tyrosine-protein phosphatase [Rhizobium sp. PDO1-076]
protein-tyrosine phosphatase family protein( domain architecture ID 1000023)
cys-based protein-tyrosine phosphatase (PTP) family protein may be a PTP or a dual-specificity phosphatase (DUSP or DSP), and may catalyze the dephosphorylation of target phosphoproteins at tyrosine or tyrosine and serine/threonine residues, respectively
List of domain hits
Name | Accession | Description | Interval | E-value | |||
PTP_DSP_cys super family | cl28904 | cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ... |
53-196 | 2.73e-33 | |||
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. The actual alignment was detected with superfamily member cd14529: Pssm-ID: 475123 [Multi-domain] Cd Length: 158 Bit Score: 116.70 E-value: 2.73e-33
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Name | Accession | Description | Interval | E-value | |||
TpbA-like | cd14529 | bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ... |
53-196 | 2.73e-33 | |||
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: 116.70 E-value: 2.73e-33
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COG3453 | COG3453 | Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ... |
61-172 | 1.28e-14 | |||
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only]; Pssm-ID: 442676 [Multi-domain] Cd Length: 125 Bit Score: 67.55 E-value: 1.28e-14
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Y_phosphatase3 | pfam13350 | Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ... |
59-171 | 6.45e-14 | |||
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families. Pssm-ID: 463853 [Multi-domain] Cd Length: 243 Bit Score: 68.04 E-value: 6.45e-14
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Name | Accession | Description | Interval | E-value | |||
TpbA-like | cd14529 | bacterial protein tyrosine and dual-specificity phosphatases related to Pseudomonas aeruginosa ... |
53-196 | 2.73e-33 | |||
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: 116.70 E-value: 2.73e-33
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COG3453 | COG3453 | Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family ... |
61-172 | 1.28e-14 | |||
Predicted phosphohydrolase, protein tyrosine phosphatase (PTP) superfamily, DUF442 family [General function prediction only]; Pssm-ID: 442676 [Multi-domain] Cd Length: 125 Bit Score: 67.55 E-value: 1.28e-14
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Y_phosphatase3 | pfam13350 | Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 ... |
59-171 | 6.45e-14 | |||
Tyrosine phosphatase family; This family is closely related to the pfam00102 and pfam00782 families. Pssm-ID: 463853 [Multi-domain] Cd Length: 243 Bit Score: 68.04 E-value: 6.45e-14
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Oca4 | COG2365 | Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms]; |
59-171 | 6.48e-14 | |||
Protein tyrosine/serine phosphatase Oca4 [Signal transduction mechanisms]; Pssm-ID: 441932 [Multi-domain] Cd Length: 248 Bit Score: 68.06 E-value: 6.48e-14
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PTP-bact | cd14503 | bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is ... |
82-179 | 6.50e-10 | |||
bacterial tyrosine-protein phosphataseS similar to Neisseria NMA1982; This subfamily is composed of bacterial tyrosine-protein phosphatases similar to Neisseria meningitidis NMA1982, which displays phosphatase activity but whose biological function is still unknown. Pssm-ID: 350353 [Multi-domain] Cd Length: 136 Bit Score: 54.94 E-value: 6.50e-10
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PFA-DSP_unk | cd18538 | unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized ... |
53-172 | 1.89e-08 | |||
unknown subfamily of atypical dual-specificity phosphatases from fungi; This uncharacterized subfamily belongs to the plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) group of atypical DSPs that present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. This unknown subgroup contains the conserved the CxxxxxR catalytic motif present in active cysteine phosphatases. Pssm-ID: 350514 [Multi-domain] Cd Length: 145 Bit Score: 51.22 E-value: 1.89e-08
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BLH_phosphatase | pfam04273 | Beta-lactamase hydrolase-like protein, phosphatase-like domain; This domain is found ... |
83-149 | 2.13e-06 | |||
Beta-lactamase hydrolase-like protein, phosphatase-like domain; This domain is found N-terminal to a beta-lactamase domain, and it may have phosphatase activity. This domain is found in Beta-lactamase hydrolase-like protein from Agrobacterium fabrum, which may play a role in cell adherence or biofilm development. Pssm-ID: 398110 [Multi-domain] Cd Length: 110 Bit Score: 44.97 E-value: 2.13e-06
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CDC14 | COG2453 | Protein-tyrosine phosphatase [Signal transduction mechanisms]; |
55-156 | 3.03e-05 | |||
Protein-tyrosine phosphatase [Signal transduction mechanisms]; Pssm-ID: 441989 [Multi-domain] Cd Length: 140 Bit Score: 42.27 E-value: 3.03e-05
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PTP_PTPDC1 | cd14506 | protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine ... |
77-156 | 9.81e-05 | |||
protein tyrosine phosphatase domain of PTP domain-containing protein 1; protein tyrosine phosphatase domain-containing protein 1 (PTPDC1) is an uncharacterized non-receptor class protein-tyrosine phosphatase (PTP). PTPs (EC 3.1.3.48) catalyze the dephosphorylation of phosphotyrosine peptides. Small interfering RNA (siRNA) knockdown of the ptpdc1 gene is associated with elongated cilia. Pssm-ID: 350356 [Multi-domain] Cd Length: 206 Bit Score: 41.57 E-value: 9.81e-05
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PFA-DSP | cd14501 | plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical ... |
53-155 | 2.52e-04 | |||
plant and fungi atypical dual-specificity phosphatase; Plant and fungi atypical dual-specificity phosphatases (PFA-DSPs) are a group of atypical DSPs present in plants, fungi, kinetoplastids, and slime molds. They share structural similarity with atypical- and lipid phosphatase DSPs from mammals. The PFA-DSP group is composed of active as well as inactive phosphatases. The best characterized member is Saccharomyces Siw14, also known as Oca3, which plays a role in actin filament organization and endocytosis. Siw14 has been shown to be an inositol pyrophosphate phosphatase, hydrolyzing the beta-phosphate from 5-diphosphoinositol pentakisphosphate (5PP-IP5or IP7). Pssm-ID: 350351 [Multi-domain] Cd Length: 149 Bit Score: 39.97 E-value: 2.52e-04
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PTP_paladin_2 | cd17660 | protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative ... |
32-159 | 2.37e-03 | |||
protein tyrosine phosphatase-like domain of paladin, repeat 2; Paladin is a putative phosphatase, which in mouse is expressed in endothelial cells during embryonic development and in arterial smooth muscle cells in adults. It has been suggested to be an antiphosphatase that regulates the activity of specific neural crest regulatory factors and thus, modulates neural crest cell formation and migration. Paladin contains two tyrosine-protein phosphatase domains. This model represents repeat 2. Pssm-ID: 350498 Cd Length: 216 Bit Score: 37.84 E-value: 2.37e-03
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DUSP23 | cd14504 | dual specificity phosphatase 23; Dual specificity phosphatase 23 (DUSP23), also known as ... |
82-155 | 6.47e-03 | |||
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: 35.72 E-value: 6.47e-03
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Blast search parameters | ||||
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