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Conserved domains on  [gi|1333126177|ref|XP_023537569|]
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serine/threonine-protein phosphatase PP1-like [Cucurbita pepo subsp. pepo]

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 ...
 13-300 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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  13 VLDDIIRRLLEGRG---GKQVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANY 89
Cdd:cd07414     1 DIDSIIERLLEVRGsrpGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  90 LFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDD 169
Cdd:cd07414    81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 170 KILCMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRG 249
Cdd:cd07414   161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333126177 250 HQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKP 300
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 ...
 13-300 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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  13 VLDDIIRRLLEGRG---GKQVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANY 89
Cdd:cd07414     1 DIDSIIERLLEVRGsrpGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  90 LFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDD 169
Cdd:cd07414    81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 170 KILCMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRG 249
Cdd:cd07414   161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333126177 250 HQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKP 300
Cdd:cd07414   241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 14-317 6.23e-168

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 469.53  E-value: 6.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  14 LDDIIRRLLEGRG---GKQVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYL 90
Cdd:PTZ00480   11 VDNIIERLLSVRGskpGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  91 FLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDDK 170
Cdd:PTZ00480   91 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 171 ILCMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGH 250
Cdd:PTZ00480  171 ILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAH 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333126177 251 QVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKPELKPSGSSSGvilKKPP 317
Cdd:PTZ00480  251 QVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQGQGASQQ---NKPG 314
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 32-300 1.24e-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: 426.24  E-value: 1.24e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177   32 LSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYLFLGDYVDRGKQSLETICLLLA 111
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  112 YKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDDKILCMHGGISPDLKSLDQITQL 191
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  192 PRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSA 271
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260
                   ....*....|....*....|....*....
gi 1333126177  272 PNYGGEFDNAGALLSVDESLVCSFEILKP 300
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKP 269
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 14-58 8.56e-21

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: 83.69  E-value: 8.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1333126177  14 LDDIIRRLLEGR---GGKQVQLSEAEIRHLCVNARQIFLSQPNLLRLK 58
Cdd:pfam16891   1 LDDIIERLLEVRgkpGGKQVQLSEAEIRALCRKAREIFLSQPMLLELE 48
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 13-300 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: 570.05  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  13 VLDDIIRRLLEGRG---GKQVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANY 89
Cdd:cd07414     1 DIDSIIERLLEVRGsrpGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  90 LFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDD 169
Cdd:cd07414    81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDE 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 170 KILCMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRG 249
Cdd:cd07414   161 KIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRA 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1333126177 250 HQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKP 300
Cdd:cd07414   241 HQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 14-317 6.23e-168

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 469.53  E-value: 6.23e-168
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  14 LDDIIRRLLEGRG---GKQVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYL 90
Cdd:PTZ00480   11 VDNIIERLLSVRGskpGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYL 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  91 FLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDDK 170
Cdd:PTZ00480   91 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 171 ILCMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGH 250
Cdd:PTZ00480  171 ILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAH 250

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333126177 251 QVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKPELKPSGSSSGvilKKPP 317
Cdd:PTZ00480  251 QVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQGQGASQQ---NKPG 314
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 32-300 1.24e-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: 426.24  E-value: 1.24e-151
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177   32 LSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYLFLGDYVDRGKQSLETICLLLA 111
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  112 YKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDDKILCMHGGISPDLKSLDQITQL 191
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  192 PRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSA 271
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260
                   ....*....|....*....|....*....
gi 1333126177  272 PNYGGEFDNAGALLSVDESLVCSFEILKP 300
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKP 269
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 12-298 4.44e-133

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 380.02  E-value: 4.44e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  12 GVLDDIIRRLLEGRGG---KQVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSAN 88
Cdd:PTZ00244    2 SLVQTLIEKMLTVKGNrtqRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  89 YLFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLID 168
Cdd:PTZ00244   82 YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVIS 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 169 DKILCMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICR 248
Cdd:PTZ00244  162 EKIICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVR 241

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1333126177 249 GHQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEIL 298
Cdd:PTZ00244  242 AHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFLII 291
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 14-300 2.62e-132

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: 377.70  E-value: 2.62e-132
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  14 LDDIIRRLLEGRggkqvQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYLFLG 93
Cdd:cd07415     2 LDQWIEQLKKCE-----LLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  94 DYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRF-NVRLWKIFTDCFNCMPVAGLIDDKIL 172
Cdd:cd07415    77 DYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDGQIF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 173 CMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDPsIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQV 252
Cdd:cd07415   157 CVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDD-REGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQL 235

