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Conserved domains on  [gi|1158588700|ref|XP_020304149|]
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hypothetical protein LOAG_00253 [Loa loa]

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 ...
 35-302 7.54e-135

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: 389.26  E-value: 7.54e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700   35 EEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDYIDRGPQSIETMIYLLCLKV 114
Cdd:smart00156   4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  115 KYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSPHLTSLEQIRQIKRP 194
Cdd:smart00156  84 LYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRP 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  195 CEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQDGYELMVGKKLITIFSAPNY 274
Cdd:smart00156 164 QEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNY 243

                          250       260
                   ....*....|....*....|....*...
gi 1158588700  275 AGQFNNAGAVVCIDDDLQVTFQQLRVPP 302
Cdd:smart00156 244 CDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 35-302 7.54e-135

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: 389.26  E-value: 7.54e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700   35 EEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDYIDRGPQSIETMIYLLCLKV 114
Cdd:smart00156   4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  115 KYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSPHLTSLEQIRQIKRP 194
Cdd:smart00156  84 LYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRP 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  195 CEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQDGYELMVGKKLITIFSAPNY 274
Cdd:smart00156 164 QEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNY 243

                          250       260
                   ....*....|....*....|....*...
gi 1158588700  275 AGQFNNAGAVVCIDDDLQVTFQQLRVPP 302
Cdd:smart00156 244 CDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 10-299 1.91e-115

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: 340.47  E-value: 1.91e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  10 LDKMIA-VLEEMGTKKGIQMNqkITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVK 88
Cdd:cd07414     2 IDSIIErLLEVRGSRPGKNVQ--LTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  89 MIFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLIS 168
Cdd:cd07414    80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 169 KRVLCMHGGLSPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIR 248
Cdd:cd07414   160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1158588700 249 AHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQVTFQQLR 299
Cdd:cd07414   240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 16-299 2.30e-96

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 293.10  E-value: 2.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  16 VLEEMGTKKGIQMNqkITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDY 95
Cdd:PTZ00480   18 LLSVRGSKPGKNVN--LTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  96 IDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLCMH 175
Cdd:PTZ00480   96 VDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMH 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 176 GGLSPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQD 255
Cdd:PTZ00480  176 GGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVED 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1158588700 256 GYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQVTFQQLR 299
Cdd:PTZ00480  256 GYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILK 299
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 60-168 1.72e-16

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: 75.33  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  60 PIKVVGDIH--GQYEDMHKLFGVIGRVPEVKMI-FLGDYIDRGPQSiETMIYLLCLKVKYrDRIFLLRGNHETPavnriy 136
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVlHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1158588700 137 gfYNECALKYG-----VGLWWDFQSFFNRMPMAGLIS 168
Cdd:pfam00149  74 --YGECLRLYPylgllARPWKRFLEVFNFLPLAGILS 108
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
63-140 2.21e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 39.23  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIgRVPEVKM-IFLGDYIDRGPQSiETMIYLLCLKvKYRDRIFLLRGNHETPAVNRIYGFYN 140
Cdd:COG2129     4 AVSDLHGNFDLLEKLLELA-RAEDADLvILAGDLTDFGTAE-EAREVLEELA-ALGVPVLAVPGNHDDPEVLDALEESG 79
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 35-302 7.54e-135

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: 389.26  E-value: 7.54e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700   35 EEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDYIDRGPQSIETMIYLLCLKV 114
Cdd:smart00156   4 EEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALKI 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  115 KYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSPHLTSLEQIRQIKRP 194
Cdd:smart00156  84 LYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLKRP 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  195 CEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQDGYELMVGKKLITIFSAPNY 274
Cdd:smart00156 164 QEPPDDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNY 243

                          250       260
                   ....*....|....*....|....*...
gi 1158588700  275 AGQFNNAGAVVCIDDDLQVTFQQLRVPP 302
Cdd:smart00156 244 CDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 10-299 1.91e-115

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: 340.47  E-value: 1.91e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  10 LDKMIA-VLEEMGTKKGIQMNqkITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVK 88
Cdd:cd07414     2 IDSIIErLLEVRGSRPGKNVQ--LTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  89 MIFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLIS 168
Cdd:cd07414    80 YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVD 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 169 KRVLCMHGGLSPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIR 248
Cdd:cd07414   160 EKIFCCHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICR 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1158588700 249 AHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQVTFQQLR 299
Cdd:cd07414   240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILK 290
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 10-302 1.66e-103

