1FJM,1JK7,3E7A,1S70,3E7B,3EGG,4G9J,3V4Y,2O8A,3N5U,1U32


Conserved Protein Domain Family
MPP_PP1_PPKL

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cd07414: MPP_PP1_PPKL 
Click on image for an interactive view with Cn3D
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain
PP1 (protein phosphatase type 1) is a serine/threonine phosphatase that regulates many cellular processes including: cell-cycle progression, protein synthesis, muscle contraction, carbohydrate metabolism, transcription and neuronal signaling, through its interaction with at least 180 known targeting proteins. PP1 occurs in all tissues and regulates many pathways, ranging from cell-cycle progression to carbohydrate metabolism. Also included here are the PPKL (PP1 and kelch-like) enzymes including the PPQ, PPZ1, and PPZ2 fungal phosphatases. These PPKLs have a large N-terminal kelch repeat in addition to a C-terminal phosphoesterase domain. The PPP (phosphoprotein phosphatase) family, to which PP1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Statistics
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PSSM-Id: 277359
Aligned: 45 rows
Threshold Bit Score: 563.502
Created: 18-Oct-2006
Updated: 2-Oct-2020
Structure
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Program:
Drawing:
Aligned Rows:
 
Conserved site includes 23 residues -Click on image for an interactive view with Cn3D
Feature 1:active site [active site]
Evidence:
  • Structure:1FJM_A; Oryctolagus cuniculus PP1 binds two Mn2+ ions and microcystin-Lr toxin.
  • Citation:PMID 7651533
  • Structure:3E7A_A; Homo sapiens PP1 binds binds two Mn2+ ions and nodularin-R toxin.

