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Conserved domains on  [gi|4193369|gb|AAD09996|]
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protein phosphatase-Z-like serine/threonine protein phosphatase [Neurospora crassa]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
207-498 0e+00

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.


The actual alignment was detected with superfamily member cd07414:

Pssm-ID: 353799 [Multi-domain]  Cd Length: 291  Bit Score: 558.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  207 DLDDFIKRLLDAAYaGKVTKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSN 286
Cdd:cd07414   1 DIDSIIERLLEVRG-SRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  287 YLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVA 366
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  367 GKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCR 446
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4193369  447 AHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
DUF601 super family cl27239
Protein of unknown function, DUF601; This family represents a conserved region found in ...
2-272 3.31e-03

Protein of unknown function, DUF601; This family represents a conserved region found in several uncharacterized plant proteins.


The actual alignment was detected with superfamily member pfam04642:

Pssm-ID: 282493 [Multi-domain]  Cd Length: 327  Bit Score: 39.49  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369      2 GNSSSKDAGASSKNRGDDDLKSYPSFSKSDTKDSSRSFRGLRSKipgGSKTDSPRNSTILSSEEVAEKmnalsgKNGRPS 81
Cdd:pfam04642  58 GKDPEKRAADKKRKQPDEDAHSPARSSRPRQEEKDASPSQQKEK---GKKEDAPQDLVVLSSRESETR------ESERKN 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     82 VH-TRPSRRDMSPSPASPSTSSPSSPSLDTATLASPTGEPLPPPSPVhNATGGHHDVRAAQESGEVDHISDQ----PPSG 156
Cdd:pfam04642 129 IPlNAPFLRDTDNLLSSGHVPAPPLPFADLMRSFTHAGAAIAPFDEL-KETNKDNYLRFAEKLGELKDEDNEyplcPSTP 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369    157 GGGANSNQQPGQ--SILVKRENTINpvydtpnqdPQNEQAVSGVAMSDIKDIDLddfiKRLLDA---AYAGKVTKSVCLK 231
Cdd:pfam04642 208 FSAAESFKQNEDenAKAVDKANKVL---------NRMKAAEAQVLALDIANIDL----AAKLEAgknAYLAAIDKENQAR 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 4193369    232 nAEIVAICHRARELFLSQPALLElDAPVKIVGDVHGQYTDL 272
Cdd:pfam04642 275 -ADLKACEEKLKKLEEEQAALIA-AARRDERRKVRAQFHDF 313
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
207-498 0e+00

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: 558.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  207 DLDDFIKRLLDAAYaGKVTKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSN 286
Cdd:cd07414   1 DIDSIIERLLEVRG-SRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  287 YLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVA 366
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  367 GKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCR 446
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4193369  447 AHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
205-502 2.46e-146

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 422.92  E-value: 2.46e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   205 DIDLDDFIKRLLdAAYAGKVTKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPN 284
Cdd:PTZ00480   8 EIDVDNIIERLL-SVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   285 SNYLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAI 364
Cdd:PTZ00480  87 SNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   365 VAGKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVV 444
Cdd:PTZ00480 167 IDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLI 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4193369   445 CRAHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKPLDSA 502
Cdd:PTZ00480 247 CRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQG 304
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
234-498 2.43e-139

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


Pssm-ID: 197547  Cd Length: 271  Bit Score: 403.13  E-value: 2.43e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     234 EIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSNYLFLGDYVDRGKQSLETILLLMCYKLK 313
Cdd:smart00156   5 EILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKIL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     314 YPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVAGKIFCVHGGLSPALGHMDDIRNIARPT 393
Cdd:smart00156  85 YPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQ 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     394 DVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCRAHMVVEDGYEFYTDRILVTIFSAPNYC 473
Cdd:smart00156 165 EPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYC 244
                          250       260
                   ....*....|....*....|....*
gi 4193369     474 GEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:smart00156 245 DRFGNKAAVLKVDKDLKLTFEQFKP 269
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
328-474 7.61e-32

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];


