mRNA-capping enzyme isoform X2 [Rattus norvegicus]
dual specificity protein phosphatase family protein( domain architecture ID 13026130)
dual specificity protein phosphatase family protein such as dual specificity phosphatases, which dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues, as well as tyrosine-specific protein phosphatases
List of domain hits
Name | Accession | Description | Interval | E-value | ||||
Mce1_N | cd17664 | N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ... |
1-146 | 1.89e-106 | ||||
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans. : Pssm-ID: 350502 Cd Length: 167 Bit Score: 316.54 E-value: 1.89e-106
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Adenylation_mRNA_capping | cd07895 | Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ... |
219-432 | 1.39e-103 | ||||
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues. : Pssm-ID: 185706 [Multi-domain] Cd Length: 215 Bit Score: 311.10 E-value: 1.39e-103
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mRNA_cap_C | pfam03919 | mRNA capping enzyme, C-terminal domain; |
436-529 | 9.39e-28 | ||||
mRNA capping enzyme, C-terminal domain; : Pssm-ID: 461093 Cd Length: 108 Bit Score: 107.30 E-value: 9.39e-28
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Name | Accession | Description | Interval | E-value | ||||||
Mce1_N | cd17664 | N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ... |
1-146 | 1.89e-106 | ||||||
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans. Pssm-ID: 350502 Cd Length: 167 Bit Score: 316.54 E-value: 1.89e-106
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Adenylation_mRNA_capping | cd07895 | Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ... |
219-432 | 1.39e-103 | ||||||
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues. Pssm-ID: 185706 [Multi-domain] Cd Length: 215 Bit Score: 311.10 E-value: 1.39e-103
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mRNA_cap_enzyme | pfam01331 | mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ... |
243-431 | 2.49e-94 | ||||||
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain of the mRNA capping enzyme. Pssm-ID: 396068 [Multi-domain] Cd Length: 194 Bit Score: 286.61 E-value: 2.49e-94
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CEG1 | COG5226 | mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification]; |
239-566 | 2.95e-39 | ||||||
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification]; Pssm-ID: 227551 [Multi-domain] Cd Length: 404 Bit Score: 148.14 E-value: 2.95e-39
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mRNA_cap_C | pfam03919 | mRNA capping enzyme, C-terminal domain; |
436-529 | 9.39e-28 | ||||||
mRNA capping enzyme, C-terminal domain; Pssm-ID: 461093 Cd Length: 108 Bit Score: 107.30 E-value: 9.39e-28
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PTZ00242 | PTZ00242 | protein tyrosine phosphatase; Provisional |
18-114 | 3.85e-07 | ||||||
protein tyrosine phosphatase; Provisional Pssm-ID: 185524 [Multi-domain] Cd Length: 166 Bit Score: 50.02 E-value: 3.85e-07
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DSPc | pfam00782 | Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ... |
29-132 | 1.15e-05 | ||||||
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region. Pssm-ID: 395632 [Multi-domain] Cd Length: 127 Bit Score: 44.95 E-value: 1.15e-05
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CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
95-132 | 3.70e-05 | ||||||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 43.81 E-value: 3.70e-05
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DSPc | smart00195 | Dual specificity phosphatase, catalytic domain; |
77-132 | 5.69e-05 | ||||||
Dual specificity phosphatase, catalytic domain; Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 43.04 E-value: 5.69e-05
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Name | Accession | Description | Interval | E-value | ||||||
Mce1_N | cd17664 | N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as ... |
1-146 | 1.89e-106 | ||||||
N-terminal triphosphatase domain of mRNA capping enzyme; mRNA capping enzyme, also known as RNA guanylyltransferase and 5'-phosphatase (RNGTT) or mammalian mRNA capping enzyme (Mce1) in mammals, is a bifunctional enzyme that catalyzes the first two steps of cap formation: (1) by removing the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end using the polynucleotide 5'-phosphatase activity (EC 3.1.3.33) of the N-terminal triphosphatase domain; and (2) by transferring the GMP moiety of GTP to the 5'-diphosphate terminus through the C-terminal mRNA guanylyltransferase domain (EC 2.7.7.50). The enzyme is also referred to as CEL-1 in Caenorhabditis elegans. Pssm-ID: 350502 Cd Length: 167 Bit Score: 316.54 E-value: 1.89e-106
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Adenylation_mRNA_capping | cd07895 | Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP ... |
219-432 | 1.39e-103 | ||||||
