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Conserved domains on  [gi|45827798|ref|NP_996756|]
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serine/threonine-protein phosphatase PP1-alpha catalytic subunit isoform 2 [Homo sapiens]

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 ...
 19-254 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: 578.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:cd07414  56 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:cd07414 136 RYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 215

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45827798 179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 254
Cdd:cd07414 216 VSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 19-254 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: 578.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:cd07414  56 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:cd07414 136 RYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 215

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45827798 179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 254
Cdd:cd07414 216 VSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 19-264 1.95e-169

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 471.84  E-value: 1.95e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:PTZ00480  65 GDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:PTZ00480 145 RYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKN 258
Cdd:PTZ00480 225 VSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQG 304


                 ....*.
gi 45827798  259 KGKYGQ 264
Cdd:PTZ00480 305 QGASQQ 310
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 19-255 1.15e-140

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: 396.97  E-value: 1.15e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798     19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:smart00156  34 GDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798     99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:smart00156 114 KYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRG 193

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827798    179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA 255
Cdd:smart00156 194 ASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 19-121 2.22e-19

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: 81.49  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798    19 GDIH--GQYYDLLRLFEYGGfPPESNYLFL--GDYVDRGKQSlETICLLLAYKIKYpENFFLLRGNHECAsinriygfYD 94
Cdd:pfam00149   7 GDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD--------YG 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 45827798    95 ECKRRY-----NIKLWKTFTDCFNCLPIAAIV 121
Cdd:pfam00149  76 ECLRLYpylglLARPWKRFLEVFNFLPLAGIL 107
 
Name Accession Description Interval E-value
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 19-254 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: 578.52  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:cd07414  56 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 135

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:cd07414 136 RYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 215

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45827798 179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 254
Cdd:cd07414 216 VSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKP 291
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 19-264 1.95e-169

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 471.84  E-value: 1.95e-169
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:PTZ00480  65 GDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:PTZ00480 145 RYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERG 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPADKN 258
Cdd:PTZ00480 225 VSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILKPAEQG 304


                 ....*.
gi 45827798  259 KGKYGQ 264
Cdd:PTZ00480 305 QGASQQ 310
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 19-255 1.15e-140

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: 396.97  E-value: 1.15e-140
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798     19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:smart00156  34 GDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKR 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798     99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:smart00156 114 KYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRPQEPPDDGLLIDLLWSDPDQPVNGFGPSIRG 193

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827798    179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA 255
Cdd:smart00156 194 ASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKPG 270
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 19-255 9.19e-135

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 382.72  E-value: 9.19e-135
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:PTZ00244  58 GDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKR 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRG 178
Cdd:PTZ00244 138 RYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRG 217

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827798  179 VSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILkPA 255
Cdd:PTZ00244 218 VSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSFLII-PA 293
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 19-255 4.55e-129

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: 368.07  E-value: 4.55e-129
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:cd07415  48 GDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLR 127

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  99 RY-NIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDR 177
Cdd:cd07415 128 KYgNANVWKYFTDLFDYLPLAALIDGQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPD-DREGWGISPR 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45827798 178 GVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA 255
Cdd:cd07415 207 GAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAA 284
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 19-241 7.44e-111

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: 319.70  E-value: 7.44e-111
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE--- 95
Cdd:cd00144   4 GDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDErtl 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  96 -CKRRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRImRPTDVPDQGLLCDLLWSDPDKDVQGWGE 174
Cdd:cd00144  84 rCLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGDFES 162

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827798 175 NDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSV 241
Cdd:cd00144 163 SSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 19-253 9.57e-97

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 286.71  E-value: 9.57e-97
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:PTZ00239  49 GDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILR 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   99 RY-NIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDR 177
Cdd:PTZ00239 129 KYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPE-EVEYWAVNSR 207

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827798  178 GVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEF-FAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 253
Cdd:PTZ00239 208 GAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNYCYRCGNIASILCLDENLQQTWKTFK 284
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 19-247 7.05e-90

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: 269.18  E-value: 7.05e-90
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKR 98
Cdd:cd07416  49 GDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKI 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  99 RYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQG------W 172
Cdd:cd07416 129 KYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRKLDRFREPPSYGPMCDLLWSDPLEDFGNektqehF 208

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798 173 GEND-RGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQ------LVTLFSAPNYCGEFDNAGAMMSVDETL 245
Cdd:cd07416 209 VHNTvRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNYLDVYNNKAAVLKYENNV 288


                ..
gi 45827798 246 MC 247
Cdd:cd07416 289 MN 290
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 19-237 3.90e-87

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: 262.58  E-value: 3.90e-87
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECK 97
Cdd:cd07417  66 GDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVK 145

