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Conserved domains on  [gi|1036967982|ref|XP_017052160|]
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serine/threonine-protein phosphatase beta isoform isoform X2 [Drosophila ficusphila]

Protein Classification

serine/threonine-protein phosphatase( domain architecture ID 10164801)

PPP (phosphoprotein phosphatase) family serine/threonine-protein phosphatase catalyzes the dephosphorylation of phosphoserine and phosphothreonine of specific target phosphoproteins

CATH:  3.60.21.10
EC:  3.1.3.16
Gene Ontology:  GO:0046872|GO:0004722|GO:0006470
PubMed:  18488168|25837850|30401537|9646865|29925267
SCOP:  3001067

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 7-297 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: 656.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   7 NVDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANY 86
Cdd:cd07414     1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  87 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDE 166
Cdd:cd07414    81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 167 KIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRA 246
Cdd:cd07414   161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1036967982 247 HQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKP 297
Cdd:cd07414   241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 7-297 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: 656.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   7 NVDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANY 86
Cdd:cd07414     1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  87 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDE 166
Cdd:cd07414    81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 167 KIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRA 246
Cdd:cd07414   161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1036967982 247 HQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKP 297
Cdd:cd07414   241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 5-300 0e+00

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 538.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   5 DLNVDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAA 84
Cdd:PTZ00480    8 EIDVDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPES 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  85 NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAII 164
Cdd:PTZ00480   88 NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 165 DEKIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLIC 244
Cdd:PTZ00480  168 DEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLIC 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036967982 245 RAHQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKPSEK 300
Cdd:PTZ00480  248 RAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQ 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 29-299 6.94e-151

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: 424.70  E-value: 6.94e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   29 MTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANYLFLGDYVDRGKQSLETICLLLA 108
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  109 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDEKIFCCHGGLSPDLQGMEQIRRL 188
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  189 MRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRAHQVVEDGYEFFARRQLVTLFSA 268
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1036967982  269 PNYCGEFDNAGGMMTVDDTLMCSFQILKPSE 299
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 8-55 7.04e-22

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: 465300 [Multi-domain]  Cd Length: 48  Bit Score: 86.77  E-value: 7.04e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1036967982   8 VDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELE 55
Cdd:pfam16891   1 LDDIIERLLEVRGKPGGKQVQLSEAEIRALCRKAREIFLSQPMLLELE 48
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
58-133 4.20e-03

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 38.07  E-value: 4.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036967982  58 LIICGDIHGQYTDLLRLFEYGGFPPAANYLFLGDYVDRGKqsLETICLLLAYKIKYPENFFLLRGNHECASINRIY 133
Cdd:COG2129     2 ILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGT--AEEAREVLEELAALGVPVLAVPGNHDDPEVLDAL 75
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 7-297 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: 656.72  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   7 NVDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANY 86
Cdd:cd07414     1 DIDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  87 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDE 166
Cdd:cd07414    81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 167 KIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRA 246
Cdd:cd07414   161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1036967982 247 HQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKP 297
Cdd:cd07414   241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 5-300 0e+00

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 538.86  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   5 DLNVDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAA 84
Cdd:PTZ00480    8 EIDVDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPES 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  85 NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAII 164
Cdd:PTZ00480   88 NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALI 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 165 DEKIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLIC 244
Cdd:PTZ00480  168 DEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLIC 247

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1036967982 245 RAHQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKPSEK 300
Cdd:PTZ00480  248 RAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQ 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 29-299 6.94e-151

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: 424.70  E-value: 6.94e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   29 MTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANYLFLGDYVDRGKQSLETICLLLA 108
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  109 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDEKIFCCHGGLSPDLQGMEQIRRL 188
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  189 MRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRAHQVVEDGYEFFARRQLVTLFSA 268
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1036967982  269 PNYCGEFDNAGGMMTVDDTLMCSFQILKPSE 299
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 8-295 1.63e-148

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 419.70  E-value: 1.63e-148
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   8 VDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANYL 87
Cdd:PTZ00244    4 VQTLIEKMLTVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  88 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDEK 167
Cdd:PTZ00244   84 FLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEK 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 168 IFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRAH 247
Cdd:PTZ00244  164 IICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAH 243

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1036967982 248 QVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQIL 295
Cdd:PTZ00244  244 QVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFLII 291
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 7-298 2.19e-134