Adenylation domain of GTP-dependent mRNA capping enzymes; RNA capping enzymes transfer GMP from GTP to the 5'-diphosphate end of nascent mRNAs to form a G(5')ppp(5')RNA cap structure. The RNA cap is found only in eukarya. RNA capping is chemically analogous to the first two steps of polynucleotide ligation. ATP-dependent polynucleotide ligases catalyze phosphodiester bond formation of nicked nucleic acid substrates using the high energy nucleotide of ATP as a cofactor in a three step reaction mechanism. Structural studies reveal a shared structure for DNA ligases and capping enzymes, with a common catalytic core composed of an adenylation or nucleotidyltransferase domain and a C-terminal OB-fold domain containing conserved sequence motifs. The adenylation domain binds ATP and contains many active site residues. Pssm-ID: 185706 [Multi-domain] Cd Length: 215 Bit Score: 311.10 E-value: 1.39e-103
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mRNA_cap_enzyme | pfam01331 | mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain ... |
243-431 | 2.49e-94 | ||||||
mRNA capping enzyme, catalytic domain; This family represents the ATP binding catalytic domain of the mRNA capping enzyme. Pssm-ID: 396068 [Multi-domain] Cd Length: 194 Bit Score: 286.61 E-value: 2.49e-94
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RNA_5'-triphosphatase | cd14502 | RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes ... |
1-146 | 4.59e-59 | ||||||
RNA 5'-triphosphatase domain; This family of RNA-specific cysteine phosphatases includes baculovirus RNA 5'-triphosphatase, dual specificity protein phosphatase 11 (DUSP11), and the RNA triphosphatase domains of metazoan and plant mRNA capping enzymes. RNA/polynucleotide 5'-triphosphatase (EC 3.1.3.33) catalyzes the removal of the gamma-phosphate from the 5'-triphosphate end of nascent mRNA to yield a diphosphate end. mRNA capping enzyme is a bifunctional enzyme that catalyzes the first two steps of cap formation. DUSP11 has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. Pssm-ID: 350352 [Multi-domain] Cd Length: 167 Bit Score: 194.03 E-value: 4.59e-59
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CEG1 | COG5226 | mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification]; |
239-566 | 2.95e-39 | ||||||
mRNA capping enzyme, guanylyltransferase (alpha) subunit [RNA processing and modification]; Pssm-ID: 227551 [Multi-domain] Cd Length: 404 Bit Score: 148.14 E-value: 2.95e-39
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DSP_DUSP11 | cd17665 | dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar ... |
9-144 | 2.69e-34 | ||||||
dual-specificity phosphatase domain of dual specificity protein phosphatase 11 and similar proteins; dual specificity protein phosphatase 11 (DUSP11), also known as RNA/RNP complex-1-interacting phosphatase or phosphatase that interacts with RNA/RNP complex 1 (PIR1), has RNA 5'-triphosphatase and diphosphatase activity, but only poor protein-tyrosine phosphatase activity. It has activity for short RNAs but is less active toward mononucleotide triphosphates, suggesting that its primary function in vivo is to dephosphorylate RNA 5'-ends. It may play a role in nuclear mRNA metabolism. Also included in this subfamily is baculovirus RNA 5'-triphosphatase for Autographa californica nuclear polyhedrosis virus. Pssm-ID: 350503 Cd Length: 169 Bit Score: 127.78 E-value: 2.69e-34
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mRNA_cap_C | pfam03919 | mRNA capping enzyme, C-terminal domain; |
436-529 | 9.39e-28 | ||||||
mRNA capping enzyme, C-terminal domain; Pssm-ID: 461093 Cd Length: 108 Bit Score: 107.30 E-value: 9.39e-28
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PTP_DSP_cys | cd14494 | cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
68-146 | 2.50e-16 | ||||||
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This superfamily is composed of cys-based phosphatases, which includes classical protein tyrosine phosphatases (PTPs) as well as dual-specificity phosphatases (DUSPs or DSPs). They are characterized by a CxxxxxR conserved catalytic loop (where C is the catalytic cysteine, x is any amino acid, and R is an arginine). PTPs are part of the tyrosine phosphorylation/dephosphorylation regulatory mechanism, and are important in the response of the cells to physiologic and pathologic changes in their environment. DUSPs show more substrate diversity (including RNA and lipids) and include pTyr, pSer, and pThr phosphatases. Pssm-ID: 350344 [Multi-domain] Cd Length: 113 Bit Score: 75.08 E-value: 2.50e-16
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Adenylation_DNA_ligase_like | cd06846 | Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent ... |
255-432 | 1.43e-12 | ||||||