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: 309.90  E-value: 1.66e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  10 LDKMIAVLEEMgtkkgiqmnQKITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKM 89
Cdd:cd07415     2 LDQWIEQLKKC---------ELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNY 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  90 IFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYG-VGLWWDFQSFFNRMPMAGLIS 168
Cdd:cd07415    73 LFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGnANVWKYFTDLFDYLPLAALID 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 169 KRVLCMHGGLSPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPTNKgDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIR 248
Cdd:cd07415   153 GQIFCVHGGLSPSIQTLDQIRALDRFQEVPHEGPMCDLLWSDPDDR-EGWGISPRGAGYLFGQDVVEEFNHNNGLTLICR 231

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1158588700 249 AHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQVTFQQLRVPP 302
Cdd:cd07415   232 AHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEAAP 285
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 63-287 3.59e-99

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: 296.59  E-value: 3.59e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNEC 142
Cdd:cd00144     2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDER 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 143 AL----KYGVGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSPHLTSLEQIRQIkRPCEPLDRGLLIDLVWSDPTNKGDGW 218
Cdd:cd00144    82 TLrclrKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNI-RPIENPDDQLVEDLLWSDPDESVGDF 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158588700 219 FYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCI 287
Cdd:cd00144   161 ESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 16-299 2.30e-96

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 293.10  E-value: 2.30e-96
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  16 VLEEMGTKKGIQMNqkITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDY 95
Cdd:PTZ00480   18 LLSVRGSKPGKNVN--LTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  96 IDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLCMH 175
Cdd:PTZ00480   96 VDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMH 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 176 GGLSPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQD 255
Cdd:PTZ00480  176 GGLSPELSNLEQIRRIMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVED 255

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1158588700 256 GYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQVTFQQLR 299
Cdd:PTZ00480  256 GYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESLMCSFQILK 299
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 16-295 3.50e-94

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 286.42  E-value: 3.50e-94
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  16 VLEEMGTKKGIQMNQKITL--EEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLG 93
Cdd:PTZ00244    7 LIEKMLTVKGNRTQRQILIreEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  94 DYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLC 173
Cdd:PTZ00244   87 DYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIIC 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 174 MHGGLSPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPTNKGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVV 253
Cdd:PTZ00244  167 MHGGLSPDLTSLASVNEIERPCDVPDRGILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVM 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1158588700 254 QDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQVTF 295
Cdd:PTZ00244  247 ERGYGFFASRQLVTVFSAPNYCGEFDNDAAVMNIDDKLQCSF 288
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 31-306 3.70e-79

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: 247.99  E-value: 3.70e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  31 KITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDYIDRGPQSIETMIYLL 110
Cdd:cd07416    15 RLSEEDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRGYFSIECVLYLW 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 111 CLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSPHLTSLEQIRQ 190
Cdd:cd07416    95 ALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLSPELKTLDDIRK 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 191 IKRPCEPLDRGLLIDLVWSDP-----TNKGDGWFY--SPRGLSYSFGKGallAACKLL-KIDL--VIRAHQVVQDGYELM 260
Cdd:cd07416   175 LDRFREPPSYGPMCDLLWSDPledfgNEKTQEHFVhnTVRGCSYFYSYR---AVCEFLqKNNLlsIIRAHEAQDAGYRMY 251

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1158588700 261 --VGKK----LITIFSAPNYAGQFNNAGAVVCIDDDLqVTFQQLRVPPGPTC 306
Cdd:cd07416   252 rkSQTTgfpsLITIFSAPNYLDVYNNKAAVLKYENNV-MNIRQFNCSPHPYW 302
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 47-302 1.61e-76

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 241.26  E-value: 1.61e-76
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  47 IMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFGVIGRVPEVKMIFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGN 126
Cdd:PTZ00239   31 IFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 127 HETPAVNRIYGFYNECALKYG-VGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSPHLTSLEQIRQIKRPCEPLDRGLLID 205
Cdd:PTZ00239  111 HESRQCTQVYGFYEEILRKYGnSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSPDMRTIDQIRTIDRKIEIPHEGPFCD 190