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: 383.47  E-value: 2.19e-134
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   7 NVDSLIQRLLEmrsCRtgkqvQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANY 86
Cdd:cd07415     1 DLDQWIEQLKK---CE-----LLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  87 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NVKLWKTFTDCFNCLPVAAIID 165
Cdd:cd07415    73 LFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALID 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 166 EKIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDkDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICR 245
Cdd:cd07415   153 GQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPD-DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICR 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1036967982 246 AHQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKPS 298
Cdd:cd07415   232 AHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAA 284
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 59-284 7.43e-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: 323.94  E-value: 7.43e-112
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  59 IICGDIHGQYTDLLRLFEYGGFPPAANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE 138
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 139 ----CKRRYNVKLWKTFTDCFNCLPVAAIIDEKIFCCHGGLSPDLQGMEQIRRLmRPTDVPDTGLLCDLLWSDPDKDVQG 214
Cdd:cd00144    81 rtlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGD 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 215 WGENDRGVSFTFGVDVVSKFLNRHELDLICRAHQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTV 284
Cdd:cd00144   160 FESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 6-303 3.91e-101

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 299.81  E-value: 3.91e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982   6 LNVDSLIQRLLEMRScrtgkqvqMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAAN 85
Cdd:PTZ00239    1 MDIDRHIATLLNGGC--------LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNAN 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  86 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NVKLWKTFTDCFNCLPVAAII 164
Cdd:PTZ00239   73 YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALI 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 165 DEKIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDkDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLIC 244
Cdd:PTZ00239  153 EGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE-EVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLIC 231

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 245 RAHQVVEDGYEF-FARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSFQILKPSEKKAK 303
Cdd:PTZ00239  232 RAHQLVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAK 291
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 43-290 1.06e-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: 278.04  E-value: 1.06e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  43 EIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAANYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRG 122
Cdd:cd07416    30 EILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRG 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 123 NHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDEKIFCCHGGLSPDLQGMEQIRRLMRPTDVPDTGLLCD 202
Cdd:cd07416   110 NHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCD 189

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 203 LLWSDPDKDVQG------WGEND-RGVSFTFGVDVVSKFLNRHELDLICRAHQVVEDGYEFFARRQ------LVTLFSAP 269
Cdd:cd07416   190 LLWSDPLEDFGNektqehFVHNTvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAP 269

                         250       260
                  ....*....|....*....|.
gi 1036967982 270 NYCGEFDNAGGMMTVDDTLMC 290
Cdd:cd07416   270 NYLDVYNNKAAVLKYENNVMN 290
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 23-282 6.87e-92

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: 276.24  E-value: 6.87e-92
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  23 TGKQVQMTEAEVRGLCLKSREIFLQQPILLELEAPLIICGDIHGQYTDLLRLFEYGGFPPAA--------NYLFLGDYVD 94
Cdd:cd07419    15 VERRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEeagdieyiDYLFLGDYVD 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  95 RGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYN------VKLWKTFTDCFNCLPVAAIIDEKI 168
Cdd:cd07419    95 RGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRLFNWLPLAALIEDKI 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 169 FCCHGGLSPDLQGMEQIRRLMRPTDVPDTG-LLCDLLWSDP-DKD-VQGWGENDR-----GVSFTFGVDVVSKFLNRHEL 240
Cdd:cd07419   175 ICVHGGIGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPtENDsVLGLRPNAIdprgtGLIVKFGPDRVMEFLEENDL 254

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1036967982 241 DLICRAHQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMM 282
Cdd:cd07419   255 QMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAIL 296
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 39-285 5.05e-91

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: 274.13  E-value: 5.05e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  39 LKSREIFLQQPILLELEAP----LIICGDIHGQYTDLLRLFEYGGFPPAAN-YLFLGDYVDRGKQSLETICLLLAYKIKY 113
Cdd:cd07417    39 LQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 114 PENFFLLRGNHECASINRIYGFYDECKRRYNVKLWKTFTDCFNCLPVAAIIDEKIFCCHGGL-SPDLQGMEQIRRLMRPT 192
Cdd:cd07417   119 PNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 193 DVPDTGLLCDLLWSDPdKDVQGWGENDRGVSFTFGVDVVSKFLNRHELDLICRAHQVVEDGYEFFARRQLVTLFSAPNYC 272
Cdd:cd07417   199 QPPDSGLMCELLWSDP-QPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYC 277

                         250
                  ....*....|...
gi 1036967982 273 GEFDNAGGMMTVD 285
Cdd:cd07417   278 DQMGNKGAFIRFK 290
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 60-292 1.69e-60