Sequence Alignment
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Format: Row Display: Color Bits: Type Selection:
Feature 1                                                                      # #               
1FJM_A         8 NLDSIIGRLLEVQgsr------pgKNVQLTENEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGF 81  Oryctolagus cun...
NP_586372      7 DLDTIIEKLLSVRnsk------lgRLVHLAEAEMRYLCEKSTDVFKQQPTLVEVKAPVKICGDVHGQYYDLLKLFEHGGF 80  Encephalitozoon...
XP_001421196   6 DVDSVIERLLSVRgqp------nnRTVQLAEGEIRALCAAAREIFLAQPCLLELEAPLKICGDVHGQYSDLLRLFEYGGF 79  Ostreococcus lu...
AAD38856       5 QVDEIIERLLDVRngr------pgKQVQLAENEIRLLCLTAKEIFMSQPNLLELEAPIKICGDIHGQYSDLLRLFEYGGF 78  Chlamydomonas r...
ACN39808       5 VLDDVIGRLLEVRgsk------pgKQVQLLEAEVRQLCILSKDIFMKQPNLLELEAPVKICGDVHGQYSDLLRLFEYGGL 78  Sitka spruce
XP_001712382  16 FLDSIILKLIPKKnkt------ikKYIQLTEKEIQFLNIECRKILCKQEIFLELKAPIKVCGDIHGQYYDLLRLFEFEGY 89  Hemiselmis ande...
CAA53214     239 DIDVAIEKLLQVGesreitktskkKNFPFHSWEIQLICYHAREIFLNQPTLLRLQAPIKVVGDVHGQFNDLLRILKLSGV 318 baker's yeast
AAB64859     397 DIDEIIQRLLDAGyaa-----krtKNVCLKNSEIIQICHKARELFLAQPALLELSPSVKIVGDVHGQYADLLRLFTKCGF 471 baker's yeast
P32945       239 DIDVAIEKLLQVGesreitktskkKNFPFHSWEIQLICYHAREIFLNQPTLLRLQAPIKVVGDVHGQFNDLLRILKLSGV 318 Saccharomyces c...
P23734        44 AFQSAQTQESTPKtngt----graTTEGLTEAEVRWLVMESRALFMSQPMLVEIAAPVRICGDVHGQYTDLLRLFDLGGF 119 Trypanosoma bru...
Feature 1                  #   #                           ##   ##   #                           
1FJM_A        82 PPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYniKLWKTFTDCFNCLPI 161 Oryctolagus cun...
NP_586372     81 PPSSNYLFLGDYVDRGKQSLETICLLLAYKIKFPNNFFLLRGNHECASINRIYGFYDECKRRYdtTVWKMFTECFNWIPV 160 Encephalitozoon...
XP_001421196  80 PPEANYLFLGDYVDRGKQGLEVICLLLAYKVKYPENFFLLRGNHECNSISRIYGFYDECKRRYniKLWRVFCDVFNCLPF 159 Ostreococcus lu...
AAD38856      79 PPEANYLFLGDYVDRGKQSLETICLLLSFKIKYPENFFLLRGNHECASINRIYGFYDECKRRYniRLWRTFTDCFNCLPV 158 Chlamydomonas r...
ACN39808      79 PPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRFnvRLWKLFTDCFNCLPV 158 Sitka spruce
XP_001712382  90 PPDSNYLFLGDYVDRGKQSIETISLMFAFKIRYPLGFFILRGNHESAMINRLYGFFDECRRRYsvKIWKLFCETFNYLPI 169 Hemiselmis ande...
CAA53214     319 PSDTNYLFLGDYVDRGKNSLETILLLLCYKIKYKDNFFMLRGNHESANVTKMYGFYDECKRRLssKVWKMFVDVFNTLPL 398 baker's yeast
AAB64859     472 PPMANYLFLGDYVDRGKQSLETILLLLCYKIKYPENFFLLRGNHECANVTRVYGFYDECKRRCniKIWKTFVDTFNTLPL 551 baker's yeast
P32945       319 PSDTNYLFLGDYVDRGKNSLETILLLLCYKIKYKDNFFMLRGNHESANVTKMYGFYDECKRRLssKVWKMFVDVFNTLPL 398 Saccharomyces c...
P23734       120 PPDANYIFLGDYVDRGDQSLETICLLLAYKLSFPETFFLLRGNHECSSINRIYGFFDECKRRYsvRLWKQFTDTFNCMPV 199 Trypanosoma bru...
Feature 1                   #                     ###        #              ###                  
1FJM_A       162 AAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkd-vqGWGENDRGVSFTFGAEVVAKFLHKHD 240 Oryctolagus cun...
NP_586372    161 CALVDGRILCMHGGISPDLKSMDQIKGIARPTDVPDEGLLCDLLWSDPDps-vrGWGENDRGVSVTFGPDTVERFLEAHN 239 Encephalitozoon...
XP_001421196 160 AAIVDEKIFCIHGGPSPELKDLQQIVQIKRPTDIPDMGMLCDFLWSDPDad-iqGWGENDRGVSYTYGTDVVGDFLHKFD 238 Ostreococcus lu...
AAD38856     159 AALIDEKILCMHGGLSPELKSLEQIKRITRPTDVPDSGLLCDLLWADPDkd-iqGWGENDRGVSYTFGPDCVTEFLQKHD 237 Chlamydomonas r...
ACN39808     159 AALIDEKILCMHGGLSPELNSLDQIRNIPRPTDVPDQGLLCDLLWSDPSne-iqGWGSNDRGVSYTFGPDKVSDFLQKLD 237 Sitka spruce
XP_001712382 170 AATIGGKIFCSHGGISPELSSFQQIKSIKRPTEIPDQGLICDLLWSDPEen-ikGWKKNDRGISFVFGKDVVFDFLKKFK 248 Hemiselmis ande...
CAA53214     399 AAIIQDKIFCVHGGISPDLHDMKQIEKVARPTDIPESGLVTDLLWSDPDpq-vtDWSENDRGVSYTFSKRNVLDFCAKFK 477 baker's yeast
AAB64859     552 AAIVTGKIFCVHGGLSPVLNSMDEIRHVSRPTDVPDFGLINDLLWSDPTds-snEWEDNERGVSFCYNKVAINKFLNKFG 630 baker's yeast
P32945       399 AAIIQDKIFCVHGGISPDLHDMKQIEKVARPTDIPESGLVTDLLWSDPDpq-vtDWSENDRGVSYTFSKRNVLDFCAKFK 477 Saccharomyces c...
P23734       200 AGLVEGRILCMHGGLSPELTDLDQIRRILRPTDVPDSGLICDLLWSDPStnmesNWSENDRGVSWTFSESVVKSFNKKFD 279 Trypanosoma bru...
Feature 1               #                       #####                      
1FJM_A       241 LDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 298 Oryctolagus cuniculus
NP_586372    240 LDLICRAHQVVEDGYEFFANRSLVTVFSAPNYCGEFENSGAIMDVDKDLVCSFQVLKP 297 Encephalitozoon cuniculi GB-M1
XP_001421196 239 FDLVVRAHQVVENGYEFFGKRQLVTVFSAPNYCGEFDNAGAMMTVDENLMCSFQILKP 296 Ostreococcus lucimarinus CCE9901
AAD38856     238 LDLVCRAHQVVEEGYEFFAKRQLVTIFSAPNYCGEFENAGAMMSVDETLMCSFQILKP 295 Chlamydomonas reinhardtii
ACN39808     238 LDLICRAHQVVEDGYQFFADRQLVTVFSAPNYCGEFDNAGAMMSVDQSLMCSFQILKP 295 Sitka spruce
XP_001712382 249 LDLICRAHQVIENGYQFFGSRGLVTVFSAPNYCGEFNNAGAVMIVKENFLCGFRILKP 306 Hemiselmis andersenii
CAA53214     478 FDLILRGHMVVEDGYEFFARKKFVTIFSAPNYCGEFHNWGAVMSVTTGMMCSFELLKP 535 baker's yeast
AAB64859     631 FDLVCRAHMVVEDGYEFFNDRSLVTVFSAPNYCGEFDNWGAVMTVSEGLLCSFELLDP 688 baker's yeast
P32945       478 FDLILRGHMVVEDGYEFFARKKFVTIFSAPNYCGEFHNWGAVMSVTTGMMCSFELLKP 535 Saccharomyces cerevisiae S288c
P23734       280 LDLICRAHQVVDAGYEFFAARQLVTVFSAPNYCDEFDNAGAFMCVDENLMCSFVQIEP 337 Trypanosoma brucei TREU927

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