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Conserved domains on  [gi|42570616|ref|NP_851258|]
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serine/threonine phosphatase 7 [Arabidopsis thaliana]

Protein Classification

metallophosphoesterase family protein; bifunctional metallophosphatase/5'-nucleotidase family protein( domain architecture ID 10164852)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)| bifunctional metallophosphatase/5'-nucleotidase contains an N-terminal metallophosphoesterase family domain that contains an active site consisting of two metal ions (usually manganese, iron, or zinc), and a 5'-nucleotidase C-terminal domain; similar to Escherichia coli UshA

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 11-388 0e+00

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: 757.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  11 WPDGGALTNDWVHGLMSCFEWSSWNLPPSQLPSLLPVNVFDSLVLTAHKILHKERNCVHIDDlDSVSNVVVVGDIHGQLH 90
Cdd:cd07418   1 WPDGGALTNEWVHELMSVFEWSSRNLPPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIDV-EDVCEVVVVGDVHGQLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  91 DLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGK 170
Cdd:cd07418  80 DVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 171 HVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLPKRTTRGKKNRRVVLLEPEPSSMKLGTLDELMQARRSVLDPPWE 250
Cdd:cd07418 160 HVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNRRVLLLEPESESLKLGTLDDLMKARRSVLDPPGE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 251 GSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEGPDAREKRTGLGGMDNGYTIDHNVES 330
Cdd:cd07418 240 GSNLIPGDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPDAREKRPGLAGMNKGYTVDHDVES 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42570616 331 GKLITIFSAPDYPQFQATEERYKNKGAYIILQAPDFSDPQFHSFEAVKPRPKAHPYYD 388
Cdd:cd07418 320 GKLITLFSAPDYPQFQATEERYNNKGAYIILQPPDFSDPQFHTFEAVKPRPKANPYYD 377
 
Name Accession Description Interval E-value
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 11-388 0e+00

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: 757.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  11 WPDGGALTNDWVHGLMSCFEWSSWNLPPSQLPSLLPVNVFDSLVLTAHKILHKERNCVHIDDlDSVSNVVVVGDIHGQLH 90
Cdd:cd07418   1 WPDGGALTNEWVHELMSVFEWSSRNLPPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIDV-EDVCEVVVVGDVHGQLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  91 DLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGK 170
Cdd:cd07418  80 DVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 171 HVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLPKRTTRGKKNRRVVLLEPEPSSMKLGTLDELMQARRSVLDPPWE 250
Cdd:cd07418 160 HVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNRRVLLLEPESESLKLGTLDDLMKARRSVLDPPGE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 251 GSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEGPDAREKRTGLGGMDNGYTIDHNVES 330
Cdd:cd07418 240 GSNLIPGDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPDAREKRPGLAGMNKGYTVDHDVES 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42570616 331 GKLITIFSAPDYPQFQATEERYKNKGAYIILQAPDFSDPQFHSFEAVKPRPKAHPYYD 388
Cdd:cd07418 320 GKLITLFSAPDYPQFQATEERYNNKGAYIILQPPDFSDPQFHTFEAVKPRPKANPYYD 377
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 45-378 6.08e-73

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: 229.41  E-value: 6.08e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616     45 LPVNVFDSLVLTAHKILHKERNCVHIDdldsvSNVVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLET 124
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS-----APVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    125 FLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYgdkGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLfrsp 204
Cdd:smart00156  75 ILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGL---- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    205 vlpkrttrgkknrrvvllepepsSMKLGTLDELMQARRSVLDPPWEgsnlIPGDVLWSDPSMT-PGLSPNeQRGIGLLWG 283
Cdd:smart00156 148 -----------------------SPDLTTLDDIRKLKRPQEPPDDG----LLIDLLWSDPDQPvNGFGPS-IRGASYIFG 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    284 PDCTEDFLKKYELKLIIRSHEgpdarekrtglggM-DNGYTIDHNvesGKLITIFSAPDYpqfqatEERYKNKGAYIILQ 362
Cdd:smart00156 200 PDAVDEFLKKNNLKLIIRAHQ-------------VvDDGYEFFAD---GKLVTIFSAPNY------CDRFGNKAAVLKVD 257

