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Conserved domains on  [gi|18413493|ref|NP_567375|]
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Calcineurin-like metallo-phosphoesterase superfamily protein [Arabidopsis thaliana]

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 ...
 6-294 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: 608.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   6 LDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYL 85
Cdd:cd07414   2 IDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  86 FLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDK 165
Cdd:cd07414  82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 166 ILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAH 245
Cdd:cd07414 162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAH 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18413493 246 QVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILK 294
Cdd:cd07414 242 QVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 6-294 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: 608.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   6 LDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYL 85
Cdd:cd07414   2 IDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  86 FLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDK 165
Cdd:cd07414  82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 166 ILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAH 245
Cdd:cd07414 162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAH 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18413493 246 QVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILK 294
Cdd:cd07414 242 QVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 3-309 3.68e-176

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 490.33  E-value: 3.68e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    3 ETLLDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAA 82
Cdd:PTZ00480   8 EIDVDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPES 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   83 NYLFLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALI 162
Cdd:PTZ00480  88 NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  163 DDKILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLIC 242
Cdd:PTZ00480 168 DEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLIC 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18413493  243 RAHQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILKASEkKGRFGFNNNVP 309
Cdd:PTZ00480 248 RAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAE-QGQGASQQNKP 313
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 27-297 1.84e-154

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: 433.18  E-value: 1.84e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493     27 ITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYLFLGDYVDRGKQSIETICLLLA 106
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    107 YKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDKILCMHGGLSPDIKSLDDIRRI 186
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    187 PRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQLVTIFSA 266
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 18413493    267 PNYCGEFDNAGALMSVDDSLTCSFQILKASE 297
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 6-53 5.97e-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: 5.97e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 18413493     6 LDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELE 53
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 ...
 6-294 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: 608.57  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   6 LDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYL 85
Cdd:cd07414   2 IDSIIERLLEVRGSRPGKNVQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYL 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  86 FLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDK 165
Cdd:cd07414  82 FLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEK 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 166 ILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAH 245
Cdd:cd07414 162 IFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAH 241

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 18413493 246 QVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILK 294
Cdd:cd07414 242 QVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 3-309 3.68e-176

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 490.33  E-value: 3.68e-176
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    3 ETLLDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAA 82
Cdd:PTZ00480   8 EIDVDNIIERLLSVRGSKPGKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPES 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   83 NYLFLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALI 162
Cdd:PTZ00480  88 NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  163 DDKILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLIC 242
Cdd:PTZ00480 168 DEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLIC 247

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18413493  243 RAHQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILKASEkKGRFGFNNNVP 309
Cdd:PTZ00480 248 RAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAE-QGQGASQQNKP 313
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 27-297 1.84e-154

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: 433.18  E-value: 1.84e-154
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493     27 ITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYLFLGDYVDRGKQSIETICLLLA 106
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    107 YKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDKILCMHGGLSPDIKSLDDIRRI 186
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKL 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    187 PRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQLVTIFSA 266
Cdd:smart00156 161 KRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSA 240

                          250       260       270
                   ....*....|....*....|....*....|.
gi 18413493    267 PNYCGEFDNAGALMSVDDSLTCSFQILKASE 297
Cdd:smart00156 241 PNYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 4-296 1.06e-148

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 419.70  E-value: 1.06e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    4 TLLDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAAN 83
Cdd:PTZ00244   2 SLVQTLIEKMLTVKGNRTQRQILIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   84 YLFLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALID 163
Cdd:PTZ00244  82 YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVIS 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  164 DKILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICR 243
Cdd:PTZ00244 162 EKIICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVR 241

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18413493  244 AHQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILKAS 296
Cdd:PTZ00244 242 AHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFLIIPAR 294
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 6-296 9.80e-139

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: 393.87  E-value: 9.80e-139
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   6 LDDIIRRLLatnngrtvKQAQITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYL 85
Cdd:cd07415   2 LDQWIEQLK--------KCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYL 73

