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Conserved domains on  [gi|17552284|ref|NP_499528|]
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Serine/threonine-protein phosphatase [Caenorhabditis elegans]

Protein Classification

serine/threonine protein phosphatase( domain architecture ID 12191156)

protein phosphatase specific for serine and threonine, similar to Methanosarcina thermophila serine/threonine-protein phosphatase PP1-arch2 and Caenorhabditis elegans putative serine/threonine-protein phosphatase C23G10.1

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 106-360 2.48e-111

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: 326.48  E-value: 2.48e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    106 ALLELQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAI 185
Cdd:smart00156  22 NLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSM 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    186 NKNYGFHAELKKRFQREevyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKtHPLACDL 265
Cdd:smart00156 102 NEIYGFYDECKRKYGER-----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPD-DGLLIDL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    266 LWADPEKDAKGFEPNkIRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVV 345
Cdd:smart00156 176 LWSDPDQPVNGFGPS-IRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVL 254

                          250
                   ....*....|....*
gi 17552284    346 VVNKMLELSFVQLKP 360
Cdd:smart00156 255 KVDKDLKLTFEQFKP 269
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 106-360 2.48e-111

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: 326.48  E-value: 2.48e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    106 ALLELQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAI 185
Cdd:smart00156  22 NLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSM 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    186 NKNYGFHAELKKRFQREevyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKtHPLACDL 265
Cdd:smart00156 102 NEIYGFYDECKRKYGER-----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPD-DGLLIDL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    266 LWADPEKDAKGFEPNkIRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVV 345
Cdd:smart00156 176 LWSDPDQPVNGFGPS-IRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVL 254

                          250
                   ....*....|....*
gi 17552284    346 VVNKMLELSFVQLKP 360
Cdd:smart00156 255 KVDKDLKLTFEQFKP 269
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 43-360 1.79e-104

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: 309.66  E-value: 1.79e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  43 LTDMIKKLLKPVFS---KAIMFDEKEIHVLLTRVFKYYTSPPNkktapsasasattsmsppkpaanaLLELQAPINICGD 119
Cdd:cd07414   2 IDSIIERLLEVRGSrpgKNVQLTEAEIRGLCLKSREIFLSQPI------------------------LLELEAPLKICGD 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 120 THGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFHAELKKRF 199
Cdd:cd07414  58 IHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 200 QREevyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHpLACDLLWADPEKDAKGFEP 279
Cdd:cd07414 138 NIK-----LWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQG-LLCDLLWSDPDKDVQGWGE 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 280 NKiRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVVNKMLELSFVQLK 359
Cdd:cd07414 212 ND-RGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290


                .
gi 17552284 360 P 360
Cdd:cd07414 291 P 291
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 46-356 2.31e-91

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 276.40  E-value: 2.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284   46 MIKKLL---KPVFSKAIMFDEKEIHVLLTRVFKYYTSPPnkktapsasasattsmsppkpaanALLELQAPINICGDTHG 122
Cdd:PTZ00244   7 LIEKMLtvkGNRTQRQILIREEDIRAVLTEVREIFMSQP------------------------MLLEIRPPVRVCGDTHG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  123 QYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFHAELKKRFQRE 202
Cdd:PTZ00244  63 QYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  203 evyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHPLaCDLLWADPEKDAKGFEPNKi 282
Cdd:PTZ00244 143 -----LFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGIL-CDLLWADPEDEVRGFLESD- 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17552284  283 RAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVVNKMLELSFV 356
Cdd:PTZ00244 216 RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFL 289
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 113-226 3.94e-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: 76.48  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284   113 PINICGDTH--GQYNDLLRIFNACGAATKTQY-LFLGDYVDRGGHSLEVimLLFSLKLAMPRKMHLLRGNHELkainkny 189
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLvLHAGDLVDRGPPSEEV--LELLERLIKYVPVYLVRGNHDF------- 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17552284   190 gFHAELKKRFQREEVYESVYNHFNQVFSYMPLCAIVS 226
Cdd:pfam00149  73 -DYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILS 108
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
116-181 5.20e-04

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 40.67  E-value: 5.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552284 116 ICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVimllfsLKLAMPRKMHLLRGNHE 181
Cdd:COG0622   4 VISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEV------LDLLRELPIVAVRGNHD 63
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 106-360 2.48e-111