Pssm-ID: 223712  Cd Length: 155  Bit Score: 119.76  E-value: 7.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  328 ANVTRVYGFYDECKR-RCNVKIWKT---FVDTFNCLPIAAIVAG-KIFCVHGGLSPALGH-MDDIRNIARPT--DVPDYG 399
Cdd:COG0639   1 MLLTALYGFYDEKLRkYGEELEWLRaagGLETFDSLPLAAVAEGgKLLCHHGGLSPGLDRlLDIIEVLDRLRacEVPHAG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4193369  400 LLNDLLWSDP-ADMDQDWEANERGVSYCFGKKVISdFLATHDFDVVCRAHMVVEDGYEFYTDRILVTIFSAPNYCG 474
Cdd:COG0639  81 HTHDLLWSDPdGGDRRIWNPGPRGVPRDGGDVTAV-FGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNYCY 155
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
208-256 1.56e-17

Serine-threonine protein phosphatase N-terminal domain; This family is often found at the N-terminus of Metallophos family, in serine-threonine protein phosphatases.


Pssm-ID: 339847 [Multi-domain]  Cd Length: 48  Bit Score: 75.94  E-value: 1.56e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 4193369    208 LDDFIKRLLDAAYAGKVTKsVCLKNAEIVAICHRARELFLSQPALLELD 256
Cdd:pfam16891   1 VDDIIERLLEVRGKPGGKQ-VQLSEAEIRALCRKAREIFLSQPMLLELE 48
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
261-304 1.83e-03

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 40.25  E-value: 1.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4193369    261 IVGDVHGQYTDLIRMFEMCPFPPNSNYLFL-GDYVDRGKQSLETI 304
Cdd:TIGR00668   5 LIGDLHGCYDELQALLERVEFDPGQDTLWLtGDLVARGPGSLEVL 49
DUF601 pfam04642
Protein of unknown function, DUF601; This family represents a conserved region found in ...
2-272 3.31e-03

Protein of unknown function, DUF601; This family represents a conserved region found in several uncharacterized plant proteins.


Pssm-ID: 282493 [Multi-domain]  Cd Length: 327  Bit Score: 39.49  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369      2 GNSSSKDAGASSKNRGDDDLKSYPSFSKSDTKDSSRSFRGLRSKipgGSKTDSPRNSTILSSEEVAEKmnalsgKNGRPS 81
Cdd:pfam04642  58 GKDPEKRAADKKRKQPDEDAHSPARSSRPRQEEKDASPSQQKEK---GKKEDAPQDLVVLSSRESETR------ESERKN 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     82 VH-TRPSRRDMSPSPASPSTSSPSSPSLDTATLASPTGEPLPPPSPVhNATGGHHDVRAAQESGEVDHISDQ----PPSG 156
Cdd:pfam04642 129 IPlNAPFLRDTDNLLSSGHVPAPPLPFADLMRSFTHAGAAIAPFDEL-KETNKDNYLRFAEKLGELKDEDNEyplcPSTP 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369    157 GGGANSNQQPGQ--SILVKRENTINpvydtpnqdPQNEQAVSGVAMSDIKDIDLddfiKRLLDA---AYAGKVTKSVCLK 231
Cdd:pfam04642 208 FSAAESFKQNEDenAKAVDKANKVL---------NRMKAAEAQVLALDIANIDL----AAKLEAgknAYLAAIDKENQAR 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 4193369    232 nAEIVAICHRARELFLSQPALLElDAPVKIVGDVHGQYTDL 272
Cdd:pfam04642 275 -ADLKACEEKLKKLEEEQAALIA-AARRDERRKVRAQFHDF 313
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
207-498 0e+00

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: 558.49  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  207 DLDDFIKRLLDAAYaGKVTKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSN 286
Cdd:cd07414   1 DIDSIIERLLEVRG-SRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  287 YLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVA 366
Cdd:cd07414  80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  367 GKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCR 446
Cdd:cd07414 160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 4193369  447 AHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
205-502 2.46e-146