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  86 FLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRY-NVRLWKTFTECFNCLPVSALIDD 164
Cdd:cd07415  74 FLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPLAALIDG 153

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 165 KILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDrEIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRA 244
Cdd:cd07415 154 QIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPD-DREGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRA 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 18413493 245 HQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILKAS 296
Cdd:cd07415 233 HQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAA 284
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 58-282 7.79e-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: 313.54  E-value: 7.79e-108
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  58 ICGDVHGQFPDLLRLFEYGGYPPAANYLFLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDE- 136
Cdd:cd00144   2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDEr 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 137 ---CKRRYNVRLWKTFTECFNCLPVSALIDDKILCMHGGLSPDIKSLDDIRRIpRPIDVPDQGILCDLLWADPDREIQGW 213
Cdd:cd00144  82 tlrCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGDF 160

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18413493 214 GENDRGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSV 282
Cdd:cd00144 161 ESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 8-295 7.68e-105

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 308.67  E-value: 7.68e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    8 DIIRRLLATNNGRTvkqaqITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYLFL 87
Cdd:PTZ00239   2 DIDRHIATLLNGGC-----LPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFI 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   88 GDYVDRGKQSIETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRY-NVRLWKTFTECFNCLPVSALIDDKI 166
Cdd:PTZ00239  77 GDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQI 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  167 LCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILCDLLWADPDrEIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAHQ 246
Cdd:PTZ00239 157 LCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE-EVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQ 235

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 18413493  247 VVEDGYEF-FAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLTCSFQILKA 295
Cdd:PTZ00239 236 LVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKE 285
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 40-283 4.24e-96

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: 286.51  E-value: 4.24e-96
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  40 KEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAANYLFLGDYVDRGKQSIETICLLLAYKVKYKFNFFLLR 119
Cdd:cd07416  29 AEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLR 108

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 120 GNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDKILCMHGGLSPDIKSLDDIRRIPRPIDVPDQGILC 199
Cdd:cd07416 109 GNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMC 188

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 200 DLLWADPDREIQG------WGEND-RGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQ------LVTIFSA 266
Cdd:cd07416 189 DLLWSDPLEDFGNektqehFVHNTvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSA 268

                       250
                ....*....|....*..
gi 18413493 267 PNYCGEFDNAGALMSVD 283
Cdd:cd07416 269 PNYLDVYNNKAAVLKYE 285
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 34-315 1.39e-94

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: 282.99  E-value: 1.39e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  34 QLCLASKEVFLSQPNLLELEAP----IKICGDVHGQFPDLLRLFEYGGYPPAAN-YLFLGDYVDRGKQSIETICLLLAYK 108
Cdd:cd07417  36 QILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFK 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 109 VKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVRLWKTFTECFNCLPVSALIDDKILCMHGGL-SPDIKSLDDIRRIP 187
Cdd:cd07417 116 LLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKID 195

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 188 RPIDVPDQGILCDLLWADPdREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQLVTIFSAP 267
Cdd:cd07417 196 RFRQPPDSGLMCELLWSDP-QPQPGRGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAP 274

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 18413493 268 NYCGEFDNAGAlmsvddsltcsFQILKASEKKGRFGFNNNVPRPGTPP 315
Cdd:cd07417 275 NYCDQMGNKGA-----------FIRFKGSDLKPKFTQFEAVPHPNVKP 311
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 27-287 1.70e-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: 277.78  E-value: 1.70e-92
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  27 ITETEIRQLCLASKEVFLSQPNLLELEAPIKICGDVHGQFPDLLRLFEYGGYPPAA--------NYLFLGDYVDRGKQSI 98
Cdd:cd07419  21 FDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEeagdieyiDYLFLGDYVDRGSHSL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  99 ETICLLLAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYN------VRLWKTFTECFNCLPVSALIDDKILCMHGG 172
Cdd:cd07419 101 ETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRLFNWLPLAALIEDKIICVHGG 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 173 LSPDIKSLDDIRRIPRPIDVP-DQGILCDLLWADP--DREIQGWGENDR-----GVSYTFGADKVAEFLQTHDLDLICRA 244
Cdd:cd07419 181 IGRSINHIHQIENLKRPITMEaGSPVVMDLLWSDPteNDSVLGLRPNAIdprgtGLIVKFGPDRVMEFLEENDLQMIIRA 260