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: 326.48  E-value: 2.48e-111
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    106 ALLELQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAI 185
Cdd:smart00156  22 NLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSM 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    186 NKNYGFHAELKKRFQREevyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKtHPLACDL 265
Cdd:smart00156 102 NEIYGFYDECKRKYGER-----IYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPD-DGLLIDL 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284    266 LWADPEKDAKGFEPNkIRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVV 345
Cdd:smart00156 176 LWSDPDQPVNGFGPS-IRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVL 254

                          250
                   ....*....|....*
gi 17552284    346 VVNKMLELSFVQLKP 360
Cdd:smart00156 255 KVDKDLKLTFEQFKP 269
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 43-360 1.79e-104

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: 309.66  E-value: 1.79e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  43 LTDMIKKLLKPVFS---KAIMFDEKEIHVLLTRVFKYYTSPPNkktapsasasattsmsppkpaanaLLELQAPINICGD 119
Cdd:cd07414   2 IDSIIERLLEVRGSrpgKNVQLTEAEIRGLCLKSREIFLSQPI------------------------LLELEAPLKICGD 57

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 120 THGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFHAELKKRF 199
Cdd:cd07414  58 IHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY 137

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 200 QREevyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHpLACDLLWADPEKDAKGFEP 279
Cdd:cd07414 138 NIK-----LWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQG-LLCDLLWSDPDKDVQGWGE 211

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 280 NKiRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVVNKMLELSFVQLK 359
Cdd:cd07414 212 ND-RGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290


                .
gi 17552284 360 P 360
Cdd:cd07414 291 P 291
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 116-347 3.86e-94

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: 281.18  E-value: 3.86e-94
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 116 ICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFHAEL 195
Cdd:cd00144   2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDER 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 196 KKRFQREEVyESVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKthPLACDLLWADPEkDAK 275
Cdd:cd00144  82 TLRCLRKGG-EELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIENPDD--QLVEDLLWSDPD-ESV 157

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 17552284 276 GFEPNKIRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVV 347
Cdd:cd00144 158 GDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 46-356 2.31e-91

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 276.40  E-value: 2.31e-91
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284   46 MIKKLL---KPVFSKAIMFDEKEIHVLLTRVFKYYTSPPnkktapsasasattsmsppkpaanALLELQAPINICGDTHG 122
Cdd:PTZ00244   7 LIEKMLtvkGNRTQRQILIREEDIRAVLTEVREIFMSQP------------------------MLLEIRPPVRVCGDTHG 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  123 QYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFHAELKKRFQRE 202
Cdd:PTZ00244  63 QYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIK 142

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  203 evyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHPLaCDLLWADPEKDAKGFEPNKi 282
Cdd:PTZ00244 143 -----LFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGIL-CDLLWADPEDEVRGFLESD- 215

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 17552284  283 RAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVVNKMLELSFV 356
Cdd:PTZ00244 216 RGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFL 289
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 108-360 7.44e-82

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: 251.74  E-value: 7.44e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 108 LELQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINK 187
Cdd:cd07415  38 QRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQ 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 188 NYGFHAELKKRFQReevyESVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHPLaCDLLW 267
Cdd:cd07415 118 VYGFYDECLRKYGN----ANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPM-CDLLW 192

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 268 ADPEkDAKGFEPNKiRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVV 347
Cdd:cd07415 193 SDPD-DREGWGISP-RGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILEL 270

                       250
                ....*....|...
gi 17552284 348 NKMLELSFVQLKP 360
Cdd:cd07415 271 DEHLNRSFKQFEA 283
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 107-362 6.40e-78

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 243.03  E-value: 6.40e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  107 LLELQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAIN 186
Cdd:PTZ00480  54 LLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASIN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  187 KNYGFHAELKKRFQREevyesVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHpLACDLL 266
Cdd:PTZ00480 134 RIYGFYDECKRRYTIK-----LWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTG-LLCDLL 207

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  267 WADPEKDAKGFEPNKiRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVV 346
Cdd:PTZ00480 208 WSDPDKDVQGWADNE-RGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMT 286

                        250
                 ....*....|....*.
gi 17552284  347 VNKMLELSFVQLKPED 362
Cdd:PTZ00480 287 IDESLMCSFQILKPAE 302
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 107-353 1.07e-74