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 206 LVWSDPTNKgDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQDGYELMVGKK-LITIFSAPNYAGQFNNAGAV 284
Cdd:PTZ00239  191 LMWSDPEEV-EYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYWFPDQnLVTVWSAPNYCYRCGNIASI 269

                         250
                  ....*....|....*...
gi 1158588700 285 VCIDDDLQVTFQQLRVPP 302
Cdd:PTZ00239  270 LCLDENLQQTWKTFKEVP 287
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 32-293 4.75e-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: 235.03  E-value: 4.75e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  32 ITLEEILALMSTAGLIMMEEGSLVEVEVPIKVVGDIHGQYEDMHKLFG--------VIGRVPEVKMIFLGDYIDRGPQSI 103
Cdd:cd07419    21 FDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDeygspvteEAGDIEYIDYLFLGDYVDRGSHSL 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 104 ETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYG------VGLWWDFQSFFNRMPMAGLISKRVLCMHGG 177
Cdd:cd07419   101 ETICLLLALKVKYPNQIHLIRGNHEAADINALFGFREECIERLGedirdgDSVWQRINRLFNWLPLAALIEDKIICVHGG 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 178 LSPHLTSLEQIRQIKRP-CEPLDRGLLIDLVWSDPTNK--------GDGWFYSPrGLSYSFGKGALLAACKLLKIDLVIR 248
Cdd:cd07419   181 IGRSINHIHQIENLKRPiTMEAGSPVVMDLLWSDPTENdsvlglrpNAIDPRGT-GLIVKFGPDRVMEFLEENDLQMIIR 259

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1158588700 249 AHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQV 293
Cdd:cd07419   260 AHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLVV 304
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 4-304 3.18e-72

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: 230.61  E-value: 3.18e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700   4 GVTAETLDKMIavlEEMGTKKgiqmnqKITLEEILALMSTAGLIMMEEGSLVEVEVP----IKVVGDIHGQYEDMHKLFG 79
Cdd:cd07417    10 KVTLEFVKEMM---EWFKDQK------KLHKKYAYQILLQVKEILKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  80 VIGRV-PEVKMIFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYGVGLWWDFQSFF 158
Cdd:cd07417    81 LNGLPsETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFSEVF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 159 NRMPMAGLISKRVLCMHGGL-SPHLTSLEQIRQIKRPCEPLDRGLLIDLVWSDPtNKGDGWFYSPRGLSYSFGKGALLAA 237
Cdd:cd07417   161 NWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFRQPPDSGLMCELLWSDP-QPQPGRGPSKRGVGCQFGPDVTKRF 239

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158588700 238 CKLLKIDLVIRAHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCID-DDLQVTFQQLRVPPGP 304
Cdd:cd07417   240 LEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKgSDLKPKFTQFEAVPHP 307
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 61-297 5.02e-41

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: 148.33  E-value: 5.02e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  61 IKVVGDIHGQYEDMHKLFGVIGR-VPEVKMIFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFY 139
Cdd:cd07420    53 VTICGDLHGKLDDLLLIFYKNGLpSPENPYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFT 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 140 NECALKY---GVGLWWDFQSFFNRMPMAGLISKRVLCMHGGLSpHLTSLEQIRQIKR---PCEPLDRGLLIDLVWSDPTN 213
Cdd:cd07420   133 KEVMQKYkdhGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS-DSTDLDLLDKIDRhkyVSTKTEWQQVVDILWSDPKA 211

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 214 KGDGWFYSPRGLSYSFGKGALLAACKLLKIDLVIRAHQVVQDGYELMVGKKLITIFSAPNYAGQFNNAGAVVCIDDDLQV 293
Cdd:cd07420   212 TKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGAYVKLGPQLTP 291


                  ....
gi 1158588700 294 TFQQ 297
Cdd:cd07420   292 HFVQ 295
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 5-285 1.40e-38