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1333126177 253 VEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKP 300
Cdd:cd07415   236 VMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 63-287 4.51e-108

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: 314.31  E-value: 4.51e-108
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  63 ICGDVHGQYKDLLRLFEYGGYPPSANYLFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDE- 141
Cdd:cd00144     2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDEr 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 142 ---CKRRFNVRLWKIFTDCFNCMPVAGLIDDKILCMHGGISPDLKSLDQITQLpRPTEIPDNGLLCDLLWSDPDPSIQGW 218
Cdd:cd00144    82 tlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGDF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333126177 219 ADSDRGISCTFGADRVVEFLEKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSV 287
Cdd:cd00144   161 ESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 14-299 1.20e-101

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 300.58  E-value: 1.20e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  14 LDDIIRRLLEGRGgkqvqLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYLFLG 93
Cdd:PTZ00239    3 IDRHIATLLNGGC-----LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  94 DYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRF-NVRLWKIFTDCFNCMPVAGLIDDKIL 172
Cdd:PTZ00239   78 DFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQIL 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 173 CMHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDPDpSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQV 252
Cdd:PTZ00239  158 CVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE-EVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQL 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1333126177 253 VEDGYEF-FAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILK 299
Cdd:PTZ00239  237 VMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFK 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 17-300 5.19e-98

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: 291.65  E-value: 5.19e-98
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  17 IIRRLLEGRGGK-----QVQLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYP------- 84
Cdd:cd07419     1 IIAHLLKPRGWKppverRFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPvteeagd 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  85 -PSANYLFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFN------VRLWKIFTDC 157
Cdd:cd07419    81 iEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 158 FNCMPVAGLIDDKILCMHGGISPDLKSLDQITQLPRPTEIPDNG-LLCDLLWSDP--DPSIQGWADSDR-----GISCTF 229
Cdd:cd07419   161 FNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITMEAGSpVVMDLLWSDPteNDSVLGLRPNAIdprgtGLIVKF 240

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333126177 230 GADRVVEFLEKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSAPNYGGEFDNAGALLSVDESLVCSFEILKP 300
Cdd:cd07419   241 GPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVVVPKLIHP 311
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 16-288 4.07e-93

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: 278.81  E-value: 4.07e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  16 DIIRR--LLEGRggkqvqLSEAEIRHLCVNARQIFLSQPNLLRLKAPMRICGDVHGQYKDLLRLFEYGGYPPSANYLFLG 93
Cdd:cd07416     4 DILKAhfMREGR------LSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLG 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  94 DYVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDDKILC 173
Cdd:cd07416    78 DYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLC 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 174 MHGGISPDLKSLDQITQLPRPTEIPDNGLLCDLLWSDP------DPSIQGWADSD-RGISCTFGADRVVEFLEKNDLDLI 246
Cdd:cd07416   158 VHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPledfgnEKTQEHFVHNTvRGCSYFYSYRAVCEFLQKNNLLSI 237

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 1333126177 247 CRGHQVVEDGYEFFAKRR------LVTIFSAPNYGGEFDNAGALLSVD 288
Cdd:cd07416   238 IRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYE 285
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 42-290 6.67e-89

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: 268.74  E-value: 6.67e-89
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  42 VNARQIFLSQPNLLRLKAP----MRICGDVHGQYKDLLRLFEYGGYPPSAN-YLFLGDYVDRGKQSLETICLLLAYKIRH 116
Cdd:cd07417    39 LQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLY 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 117 PNKVFLLRGNHEDAKINRIYGFYDECKRRFNVRLWKIFTDCFNCMPVAGLIDDKILCMHGGI-SPDLKSLDQITQLPRPT 195
Cdd:cd07417   119 PNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFR 198

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 196 EIPDNGLLCDLLWSDPDPSiQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQVVEDGYEFFAKRRLVTIFSAPNYG 275
Cdd:cd07417   199 QPPDSGLMCELLWSDPQPQ-PGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYC 277

                         250
                  ....*....|....*
gi 1333126177 276 GEFDNAGALLSVDES 290
Cdd:cd07417   278 DQMGNKGAFIRFKGS 292
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 44-295 5.08e-65