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: 234.26  E-value: 1.07e-74
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 107 LLELQAPINICGDTHGQYNDLLRIF--------NACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRG 178
Cdd:cd07419  43 VLRLRAPIKIFGDIHGQFGDLMRLFdeygspvtEEAGDIEYIDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRG 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 179 NHELKAINKNYGFHAELKKRFqREEVYE--SVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETA 256
Cdd:cd07419 123 NHEAADINALFGFREECIERL-GEDIRDgdSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPITME 201

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 257 KTHPLACDLLWADP-EKDA-KGFEPNKIRAISN----VFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFS 330
Cdd:cd07419 202 AGSPVVMDLLWSDPtENDSvLGLRPNAIDPRGTglivKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFS 281

                       250       260
                ....*....|....*....|...
gi 17552284 331 ASRYQIELCNYAAVVVVNKMLEL 353
Cdd:cd07419 282 ATNYCGTAGNAGAILVLGRDLVV 304
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 107-345 2.98e-67

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: 214.86  E-value: 2.98e-67
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 107 LLELQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAIN 186
Cdd:cd07416  38 LLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLT 117

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 187 KNYGFHAELKKRFQreevyESVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHPLaCDLL 266
Cdd:cd07416 118 EYFTFKQECKIKYS-----ERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPM-CDLL 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 267 WADP------EKDAKGFEPNKIRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRR------LITVFSASRY 334
Cdd:cd07416 192 WSDPledfgnEKTQEHFVHNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNY 271

                       250
                ....*....|.
gi 17552284 335 QIELCNYAAVV 345
Cdd:cd07416 272 LDVYNNKAAVL 282
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 110-382 7.38e-64

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 206.21  E-value: 7.38e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  110 LQAPINICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNY 189
Cdd:PTZ00239  41 VRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVY 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  190 GFHAELKKRFQReevyESVYNHFNQVFSYMPLCAIVSKRILCMHGGISPHLKSLDDIRAIPLPLETAKTHPLaCDLLWAD 269
Cdd:PTZ00239 121 GFYEEILRKYGN----SNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPF-CDLMWSD 195

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  270 PEkDAKGFEPNKiRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAF-FADRRLITVFSASRYQIELCNYAAVVVVN 348
Cdd:PTZ00239 196 PE-EVEYWAVNS-RGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLD 273

                        250       260       270
                 ....*....|....*....|....*....|....
gi 17552284  349 KMLELSFVQLKpedfevrrdECEENAKDQTTSNV 382
Cdd:PTZ00239 274 ENLQQTWKTFK---------EVPESAKSINPKNV 298
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 114-357 1.43e-62

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: 203.26  E-value: 1.43e-62
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 114 INICGDTHGQYNDLLRIFNACGAATKTQ-YLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFH 192
Cdd:cd07417  62 ITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFE 141

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 193 AELKKRFQreevyESVYNHFNQVFSYMPLCAIVSKRILCMHGGI-SPHLKSLDDIRAI---PLPLETAkthpLACDLLWA 268
Cdd:cd07417 142 GEVKAKYN-----EQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIdrfRQPPDSG----LMCELLWS 212

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 269 DPEKdAKGFEPNKiRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVVN 348
Cdd:cd07417 213 DPQP-QPGRGPSK-RGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFK 290

                       250
                ....*....|
gi 17552284 349 KM-LELSFVQ 357
Cdd:cd07417 291 GSdLKPKFTQ 300
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 114-357 6.83e-49

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: 167.20  E-value: 6.83e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 114 INICGDTHGQYNDLLRIFNACG-AATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFH 192
Cdd:cd07420  53 VTICGDLHGKLDDLLLIFYKNGlPSPENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFT 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 193 AELKKRFQREEvyESVYNHFNQVFSYMPLCAIVSKRILCMHGGISPH-----LKSLDDIRAIPLPLETAKThplaCDLLW 267
Cdd:cd07420 133 KEVMQKYKDHG--KKILRLLEDVFSWLPLATIIDNKVLVVHGGISDStdldlLDKIDRHKYVSTKTEWQQV----VDILW 206

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 268 ADPeKDAKGFEPNKIRAISNVFGKKEVDDLCKRLDIDLIVRAHQVVEYGYAFFADRRLITVFSASRYQIELCNYAAVVVV 347
Cdd:cd07420 207 SDP-KATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKL 285

                       250
                ....*....|
gi 17552284 348 NKMLELSFVQ 357
Cdd:cd07420 286 GPQLTPHFVQ 295
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 116-364 1.61e-36

