |
367-528 | 7.04e-09 | ||||||||
Small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II; This group of sequences represents the small chain of the glutamine-dependent form of carbamoyl phosphate synthase, CPSase II. CPSase II catalyzes the production of carbomyl phosphate (CP) from bicarbonate, glutamine and two molecules of MgATP. The reaction is believed to proceed by a series of four biochemical reactions involving a minimum of three discrete highly reactive intermediates. The synthesis of CP is critical for the initiation of two separate biosynthetic pathways. In one CP is coupled to aspartate, its carbon and nitrogen nuclei ultimately incorporated into the aromatic moieties of pyrimidine nucleotides. In the second pathway CP is condensed with ornithine at the start of the urea cycle and is utilized for the detoxification of ammonia and biosynthesis of arginine. CPSases may be encoded by one or by several genes, depending on the species. The E.coli enzyme is a heterodimer consisting of two polypeptide chains referred to as the small and large subunit. Ammonia an intermediate during the biosynthesis of carbomyl phosphate produced by the hydrolysis of glutamine in the small subunit of the enzyme is delivered via a molecular tunnel between the remotely located carboxyphosphate active site in the large subunit. CPSase IIs belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. This group also contains the sequence from the mammalian urea cycle form which has lost the active site Cys, resulting in an ammonia-dependent form, CPSase I. Pssm-ID: 153215 [Multi-domain] Cd Length: 178 Bit Score: 55.20 E-value: 7.04e-09
|
||||||||||||
| puuD | PRK11366 | gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional |
304-537 | 8.94e-08 | ||||||||
gamma-glutamyl-gamma-aminobutyrate hydrolase; Provisional Pssm-ID: 183101 [Multi-domain] Cd Length: 254 Bit Score: 53.37 E-value: 8.94e-08
|
||||||||||||
| PRK12564 | PRK12564 | carbamoyl-phosphate synthase small subunit; |
367-529 | 8.84e-07 | ||||||||
carbamoyl-phosphate synthase small subunit; Pssm-ID: 237139 [Multi-domain] Cd Length: 360 Bit Score: 51.23 E-value: 8.84e-07
|
||||||||||||
| CarA | COG0505 | Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide ... |
350-529 | 2.50e-06 | ||||||||
Carbamoylphosphate synthase small subunit [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Carbamoylphosphate synthase small subunit is part of the Pathway/BioSystem: Arginine biosynthesis Pssm-ID: 440271 [Multi-domain] Cd Length: 361 Bit Score: 49.63 E-value: 2.50e-06
|
||||||||||||
| GATase1_IGP_Synthase | cd01748 | Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate ... |
310-389 | 1.66e-05 | ||||||||
Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS); Type 1 glutamine amidotransferase (GATase1) domain found in imidazole glycerol phosphate synthase (IGPS). IGPS incorporates ammonia derived from glutamine into N1-[(5'-phosphoribulosyl)-formimino]-5-aminoimidazole-4-carboxamide ribonucleotide (PRFAR) to form 5'-(5-aminoimidazole-4-carboxamide) ribonucleotide (AICAR) and imidazole glycerol phosphate (IGP). The glutamine amidotransferase domain generates the ammonia nucleophile which is channeled from the glutaminase active site to the PRFAR active site. IGPS belong to the triad family of amidotransferases having a conserved Cys-His-Glu catalytic triad in the glutaminase active site. Pssm-ID: 153219 [Multi-domain] Cd Length: 198 Bit Score: 45.95 E-value: 1.66e-05
|
||||||||||||
| hisH | PRK13143 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
311-389 | 6.95e-05 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237289 [Multi-domain] Cd Length: 200 Bit Score: 44.09 E-value: 6.95e-05
|
||||||||||||
| HisH | COG0118 | Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid ... |
310-389 | 8.39e-05 | ||||||||
Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH [Amino acid transport and metabolism]; Imidazoleglycerol phosphate synthase glutamine amidotransferase subunit HisH is part of the Pathway/BioSystem: Histidine biosynthesis Pssm-ID: 439888 [Multi-domain] Cd Length: 196 Bit Score: 43.49 E-value: 8.39e-05
|
||||||||||||
| SIMIBI | cd01983 | SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal ... |
5-53 | 2.91e-04 | ||||||||
SIMIBI (signal recognition particle, MinD and BioD)-class NTPases; SIMIBI (after signal recognition particle, MinD, and BioD), consists of signal recognition particle (SRP) GTPases, the assemblage of MinD-like ATPases, which are involved in protein localization, chromosome partitioning, and membrane transport, and a group of metabolic enzymes with kinase or related phosphate transferase activity. Functionally, proteins in this superfamily use the energy from hydrolysis of NTP to transfer electron or ion. Pssm-ID: 349751 [Multi-domain] Cd Length: 107 Bit Score: 40.49 E-value: 2.91e-04
|
||||||||||||
| hisH | PRK13146 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
315-389 | 3.26e-04 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237290 [Multi-domain] Cd Length: 209 Bit Score: 42.08 E-value: 3.26e-04
|
||||||||||||
| GATase1_1 | cd01741 | Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group ... |
312-389 | 7.22e-04 | ||||||||
Subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain; This group contains a subgroup of proteins having the Type 1 glutamine amidotransferase (GATase1) domain. GATase activity catalyses the transfer of ammonia from the amide side chain of glutamine to an acceptor substrate. Glutamine amidotransferases (GATase) includes the triad family of amidotransferases which have a conserved Cys-His-Glu catalytic triad in the glutaminase active site. In this subgroup this triad is conserved. GATase activity can be found in a range of biosynthetic enzymes, including: glutamine amidotransferase, formylglycinamide ribonucleotide, GMP synthetase , anthranilate synthase component II, glutamine-dependent carbamoyl phosphate synthase, cytidine triphosphate synthetase, gamma-glutamyl hydrolase, imidazole glycerol phosphate synthase and, cobyric acid synthase. Glutamine amidotransferase (GATase) domains can occur either as single polypeptides, as in glutamine amidotransferases, or as domains in a much larger multifunctional synthase protein, such as CPSase. Pssm-ID: 153212 [Multi-domain] Cd Length: 188 Bit Score: 40.69 E-value: 7.22e-04
|
||||||||||||
| GuaA1 | COG0518 | GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP ... |
360-389 | 1.93e-03 | ||||||||
GMP synthase, glutamine amidotransferase domain [Nucleotide transport and metabolism]; GMP synthase, glutamine amidotransferase domain is part of the Pathway/BioSystem: Purine biosynthesis Pssm-ID: 440284 [Multi-domain] Cd Length: 225 Bit Score: 39.93 E-value: 1.93e-03
|
||||||||||||
| PRK07765 | PRK07765 | aminodeoxychorismate/anthranilate synthase component II; |
350-388 | 2.14e-03 | ||||||||
aminodeoxychorismate/anthranilate synthase component II; Pssm-ID: 181107 [Multi-domain] Cd Length: 214 Bit Score: 39.65 E-value: 2.14e-03
|
||||||||||||
| hisH | PRK13141 | imidazole glycerol phosphate synthase subunit HisH; Provisional |
315-389 | 5.18e-03 | ||||||||
imidazole glycerol phosphate synthase subunit HisH; Provisional Pssm-ID: 237288 [Multi-domain] Cd Length: 205 Bit Score: 38.57 E-value: 5.18e-03
|
||||||||||||
| Blast search parameters | ||||
|