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 422.92  E-value: 2.46e-146
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   205 DIDLDDFIKRLLdAAYAGKVTKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPN 284
Cdd:PTZ00480   8 EIDVDNIIERLL-SVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPE 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   285 SNYLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAI 364
Cdd:PTZ00480  87 SNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAAL 166
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   365 VAGKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVV 444
Cdd:PTZ00480 167 IDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLI 246
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 4193369   445 CRAHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKPLDSA 502
Cdd:PTZ00480 247 CRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQG 304
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
234-498 2.43e-139

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


Pssm-ID: 197547  Cd Length: 271  Bit Score: 403.13  E-value: 2.43e-139
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     234 EIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSNYLFLGDYVDRGKQSLETILLLMCYKLK 313
Cdd:smart00156   5 EILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKIL 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     314 YPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVAGKIFCVHGGLSPALGHMDDIRNIARPT 393
Cdd:smart00156  85 YPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQ 164
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     394 DVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCRAHMVVEDGYEFYTDRILVTIFSAPNYC 473
Cdd:smart00156 165 EPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYC 244
                          250       260
                   ....*....|....*....|....*
gi 4193369     474 GEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:smart00156 245 DRFGNKAAVLKVDKDLKLTFEQFKP 269
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
211-493 2.64e-126

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 370.77  E-value: 2.64e-126
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   211 FIKRLLdAAYAGKVTKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSNYLFL 290
Cdd:PTZ00244   7 LIEKML-TVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFL 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   291 GDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVAGKIF 370
Cdd:PTZ00244  86 GDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKII 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   371 CVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCRAHMV 450
Cdd:PTZ00244 166 CMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQV 245
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 4193369   451 VEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSF 493
Cdd:PTZ00244 246 MERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSF 288
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
207-498 3.22e-120

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: 354.97  E-value: 3.22e-120
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  207 DLDDFIKRLLdaayagkvtKSVCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSN 286
Cdd:cd07415   1 DLDQWIEQLK---------KCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTN 71
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  287 YLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRR-CNVKIWKTFVDTFNCLPIAAIV 365
Cdd:cd07415  72 YLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKyGNANVWKYFTDLFDYLPLAALI 151
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  366 AGKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADmDQDWEANERGVSYCFGKKVISDFLATHDFDVVC 445
Cdd:cd07415 152 DGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDD-REGWGISPRGAGYLFGQDVVEEFNHNNGLTLIC 230
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 4193369  446 RAHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:cd07415 231 RAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
261-483 2.08e-104

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: 312.38  E-value: 2.08e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  261 IVGDVHGQYTDLIRMFEMCPFPPNSNYLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDE- 339
Cdd:cd00144   2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDEr 81
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  340 ---CKRRCNVKIWKTFVDTFNCLPIAAIVAGKIFCVHGGLSPALGHMDDIRNIaRPTDVPDYGLLNDLLWSDPADMDQDW 416
Cdd:cd00144  82 tlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGDF 160
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4193369  417 EANERGVSYCFGKKVISDFLATHDFDVVCRAHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVM 483
Cdd:cd00144 161 ESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAAL 227
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
207-509 8.31e-93

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 285.17  E-value: 8.31e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   207 DLDDFIKRLLDAAyagkvtksvCLKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSN 286
Cdd:PTZ00239   2 DIDRHIATLLNGG---------CLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNAN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   287 YLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRC-NVKIWKTFVDTFNCLPIAAIV 365
Cdd:PTZ00239  73 YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALI 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   366 AGKIFCVHGGLSPALGHMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQdWEANERGVSYCFGKKVISDFLATHDFDVVC 445
Cdd:PTZ00239 153 EGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEY-WAVNSRGAGYLFGAKVTKEFCRLNDLTLIC 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4193369   446 RAHMVVEDGYEF-YTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKPLDSAALKTHIK 509
Cdd:PTZ00239 232 RAHQLVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPK 296
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
222-491 3.63e-92

