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Conserved domains on  [gi|922580314|ref|NP_001299879|]
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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 ...
 164-437 4.52e-146

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: 417.77  E-value: 4.52e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   164 YTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFT 243
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   244 YKICYPENIVLLRGNHEIARVNKKYGFYEECVtsiPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDEL 323
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECK---RKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   324 RNHPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITI 403
Cdd:smart00156 158 RKLKRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTI 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 922580314   404 FSAPMYCNFYKNAGCVLKVDETLGIQMIAFVPAS 437
Cdd:smart00156 238 FSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 164-437 4.52e-146

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: 417.77  E-value: 4.52e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   164 YTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFT 243
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   244 YKICYPENIVLLRGNHEIARVNKKYGFYEECVtsiPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDEL 323
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECK---RKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   324 RNHPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITI 403
Cdd:smart00156 158 RKLKRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTI 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 922580314   404 FSAPMYCNFYKNAGCVLKVDETLGIQMIAFVPAS 437
Cdd:smart00156 238 FSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 194-422 1.09e-112

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: 331.26  E-value: 1.09e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 194 VVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEE 273
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 274 CVTS-IPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDELRNHpKPIRNPFRGIVNDMLWADPDPSVFE 352
Cdd:cd00144   81 RTLRcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 353 WKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITIFSAPMYCNFYKNAGCVLKV 422
Cdd:cd00144  160 FESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 139-438 1.58e-83

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 259.98  E-value: 1.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 139 QERIDFVDFLDRHYQVIQAGVHK-IQYTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPP 217
Cdd:PTZ00480   6 KGEIDVDNIIERLLSVRGSKPGKnVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 218 ETVYVFTGDYVDRGMMSLECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEECVTsipKCGEEIWALFQRCFNNLP 297
Cdd:PTZ00480  86 ESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR---RYTIKLWKTFTDCFNCLP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 298 ISALIATKILCMHGGLSPALTCLDELRNHPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLG 377
Cdd:PTZ00480 163 VAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHE 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922580314 378 VELIIRAHQMCFDGYWVLSGRKLITIFSAPMYCNFYKNAGCVLKVDETLGIQMIAFVPASE 438
Cdd:PTZ00480 243 LDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQ 303
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 194-303 3.11e-14

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: 68.78  E-value: 3.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314  194 VVVGDLH--GQFNDLINMF-ILLGRPPETVYVFTGDYVDRGMMSlECIMLLFTYKICYpENIVLLRGNHEIARVNKKYGF 270
Cdd:pfam00149   4 LVIGDLHlpGQLDDLLELLkKLLEEGKPDLVLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYGECLRLY 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 922580314  271 YEECVTSIPkcgeeiWALFQRCFNNLPISALIA 303
Cdd:pfam00149  82 PYLGLLARP------WKRFLEVFNFLPLAGILS 108
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 164-437 4.52e-146

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: 417.77  E-value: 4.52e-146
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   164 YTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFT 243
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   244 YKICYPENIVLLRGNHEIARVNKKYGFYEECVtsiPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDEL 323
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECK---RKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDI 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314   324 RNHPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITI 403
Cdd:smart00156 158 RKLKRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTI 237

                          250       260       270
                   ....*....|....*....|....*....|....
gi 922580314   404 FSAPMYCNFYKNAGCVLKVDETLGIQMIAFVPAS 437
Cdd:smart00156 238 FSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 194-422 1.09e-112

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: 331.26  E-value: 1.09e-112
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 194 VVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEE 273
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 274 CVTS-IPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDELRNHpKPIRNPFRGIVNDMLWADPDPSVFE 352
Cdd:cd00144   81 RTLRcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGD 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 353 WKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITIFSAPMYCNFYKNAGCVLKV 422
Cdd:cd00144  160 FESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 162-426 1.25e-103

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: 310.43  E-value: 1.25e-103
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 162 IQYTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLL 241
Cdd:cd07414   21 VQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 242 FTYKICYPENIVLLRGNHEIARVNKKYGFYEECVTsipKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLD 321
Cdd:cd07414  101 LAYKIKYPENFFLLRGNHECASINRIYGFYDECKR---RYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSME 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 322 ELRNHPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLI 401
Cdd:cd07414  178 QIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLV 257

                        250       260
                 ....*....|....*....|....*
gi 922580314 402 TIFSAPMYCNFYKNAGCVLKVDETL 426
Cdd:cd07414  258 TLFSAPNYCGEFDNAGAMMSVDETL 282
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 176-436 9.46e-89