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: 136.47  E-value: 1.61e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 116 ICGDTHGQYNDLLRIFNACGAATKTQ-YLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLRGNHELKAINKNYGFHAE 194
Cdd:cd07418  70 VVGDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQE 149

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 195 LKKRFQREEvyESVYNHFNQVFSYMPLCAIVSKRILCMHGGI---------------------------SPHLKSLDDI- 246
Cdd:cd07418 150 VLTKYGDKG--KHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLm 227

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 247 --RAIPLPLETAKTHPLACDLLWADPEKDaKGFEPNKIRAISNVFGKKEVDDLCKRLDIDLIVRAHQ------------V 312
Cdd:cd07418 228 kaRRSVLDPPGEGSNLIPGDVLWSDPSLT-PGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaG 306

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 17552284 313 VEYGYAFFAD---RRLITVFSASRY-QIELC-----NYAAvvvvnkmlelsFVQLKPEDFE 364
Cdd:cd07418 307 MNKGYTVDHDvesGKLITLFSAPDYpQFQATeerynNKGA-----------YIILQPPDFS 356
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 113-226 3.94e-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: 76.48  E-value: 3.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284   113 PINICGDTH--GQYNDLLRIFNACGAATKTQY-LFLGDYVDRGGHSLEVimLLFSLKLAMPRKMHLLRGNHELkainkny 189
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLvLHAGDLVDRGPPSEEV--LELLERLIKYVPVYLVRGNHDF------- 72

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 17552284   190 gFHAELKKRFQREEVYESVYNHFNQVFSYMPLCAIVS 226
Cdd:pfam00149  73 -DYGECLRLYPYLGLLARPWKRFLEVFNFLPLAGILS 108
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 118-238 5.02e-08

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: 52.69  E-value: 5.02e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 118 GDTHGQYNDLLRIFNACG--------AATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPR---KMHLLRGNHELKAIN 186
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGvidsndrwIGGDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKaggKVILLLGNHELMNLC 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 17552284 187 KNygFHA----ELKKRFQREEVYESVYNHFNQVFSY---MPLCAIVSKrILCMHGGISP 238
Cdd:cd07425  84 GD--FRYvhprGLNEFGGVAKRRYALLSDGGYIGRYlrtHPVVLVVND-ILFVHGGLGP 139
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 118-186 1.49e-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: 51.16  E-value: 1.49e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 118 GDTHGQYNDLLRIFNACGAATKTQYLF-LGDYVDRGGHSLEVIMLlfslkLAMPRkMHLLRGNHELKAIN 186
Cdd:cd07424   7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLEVLEL-----LKQPW-FHAVQGNHEQMAID 70
PHA02239 PHA02239
putative protein phosphatase
 114-181 4.64e-07

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 50.38  E-value: 4.64e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  114 INICGDTHGQYNDLLRIFNACGAATKTQ--YLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLLrGNHE 181
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKINNERKPEetIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHD 71
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 115-214 1.90e-05

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: 45.23  E-value: 1.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 115 NICGDTHGQYNDLLRIFNACGAATKT--------QYLFLGDYVDRGGHSLEVIMLLFSLKLAmpRKMHLLRGNHELKAIn 186
Cdd:cd07413   2 DLIGDVHGCAHTLDRLLDLLGYRLQGgvwrhprrQALFVGDLIDRGPRIREVLHRVHAMVDA--GEALCVMGNHEFNAL- 78

                        90       100
                ....*....|....*....|....*...
gi 17552284 187 knyGFHAELKKRFQREEVYESVYNHFNQ 214
Cdd:cd07413  79 ---AWHTPAPPGSGRQYVREHSPKNARQ 103
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
118-289 2.99e-05

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 45.16  E-value: 2.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  118 GDTHGQYNDLLRI-----FNAcgaaTKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMprKMHLlrGNHELKAINKNYGFh 192
Cdd:PRK00166   7 GDIQGCYDELQRLlekidFDP----AKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSA--VTVL--GNHDLHLLAVAAGI- 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  193 AELKKRfqreevyesvyNHFNQVFS------------YMPLCAIVSKRILCM-HGGISPHLkSLDDIRAIPLPLETAKTH 259
Cdd:PRK00166  78 KRNKKK-----------DTLDPILEapdrdelldwlrHQPLLHVDEELGLVMvHAGIPPQW-DLATALALAREVEAVLRS 145

