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Conserved domains on  [gi|1972227248|ref|NP_001380043|]
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Serine/threonine-protein phosphatase [Caenorhabditis elegans]

Protein Classification

serine/threonine protein phosphatase( domain architecture ID 12191156)

protein phosphatase specific for serine and threonine, similar to Methanosarcina thermophila serine/threonine-protein phosphatase PP1-arch2 and Caenorhabditis elegans putative serine/threonine-protein phosphatase C23G10.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 2-254 2.34e-102

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


:

Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 300.67  E-value: 2.34e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248    2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:smart00156  14 KEIFRQEPNLVEVS-APVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   82 RGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:smart00156  93 RGNHESRSMNEIYGFYDEC----KRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  162 YGLACDLLWSDPAQPErNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQlfkeMYPQGCVLRFGGRLISLFSALNY 241
Cdd:smart00156 169 DGLLIDLLWSDPDQPV-NGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQ----VVDDGYEFFADGKLVTIFSAPNY 243

                          250
                   ....*....|....
gi 1972227248  242 EGHKNNS-SVLKLE 254
Cdd:smart00156 244 CDRFGNKaAVLKVD 257
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 2-254 2.34e-102

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 300.67  E-value: 2.34e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248    2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:smart00156  14 KEIFRQEPNLVEVS-APVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   82 RGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:smart00156  93 RGNHESRSMNEIYGFYDEC----KRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  162 YGLACDLLWSDPAQPErNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQlfkeMYPQGCVLRFGGRLISLFSALNY 241
Cdd:smart00156 169 DGLLIDLLWSDPDQPV-NGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQ----VVDDGYEFFADGKLVTIFSAPNY 243

                          250
                   ....*....|....
gi 1972227248  242 EGHKNNS-SVLKLE 254
Cdd:smart00156 244 CDRFGNKaAVLKVD 257
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 2-248 1.36e-96

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.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 286.54  E-value: 1.36e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:cd07414    36 REIFLSQPILLELE-APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  82 RGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:cd07414   115 RGNHECASINRIYGFYDEC----KRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 162 YGLACDLLWSDPaQPERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvlRFGGR-LISLFSALN 240
Cdd:cd07414   191 QGLLCDLLWSDP-DKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYE-----FFAKRqLVTLFSAPN 264


                  ....*...
gi 1972227248 241 YEGHKNNS 248
Cdd:cd07414   265 YCGEFDNA 272
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 2-251 5.75e-72

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 224.92  E-value: 5.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:PTZ00480   45 RDIFISQPILLELE-APLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  82 RGNHEDVNTTLNYGFYDECLEQWKndegEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:PTZ00480  124 RGNHECASINRIYGFYDECKRRYT----IKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 162 YGLACDLLWSDPAQpERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvlRFGGR-LISLFSALN 240
Cdd:PTZ00480  200 TGLLCDLLWSDPDK-DVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYE-----FFSKRqLVTLFSAPN 273

                         250
                  ....*....|.
gi 1972227248 241 YEGHKNNSSVL 251
Cdd:PTZ00480  274 YCGEFDNAGSM 284
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 18-131 2.87e-16

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 73.40  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  18 PITVVADMH--GQSIHLLRIFlTNEAPPNQKYLFL--GDYVDRGSQSVVVMcLLFCMKHRYpQHVFLLRGNHEDvnttln 93
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELL-KKLLEEGKPDLVLhaGDLVDRGPPSEEVL-ELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1972227248  94 ygFYDECLEQWKNDEG-EKVWRMFIDTFNCMPLAAVIGG 131
Cdd:pfam00149  73 --DYGECLRLYPYLGLlARPWKRFLEVFNFLPLAGILSG 109
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 2-254 2.34e-102

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547 [Multi-domain]  Cd Length: 271  Bit Score: 300.67  E-value: 2.34e-102
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248    2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:smart00156  14 KEIFRQEPNLVEVS-APVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLL 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   82 RGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:smart00156  93 RGNHESRSMNEIYGFYDEC----KRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  162 YGLACDLLWSDPAQPErNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQlfkeMYPQGCVLRFGGRLISLFSALNY 241
Cdd:smart00156 169 DGLLIDLLWSDPDQPV-NGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQ----VVDDGYEFFADGKLVTIFSAPNY 243

                          250
                   ....*....|....
gi 1972227248  242 EGHKNNS-SVLKLE 254
Cdd:smart00156 244 CDRFGNKaAVLKVD 257
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 2-248 1.36e-96

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.


