serine/threonine-protein phosphatase catalyzes the dephosphorylation of phosphoserine and phosphothreonine residues of specific protein substrates; contains a C-terminal PP2C domain that does not seem to play a role in catalysis, but may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
23-273
2.11e-92
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
:
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 276.90 E-value: 2.11e-92
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
280-351
3.55e-25
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteriztic of mammalian PP2Cs. This domain consists of three antiparallel alpha helices, one of which packs against two corresponding alpha-helices of the N-terminal domain. The C-terminal domain does not seem to play a role in catalysis, but it may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain.
:
Pssm-ID: 429684 Cd Length: 79 Bit Score: 97.19 E-value: 3.55e-25
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
23-273
2.11e-92
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 276.90 E-value: 2.11e-92
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
19-273
1.13e-85
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 214625 [Multi-domain] Cd Length: 252 Bit Score: 259.61 E-value: 1.13e-85
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
280-351
3.55e-25
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteriztic of mammalian PP2Cs. This domain consists of three antiparallel alpha helices, one of which packs against two corresponding alpha-helices of the N-terminal domain. The C-terminal domain does not seem to play a role in catalysis, but it may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain.
Pssm-ID: 429684 Cd Length: 79 Bit Score: 97.19 E-value: 3.55e-25
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
23-273
2.11e-92
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 238083 [Multi-domain] Cd Length: 254 Bit Score: 276.90 E-value: 2.11e-92
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
19-273
1.13e-85
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and deduced catalytic mechanism of PP2C phosphatases are similar to the PP1, PP2A, PP2B family of protein Ser/Thr phosphatases, with which PP2C shares no sequence similarity.
Pssm-ID: 214625 [Multi-domain] Cd Length: 252 Bit Score: 259.61 E-value: 1.13e-85
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
280-351
3.55e-25
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is involved in regulating cellular responses to stress in various eukaryotes. It consists of two domains: an N-terminal catalytic domain and a C-terminal domain characteriztic of mammalian PP2Cs. This domain consists of three antiparallel alpha helices, one of which packs against two corresponding alpha-helices of the N-terminal domain. The C-terminal domain does not seem to play a role in catalysis, but it may provide protein substrate specificity due to the cleft that is created between it and the catalytic domain.
Pssm-ID: 429684 Cd Length: 79 Bit Score: 97.19 E-value: 3.55e-25
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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Functional characterization of the conserved domain architecture found on the query.
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This image shows a graphical summary of conserved domains identified on the query sequence.
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if a domain or superfamily has been annotated with functional sites (conserved features),
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click on the bars or triangles to view your query sequence embedded in a multiple sequence alignment of the proteins used to develop the corresponding domain model.
The table lists conserved domains identified on the query sequence. Click on the plus sign (+) on the left to display full descriptions, alignments, and scores.
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Concise Display shows only the best scoring domain model, in each hit category listed below except non-specific hits, for each region on the query sequence.
(labeled illustration) Standard Display shows only the best scoring domain model from each source, in each hit category listed below for each region on the query sequence.
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Retrieve proteins that contain one or more of the domains present in the query sequence, using the Conserved Domain Architecture Retrieval Tool
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