bifunctional phosphatase PAP2/dual specificity phosphatase (DSP) family protein containing a C-terminal DSP domain that may dephosphorylate phosphotyrosine, phosphoserine, and phosphothreonine residues in target proteins, and an N-terminal phosphatase PAP2 domain that may be a histidine phosphatase that catalyzes the dephosphorylation of phospholipids
cys-based protein tyrosine phosphatase and dual-specificity phosphatase superfamily; This ...
308-439
2.51e-28
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 cd14527:
Pssm-ID: 475123 [Multi-domain] Cd Length: 136 Bit Score: 108.52 E-value: 2.51e-28
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
53-205
8.20e-24
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.
:
Pssm-ID: 239481 Cd Length: 186 Bit Score: 97.77 E-value: 8.20e-24
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
308-439
2.51e-28
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: 108.52 E-value: 2.51e-28
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
53-205
8.20e-24
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.
Pssm-ID: 239481 Cd Length: 186 Bit Score: 97.77 E-value: 8.20e-24
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
372-410
1.36e-04
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: 41.48 E-value: 1.36e-04
unknown subfamily of bacterial and plant dual specificity protein phosphatases; This subfamily ...
308-439
2.51e-28
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: 108.52 E-value: 2.51e-28
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of ...
53-205
8.20e-24
PAP2_like proteins, Aur1_like subfamily. Yeast Aur1p or Ipc1p is necessary for the addition of inositol phosphate to ceramide, an essential step in yeast sphingolipid synthesis, and is the target of several antifungal compounds such as aureobasidin.
Pssm-ID: 239481 Cd Length: 186 Bit Score: 97.77 E-value: 8.20e-24
Dual specificity phosphatase, catalytic domain; Ser/Thr and Tyr protein phosphatases. The ...
372-410
1.36e-04
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: 41.48 E-value: 1.36e-04
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, ...
122-203
2.18e-04
PAP2_like proteins, a super-family of histidine phosphatases and vanadium haloperoxidases, includes type 2 phosphatidic acid phosphatase or lipid phosphate phosphatase (LPP), Glucose-6-phosphatase, Phosphatidylglycerophosphatase B and bacterial acid phosphatase, vanadium chloroperoxidases, vanadium bromoperoxidases, and several other mostly uncharacterized subfamilies. Several members of this superfamily have been predicted to be transmembrane proteins.
Pssm-ID: 238813 [Multi-domain] Cd Length: 122 Bit Score: 40.91 E-value: 2.18e-04
Database: CDSEARCH/cdd Low complexity filter: no Composition Based Adjustment: yes E-value threshold: 0.01
References:
Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
of the residues that compose this conserved feature have been mapped to the query sequence.
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