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: 206.88  E-value: 5.08e-65
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  44 ARQIFLSQPNLLRLKA----PMRICGDVHGQYKDLLRLFEYGGYPPSAN-YLFLGDYVDRGKQSLETICLLLAYKIRHPN 118
Cdd:cd07420    32 ARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPN 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 119 KVFLLRGNHEDAKINRIYGFYDECKRRFNV---RLWKIFTDCFNCMPVAGLIDDKILCMHGGISpDLKSLDQITQLPR-- 193
Cdd:cd07420   112 AVHLNRGNHEDHIMNLRYGFTKEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDLLDKIDRhk 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 194 ----PTEIPDnglLCDLLWSDPDPSIQGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQVVEDGYEFFAKRRLVTIF 269
Cdd:cd07420   191 yvstKTEWQQ---VVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIF 267

                         250       260
                  ....*....|....*....|....*.
gi 1333126177 270 SAPNYGGEFDNAGALLSVDESLVCSF 295
Cdd:cd07420   268 SASNYYEEGSNRGAYVKLGPQLTPHF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 25-274 5.40e-48

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: 164.97  E-value: 5.40e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  25 RGGKQVQLSEA----EIRHLCVNARQIFLSQPNLLRL----KAPMRICGDVHGQYKDLLRLFEYGGyPPSAN--YLFLGD 94
Cdd:cd07418    24 RNLPPSELPSVlpvnVFDSLVLTAHKILHREPNCVRIdvedVCEVVVVGDVHGQLHDVLFLLEDAG-FPDQNrfYVFNGD 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  95 YVDRGKQSLETICLLLAYKIRHPNKVFLLRGNHEDAKINRIYGFYDECKRRFNVR---LWKIFTDCFNCMPVAGLIDDKI 171
Cdd:cd07418   103 YVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRV 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177 172 LCMHGGI---------------------------SPDLKSLDQITQLPR-----PTE----IPDngllcDLLWSDPDPSI 215
Cdd:cd07418   183 YTAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRsvldpPGEgsnlIPG-----DVLWSDPSLTP 257

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333126177 216 QGWADSDRGISCTFGADRVVEFLEKNDLDLICRGHQvvedGYEFFAKR-------------------RLVTIFSAPNY 274
Cdd:cd07418   258 GLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHE----GPDAREKRpglagmnkgytvdhdvesgKLITLFSAPDY 331
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 14-58 8.56e-21

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: 83.69  E-value: 8.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 1333126177  14 LDDIIRRLLEGR---GGKQVQLSEAEIRHLCVNARQIFLSQPNLLRLK 58
Cdd:pfam16891   1 LDDIIERLLEVRgkpGGKQVQLSEAEIRALCRKAREIFLSQPMLLELE 48
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 61-167 1.17e-17

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: 77.25  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  61 MRI--CGDVH--GQYKDLLRLFEYGGyPPSANYLFL--GDYVDRGKQSlETICLLLAYKIRHpNKVFLLRGNHEDAkinr 134
Cdd:pfam00149   1 MRIlvIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD---- 73

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1333126177 135 iygfYDECKRRF-----NVRLWKIFTDCFNCMPVAGLI 167
Cdd:pfam00149  74 ----YGECLRLYpylglLARPWKRFLEVFNFLPLAGIL 107
PHA02239 PHA02239
putative protein phosphatase
 66-140 1.05e-07

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 51.92  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  66 DVHGQYKDLLRLFE--YGGYPPSANYLFLGDYVDRGKQSLETICLLLAYKIRHPNKVFLLrGNHED------AKINRIyG 137
Cdd:PHA02239    8 DIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHDDefynimENVDRL-S 85


                  ...
gi 1333126177 138 FYD 140
Cdd:PHA02239   86 IYD 88
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 63-134 1.29e-06

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: 48.67  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  63 ICGDVHGQYKDLLRLFEYGGYPPSANYL----------FLGDYVDRGKQSLEtiCLLLAYKIRHPNKVFLLRGNHEDaKI 132
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGYQKKEEGLyvhpegrklvFLGDLVDRGPDSID--VLRLVMNMVKAGKALYVPGNHCN-KL 78


                  ..
gi 1333126177 133 NR 134
Cdd:cd07423    79 YR 80
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 65-134 5.09e-06