Pssm-ID: 277359 [Multi-domain]  Cd Length: 291  Bit Score: 286.54  E-value: 1.36e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:cd07414    36 REIFLSQPILLELE-APLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  82 RGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:cd07414   115 RGNHECASINRIYGFYDEC----KRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 162 YGLACDLLWSDPaQPERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvlRFGGR-LISLFSALN 240
Cdd:cd07414   191 QGLLCDLLWSDP-DKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYE-----FFAKRqLVTLFSAPN 264


                  ....*...
gi 1972227248 241 YEGHKNNS 248
Cdd:cd07414   265 YCGEFDNA 272
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 1-241 7.94e-92

PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of phosphoprotein phosphatases (PPP's) including PP4 and PP6. PP2A (Protein phosphatase 2A) is a critical regulator of many cellular activities. PP2A comprises about 1% of total cellular proteins. PP2A, together with protein phosphatase 1 (PP1), accounts for more than 90% of all serine/threonine phosphatase activities in most cells and tissues. The PP2A subunit in addition to having a catalytic domain homologous to PP1, has a unique C-terminal tail, containing a motif that is conserved in the catalytic subunits of all PP2A-like phosphatases including PP4 and PP6, and has an important role in PP2A regulation. The PP2A-like family of phosphatases all share a similar heterotrimeric architecture, that includes: a 65kDa scaffolding subunit (A), a 36kDa catalytic subunit (C), and one of 18 regulatory subunits (B). The PPP (phosphoprotein phosphatase) family, to which PP2A belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, 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.


Pssm-ID: 277360 [Multi-domain]  Cd Length: 285  Bit Score: 274.46  E-value: 7.94e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   1 MKKAFLEQPALLEISNePITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFL 80
Cdd:cd07415    27 AKEILVKESNVQRVRS-PVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  81 LRGNHEDVNTTLNYGFYDECLEQWKNdegEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVP 160
Cdd:cd07415   106 LRGNHESRQITQVYGFYDECLRKYGN---ANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVP 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 161 PYGLACDLLWSDPAqpERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEmypqGCVLRFGGRLISLFSALN 240
Cdd:cd07415   183 HEGPMCDLLWSDPD--DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVME----GYQWMFNNKLVTVWSAPN 256


                  .
gi 1972227248 241 Y 241
Cdd:cd07415   257 Y 257
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 20-253 1.42e-82

phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; The PPP (phosphoprotein phosphatase) family is one of two known protein phosphatase families specific for serine and threonine. This family includes: PP1, 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.


Pssm-ID: 277316 [Multi-domain]  Cd Length: 229  Bit Score: 248.83  E-value: 1.42e-82
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  20 TVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLLRGNHEDVNTTLNYGFYDE 99
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 100 CLEQWKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIeRPLVVPPYGLACDLLWSDPAQPErN 179
Cdd:cd00144    81 RTLRCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESV-G 158

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1972227248 180 GWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYpqgcVLRFGGRLISLFSALNYEGHKNNS-SVLKL 253
Cdd:cd00144   159 DFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGY----EFLHGGKLITIFSAPNYCGKGGNKlAALVV 229
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 2-251 5.75e-72