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 18413493 245 HQVVEDGYEFFAKRQLVTIFSAPNYCGEFDNAGALMSVDDSLT 287
Cdd:cd07419 261 HECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLV 303
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 39-290 2.54e-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: 194.93  E-value: 2.54e-60
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  39 SKEVFLSQPNLLELEA----PIKICGDVHGQFPDLLRLFEYGGYPPAAN-YLFLGDYVDRGKQSIETICLLLAYKVKYKF 113
Cdd:cd07420  32 ARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPN 111

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 114 NFFLLRGNHECASINRVYGFYDECKRRYNV---RLWKTFTECFNCLPVSALIDDKILCMHGGLSpDIKSLDDIRRIPRPI 190
Cdd:cd07420 112 AVHLNRGNHEDHIMNLRYGFTKEVMQKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDLLDKIDRHK 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 191 DVPD----QGILcDLLWADPDREIQGWGENDRGVSYTFGADKVAEFLQTHDLDLICRAHQVVEDGYEFFAKRQLVTIFSA 266
Cdd:cd07420 191 YVSTktewQQVV-DILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSA 269

                       250       260
                ....*....|....*....|....
gi 18413493 267 PNYCGEFDNAGALMSVDDSLTCSF 290
Cdd:cd07420 270 SNYYEEGSNRGAYVKLGPQLTPHF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 31-269 1.33e-46

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: 161.51  E-value: 1.33e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  31 EIRQLCLASKEVFLSQPNLLELE----APIKICGDVHGQFPDLLRLFEYGGyPPAAN--YLFLGDYVDRGKQSIETICLL 104
Cdd:cd07418  39 VFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAG-FPDQNrfYVFNGDYVDRGAWGLETFLLL 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 105 LAYKVKYKFNFFLLRGNHECASINRVYGFYDECKRRYNVR---LWKTFTECFNCLPVSALIDDKILCMHGGL-------- 173
Cdd:cd07418 118 LSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpk 197

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493 174 -------------------SPDIKSLDDIRRIPRP-IDVPDQG---ILCDLLWADPDREiQGWGEND-RGVSYTFGADKV 229
Cdd:cd07418 198 rkkqkgknrrvlllepeseSLKLGTLDDLMKARRSvLDPPGEGsnlIPGDVLWSDPSLT-PGLSPNKqRGIGLLWGPDCT 276

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 18413493 230 AEFLQTHDLDLICRAHQvvedGYEFFAKR-------------------QLVTIFSAPNY 269
Cdd:cd07418 277 EEFLEKNNLKLIIRSHE----GPDAREKRpglagmnkgytvdhdvesgKLITLFSAPDY 331
STPPase_N pfam16891
Serine-threonine protein phosphatase N-terminal domain; This family is often found at the ...
 6-53 5.97e-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: 5.97e-22
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 18413493     6 LDDIIRRLLATNNGRTVKQAQITETEIRQLCLASKEVFLSQPNLLELE 53
Cdd:pfam16891   1 LDDIIERLLEVRGKPGGKQVQLSEAEIRALCRKAREIFLSQPMLLELE 48
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 55-162 9.93e-20

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: 83.03  E-value: 9.93e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493    55 PIKICGDVH--GQFPDLLRLFEYGGyPPAANYLFL--GDYVDRGKQSiETICLLLAYKVKYKfNFFLLRGNHECAsinrv 130
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKYV-PVYLVRGNHDFD----- 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 18413493   131 ygfYDECKRRY-----NVRLWKTFTECFNCLPVSALI 162
Cdd:pfam00149  74 ---YGECLRLYpylglLARPWKRFLEVFNFLPLAGIL 107
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 60-158 3.57e-07

