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 ...
95-363
7.32e-103
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: 306.95 E-value: 7.32e-103
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
357-435
5.04e-44
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: 148.81 E-value: 5.04e-44
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
95-363
7.32e-103
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: 306.95 E-value: 7.32e-103
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
89-361
8.82e-100
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: 298.91 E-value: 8.82e-100
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
357-435
5.04e-44
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: 148.81 E-value: 5.04e-44
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
95-363
7.32e-103
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: 306.95 E-value: 7.32e-103
Serine/threonine phosphatases, family 2C, catalytic domain; The protein architecture and ...
89-361
8.82e-100
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: 298.91 E-value: 8.82e-100
Protein serine/threonine phosphatase 2C, C-terminal domain; Protein phosphatase 2C (PP2C) is ...
357-435
5.04e-44
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: 148.81 E-value: 5.04e-44
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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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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(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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