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  98 RRYNIKLWKTFTDCFNCLPIAAIVDEKIFCCHGGL-SPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPdKDVQGWGEND 176
Cdd:cd07417 146 AKYNEQMFNLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDP-QPQPGRGPSK 224

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45827798 177 RGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGA 237
Cdd:cd07417 225 RGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGA 285
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 19-239 1.23e-83

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: 253.52  E-value: 1.23e-83
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPES--------NYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIY 90
Cdd:cd07419  54 GDIHGQFGDLMRLFDEYGSPVTEeagdieyiDYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINALF 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  91 GFYDECKRRYN------IKLWKTFTDCFNCLPIAAIVDEKIFCCHGGLSPDLQSMEQIRRIMRP-TDVPDQGLLCDLLWS 163
Cdd:cd07419 134 GFREECIERLGedirdgDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINHIHQIENLKRPiTMEAGSPVVMDLLWS 213

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798 164 DP-DKD-VQGWGENDR-----GVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAG 236
Cdd:cd07419 214 DPtENDsVLGLRPNAIdprgtGLIVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAG 293


                ...
gi 45827798 237 AMM 239
Cdd:cd07419 294 AIL 296
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 19-249 2.39e-59

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: 191.08  E-value: 2.39e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECK 97
Cdd:cd07420  57 GDLHGKLDDLLLIFYKNGLPSPENpYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVM 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  98 RRYNI---KLWKTFTDCFNCLPIAAIVDEKIFCCHGGLS--PDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGW 172
Cdd:cd07420 137 QKYKDhgkKILRLLEDVFSWLPLATIIDNKVLVVHGGISdsTDLDLLDKIDRHKYVSTKTEWQQVVDILWSDPKATKGCK 216

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45827798 173 GENDRGVSFTFGAEVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSF 249
Cdd:cd07420 217 PNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTPHF 293
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 19-274 1.26e-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: 160.35  E-value: 1.26e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECK 97
Cdd:cd07418  72 GDVHGQLHDVLFLLEDAGFPDQNRfYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVL 151

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  98 RRYNIK---LWKTFTDCFNCLPIAAIVDEKIFCCHGGL--SPD----------------------------LQSMEQIRR 144
Cdd:cd07418 152 TKYGDKgkhVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrSPSlpkrkkqkgknrrvlllepeseslklgtLDDLMKARR 231

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798 145 IMrpTDVPDQGLLC---DLLWSDPDKDvQGWGEND-RGVSFTFGAEVVAKFLHKHDLDLICRAHQvvedGYEFFAKR--- 217
Cdd:cd07418 232 SV--LDPPGEGSNLipgDVLWSDPSLT-PGLSPNKqRGIGLLWGPDCTEEFLEKNNLKLIIRSHE----GPDAREKRpgl 304

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45827798 218 ----------------QLVTLFSAPNYCG------EFDNAGAmmsvdetlmcsFQILKPADKNKGKYGQFSGLNPggRP 274
Cdd:cd07418 305 agmnkgytvdhdvesgKLITLFSAPDYPQfqateeRYNNKGA-----------YIILQPPDFSDPQFHTFEAVKP--RP 370
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 19-121 2.22e-19

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: 81.49  E-value: 2.22e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798    19 GDIH--GQYYDLLRLFEYGGfPPESNYLFL--GDYVDRGKQSlETICLLLAYKIKYpENFFLLRGNHECAsinriygfYD 94
Cdd:pfam00149   7 GDLHlpGQLDDLLELLKKLL-EEGKPDLVLhaGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD--------YG 75

                          90       100       110
                  ....*....|....*....|....*....|..
gi 45827798    95 ECKRRY-----NIKLWKTFTDCFNCLPIAAIV 121
Cdd:pfam00149  76 ECLRLYpylglLARPWKRFLEVFNFLPLAGIL 107
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 19-129 7.39e-10

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: 57.33  E-value: 7.39e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYLF-LGDYVDRGKQSLEtiCLLLaykIKYPEnFFLLRGNHECASINRIYGFYDECK 97
Cdd:cd07424   7 GDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLE--VLEL---LKQPW-FHAVQGNHEQMAIDALRGGDDVMW 80

                        90       100       110       120
                ....*....|....*....|....*....|....*....|...
gi 45827798  98 RRYNIKLW--------KTFTDCFNCLPIAAIV---DEKIFCCH 129
Cdd:cd07424  81 RANGGGWFfdlpdeeaKVLLEKLHHLPIAIEVesrNGKVGIVH 123
PHA02239 PHA02239
putative protein phosphatase
 20-108 2.50e-07

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 50.38  E-value: 2.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   20 DIHGQYYDLLRLFE--YGGFPPESNYLFLGDYVDRGKQSLETICLLLAYkIKYPENFFLLRGNHE------CASINRIyG 91
Cdd:PHA02239   8 DIHGEYQKLLTIMDkiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDL-MSNDDNVVTLLGNHDdefyniMENVDRL-S 85