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: 272.15  E-value: 9.46e-89
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 176 AQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFTYKICYPENIVLL 255
Cdd:cd07415   27 AKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 256 RGNHEIARVNKKYGFYEECvtsIPKCGEE-IWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDELRNHPKPIRNPF 334
Cdd:cd07415  107 RGNHESRQITQVYGFYDEC---LRKYGNAnVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPH 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 335 RGIVNDMLWADPDPSVFeWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITIFSAPMYCNFYK 414
Cdd:cd07415  184 EGPMCDLLWSDPDDREG-WGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCG 262

                        250       260
                 ....*....|....*....|..
gi 922580314 415 NAGCVLKVDETLGIQMIAFVPA 436
Cdd:cd07415  263 NVASILELDEHLNRSFKQFEAA 284
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 139-438 1.58e-83

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 259.98  E-value: 1.58e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 139 QERIDFVDFLDRHYQVIQAGVHK-IQYTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPP 217
Cdd:PTZ00480   6 KGEIDVDNIIERLLSVRGSKPGKnVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPP 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 218 ETVYVFTGDYVDRGMMSLECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEECVTsipKCGEEIWALFQRCFNNLP 297
Cdd:PTZ00480  86 ESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR---RYTIKLWKTFTDCFNCLP 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 298 ISALIATKILCMHGGLSPALTCLDELRNHPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLG 377
Cdd:PTZ00480 163 VAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHE 242

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922580314 378 VELIIRAHQMCFDGYWVLSGRKLITIFSAPMYCNFYKNAGCVLKVDETLGIQMIAFVPASE 438
Cdd:PTZ00480 243 LDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQ 303
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 166-437 2.30e-78

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 245.59  E-value: 2.30e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 166 KEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFTYK 245
Cdd:PTZ00244  27 EEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 246 ICYPENIVLLRGNHEIARVNKKYGFYEECVTsipKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDELRN 325
Cdd:PTZ00244 107 IVYPENFFLLRGNHECASINKMYGFFDDVKR---RYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNE 183

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 326 HPKPIRNPFRGIVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITIFS 405
Cdd:PTZ00244 184 IERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFS 263

                        250       260       270
                 ....*....|....*....|....*....|..
gi 922580314 406 APMYCNFYKNAGCVLKVDETLGIQMIaFVPAS 437
Cdd:PTZ00244 264 APNYCGEFDNDAAVMNIDDKLQCSFL-IIPAR 294
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 164-428 6.41e-72

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: 229.63  E-value: 6.41e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 164 YTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETV--------YVFTGDYVDRGMMSL 235
Cdd:cd07419   21 FDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEagdieyidYLFLGDYVDRGSHSL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 236 ECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEECVTSI---PKCGEEIWALFQRCFNNLPISALIATKILCMHGG 312
Cdd:cd07419  101 ETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLgedIRDGDSVWQRINRLFNWLPLAALIEDKIICVHGG 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 313 LSPALTCLDELRNHPKPIRNPFRG-IVNDMLWADP---DP-SVFEWKA-SSRGSG--FTFGTNVIDDVCKRLGVELIIRA 384
Cdd:cd07419  181 IGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPtenDSvLGLRPNAiDPRGTGliVKFGPDRVMEFLEENDLQMIIRA 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....
gi 922580314 385 HQMCFDGYWVLSGRKLITIFSAPMYCNFYKNAGCVLKVDETLGI 428
Cdd:cd07419  261 HECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVV 304
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 129-423 8.11e-72

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: 229.45  E-value: 8.11e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 129 GPEMTAQNRTQEridFVDFLDRHYQViQAGVHKiqytKEEFEnVIYEAQTIFSSEKALVDID-PPCV---VVGDLHGQFN 204
Cdd:cd07417    3 GPKLEDGKVTLE---FVKEMMEWFKD-QKKLHK----KYAYQ-ILLQVKEILKKLPSLVEITiPEGEkitVCGDTHGQFY 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 205 DLINMFILLGRPPET-VYVFTGDYVDRGMMSLECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEECVTsipKCGE 283
Cdd:cd07417   74 DLLNIFELNGLPSETnPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKA---KYNE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 284 EIWALFQRCFNNLPISALIATKILCMHGGL--SPALTcLDELRNhPKPIRNPFR-GIVNDMLWADPDPSVFEwKASSRGS 360
Cdd:cd07417  151 QMFNLFSEVFNWLPLAHLINGKVLVVHGGLfsDDGVT-LDDIRK-IDRFRQPPDsGLMCELLWSDPQPQPGR-GPSKRGV 227

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922580314 361 GFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGRKLITIFSAPMYCNFYKNAGCVLKVD 423
Cdd:cd07417  228 GCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFK 290
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 165-435 9.28e-69