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: 283.81  E-value: 3.63e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  222 GKVTKSVCLKnaeivaICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNSNYLFLGDYVDRGKQSL 301
Cdd:cd07416  14 GRLSEEDALR------IITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSI 87
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  302 ETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAIVAGKIFCVHGGLSPALG 381
Cdd:cd07416  88 ECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELK 167
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  382 HMDDIRNIARPTDVPDYGLLNDLLWSDPADMDQDWEANE-------RGVSYCFGKKVISDFLATHDFDVVCRAHMVVEDG 454
Cdd:cd07416 168 TLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNEKTQEhfvhntvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAG 247
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 4193369  455 YEFY-----TD-RILVTIFSAPNYCGEFDNWGAVMAVSTELLC 491
Cdd:cd07416 248 YRMYrksqtTGfPSLITIFSAPNYLDVYNNKAAVLKYENNVMN 290
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
230-498 1.28e-80

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: 254.29  E-value: 1.28e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  230 LKNAEIVAICHRARELFLSQPALLELDAPVKIVGDVHGQYTDLIRMFEMCPFPPNS--------NYLFLGDYVDRGKQSL 301
Cdd:cd07419  21 FDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEeagdieyiDYLFLGDYVDRGSHSL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  302 ETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCN------VKIWKTFVDTFNCLPIAAIVAGKIFCVHGG 375
Cdd:cd07419 101 ETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRLFNWLPLAALIEDKIICVHGG 180
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  376 LSPALGHMDDIRNIARPTDVPDYG-LLNDLLWSDPADMDQ-------DWEANERGVSYCFGKKVISDFLATHDFDVVCRA 447
Cdd:cd07419 181 IGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPTENDSvlglrpnAIDPRGTGLIVKFGPDRVMEFLEENDLQMIIRA 260
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|.
gi 4193369  448 HMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAVMAVSTELLCSFELLKP 498
Cdd:cd07419 261 HECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
210-482 4.26e-76

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  Cd Length: 316  Bit Score: 242.55  E-value: 4.26e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  210 DFIKRLLDAAyagKVTKSVCLKNAeiVAICHRARELFLSQPALLELDAP----VKIVGDVHGQYTDLIRMFEMCPFPPNS 285
Cdd:cd07417  14 EFVKEMMEWF---KDQKKLHKKYA--YQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSET 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  286 N-YLFLGDYVDRGKQSLETILLLMCYKLKYPENFFLLRGNHECANVTRVYGFYDECKRRCNVKIWKTFVDTFNCLPIAAI 364
Cdd:cd07417  89 NpYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHL 168
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  365 VAGKIFCVHGGLSPALG-HMDDIRNIARPTDVPDYGLLNDLLWSDPadmdQDWE---ANERGVSYCFGKKVISDFLATHD 440
Cdd:cd07417 169 INGKVLVVHGGLFSDDGvTLDDIRKIDRFRQPPDSGLMCELLWSDP----QPQPgrgPSKRGVGCQFGPDVTKRFLEENN 244
                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 4193369  441 FDVVCRAHMVVEDGYEFYTDRILVTIFSAPNYCGEFDNWGAV 482
Cdd:cd07417 245 LDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAF 286
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
238-493 7.65e-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: 162.58  E-value: 7.65e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  238 ICHRARELFLSQPALLELDA----PVKIVGDVHGQYTDLIRMFEMCPFPPNSN-YLFLGDYVDRGKQSLETILLLMCYKL 312
Cdd:cd07420  28 ILREARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVL 107
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  313 KYPENFFLLRGNHECANVTRVYGFYDECKRRCNV---KIWKTFVDTFNCLPIAAIVAGKIFCVHGGLSPALgHMDDIRNI 389
Cdd:cd07420 108 VYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGISDST-DLDLLDKI 186
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  390 AR---PTDVPDYGLLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFDVVCRAHMVVEDGYEFYTDRILVTI 466
Cdd:cd07420 187 DRhkyVSTKTEWQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITI 266
                       250       260
                ....*....|....*....|....*..
gi 4193369  467 FSAPNYCGEFDNWGAVMAVSTELLCSF 493
Cdd:cd07420 267 FSASNYYEEGSNRGAYVKLGPQLTPHF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
242-472 1.86e-39