                         90
                 ....*....|....*...
gi 45827798   92 FYD-ECKRRYNIKLWKTF 108
Cdd:PHA02239  86 IYDiEWLSRYCIETLNSY 103
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 19-82 4.31e-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: 45.34  E-value: 4.31e-06
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45827798  19 GDIHGQYYDLLRLF--EYGGFPPESNYLFLGDYVDRGKQSLETICLLLAyKIKYPENFFLLRGNHE 82
Cdd:cd00838   4 SDIHGNLEALEAVLeaALAKAEKPDLVICLGDLVDYGPDPEEVELKALR-LLLAGIPVYVVPGNHD 68
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
19-82 8.36e-06

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 46.31  E-value: 8.36e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45827798   19 GDIHGQYYDLLRLFEYGGFPPESNYL-FLGDYVDRGKQSLETicllLAYKIKYPENFFLLRGNHE 82
Cdd:PRK00166   7 GDIQGCYDELQRLLEKIDFDPAKDTLwLVGDLVNRGPDSLEV----LRFVKSLGDSAVTVLGNHD 67
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 19-134 2.69e-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: 44.21  E-value: 2.69e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNY--------LFLGDYVDRGKQSLETICLLLAYK---IKYPENFFLLRGNHECASI- 86
Cdd:cd07425   4 GDLHGDLDRLRTILKLAGVIDSNDRwiggdtvvVQTGDILDRGDDEIEILKLLEKLKrqaRKAGGKVILLLGNHELMNLc 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 45827798  87 --------NRIYGFYDECKRRYniKLWKTFTDCFNCL---PIAAIVDEKIFcCHGGLSP 134
Cdd:cd07425  84 gdfryvhpRGLNEFGGVAKRRY--ALLSDGGYIGRYLrthPVVLVVNDILF-VHGGLGP 139
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 19-82 2.69e-05

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: 44.46  E-value: 2.69e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 45827798  19 GDIHGQYYDLLRLFEYGGFPPESNYL-FLGDYVDRGKQSLETicllLAYKIKYPENFFLLRGNHE 82
Cdd:cd07422   5 GDIQGCYDELQRLLEKINFDPAKDRLwLVGDLVNRGPDSLET----LRFVKSLGDSAVVVLGNHD 65
PRK09968 PRK09968
protein-serine/threonine phosphatase;
19-87 7.34e-05

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 42.96  E-value: 7.34e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   19 GDIHGQYYDLLRLFEYGGFPPESNYLF-LGDYVDRGKQSLETICLLlaykikYPENFFLLRGNHECASIN 87
Cdd:PRK09968  21 GDIHGEYQLLQSRLHQLSFCPETDLLIsVGDNIDRGPESLNVLRLL------NQPWFISVKGNHEAMALD 84
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 19-84 2.41e-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: 41.72  E-value: 2.41e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45827798  19 GDIHGQYYDLLRLFE--YGGFPPE----SNYLFLGDYVDRGKQSLETICLLLAYKIKYP-ENFFLLRGNHECA 84
Cdd:cd07421   8 GDIHGYISKLNNLWLnlQSALGPSdfasALVIFLGDYCDRGPETRKVIDFLISLPEKHPkQRHVFLCGNHDFA 80
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 19-137 4.45e-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: 40.58  E-value: 4.45e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798  19 GDIHGQYYDLLRLFE---------YGGFPPESNYL-FLGDYVDRGKQSLEtiCLLLAYKIKYPENFFLLRGNHEcasiNR 88
Cdd:cd07423   4 GDVHGCYDELVELLEklgyqkkeeGLYVHPEGRKLvFLGDLVDRGPDSID--VLRLVMNMVKAGKALYVPGNHC----NK 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45827798  89 IYGFYDECKRRYNIKLWKT------------------FTDCFNCLPIAAIVDE-KIFCCHGGLSPDLQ 137
Cdd:cd07423  78 LYRYLKGRNVQLAHGLETTveelealskeerpefrerFAEFLESLPSHLVLDGgRLVVAHAGIKEEMI 145
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 19-93 2.50e-03

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 38.53  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45827798   19 GDIHGQYYDLLRLFEYGGFP--------PESNYL-FLGDYVDRGKQSLETI---CLLLAYKIKYpenffLLRGNHeCasi 86
Cdd:PRK13625   7 GDIHGCYQEFQALTEKLGYNwssglpvhPDQRKLaFVGDLTDRGPHSLRMIeivWELVEKKAAY-----YVPGNH-C--- 77


                 ....*..
gi 45827798   87 NRIYGFY 93
Cdd:PRK13625  78 NKLYRFF 84
 
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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