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: 221.41  E-value: 9.28e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 165 TKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGDYVDRGMMSLECIMLLFTY 244
Cdd:cd07416   17 SEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWAL 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 245 KICYPENIVLLRGNHEIARVNKKYGFYEECvtsIPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPALTCLDELR 324
Cdd:cd07416   97 KILYPKTLFLLRGNHECRHLTEYFTFKQEC---KIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIR 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 325 NHPKPIRNPFRGIVNDMLWADP------DPSVFEWKASS-RGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLsg 397
Cdd:cd07416  174 KLDRFREPPSYGPMCDLLWSDPledfgnEKTQEHFVHNTvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMY-- 251

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 922580314 398 RK--------LITIFSAPMYCNFYKNAGCVLKVD-ETLGIQMIAFVP 435
Cdd:cd07416  252 RKsqttgfpsLITIFSAPNYLDVYNNKAAVLKYEnNVMNIRQFNCSP 298
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 148-437 8.40e-67

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 216.22  E-value: 8.40e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 148 LDRH-YQVIQAGVhkiqYTKEEFENVIYEAQTIFSSEKALVDIDPPCVVVGDLHGQFNDLINMFILLGRPPETVYVFTGD 226
Cdd:PTZ00239   3 IDRHiATLLNGGC----LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 227 YVDRGMMSLECIMLLFTYKICYPENIVLLRGNHEIARVNKKYGFYEECVTSIPKCGEeiWALFQRCFNNLPISALIATKI 306
Cdd:PTZ00239  79 FVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNP--WRLFMDVFDCLPLAALIEGQI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 307 LCMHGGLSPALTCLDELRNHPKPIRNPFRGIVNDMLWADPDpSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQ 386
Cdd:PTZ00239 157 LCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE-EVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQ 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 922580314 387 MCFDG--YWvLSGRKLITIFSAPMYCNFYKNAGCVLKVDETLGIQMIAF--VPAS 437
Cdd:PTZ00239 236 LVMEGykYW-FPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFkeVPES 289
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 171-422 2.16e-52

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: 178.37  E-value: 2.16e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 171 NVIYEAQTIFsseKALVDIDP-------PCVVVGDLHGQFNDLINMFILLGRP-PETVYVFTGDYVDRGMMSLECIMLLF 242
Cdd:cd07420   27 LILREARKSL---KQLPNISRvstsyskEVTICGDLHGKLDDLLLIFYKNGLPsPENPYVFNGDFVDRGKRSIEILMILF 103

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 243 TYKICYPENIVLLRGNHEIARVNKKYGFYEECVTSIPKCGEEIWALFQRCFNNLPISALIATKILCMHGGLSPAlTCLDE 322
Cdd:cd07420  104 AFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGISDS-TDLDL 182

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 323 L----RNHPKPIRNPFRGIVnDMLWADPDPSVFEWKASSRGSGFTFGTNVIDDVCKRLGVELIIRAHQMCFDGYWVLSGR 398
Cdd:cd07420  183 LdkidRHKYVSTKTEWQQVV-DILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNN 261

                        250       260
                 ....*....|....*....|....
gi 922580314 399 KLITIFSAPMYCNFYKNAGCVLKV 422
Cdd:cd07420  262 KVITIFSASNYYEEGSNRGAYVKL 285
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 168-417 2.80e-44

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: 159.19  E-value: 2.80e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 168 EFENVIYEAQTIFSSEKALVDID----PPCVVVGDLHGQFNDLINMFILLGRPPET-VYVFTGDYVDRGMMSLECIMLLF 242
Cdd:cd07418   39 VFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNrFYVFNGDYVDRGAWGLETFLLLL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 243 TYKICYPENIVLLRGNHEIARVNKKYGFYEECVTSIPKCGEEIWALFQRCFNNLPISALIATKILCMHGGL--------- 313
Cdd:cd07418  119 SWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkr 198

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 314 ------------------SPALTCLDELRNHPKPIRNP-FRG---IVNDMLWADPDPSVFEWKASSRGSGFTFGTNVIDD 371
Cdd:cd07418  199 kkqkgknrrvlllepeseSLKLGTLDDLMKARRSVLDPpGEGsnlIPGDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEE 278

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922580314 372 VCKRLGVELIIRAHQ------------MCFDGYWV---LSGRKLITIFSAPMYCNF------YKNAG 417
Cdd:cd07418  279 FLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVdhdVESGKLITLFSAPDYPQFqateerYNNKG 345
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 194-303 3.11e-14

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: 68.78  E-value: 3.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314  194 VVVGDLH--GQFNDLINMF-ILLGRPPETVYVFTGDYVDRGMMSlECIMLLFTYKICYpENIVLLRGNHEIARVNKKYGF 270
Cdd:pfam00149   4 LVIGDLHlpGQLDDLLELLkKLLEEGKPDLVLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFDYGECLRLY 81

                          90       100       110
                  ....*....|....*....|....*....|...
gi 922580314  271 YEECVTSIPkcgeeiWALFQRCFNNLPISALIA 303
Cdd:pfam00149  82 PYLGLLARP------WKRFLEVFNFLPLAGILS 108
PHA02239 PHA02239
putative protein phosphatase
 195-260 6.05e-08