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: 147.25  E-value: 1.86e-39
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  242 ARELFLSQPALLELD----APVKIVGDVHGQYTDLIRMFEMCPFP-PNSNYLFLGDYVDRGKQSLETILLLMCYKLKYPE 316
Cdd:cd07418  47 AHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPdQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPD 126
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  317 NFFLLRGNHECANVTRVYGFYDECKRRCN---VKIWKTFVDTFNCLPIAAIVAGKIFCVHGGL----------------- 376
Cdd:cd07418 127 RVYLLRGNHESKFCTSMYGFEQEVLTKYGdkgKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknr 206
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  377 ----------SPALGHMDDIRNIARPT-DVPDYG---LLNDLLWSDPADMDQDWEANERGVSYCFGKKVISDFLATHDFD 442
Cdd:cd07418 207 rvlllepeseSLKLGTLDDLMKARRSVlDPPGEGsnlIPGDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLK 286
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 4193369  443 VVCRAH------------MVVEDGYEFYTDRI---LVTIFSAPNY 472
Cdd:cd07418 287 LIIRSHegpdarekrpglAGMNKGYTVDHDVEsgkLITLFSAPDY 331
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
328-474 7.61e-32

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];


Pssm-ID: 223712  Cd Length: 155  Bit Score: 119.76  E-value: 7.61e-32
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  328 ANVTRVYGFYDECKR-RCNVKIWKT---FVDTFNCLPIAAIVAG-KIFCVHGGLSPALGH-MDDIRNIARPT--DVPDYG 399
Cdd:COG0639   1 MLLTALYGFYDEKLRkYGEELEWLRaagGLETFDSLPLAAVAEGgKLLCHHGGLSPGLDRlLDIIEVLDRLRacEVPHAG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 4193369  400 LLNDLLWSDP-ADMDQDWEANERGVSYCFGKKVISdFLATHDFDVVCRAHMVVEDGYEFYTDRILVTIFSAPNYCG 474
Cdd:COG0639  81 HTHDLLWSDPdGGDRRIWNPGPRGVPRDGGDVTAV-FGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNYCY 155
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
208-256 1.56e-17

Serine-threonine protein phosphatase N-terminal domain; This family is often found at the N-terminus of Metallophos family, in serine-threonine protein phosphatases.


Pssm-ID: 339847 [Multi-domain]  Cd Length: 48  Bit Score: 75.94  E-value: 1.56e-17
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 4193369    208 LDDFIKRLLDAAYAGKVTKsVCLKNAEIVAICHRARELFLSQPALLELD 256
Cdd:pfam16891   1 VDDIIERLLEVRGKPGGKQ-VQLSEAEIRALCRKAREIFLSQPMLLELE 48
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
258-328 4.58e-12

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: 333878 [Multi-domain]  Cd Length: 79  Bit Score: 61.63  E-value: 4.58e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 4193369    258 PVKIVGDVH--GQYTDLIRMFEMCPFPPNsNYLFL--GDYVDRGKQSLEtILLLMCYKLKYpENFFLLRGNHECA 328
Cdd:pfam00149   2 RILVIGDLHgpGQLDDLLELLKKLLEEEK-PDLVLhaGDLVDRGPWETE-VLELLERLIAY-VPVYLVRGNHDLS 73
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
261-373 4.29e-08

PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine and tyrosine phosphatases thought to modulate the expression of proteins that protect the cell upon accumulation of misfolded proteins in the periplasm. The PPP (phosphoprotein phosphatase) family, to which PrpA and PrpB belong, is one of two known protein phosphatase families specific for serine and threonine. This family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, 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: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 53.47  E-value: 4.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369  261 IVGDVHGQYTDLIRMFEMCPFPPNSNYLF-LGDYVDRGKQSLETILLlmcykLKYPEnFFLLRGNHECANVTRVYG---- 335
Cdd:cd07424   5 VVGDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLEVLEL-----LKQPW-FHAVQGNHEQMAIDALRGgddv 78
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 4193369  336 ---------FYDeckrrCNVKIWKTFVDTFNCLPIAAIV---AGKIFCVH 373
Cdd:cd07424  79 mwrangggwFFD-----LPDEEAKVLLEKLHHLPIAIEVesrNGKVGIVH 123
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
261-326 2.29e-07