                          330
                   ....*....|....*.
gi 42570616    363 apDFSDPQFHSFEAVK 378
Cdd:smart00156 258 --KDLKLTFEQFKPGK 271
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 79-386 2.35e-39

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 143.03  E-value: 2.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616   79 VVVVGDIHGQLHDLLFLLKDTG-FPCQNrcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGF 157
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGGdIPNAN--YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  158 EKEVLTKYGDKGKhvYRKCLGCFEGLPLASIISGRVYTAHGGLfrspvlpkrttrgkknrrvvllepepsSMKLGTLDEL 237
Cdd:PTZ00239 123 YEEILRKYGNSNP--WRLFMDVFDCLPLAALIEGQILCVHGGL---------------------------SPDMRTIDQI 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  238 MQARRSVlDPPWEGSNLipgDVLWSDPSMTPGLSPNeQRGIGLLWGPDCTEDFLKKYELKLIIRSHEgpdarekrtglgG 317
Cdd:PTZ00239 174 RTIDRKI-EIPHEGPFC---DLMWSDPEEVEYWAVN-SRGAGYLFGAKVTKEFCRLNDLTLICRAHQ------------L 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42570616  318 MDNGYtiDHNVESGKLITIFSAPDYPqfqateerYKNKGAYIILQAPDFSDPQFHSFEAVKPRPKAHPY 386
Cdd:PTZ00239 237 VMEGY--KYWFPDQNLVTVWSAPNYC--------YRCGNIASILCLDENLQQTWKTFKEVPESAKSINP 295
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 79-191 6.12e-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: 73.40  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    79 VVVVGDIH--GQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPdrVYLLRGNHESKYCtsmyg 156
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP--VYLVRGNHDFDYG----- 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 42570616   157 fEKEVLTKYGDKGKHVYRKCLGCFEGLPLASIISG 191
Cdd:pfam00149  76 -ECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
 
Name Accession Description Interval E-value
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 11-388 0e+00

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: 757.41  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  11 WPDGGALTNDWVHGLMSCFEWSSWNLPPSQLPSLLPVNVFDSLVLTAHKILHKERNCVHIDDlDSVSNVVVVGDIHGQLH 90
Cdd:cd07418   1 WPDGGALTNEWVHELMSVFEWSSRNLPPSELPSVLPVNVFDSLVLTAHKILHREPNCVRIDV-EDVCEVVVVGDVHGQLH 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  91 DLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGK 170
Cdd:cd07418  80 DVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGK 159

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 171 HVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLPKRTTRGKKNRRVVLLEPEPSSMKLGTLDELMQARRSVLDPPWE 250
Cdd:cd07418 160 HVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQKGKNRRVLLLEPESESLKLGTLDDLMKARRSVLDPPGE 239

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 251 GSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEGPDAREKRTGLGGMDNGYTIDHNVES 330
Cdd:cd07418 240 GSNLIPGDVLWSDPSLTPGLSPNKQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEGPDAREKRPGLAGMNKGYTVDHDVES 319

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42570616 331 GKLITIFSAPDYPQFQATEERYKNKGAYIILQAPDFSDPQFHSFEAVKPRPKAHPYYD 388
Cdd:cd07418 320 GKLITLFSAPDYPQFQATEERYNNKGAYIILQPPDFSDPQFHTFEAVKPRPKANPYYD 377
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 12-385 4.40e-80

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: 249.48  E-value: 4.40e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  12 PDGGALTNDWVHGLMSCFewsswnlppsQLPSLLPVNVFDSLVLTAHKILHKERNCVHIDdLDSVSNVVVVGDIHGQLHD 91
Cdd:cd07417   6 LEDGKVTLEFVKEMMEWF----------KDQKKLHKKYAYQILLQVKEILKKLPSLVEIT-IPEGEKITVCGDTHGQFYD 74

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  92 LLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKgkh 171
Cdd:cd07417  75 LLNIFELNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQ--- 151