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: 195.32  E-value: 1.69e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  60 ICGDIHGQYTDLLRLFEYGGFPPAAN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE 138
Cdd:cd07420    55 ICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKE 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 139 CKRRYNV---KLWKTFTDCFNCLPVAAIIDEKIFCCHGGLS--PDLQGMEQIRRLMRPTDVPDTGLLCDLLWSDPDKDVQ 213
Cdd:cd07420   135 VMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGISdsTDLDLLDKIDRHKYVSTKTEWQQVVDILWSDPKATKG 214

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036967982 214 GWGENDRGVSFTFGVDVVSKFLNRHELDLICRAHQVVEDGYEFFARRQLVTLFSAPNYCGEFDNAGGMMTVDDTLMCSF 292
Cdd:cd07420   215 CKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTPHF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 37-271 1.15e-47

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: 164.59  E-value: 1.15e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  37 LCLKSREIFLQQPILLELE----APLIICGDIHGQYTDLLRLFEYGGFP-PAANYLFLGDYVDRGKQSLETICLLLAYKI 111
Cdd:cd07418    43 LVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPdQNRFYVFNGDYVDRGAWGLETFLLLLSWKV 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 112 KYPENFFLLRGNHECASINRIYGFYDECKRRYN---VKLWKTFTDCFNCLPVAAIIDEKIFCCHGGL-------SPDLQG 181
Cdd:cd07418   123 LLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGdkgKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpKRKKQK 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982 182 MEQIRRLMRPTD--VPDTGLLCDL----------------------LWSDPDKDvQGWGEND-RGVSFTFGVDVVSKFLN 236
Cdd:cd07418   203 GKNRRVLLLEPEseSLKLGTLDDLmkarrsvldppgegsnlipgdvLWSDPSLT-PGLSPNKqRGIGLLWGPDCTEEFLE 281

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1036967982 237 RHELDLICRAHQ------------VVEDGYEF---FARRQLVTLFSAPNY 271
Cdd:cd07418   282 KNNLKLIIRSHEgpdarekrpglaGMNKGYTVdhdVESGKLITLFSAPDY 331
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 8-55 7.04e-22

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: 465300 [Multi-domain]  Cd Length: 48  Bit Score: 86.77  E-value: 7.04e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1036967982   8 VDSLIQRLLEMRSCRTGKQVQMTEAEVRGLCLKSREIFLQQPILLELE 55
Cdd:pfam16891   1 LDDIIERLLEVRGKPGGKQVQLSEAEIRALCRKAREIFLSQPMLLELE 48
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 57-164 2.50e-21

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: 87.27  E-value: 2.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  57 PLIICGDIH--GQYTDLLRLFEYGGFPPAANY-LFLGDYVDRGKQSlETICLLLAYKIKYpENFFLLRGNHECAsinriy 133
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLvLHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1036967982 134 gfYDECKRRY-----NVKLWKTFTDCFNCLPVAAII 164
Cdd:pfam00149  74 --YGECLRLYpylglLARPWKRFLEVFNFLPLAGIL 107
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 62-172 6.95e-11

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: 60.79  E-value: 6.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  62 GDIHGQYTDLLRLFEYGGFPPAANYLF-LGDYVDRGKQSLEtiCLLLaykIKYPEnFFLLRGNHECASINRIYGFYDECK 140
Cdd:cd07424     7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLE--VLEL---LKQPW-FHAVQGNHEQMAIDALRGGDDVMW 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1036967982 141 RRYNVKLW--------KTFTDCFNCLPVAAII---DEKIFCCH 172
Cdd:cd07424    81 RANGGGWFfdlpdeeaKVLLEKLHHLPIAIEVesrNGKVGIVH 123
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 59-125 2.67e-07

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: 48.80  E-value: 2.67e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1036967982  59 IICGDIHGQYTDLLRLF--EYGGFPPAANYLFLGDYVDRGKQSLETICLLLAyKIKYPENFFLLRGNHE 125
Cdd:cd00838     1 LVISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALR-LLLAGIPVYVVPGNHD 68
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
62-125 5.74e-07

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 50.16  E-value: 5.74e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036967982  62 GDIHGQYTDLLRLFEYGGFPPAANYL-FLGDYVDRGKQSLETicllLAYKIKYPENFFLLRGNHE 125
Cdd:PRK00166    7 GDIQGCYDELQRLLEKIDFDPAKDTLwLVGDLVNRGPDSLEV----LRFVKSLGDSAVTVLGNHD 67
PHA02239 PHA02239
putative protein phosphatase
 63-143 3.89e-06