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 224.92  E-value: 5.75e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:PTZ00480   45 RDIFISQPILLELE-APLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLL 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  82 RGNHEDVNTTLNYGFYDECLEQWKndegEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:PTZ00480  124 RGNHECASINRIYGFYDECKRRYT----IKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPD 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 162 YGLACDLLWSDPAQpERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvlRFGGR-LISLFSALN 240
Cdd:PTZ00480  200 TGLLCDLLWSDPDK-DVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYE-----FFSKRqLVTLFSAPN 273

                         250
                  ....*....|.
gi 1972227248 241 YEGHKNNSSVL 251
Cdd:PTZ00480  274 YCGEFDNAGSM 284
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 2-254 6.92e-72

PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein phosphatase in its regulation by a second messenger (calcium and calmodulin). PP2B is involved in many biological processes including immune responses, the second messenger cAMP pathway, sodium/potassium ion transport in the nephron, cell cycle progression in lower eukaryotes, cardiac hypertrophy, and memory formation. PP2B is highly conserved from yeast to humans, but is absent from plants. PP2B is a heterodimer consisting of a catalytic subunit (CnA) and a regulatory subunit (CnB); CnB contains four Ca2+ binding motifs referred to as EF hands. The PPP (phosphoprotein phosphatase) family, to which PP2B belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, 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.


Pssm-ID: 277361 [Multi-domain]  Cd Length: 305  Bit Score: 224.11  E-value: 6.92e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEIsNEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:cd07416    29 AEILRQEPNLLRI-EAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  82 RGNHEDVNTTLNYGFYDECLEQWkndeGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:cd07416   108 RGNHECRHLTEYFTFKQECKIKY----SERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPS 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 162 YGLACDLLWSDPAQPERNGWGLSH------RGISFTYGKSVVEEFCAKNDIALVIRGHQLFKE---MYPQGCVLRFGGrL 232
Cdd:cd07416   184 YGPMCDLLWSDPLEDFGNEKTQEHfvhntvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAgyrMYRKSQTTGFPS-L 262

                         250       260
                  ....*....|....*....|...
gi 1972227248 233 ISLFSALNYEGHKNN-SSVLKLE 254
Cdd:cd07416   263 ITIFSAPNYLDVYNNkAAVLKYE 285
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 1-254 4.81e-69

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 216.70  E-value: 4.81e-69
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   1 MKKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFL 80
Cdd:PTZ00244   37 VREIFMSQPMLLEIR-PPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  81 LRGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVP 160
Cdd:PTZ00244  116 LRGNHECASINKMYGFFDDV----KRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVP 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 161 PYGLACDLLWSDPaQPERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMYPqgcvlRFGGR-LISLFSAL 239
Cdd:PTZ00244  192 DRGILCDLLWADP-EDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYG-----FFASRqLVTVFSAP 265

                         250
                  ....*....|....*.
gi 1972227248 240 NYEGH-KNNSSVLKLE 254
Cdd:PTZ00244  266 NYCGEfDNDAAVMNID 281
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 1-241 2.27e-65

PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a member of the PPP gene family of protein phosphatases that is highly conserved among eukaryotes and widely expressed in mammalian tissues. PP5 has a C-terminal phosphatase domain and an extended N-terminal TPR (tetratricopeptide repeat) domain containing three TPR motifs. The PPP (phosphoprotein phosphatase) family, to which PP5 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, 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.


Pssm-ID: 277362 [Multi-domain]  Cd Length: 316  Bit Score: 207.88  E-value: 2.27e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   1 MKKAFLEQPALLEISNEP---ITVVADMHGQSIHLLRIFLTNEAP-PNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQ 76
Cdd:cd07417    41 VKEILKKLPSLVEITIPEgekITVCGDTHGQFYDLLNIFELNGLPsETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPN 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  77 HVFLLRGNHEDVNTTLNYGFYDECleqwKNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGispwLES-----LEDIN 151
Cdd:cd07417   121 HFHLNRGNHETDNMNKIYGFEGEV----KAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGG----LFSddgvtLDDIR 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 152 SIERPLVVPPYGLACDLLWSDPaQPeRNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHqlfkEMYPQGCVLRFGGR 231
Cdd:cd07417   193 KIDRFRQPPDSGLMCELLWSDP-QP-QPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSH----EVKDEGYEVEHDGK 266