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: 143.79  E-value: 1.40e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700   5 VTAETLDKMIAVLEEmGTKKGI--QMNQKITLEEILALMSTAGLIMMEEGSLVEVEV----PIKVVGDIHGQYEDMHKLF 78
Cdd:cd07418     7 LTNEWVHELMSVFEW-SSRNLPpsELPSVLPVNVFDSLVLTAHKILHREPNCVRIDVedvcEVVVVGDVHGQLHDVLFLL 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  79 GVIGRVPEVKM-IFLGDYIDRGPQSIETMIYLLCLKVKYRDRIFLLRGNHETPAVNRIYGFYNECALKYG---VGLWWDF 154
Cdd:cd07418    86 EDAGFPDQNRFyVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGdkgKHVYRKC 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 155 QSFFNRMPMAGLISKRVLCMHGGL---------------------------SPHLTSLEQIRQIKRP-CEPLDRGL-LI- 204
Cdd:cd07418   166 LGCFEGLPLASIIAGRVYTAHGGLfrspslpkrkkqkgknrrvlllepeseSLKLGTLDDLMKARRSvLDPPGEGSnLIp 245

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700 205 -DLVWSDPTNKgDGWFYS-PRGLSYSFGKGALLAACKLLKIDLVIRAHQ------------VVQDGY----ELMVGkKLI 266
Cdd:cd07418   246 gDVLWSDPSLT-PGLSPNkQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYtvdhDVESG-KLI 323

                         330       340
                  ....*....|....*....|....*.
gi 1158588700 267 TIFSAPNYAgQF-------NNAGAVV 285
Cdd:cd07418   324 TLFSAPDYP-QFqateeryNNKGAYI 348
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 60-168 1.72e-16

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: 75.33  E-value: 1.72e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  60 PIKVVGDIH--GQYEDMHKLFGVIGRVPEVKMI-FLGDYIDRGPQSiETMIYLLCLKVKYrDRIFLLRGNHETPavnriy 136
Cdd:pfam00149   2 RILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVlHAGDLVDRGPPS-EEVLELLERLIKY-VPVYLVRGNHDFD------ 73

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1158588700 137 gfYNECALKYG-----VGLWWDFQSFFNRMPMAGLIS 168
Cdd:pfam00149  74 --YGECLRLYPylgllARPWKRFLEVFNFLPLAGILS 108
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 63-153 5.09e-09

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: 56.17  E-value: 5.09e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIGRVPEVKMIF-LGDYIDRGPQSIEtmiyllCLKVKYRDRIFLLRGNHETPAVNRIYGFYNE 141
Cdd:cd07424     5 VVGDIHGHFQRLQRALDAVGFDPARDRLIsVGDLVDRGPESLE------VLELLKQPWFHAVQGNHEQMAIDALRGGDDV 78

                          90
                  ....*....|..
gi 1158588700 142 CALKYGvGLWWD 153
Cdd:cd07424    79 MWRANG-GGWFF 89
PHA02239 PHA02239
putative protein phosphatase
 61-128 1.34e-08

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 55.39  E-value: 1.34e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  61 IKVVGDIHGQYEDMHKLFGVIG--RVPEVKMIFLGDYIDRGPQSIETMIYLLCLKVKyRDRIFLLRGNHE 128
Cdd:PHA02239    3 IYVVPDIHGEYQKLLTIMDKINneRKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSN-DDNVVTLLGNHD 71
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 63-138 7.35e-07

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: 50.21  E-value: 7.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIGRV---------PEV-KMIFLGDYIDRGPQSIETMiyLLCLKVKYRDRIFLLRGNHEtpav 132
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGYQkkeeglyvhPEGrKLVFLGDLVDRGPDSIDVL--RLVMNMVKAGKALYVPGNHC---- 75


                  ....*.
gi 1158588700 133 NRIYGF 138
Cdd:cd07423    76 NKLYRY 81
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 61-139 1.92e-06

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 48.93  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  61 IKVVGDIHGQYEDMHKLFGVIGRV--------PE-VKMIFLGDYIDRGPQSIEtMIYLLCLKVKyRDRIFLLRGNHetpa 131
Cdd:PRK13625    3 YDIIGDIHGCYQEFQALTEKLGYNwssglpvhPDqRKLAFVGDLTDRGPHSLR-MIEIVWELVE-KKAAYYVPGNH---- 76


                  ....*...
gi 1158588700 132 VNRIYGFY 139
Cdd:PRK13625   77 CNKLYRFF 84
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 63-199 2.44e-06