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: 46.54  E-value: 5.09e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333126177  65 GDVHGQYKDLLRLFEYGGYPPSANYLF-LGDYVDRGKQSLEtiCLLLaykIRHPnKVFLLRGNHEDAKINR 134
Cdd:cd07424     7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLE--VLEL---LKQP-WFHAVQGNHEQMAIDA 71
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 65-128 6.69e-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: 6.69e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333126177  65 GDVHGQYKDLLRLFEYGGYPPSANYL-FLGDYVDRGKQSLETicllLAYKIRHPNKVFLLRGNHE 128
Cdd:cd07422     5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLET----LRFVKSLGDSAVVVLGNHD 65
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
65-128 9.79e-06

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 46.31  E-value: 9.79e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333126177  65 GDVHGQYKDLLRLFEYGGYPPSANYL-FLGDYVDRGKQSLETicllLAYKIRHPNKVFLLRGNHE 128
Cdd:PRK00166    7 GDIQGCYDELQRLLEKIDFDPAKDTLwLVGDLVNRGPDSLEV----LRFVKSLGDSAVTVLGNHD 67
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 61-130 1.15e-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: 46.34  E-value: 1.15e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333126177  61 MRIC-GDVHGQYKDLLRLFE--YGGYPP----SANYLFLGDYVDRGKQSLETICLLLAYKIRHPNK--VFLLrGNHEDA 130
Cdd:cd07421     3 VVICvGDIHGYISKLNNLWLnlQSALGPsdfaSALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQrhVFLC-GNHDFA 80
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 63-128 1.22e-05

metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also known as metallophosphoesterases, phosphodiesterases (PDEs), binuclear metallophosphoesterases, and dimetal-containing phosphoesterases (DMPs), represent a diverse superfamily of enzymes with a conserved domain containing an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. This superfamily includes: the phosphoprotein phosphatases (PPPs), Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 44.18  E-value: 1.22e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333126177  63 ICGDVHGQYKDLLRLF--EYGGYPPSANYLFLGDYVDRGKQSLETICLLLAyKIRHPNKVFLLRGNHE 128
Cdd:cd00838     2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALR-LLLAGIPVYVVPGNHD 68
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 63-139 1.96e-05

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 45.08  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  63 ICGDVHGQYKDLLRLFEYGGY---------PPSANYLFLGDYVDRGKQSLETICLLlaYKIRHPNKVFLLRGNHedakIN 133
Cdd:PRK13625    5 IIGDIHGCYQEFQALTEKLGYnwssglpvhPDQRKLAFVGDLTDRGPHSLRMIEIV--WELVEKKAAYYVPGNH----CN 78


                  ....*.
gi 1333126177 134 RIYGFY 139
Cdd:PRK13625   79 KLYRFF 84
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 65-180 4.26e-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: 40.74  E-value: 4.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333126177  65 GDVHGQYKDLLRLFEYGGYPPSANY--------LFLGDYVDRGKQSLETICLLLAYK---IRHPNKVFLLRGNHEdakIN 133
Cdd:cd07425     4 GDLHGDLDRLRTILKLAGVIDSNDRwiggdtvvVQTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHE---LM 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333126177 134 RIYG------------FYDECKRRF-----NVRLWKIFTDcfncMPVAGLIDDkILCMHGGISP 180
Cdd:cd07425    81 NLCGdfryvhprglneFGGVAKRRYallsdGGYIGRYLRT----HPVVLVVND-ILFVHGGLGP 139
PRK09968 PRK09968
protein-serine/threonine phosphatase;
65-128 2.75e-03

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 38.34  E-value: 2.75e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333126177  65 GDVHGQYKDLL-RLFEYGGYPPSANYLFLGDYVDRGKQSLETICLLlaykirhpNKVFL--LRGNHE 128
Cdd:PRK09968   21 GDIHGEYQLLQsRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLL--------NQPWFisVKGNHE 79
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 63-128 3.90e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. 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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 37.91  E-value: 3.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333126177  63 ICGDVHGQYKDLLRLFEYGGYP--------PSANYLFLGDYVDRGKQSLETICLLLAykIRHPNKVFLLRGNHE 128
Cdd:cd07413     3 LIGDVHGCAHTLDRLLDLLGYRlqggvwrhPRRQALFVGDLIDRGPRIREVLHRVHA--MVDAGEALCVMGNHE 74
 
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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