                         250
                  ....*....|
gi 1972227248 232 LISLFSALNY 241
Cdd:cd07417   267 CITVFSAPNY 276
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 2-254 1.06e-64

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 205.82  E-value: 1.06e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEISnEPITVVADMHGQSIHLLRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLL 81
Cdd:PTZ00239   29 KEIFLEESNVQPVR-APVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLL 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  82 RGNHEDVNTTLNYGFYDECLEQWKNdegEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIERPLVVPP 161
Cdd:PTZ00239  108 RGNHESRQCTQVYGFYEEILRKYGN---SNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPH 184

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 162 YGLACDLLWSDPAQPERngWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQLFKEMY----PQgcvlrfgGRLISLFS 237
Cdd:PTZ00239  185 EGPFCDLMWSDPEEVEY--WAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYkywfPD-------QNLVTVWS 255

                         250
                  ....*....|....*...
gi 1972227248 238 ALNYEGHKNN-SSVLKLE 254
Cdd:PTZ00239  256 APNYCYRCGNiASILCLD 273
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 5-253 1.59e-63

Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase domain; Bsu1 encodes a nuclear serine-threonine protein phosphatase found in plants and protozoans. Bsu1 has a C-terminal phosphatase domain and an N-terminal Kelch-repeat domain. Bsu1 is preferentially expressed in elongating plant cells. It modulates the phosphorylation state of Bes1, a transcriptional regulator phosphorylated by the glycogen synthase kinase Bin2, as part of a steroid hormone signal transduction pathway. The PPP (phosphoprotein phosphatase) family, to which Bsu1 belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, 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.


Pssm-ID: 277363 [Multi-domain]  Cd Length: 311  Bit Score: 203.06  E-value: 1.59e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   5 FLEQPALLEIsNEPITVVADMHGQSIHLLRIFLTNEAPPNQK--------YLFLGDYVDRGSQSVVVMCLLFCMKHRYPQ 76
Cdd:cd07419    37 FRQEPSVLRL-RAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPN 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  77 HVFLLRGNHEDVNTTLNYGFYDECLEQWKND--EGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPWLESLEDINSIE 154
Cdd:cd07419   116 QIHLIRGNHEAADINALFGFREECIERLGEDirDGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLK 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 155 RPLVVPPYG-LACDLLWSDPAQP------ERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHQlfkemypqgCVL- 226
Cdd:cd07419   196 RPITMEAGSpVVMDLLWSDPTENdsvlglRPNAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIRAHE---------CVMd 266

                         250       260       270
                  ....*....|....*....|....*....|..
gi 1972227248 227 ---RF-GGRLISLFSALNYEG-HKNNSSVLKL 253
Cdd:cd07419   267 gfeRFaQGHLITLFSATNYCGtAGNAGAILVL 298
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 2-253 3.97e-46

Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal degeneration C) is a vertebrate serine-threonine protein phosphatase that is required to prevent light-induced retinal degeneration. In addition to its catalytic domain, RdgC has two C-terminal EF hands. Homologs of RdgC include the human phosphatases protein phosphatase with EF hands 1 and -2 (PPEF-1 and -2). PPEF-1 transcripts are present at low levels in the retina, PPEF-2 transcripts and PPEF-2 protein are present at high levels in photoreceptors. The PPP (phosphoprotein phosphatase) family, to which RdgC belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, 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.