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: 48.06  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1158588700  63 VVGDIHGQYE---DMHKLFGVI---GRVP--EVKMIFLGDYIDRGPQSIETMIYLLCLKVKYRD---RIFLLRGNHETPA 131
Cdd:cd07425     2 AIGDLHGDLDrlrTILKLAGVIdsnDRWIggDTVVVQTGDILDRGDDEIEILKLLEKLKRQARKaggKVILLLGNHELMN 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158588700 132 VNRIYGFYNECALKYGVGLWWDFQSFFNRMPMAG--LISKRV-------LCMHGGLSPHLTSLEQIRQIKRPCEPLD 199
Cdd:cd07425    82 LCGDFRYVHPRGLNEFGGVAKRRYALLSDGGYIGryLRTHPVvlvvndiLFVHGGLGPLWSRGYSLETKNGACERSA 158
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 63-128 2.67e-06

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 46.49  E-value: 2.67e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158588700  63 VVGDIHGQYEDMHKLFG--VIGRVPEVKMIFLGDYIDRGPQSIETMIYLLcLKVKYRDRIFLLRGNHE 128
Cdd:cd00838     2 VISDIHGNLEALEAVLEaaLAKAEKPDLVICLGDLVDYGPDPEEVELKAL-RLLLAGIPVYVVPGNHD 68
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
 64-128 1.35e-05

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


Pssm-ID: 163664  Cd Length: 304  Bit Score: 46.73  E-value: 1.35e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1158588700  64 VGDIHGQYEDMHKLFGVIGRV--PEV----KMIFLGDYIDRGPQSIETMIYLLCLKVKYRD-RIFLLRGNHE 128
Cdd:cd07421     7 VGDIHGYISKLNNLWLNLQSAlgPSDfasaLVIFLGDYCDRGPETRKVIDFLISLPEKHPKqRHVFLCGNHD 78
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 63-128 4.64e-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: 44.84  E-value: 4.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIGRVPEV-KMIFLGDYIDRGPQSIETMIYLLCLkvkyRDRIFLLRGNHE 128
Cdd:cd07422     3 AIGDIQGCYDELQRLLEKINFDPAKdRLWLVGDLVNRGPDSLETLRFVKSL----GDSAVVVLGNHD 65
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
63-128 5.78e-05

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 44.77  E-value: 5.78e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIGRVPEV-KMIFLGDYIDRGPQSIETMIYLlclkVKYRDRIFLLRGNHE 128
Cdd:PRK00166    5 AIGDIQGCYDELQRLLEKIDFDPAKdTLWLVGDLVNRGPDSLEVLRFV----KSLGDSAVTVLGNHD 67
PRK09968 PRK09968
protein-serine/threonine phosphatase;
61-133 6.18e-05

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 44.11  E-value: 6.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158588700  61 IKVVGDIHGQYEDMHKLFGVIGRVPEVKM-IFLGDYIDRGPQSIETmiyllcLKVKYRDRIFLLRGNHETPAVN 133
Cdd:PRK09968   17 IWVVGDIHGEYQLLQSRLHQLSFCPETDLlISVGDNIDRGPESLNV------LRLLNQPWFISVKGNHEAMALD 84
pphA PRK11439
protein-serine/threonine phosphatase;
61-133 2.13e-04

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 42.44  E-value: 2.13e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1158588700  61 IKVVGDIHGQYEDMHKLFGVIGRVP-EVKMIFLGDYIDRGPQSIEtmiyllCLKVKYRDRIFLLRGNHETPAVN 133
Cdd:PRK11439   19 IWLVGDIHGCFEQLMRKLRHCRFDPwRDLLISVGDLIDRGPQSLR------CLQLLEEHWVRAVRGNHEQMALD 86
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 63-132 3.60e-04

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: 41.77  E-value: 3.60e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIG--------RVPEVKMIFLGDYIDRGPQsIETMIYLLCLKVKYRDRIFLLrGNHETPAV 132
Cdd:cd07413     3 LIGDVHGCAHTLDRLLDLLGyrlqggvwRHPRRQALFVGDLIDRGPR-IREVLHRVHAMVDAGEALCVM-GNHEFNAL 78
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
63-140 2.21e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 39.23  E-value: 2.21e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1158588700  63 VVGDIHGQYEDMHKLFGVIgRVPEVKM-IFLGDYIDRGPQSiETMIYLLCLKvKYRDRIFLLRGNHETPAVNRIYGFYN 140
Cdd:COG2129     4 AVSDLHGNFDLLEKLLELA-RAEDADLvILAGDLTDFGTAE-EAREVLEELA-ALGVPVLAVPGNHDDPEVLDALEESG 79
 
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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