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH 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, and PrpA/PrpB. 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: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 51.78  E-value: 2.29e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4193369  261 IVGDVHGQYTDLIRMFEMCPFPPNSNYL-FLGDYVDRGKQSLETilLLMCYKLKypENFFLLRGNHE 326
Cdd:cd07422   3 AIGDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLET--LRFVKSLG--DSAVVVLGNHD 65
pphA PRK11439
serine/threonine protein phosphatase 1; Provisional
261-326 1.64e-06

serine/threonine protein phosphatase 1; Provisional


Pssm-ID: 236911  Cd Length: 218  Bit Score: 48.99  E-value: 1.64e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4193369   261 IVGDVHGQYTDLIRMFEMCPFPPNSNYLF-LGDYVDRGKQSLETILLLMCyklkypENFFLLRGNHE 326
Cdd:PRK11439  21 LVGDIHGCFEQLMRKLRHCRFDPWRDLLIsVGDLIDRGPQSLRCLQLLEE------HWVRAVRGNHE 81
apaH PRK00166
diadenosine tetraphosphatase; Reviewed
261-326 2.25e-06

diadenosine tetraphosphatase; Reviewed


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 49.01  E-value: 2.25e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4193369   261 IVGDVHGQYTDLIRMFEMCPFPPNSNYL-FLGDYVDRGKQSLETILLLMcyklKYPENFFLLRGNHE 326
Cdd:PRK00166   5 AIGDIQGCYDELQRLLEKIDFDPAKDTLwLVGDLVNRGPDSLEVLRFVK----SLGDSAVTVLGNHD 67
PHA02239 PHA02239
putative protein phosphatase
261-338 4.39e-06

putative protein phosphatase


Pssm-ID: 107154  Cd Length: 235  Bit Score: 47.68  E-value: 4.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   261 IVGDVHGQYTDLIRMFEMC--PFPPNSNYLFLGDYVDRGKQSLETILLLMCYKLKyPENFFLLRGNHE------CANVTR 332
Cdd:PHA02239   5 VVPDIHGEYQKLLTIMDKInnERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHDdefyniMENVDR 83

                 ....*.
gi 4193369   333 VyGFYD 338
Cdd:PHA02239  84 L-SIYD 88
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
261-326 1.54e-05

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: 44.57  E-value: 1.54e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 4193369  261 IVGDVHGQYTDLIRMFEM--CPFPPNSNYLFLGDYVDRGKQSLETILLLmCYKLKYPENFFLLRGNHE 326
Cdd:cd00838   2 VISDIHGNLEALEAVLEAalAKAEKPDLVICLGDLVDYGPDPEEVELKA-LRLLLAGIPVYVVPGNHD 68
PRK09968 PRK09968
serine/threonine-specific protein phosphatase 2; Provisional
261-326 9.28e-05

serine/threonine-specific protein phosphatase 2; Provisional


Pssm-ID: 182173 [Multi-domain]  Cd Length: 218  Bit Score: 43.73  E-value: 9.28e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4193369   261 IVGDVHGQYTDLIRMFEMCPFPPNSNYLF-LGDYVDRGKQSLETILLlmcykLKYPEnFFLLRGNHE 326
Cdd:PRK09968  19 VVGDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRL-----LNQPW-FISVKGNHE 79
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
261-308 1.69e-04