Pssm-ID: 277364 [Multi-domain]  Cd Length: 297  Bit Score: 157.57  E-value: 3.97e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   2 KKAFLEQPALLEISNEP---ITVVADMHGQSIHLLRIFLTNEAP-PNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQH 77
Cdd:cd07420    33 RKSLKQLPNISRVSTSYskeVTICGDLHGKLDDLLLIFYKNGLPsPENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNA 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  78 VFLLRGNHEDVNTTLNYGFYDECLEQWKnDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGISPwLESLEDINSIERPL 157
Cdd:cd07420   113 VHLNRGNHEDHIMNLRYGFTKEVMQKYK-DHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGISD-STDLDLLDKIDRHK 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 158 VVP---PYGLACDLLWSDPaQPERNGWGLSHRGISFTYGKSVVEEFCAKNDIALVIRGHqlfkEMYPQGCVLRFGGRLIS 234
Cdd:cd07420   191 YVStktEWQQVVDILWSDP-KATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSH----ECKPEGYEFCHNNKVIT 265

                         250       260
                  ....*....|....*....|
gi 1972227248 235 LFSALN-YEGHKNNSSVLKL 253
Cdd:cd07420   266 IFSASNyYEEGSNRGAYVKL 285
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 8-254 1.59e-40

PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly expressed in a subset of stomata and thought to play an important role in sensory signaling. PP7 acts as a positive regulator of signaling downstream of cryptochrome blue light photoreceptors. PP7 also controls amplification of phytochrome signaling, and interacts with nucleotidediphosphate kinase 2 (NDPK2), a positive regulator of phytochrome signalling. In addition, PP7 interacts with heat shock transcription factor HSF and up-regulates protective heat shock proteins. PP7 may also play a role in salicylic acid-dependent defense signaling. The PPP (phosphoprotein phosphatase) family, to which PP7 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, 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.


Pssm-ID: 163661 [Multi-domain]  Cd Length: 377  Bit Score: 144.94  E-value: 1.59e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248   8 QPALLEI---SNEPITVVADMHGQSIHLLRIFLTNEAP-PNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQHVFLLRG 83
Cdd:cd07418    54 EPNCVRIdveDVCEVVVVGDVHGQLHDVLFLLEDAGFPdQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRG 133

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  84 NHEDVNTTLNYGFYDECLEQWkNDEGEKVWRMFIDTFNCMPLAAVIGGKVFCAHGGI----------------------- 140
Cdd:cd07418   134 NHESKFCTSMYGFEQEVLTKY-GDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvllle 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 141 ----SPWLESLEDINSIERPLVVPPYG----LACDLLWSDPAQPErngwGLSH---RGISFTYGKSVVEEFCAKNDIALV 209
Cdd:cd07418   213 peseSLKLGTLDDLMKARRSVLDPPGEgsnlIPGDVLWSDPSLTP----GLSPnkqRGIGLLWGPDCTEEFLEKNNLKLI 288

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972227248 210 IRGHQL--FKEMYPQGCVLRFG---------GRLISLFSALNY-------EGHKNNSSVLKLE 254
Cdd:cd07418   289 IRSHEGpdAREKRPGLAGMNKGytvdhdvesGKLITLFSAPDYpqfqateERYNNKGAYIILQ 351
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 18-131 2.87e-16

Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, including protein phosphoserine phosphatases, nucleotidases, sphingomyelin phosphodiesterases and 2'-3' cAMP phosphodiesterases as well as nucleases such as bacterial SbcD or yeast MRE11. The most conserved regions in this superfamily centre around the metal chelating residues.


Pssm-ID: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 73.40  E-value: 2.87e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  18 PITVVADMH--GQSIHLLRIFlTNEAPPNQKYLFL--GDYVDRGSQSVVVMcLLFCMKHRYpQHVFLLRGNHEDvnttln 93
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELL-KKLLEEGKPDLVLhaGDLVDRGPPSEEVL-ELLERLIKY-VPVYLVRGNHDF------ 72

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1972227248  94 ygFYDECLEQWKNDEG-EKVWRMFIDTFNCMPLAAVIGG 131
Cdd:pfam00149  73 --DYGECLRLYPYLGLlARPWKRFLEVFNFLPLAGILSG 109
PHA02239 PHA02239
putative protein phosphatase
 19-87 2.99e-08

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 53.46  E-value: 2.99e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1972227248  19 ITVVADMHGQSIHLLRIF--LTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRyPQHVFLLRGNHED 87
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMdkINNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHDD 72
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 42-267 7.29e-07

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, 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.