Adenylation domain of proteins similar to ATP-dependent polynucleotide ligases; ATP-dependent polynucleotide ligases catalyze the phosphodiester bond formation of nicked nucleic acid substrates using ATP as a cofactor in a three step reaction mechanism. This family includes ATP-dependent DNA and RNA ligases. DNA ligases play a vital role in the diverse processes of DNA replication, recombination and repair. ATP-dependent DNA ligases have a highly modular architecture, consisting of a unique arrangement of two or more discrete domains, including a DNA-binding domain, an adenylation or nucleotidyltransferase (NTase) domain, and an oligonucleotide/oligosaccharide binding (OB)-fold domain. The adenylation domain binds ATP and contains many active site residues. Together with the C-terminal OB-fold domain, it comprises a catalytic core unit that is common to most members of the ATP-dependent DNA ligase family. The catalytic core contains six conserved sequence motifs (I, III, IIIa, IV, V and VI) that define this family of related nucleotidyltransferases including eukaryotic GRP-dependent mRNA-capping enzymes. The catalytic core contains both the active site as well as many DNA-binding residues. The RNA circularization protein from archaea and bacteria contains the minimal catalytic unit, the adenylation domain, but does not contain an OB-fold domain. This family also includes the m3G-cap binding domain of snurportin, a nuclear import adaptor that binds m3G-capped spliceosomal U small nucleoproteins (snRNPs), but doesn't have enzymatic activity. Pssm-ID: 185704 [Multi-domain] Cd Length: 182 Bit Score: 66.29 E-value: 1.43e-12
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CDC14_C | cd14499 | C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division ... |
3-125 | 2.64e-09 | ||||||
C-terminal dual-specificity phosphatase domain of CDC14 family proteins; The cell division control protein 14 (CDC14) family is highly conserved in all eukaryotes, although the roles of its members seem to have diverged during evolution. Yeast Cdc14, the best characterized member of this family, is a dual-specificity phosphatase that plays key roles in cell cycle control. It preferentially dephosphorylates cyclin-dependent kinase (CDK) targets, which makes it the main antagonist of CDK in the cell. Cdc14 functions at the end of mitosis and it triggers the events that completely eliminates the activity of CDK and other mitotic kinases. It is also involved in coordinating the nuclear division cycle with cytokinesis through the cytokinesis checkpoint, and in chromosome segregation. Cdc14 phosphatases also function in DNA replication, DNA damage checkpoint, and DNA repair. Vertebrates may contain more than one Cdc14 homolog; humans have three (CDC14A, CDC14B, and CDC14C). CDC14 family proteins contain a highly conserved N-terminal pseudophosphatase domain that contributes to substrate specificity and a C-terminal catalytic dual-specificity phosphatase domain with the PTP signature motif. Pssm-ID: 350349 [Multi-domain] Cd Length: 174 Bit Score: 56.69 E-value: 2.64e-09
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PTZ00242 | PTZ00242 | protein tyrosine phosphatase; Provisional |
18-114 | 3.85e-07 | ||||||
protein tyrosine phosphatase; Provisional Pssm-ID: 185524 [Multi-domain] Cd Length: 166 Bit Score: 50.02 E-value: 3.85e-07
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PTP-IVa | cd14500 | protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), ... |
45-122 | 1.09e-05 | ||||||
protein tyrosine phosphatase type IVA family; Protein tyrosine phosphatases type IVA (PTP-IVa), also known as protein-tyrosine phosphatases of regenerating liver (PRLs) constitute a family of small, prenylated phosphatases that are the most oncogenic of all PTPs. They stimulate progression from G1 into S phase during mitosis and enhances cell proliferation, cell motility and invasive activity, and promotes cancer metastasis. They associate with magnesium transporters of the cyclin M (CNNM) family, which results in increased intracellular magnesium levels that promote oncogenic transformation. Vertebrates contain three members: PRL-1, PRL-2, and PRL-3. Pssm-ID: 350350 [Multi-domain] Cd Length: 156 Bit Score: 45.67 E-value: 1.09e-05
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DSPc | pfam00782 | Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ... |
29-132 | 1.15e-05 | ||||||
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The enzyme's tertiary fold is highly similar to that of tyrosine-specific phosphatases, except for a "recognition" region. Pssm-ID: 395632 [Multi-domain] Cd Length: 127 Bit Score: 44.95 E-value: 1.15e-05
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CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
95-132 | 3.70e-05 | ||||||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 43.81 E-value: 3.70e-05
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DSPc | smart00195 | Dual specificity phosphatase, catalytic domain; |
77-132 | 5.69e-05 | ||||||
Dual specificity phosphatase, catalytic domain; Pssm-ID: 214551 [Multi-domain] Cd Length: 138 Bit Score: 43.04 E-value: 5.69e-05
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DUSP23 | cd14504 | dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ... |
69-135 | 1.23e-04 | ||||||
dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as VH1-like phosphatase Z (VHZ) or low molecular mass dual specificity phosphatase 3 (LDP-3), functions as a protein-serine/threonine phosphatase (EC 3.1.3.16) and a protein-tyrosine-phosphatase (EC 3.1.3.48). It deactivates its MAPK substrates by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. DUSP23 is an atypical DUSP; it contains the catalytic dual specificity phosphatase domain but lacks the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. It is able to enhance activation of JNK and p38 MAPK, and has been shown to dephosphorylate p44-ERK1 (MAPK3) in vitro. It has been associated with cell growth and human primary cancers. It has also been identified as a cell-cell adhesion regulatory protein; it promotes the dephosphorylation of beta-catenin at Tyr 142 and enhances the interaction between alpha- and beta-catenin. Pssm-ID: 350354 [Multi-domain] Cd Length: 142 Bit Score: 42.26 E-value: 1.23e-04
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DSP_laforin-like | cd14526 | dual specificity phosphatase domain of laforin and similar domains; This family is composed of ... |
95-137 | 1.91e-04 | ||||||
dual specificity phosphatase domain of laforin and similar domains; This family is composed of glucan phosphatases including vertebrate dual specificity protein phosphatase laforin, also called lafora PTPase (LAFPTPase), and plant starch excess4 (SEX4). Laforin is a glycogen phosphatase; its gene is mutated in Lafora progressive myoclonus epilepsy or Lafora disease (LD), a fatal autosomal recessive neurodegenerative disorder characterized by the presence of progressive neurological deterioration, myoclonus, and epilepsy. One characteristic of LD is the accumulation of insoluble glucans. Laforin prevents LD by at least two mechanisms: by preventing hyperphosphorylation of glycogen by dephosphorylating it, allowing proper glycogen formation, and by promoting the ubiquitination of proteins involved in glycogen metabolism via its interaction with malin. Laforin contains an N-terminal CBM20 (carbohydrate-binding module, family 20) domain and a C-terminal catalytic dual specificity phosphatase (DSP) domain. Plant SEX4 regulate starch metabolism by selectively dephosphorylating glucose moieties within starch glucan chains. It contains an N-terminal catalytic DSP domain and a C-terminal Early (E) set domain. Pssm-ID: 350375 [Multi-domain] Cd Length: 146 Bit Score: 41.80 E-value: 1.91e-04
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TpbA-like | cd14529 | bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ... |
24-147 | 3.15e-04 | ||||||
bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa TpbA; This subfamily contains bacterial protein tyrosine phosphatases (PTPs) and dual-specificity phosphatases (DUSPs) related to Pseudomonas aeruginosa TpbA, a DUSP that negatively regulates biofilm formation by converting extracellular quorum sensing signals and to Mycobacterium tuberculosis PtpB, a PTP virulence factor that attenuates host immune defenses by interfering with signal transduction pathways in macrophages. PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides, while DUSPs function as protein-serine/threonine phosphatases (EC 3.1.3.16) and PTPs. Pssm-ID: 350378 [Multi-domain] Cd Length: 158 Bit Score: 41.59 E-value: 3.15e-04
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DSP | cd14498 | dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in ... |
77-132 | 4.09e-03 | ||||||
dual-specificity phosphatase domain; The dual-specificity phosphatase domain is found in typical and atypical dual-specificity phosphatases (DUSPs), which function as protein-serine/threonine phosphatases (EC 3.1.3.16) and protein-tyrosine-phosphatases (EC 3.1.3.48). Typical DUSPs, also called mitogen-activated protein kinase (MAPK) phosphatases (MKPs), deactivate MAPKs by dephosphorylating the threonine and tyrosine residues in the conserved Thr-Xaa-Tyr motif residing in their activation sites. All MKPs contain an N-terminal Cdc25/rhodanese-like domain, which is responsible for MAPK-binding, and a C-terminal catalytic dual specificity phosphatase domain. Atypical DUSPs contain the catalytic dual specificity phosphatase domain but lack the N-terminal Cdc25/rhodanese-like domain that is present in typical DUSPs or MKPs. Also included in this family are dual specificity phosphatase-like domains of catalytically inactive members such as serine/threonine/tyrosine-interacting protein (STYX) and serine/threonine/tyrosine interacting like 1 (STYXL1), as well as active phosphatases with substrates that are not phosphoproteins such as PTP localized to the mitochondrion 1 (PTPMT1), which is a lipid phosphatase, and laforin, which is a glycogen phosphatase. Pssm-ID: 350348 [Multi-domain] Cd Length: 135 Bit Score: 37.91 E-value: 4.09e-03
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DSP_bac | cd14527 | unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ... |
69-132 | 9.51e-03 | ||||||
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily is composed of uncharacterized bacterial and plant dual-specificity protein phosphatases. DUSPs function as a protein-serine/threonine phosphatases (EC 3.1.3.16) and a protein-tyrosine-phosphatases (EC 3.1.3.48). Pssm-ID: 350376 [Multi-domain] Cd Length: 136 Bit Score: 36.87 E-value: 9.51e-03
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Blast search parameters | ||||
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