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 17552284  260 PLACDLLWA----DPEK---DAKGFEpnKIRAISNVF 289
Cdd:PRK00166 146 DDYRDFLANmygnEPDRwspDLTGLE--RLRYIINAF 180
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 116-182 1.09e-04

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: 41.87  E-value: 1.09e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284 116 ICGDTHGQYnDLLRIFNACGAATKTQY---LFLGDYVDRGGHSLEVIMLLFSLKLAmPRKMHLLRGNHEL 182
Cdd:cd00838   2 VISDIHGNL-EALEAVLEAALAKAEKPdlvICLGDLVDYGPDPEEVELKALRLLLA-GIPVYVVPGNHDI 69
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 116-183 1.82e-04

Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein phosphatase E) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases and a key signal transduction pathway component controlling the expression of spore germination receptors GerA and GerK in Bacillus subtilis. PrpE is closely related to ApaH (also known symmetrical Ap(4)A hydrolase and bis(5'nucleosyl)-tetraphosphatase). PrpE has specificity for phosphotyrosine only, unlike the serine/threonine phosphatases to which it is related. The Bacilli members of this family are single domain proteins while the other members have N- and C-terminal domains in addition to this phosphatase domain. Pnkp is the end-healing and end-sealing component of an RNA repair system present in bacteria. It is composed of three catalytic modules: an N-terminal polynucleotide 5' kinase, a central 2',3' phosphatase, and a C-terminal ligase. Pnkp is a Mn(2+)-dependent phosphodiesterase-monoesterase that dephosphorylates 2',3'-cyclic phosphate RNA ends. An RNA binding site is suggested by a continuous tract of positive surface potential flanking the active site. The PPP (phosphoprotein phosphatase) family, to which PrpE belongs, is one of two known protein phosphatase families specific for serine and threonine. The PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 42.50  E-value: 1.82e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552284 116 ICGDTHGQYNDLLRIFNACGAATKTQYL----------FLGDYVDRGGHSLEVIMLLFSLKLAMPRKMHLlrGNHELK 183
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYQKKEEGLyvhpegrklvFLGDLVDRGPDSIDVLRLVMNMVKAGKALYVP--GNHCNK 77
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 116-182 3.18e-04

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


Pssm-ID: 163664  Cd Length: 304  Bit Score: 42.11  E-value: 3.18e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 17552284 116 IC-GDTHG---QYNDLLRIFNAC---GAATKTQYLFLGDYVDRGGHSLEVIMLLFSLKLAMPRKMH-LLRGNHEL 182
Cdd:cd07421   5 ICvGDIHGyisKLNNLWLNLQSAlgpSDFASALVIFLGDYCDRGPETRKVIDFLISLPEKHPKQRHvFLCGNHDF 79
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
116-181 5.20e-04

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 40.67  E-value: 5.20e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552284 116 ICGDTHGQYNDLLRIFNACGAATKTQYLFLGDYVDRGGHSLEVimllfsLKLAMPRKMHLLRGNHE 181
Cdd:COG0622   4 VISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEV------LDLLRELPIVAVRGNHD 63
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 118-182 6.44e-04

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: 40.99  E-value: 6.44e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 17552284 118 GDTHGQYNDLLRIFNACGAATKTQYL-FLGDYVDRGGHSLEVIMLLFSLKLAMprKMHLlrGNHEL 182
Cdd:cd07422   5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLETLRFVKSLGDSA--VVVL--GNHDL 66
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 114-236 1.03e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 40.46  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 17552284  114 INICGDTHGQYNDLLRIFNACGAATKT---------QYLFLGDYVDRGGHSLEVIMllFSLKLAMPRKMHLLRGNHelka 184
Cdd:PRK13625   3 YDIIGDIHGCYQEFQALTEKLGYNWSSglpvhpdqrKLAFVGDLTDRGPHSLRMIE--IVWELVEKKAAYYVPGNH---- 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 17552284  185 INKNYGF---------H------AELKKRFQREEvyESVYNHFNQVFSYMPLCAIV-SKRILCMHGGI 236
Cdd:PRK13625  77 CNKLYRFflgrnvtiaHglettvAEYEALPSHKQ--NMIKEKFITLYEQAPLYHILdEGRLVVAHAGI 142
 
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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