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 47.30  E-value: 3.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  63 DIHGQYTDLLRLFE--YGGFPPAANYLFLGDYVDRGKQSLETICLLLAYkIKYPENFFLLRGNHE------CASINRIyG 134
Cdd:PHA02239    8 DIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDdefyniMENVDRL-S 85

                          90
                  ....*....|
gi 1036967982 135 FYD-ECKRRY 143
Cdd:PHA02239   86 IYDiEWLSRY 95
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 62-125 7.12e-06

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: 46.77  E-value: 7.12e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1036967982  62 GDIHGQYTDLLRLFEYGGFPPAANYL-FLGDYVDRGKQSLETicllLAYKIKYPENFFLLRGNHE 125
Cdd:cd07422     5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLET----LRFVKSLGDSAVVVLGNHD 65
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 58-127 1.67e-05

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: 45.96  E-value: 1.67e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1036967982  58 LIIC-GDIHGQYTDLLRLFE--YGGFPP----AANYLFLGDYVDRGKQSLETICLLLAYKIKYP-ENFFLLRGNHECA 127
Cdd:cd07421     3 VVICvGDIHGYISKLNNLWLnlQSALGPsdfaSALVIFLGDYCDRGPETRKVIDFLISLPEKHPkQRHVFLCGNHDFA 80
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 62-177 5.36e-05

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: 43.44  E-value: 5.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  62 GDIHGQYTDLLRLFEYGGFPP------AANYLF--LGDYVDRGKQSLETICLLLAYK---IKYPENFFLLRGNHECASI- 129
Cdd:cd07425     4 GDLHGDLDRLRTILKLAGVIDsndrwiGGDTVVvqTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLc 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1036967982 130 --------NRIYGFYDECKRRYnvKLWKTFTDCFNCL---PVAAIIDEKIFcCHGGLSP 177
Cdd:cd07425    84 gdfryvhpRGLNEFGGVAKRRY--ALLSDGGYIGRYLrthPVVLVVNDILF-VHGGLGP 139
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 59-181 1.08e-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: 1.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  59 IIcGDIHGQYTDLLRLFE---------YGGFPPAANYL-FLGDYVDRGKQSLEtiCLLLAYKIKYPENFFLLRGNHEcas 128
Cdd:cd07423     2 II-GDVHGCYDELVELLEklgyqkkeeGLYVHPEGRKLvFLGDLVDRGPDSID--VLRLVMNMVKAGKALYVPGNHC--- 75

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1036967982 129 iNRIYGF------------------YDECKRRYNVKLWKTFTDCFNCLPVAAIIDE-KIFCCHGGLSPDLQG 181
Cdd:cd07423    76 -NKLYRYlkgrnvqlahglettveeLEALSKEERPEFRERFAEFLESLPSHLVLDGgRLVVAHAGIKEEMIG 146
PRK09968 PRK09968
protein-serine/threonine phosphatase;
62-130 2.72e-04

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 41.42  E-value: 2.72e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  62 GDIHGQYTDLL-RLFEYGGFPPAANYLFLGDYVDRGKQSLETICLLlaykiKYPEnFFLLRGNHECASIN 130
Cdd:PRK09968   21 GDIHGEYQLLQsRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLL-----NQPW-FISVKGNHEAMALD 84
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 60-178 5.50e-04

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.84  E-value: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1036967982  60 ICGDIHGQYTDLLRLFEYGGF---------PPAANYLFLGDYVDRGKQSLETI---CLLLAYKIKYpenffLLRGNHeCa 127
Cdd:PRK13625    5 IIGDIHGCYQEFQALTEKLGYnwssglpvhPDQRKLAFVGDLTDRGPHSLRMIeivWELVEKKAAY-----YVPGNH-C- 77

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1036967982 128 siNRIYGFYdecKRRyNVKL----------WKT------------FTDCFNCLPVAAIIDE-KIFCCHGGLSPD 178
Cdd:PRK13625   78 --NKLYRFF---LGR-NVTIahglettvaeYEAlpshkqnmikekFITLYEQAPLYHILDEgRLVVAHAGIRQD 145
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
58-133 4.20e-03

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 38.07  E-value: 4.20e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1036967982  58 LIICGDIHGQYTDLLRLFEYGGFPPAANYLFLGDYVDRGKqsLETICLLLAYKIKYPENFFLLRGNHECASINRIY 133
Cdd:COG2129     2 ILAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGT--AEEAREVLEELAALGVPVLAVPGNHDDPEVLDAL 75
 
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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