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 53.46  E-value: 6.05e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 922580314 195 VVGDLHGQFNDLINMF--ILLGRPPETVYVFTGDYVDRGMMSLECIMLLFTYkICYPENIVLLRGNHE 260
Cdd:PHA02239   5 VVPDIHGEYQKLLTIMdkINNERKPEETIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHD 71
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 194-261 9.10e-08

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: 50.73  E-value: 9.10e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 194 VVVGDLHGQFNDL--INMFILLGRPPETVYVFTGDYVDRGMMSLECImLLFTYKICYPENIVLLRGNHEI 261
Cdd:cd00838    1 LVISDIHGNLEALeaVLEAALAKAEKPDLVICLGDLVDYGPDPEEVE-LKALRLLLAGIPVYVVPGNHDI 69
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 195-260 1.22e-04

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: 43.07  E-value: 1.22e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922580314 195 VVGDLHGQFNDLINMFILLGRPPETVYVFT-GDYVDRGMMSLECIMLL----FTYkicypenivlLRGNHE 260
Cdd:cd07424    5 VVGDIHGHFQRLQRALDAVGFDPARDRLISvGDLVDRGPESLEVLELLkqpwFHA----------VQGNHE 65
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 194-261 2.02e-04

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, 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: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 42.29  E-value: 2.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 194 VVVGDLHGQFNDLINMFILLG--------RPPETVYVFTGDYVDRGMMSLECIMLLftYKIcYPE------NIVLLRGNH 259
Cdd:cd07425    1 VAIGDLHGDLDRLRTILKLAGvidsndrwIGGDTVVVQTGDILDRGDDEIEILKLL--EKL-KRQarkaggKVILLLGNH 77


                 ..
gi 922580314 260 EI 261
Cdd:cd07425   78 EL 79
pphA PRK11439
protein-serine/threonine phosphatase;
195-260 4.68e-04

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 41.29  E-value: 4.68e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922580314 195 VVGDLHGQFNDLINMFILLG-RPPETVYVFTGDYVDRGMMSLECIMLLftykicYPENIVLLRGNHE 260
Cdd:PRK11439  21 LVGDIHGCFEQLMRKLRHCRfDPWRDLLISVGDLIDRGPQSLRCLQLL------EEHWVRAVRGNHE 81
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 195-271 3.30e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 38.92  E-value: 3.30e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922580314 195 VVGDLHGQFNDLINMFILLG---------RPPETVYVFTGDYVDRGMMSLEciMLLFTYKICYPENIVLLRGNHeiarVN 265
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKLGynwssglpvHPDQRKLAFVGDLTDRGPHSLR--MIEIVWELVEKKAAYYVPGNH----CN 78


                 ....*.
gi 922580314 266 KKYGFY 271
Cdd:PRK13625  79 KLYRFF 84
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 194-262 3.67e-03

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: 39.41  E-value: 3.67e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922580314 194 VVVGDLHGQFNDLINMFILLGR--PPE----TVYVFTGDYVDRGMMSLECIMLLFTYKICYPENI-VLLRGNHEIA 262
Cdd:cd07421    5 ICVGDIHGYISKLNNLWLNLQSalGPSdfasALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRhVFLCGNHDFA 80
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 195-260 5.55e-03

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: 38.26  E-value: 5.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922580314 195 VVGDLHGQFNDLINMFILLG---------RPPE--TVyVFTGDYVDRGMMSLECimLLFTYKICYPENIVLLRGNHE 260
Cdd:cd07423    2 IIGDVHGCYDELVELLEKLGyqkkeeglyVHPEgrKL-VFLGDLVDRGPDSIDV--LRLVMNMVKAGKALYVPGNHC 75
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 195-261 6.38e-03

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: 38.29  E-value: 6.38e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922580314 195 VVGDLHGQFNDLInmfILLGR----PPETVYVFTGDYVDRGMMSLECimLLFTYKICypENIVLLRGNHEI 261
Cdd:cd07422    3 AIGDIQGCYDELQ---RLLEKinfdPAKDRLWLVGDLVNRGPDSLET--LRFVKSLG--DSAVVVLGNHDL 66
PRK09968 PRK09968
protein-serine/threonine phosphatase;
195-260 7.31e-03

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 37.95  E-value: 7.31e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922580314 195 VVGDLHGQFNDLINMFILLGRPPET-VYVFTGDYVDRGMMSLECIMLLFTykicypENIVLLRGNHE 260
Cdd:PRK09968  19 VVGDIHGEYQLLQSRLHQLSFCPETdLLISVGDNIDRGPESLNVLRLLNQ------PWFISVKGNHE 79
 
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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