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 49.44  E-value: 7.29e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  42 PPNQKYLFLGDYVDRGSQSVVVMCLLfcMKHRYPQHVFLLRGNHED--------VNTTLNYGFyDECLEQWKN---DEGE 110
Cdd:cd07423    33 PEGRKLVFLGDLVDRGPDSIDVLRLV--MNMVKAGKALYVPGNHCNklyrylkgRNVQLAHGL-ETTVEELEAlskEERP 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 111 KVWRMFIDTFNCMPLAAVI-GGKVFCAHGGISPwleslEDI----NSIeRPLV--------VPPYGLacdllwsdpaqPE 177
Cdd:cd07423   110 EFRERFAEFLESLPSHLVLdGGRLVVAHAGIKE-----EMIgrgsKRV-RDFClygdttgeTDEDGL-----------PV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 178 RNGWGLSHRGisftygksvveefcakndIALVIRGHQLFKEmyP----------QGCVlrFGGRLislfSALNY-Eghkn 246
Cdd:cd07423   173 RRDWAKDYRG------------------KALVVYGHTPVPE--PrwlnntinidTGCV--FGGKL----TALRYpE---- 222

                         250       260
                  ....*....|....*....|.
gi 1972227248 247 nssvlkLEFVGqrVKVKQVLY 267
Cdd:cd07423   223 ------MELVS--VPAKQPYA 235
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 22-86 1.73e-04

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, 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.


Pssm-ID: 163664  Cd Length: 304  Bit Score: 42.49  E-value: 1.73e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1972227248  22 VADMHGQSIHL------LRIFLTNEAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRYPQ--HVFLLrGNHE 86
Cdd:cd07421     7 VGDIHGYISKLnnlwlnLQSALGPSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKqrHVFLC-GNHD 78
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 42-259 1.44e-03

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 39.30  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248  42 PPNQKYLFLGDYVDRGSQSVVVMCLLFCMKHRypQHVFLLRGNHEDV--------NTTLNYGFyDECLEQWKN---DEGE 110
Cdd:PRK13625   35 PDQRKLAFVGDLTDRGPHSLRMIEIVWELVEK--KAAYYVPGNHCNKlyrfflgrNVTIAHGL-ETTVAEYEAlpsHKQN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 111 KVWRMFIDTFNCMPLAAVI-GGKVFCAHGGISPwleslEDINSIERPlvVPPYGLACDL---LWSDpAQPERNGWGLSHR 186
Cdd:PRK13625  112 MIKEKFITLYEQAPLYHILdEGRLVVAHAGIRQ-----DYIGRQDKK--VQTFVLYGDItgeKHPD-GSPVRRDWAKEYK 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1972227248 187 GisftygksvveefcakndIALVIRGHQLFKEmyPQ----------GCVlrFGGRLislfSALNYEGHKNNSSVLKLEFV 256
Cdd:PRK13625  184 G------------------TAWIVYGHTPVKE--PRfvnhtvnidtGCV--FGGRL----TALRYPEMETVSVPSSLPFV 237


                  ...
gi 1972227248 257 GQR 259
Cdd:PRK13625  238 PEK 240
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 21-86 2.25e-03

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing 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. This superfamily includes: the phosphoprotein phosphatases (PPPs), 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.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 37.63  E-value: 2.25e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1972227248  21 VVADMHGQSIHLLRIFLTN--EAPPNQKYLFLGDYVDRGSQSVVVMCLLFCMK-HRYPqhVFLLRGNHE 86
Cdd:cd00838     2 VISDIHGNLEALEAVLEAAlaKAEKPDLVICLGDLVDYGPDPEEVELKALRLLlAGIP--VYVVPGNHD 68
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options: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.
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