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: 42.89  E-value: 1.69e-04
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 4193369  261 IVGDVHGQYTDLIRMFEMCPF----------PPNSNYLFLGDYVDRGKQSLETILLLM 308
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYqkkeeglyvhPEGRKLVFLGDLVDRGPDSIDVLRLVM 59
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
262-328 6.93e-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: 41.72  E-value: 6.93e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 4193369  262 VGDVHGQYTDLIRMF---EMCPFP---PNSNYLFLGDYVDRGKQSLETILLLMCYKLKYP-ENFFLLRGNHECA 328
Cdd:cd07421   7 VGDIHGYISKLNNLWlnlQSALGPsdfASALVIFLGDYCDRGPETRKVIDFLISLPEKHPkQRHVFLCGNHDFA 80
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
261-422 1.11e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.46  E-value: 1.11e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   261 IVGDVHGQYTDLIRMFEM--------CPFPPNSNYL-FLGDYVDRGKQSLETILLLM---------------CYKLkYpe 316
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKlgynwssgLPVHPDQRKLaFVGDLTDRGPHSLRMIEIVWelvekkaayyvpgnhCNKL-Y-- 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369   317 NFFLlrGNhecaNVTRVYGF------YDECKRRCNVKIWKTFVDTFNCLPIAAIV-AGKIFCVHGGLspalgHMDDIRNi 389
Cdd:PRK13625  82 RFFL--GR----NVTIAHGLettvaeYEALPSHKQNMIKEKFITLYEQAPLYHILdEGRLVVAHAGI-----RQDYIGR- 149
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 4193369   390 aRPTDVPDYGLLNDL---LWSDPADMDQDWEANERG 422
Cdd:PRK13625 150 -QDKKVQTFVLYGDItgeKHPDGSPVRRDWAKEYKG 184
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
261-304 1.83e-03

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 40.25  E-value: 1.83e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 4193369    261 IVGDVHGQYTDLIRMFEMCPFPPNSNYLFL-GDYVDRGKQSLETI 304
Cdd:TIGR00668   5 LIGDLHGCYDELQALLERVEFDPGQDTLWLtGDLVARGPGSLEVL 49
bacter_Pnkp TIGR04075
polynucleotide kinase-phosphatase; Members of this protein family are the bacterial ...
258-326 2.37e-03

polynucleotide kinase-phosphatase; Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring. [Transcription, RNA processing]


Pssm-ID: 274963 [Multi-domain]  Cd Length: 851  Bit Score: 40.37  E-value: 2.37e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369    258 PVKIVGDVHGQYTDL----------------IRMFEMCPfPPNSNYLFLGDYVDRGKQSLETILLLMcyKLKYPENFFLL 321
Cdd:TIGR04075 181 PFDIIGDVHGCRDELetlleelgyqierdegGRGVDVTH-PEGRKAVFVGDLVDRGPDSPGVLRLVM--GMVAAGTALCV 257

                  ....*
gi 4193369    322 RGNHE 326
Cdd:TIGR04075 258 PGNHD 262
DUF601 pfam04642
Protein of unknown function, DUF601; This family represents a conserved region found in ...
2-272 3.31e-03

Protein of unknown function, DUF601; This family represents a conserved region found in several uncharacterized plant proteins.


Pssm-ID: 282493 [Multi-domain]  Cd Length: 327  Bit Score: 39.49  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369      2 GNSSSKDAGASSKNRGDDDLKSYPSFSKSDTKDSSRSFRGLRSKipgGSKTDSPRNSTILSSEEVAEKmnalsgKNGRPS 81
Cdd:pfam04642  58 GKDPEKRAADKKRKQPDEDAHSPARSSRPRQEEKDASPSQQKEK---GKKEDAPQDLVVLSSRESETR------ESERKN 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369     82 VH-TRPSRRDMSPSPASPSTSSPSSPSLDTATLASPTGEPLPPPSPVhNATGGHHDVRAAQESGEVDHISDQ----PPSG 156
Cdd:pfam04642 129 IPlNAPFLRDTDNLLSSGHVPAPPLPFADLMRSFTHAGAAIAPFDEL-KETNKDNYLRFAEKLGELKDEDNEyplcPSTP 207
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4193369    157 GGGANSNQQPGQ--SILVKRENTINpvydtpnqdPQNEQAVSGVAMSDIKDIDLddfiKRLLDA---AYAGKVTKSVCLK 231
Cdd:pfam04642 208 FSAAESFKQNEDenAKAVDKANKVL---------NRMKAAEAQVLALDIANIDL----AAKLEAgknAYLAAIDKENQAR 274
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 4193369    232 nAEIVAICHRARELFLSQPALLElDAPVKIVGDVHGQYTDL 272
Cdd:pfam04642 275 -ADLKACEEKLKKLEEEQAALIA-AARRDERRKVRAQFHDF 313
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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