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: 50.01  E-value: 3.57e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  60 GDVHGQFPDLLRLFEYGGYPPAANYLF-LGDYVDRGKQSIETICLLlaykvkyKFN-FFLLRGNHECASINRVYGFYDEC 137
Cdd:cd07424   7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLEVLELL-------KQPwFHAVQGNHEQMAIDALRGGDDVM 79

                        90       100
                ....*....|....*....|....*....
gi 18413493 138 KRRYNVRLW--------KTFTECFNCLPV 158
Cdd:cd07424  80 WRANGGGWFfdlpdeeaKVLLEKLHHLPI 108
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 58-123 1.33e-06

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: 46.88  E-value: 1.33e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 18413493  58 ICGDVHGQFPDLLRLF--EYGGYPPAANYLFLGDYVDRGKQSIETICLLLAyKVKYKFNFFLLRGNHE 123
Cdd:cd00838   2 VISDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALR-LLLAGIPVYVVPGNHD 68
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 60-175 1.86e-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: 44.98  E-value: 1.86e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493  60 GDVHGQFPDLLRLFEYGG------YPPAANYLF--LGDYVDRGKQSIETICLLL-----AYKVKYKfnFFLLRGNHE--- 123
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGvidsndRWIGGDTVVvqTGDILDRGDDEIEILKLLEklkrqARKAGGK--VILLLGNHElmn 81

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18413493 124 -CASINRVY-----GFYDECKRRYnvRLWKTFTECFNCL---PVSALIDDkILCMHGGLSP 175
Cdd:cd07425  82 lCGDFRYVHprglnEFGGVAKRRY--ALLSDGGYIGRYLrthPVVLVVND-ILFVHGGLGP 139
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 58-103 7.16e-05

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: 43.27  E-value: 7.16e-05
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 18413493  58 ICGDVHGQFPDLLRLFEYGGYPPAANYL----------FLGDYVDRGKQSIETICL 103
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYQKKEEGLyvhpegrklvFLGDLVDRGPDSIDVLRL 57
PHA02239 PHA02239
putative protein phosphatase
 56-141 1.21e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 42.67  E-value: 1.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   56 IKICGDVHGQFPDLLRLFE--YGGYPPAANYLFLGDYVDRGKQSIETiclllaykVKYKFNFFL-------LRGNHE--- 123
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDV--------VNYIFDLMSnddnvvtLLGNHDdef 74

                         90       100
                 ....*....|....*....|..
gi 18413493  124 ---CASINRVyGFYD-ECKRRY 141
Cdd:PHA02239  75 yniMENVDRL-SIYDiEWLSRY 95
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 58-125 2.84e-03

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 163664  Cd Length: 304  Bit Score: 39.02  E-value: 2.84e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18413493  58 IC-GDVHGQFPDLLRLFE--YGGYPP----AANYLFLGDYVDRGKQSIETICLLLAYKVKY-KFNFFLLRGNHECA 125
Cdd:cd07421   5 ICvGDIHGYISKLNNLWLnlQSALGPsdfaSALVIFLGDYCDRGPETRKVIDFLISLPEKHpKQRHVFLCGNHDFA 80
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 56-134 3.23e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 38.53  E-value: 3.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18413493   56 IKICGDVHGQFPDLLRLFEYGGY---------PPAANYLFLGDYVDRGKQS---IETICLLLAYKVKYkfnffLLRGNHe 123
Cdd:PRK13625   3 YDIIGDIHGCYQEFQALTEKLGYnwssglpvhPDQRKLAFVGDLTDRGPHSlrmIEIVWELVEKKAAY-----YVPGNH- 76

                         90
                 ....*....|.
gi 18413493  124 CasiNRVYGFY 134
Cdd:PRK13625  77 C---NKLYRFF 84
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
60-101 7.58e-03

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 37.45  E-value: 7.58e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 18413493   60 GDVHGQFPDLLRLFEYGGYPPAANYL-FLGDYVDRGKQSIETI 101
Cdd:PRK00166   7 GDIQGCYDELQRLLEKIDFDPAKDTLwLVGDLVNRGPDSLEVL 49
 
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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