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 172 VYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLpkrttrgkknrrvvllepepssmklgTLDELMQARRSvLDPPWEG 251
Cdd:cd07417 152 MFNLFSEVFNWLPLAHLINGKVLVVHGGLFSDDGV--------------------------TLDDIRKIDRF-RQPPDSG 204

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 252 snlIPGDVLWSDPSMTPGLSPNeQRGIGLLWGPDCTEDFLKKYELKLIIRSHEgpdarekrtglgGMDNGYTIDHNvesG 331
Cdd:cd07417 205 ---LMCELLWSDPQPQPGRGPS-KRGVGCQFGPDVTKRFLEENNLDYIIRSHE------------VKDEGYEVEHD---G 265

                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....
gi 42570616 332 KLITIFSAPDYPQFQAteerykNKGAYIILQAPDfSDPQFHSFEAVkPRPKAHP 385
Cdd:cd07417 266 KCITVFSAPNYCDQMG------NKGAFIRFKGSD-LKPKFTQFEAV-PHPNVKP 311
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 80-361 4.45e-75

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: 233.42  E-value: 4.45e-75
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  80 VVVGDIHGQLHDLLFLLKDTGFPCqNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEK 159
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPP-EDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 160 EVLTKYGDK-GKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSpvlpkrttrgkknrrvvllepepssmkLGTLDELM 238
Cdd:cd00144  80 ERTLRCLRKgGEELWREFNEVFNYLPLAALVDGKILCVHGGLSPD---------------------------LTLLDQIR 132

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 239 QARrsvldPPWEGSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEGPdarekrtglggm 318
Cdd:cd00144 133 NIR-----PIENPDDQLVEDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPV------------ 195

                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 42570616 319 DNGYTIDHNvesGKLITIFSAPDYPQFqateerYKNKGAYIIL 361
Cdd:cd00144 196 EGGYEFLHG---GKLITIFSAPNYCGK------GGNKLAALVV 229
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 45-378 6.08e-73

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: 229.41  E-value: 6.08e-73
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616     45 LPVNVFDSLVLTAHKILHKERNCVHIDdldsvSNVVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLET 124
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS-----APVTVCGDIHGQFDDLLRLFDKNGQPPETN-YVFLGDYVDRGPFSIEV 74

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    125 FLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYgdkGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLfrsp 204
Cdd:smart00156  75 ILLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGL---- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    205 vlpkrttrgkknrrvvllepepsSMKLGTLDELMQARRSVLDPPWEgsnlIPGDVLWSDPSMT-PGLSPNeQRGIGLLWG 283
Cdd:smart00156 148 -----------------------SPDLTTLDDIRKLKRPQEPPDDG----LLIDLLWSDPDQPvNGFGPS-IRGASYIFG 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    284 PDCTEDFLKKYELKLIIRSHEgpdarekrtglggM-DNGYTIDHNvesGKLITIFSAPDYpqfqatEERYKNKGAYIILQ 362
Cdd:smart00156 200 PDAVDEFLKKNNLKLIIRAHQ-------------VvDDGYEFFAD---GKLVTIFSAPNY------CDRFGNKAAVLKVD 257

                          330
                   ....*....|....*.
gi 42570616    363 apDFSDPQFHSFEAVK 378
Cdd:smart00156 258 --KDLKLTFEQFKPGK 271
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 44-377 8.06e-68

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: 216.68  E-value: 8.06e-68
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  44 LLPVNVFDSLVLTAHKILHKERNCVHIDdldsvSNVVVVGDIHGQLHDLLFLLKdTGFPCQNRCYVFNGDYVDRGAWGLE 123
Cdd:cd07415  14 LLPESEVKSLCEKAKEILVKESNVQRVR-----SPVTVCGDIHGQFYDLLELFR-IGGDVPDTNYLFLGDYVDRGYYSVE 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 124 TFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGkhVYRKCLGCFEGLPLASIISGRVYTAHGGLfrS 203
Cdd:cd07415  88 TFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNAN--VWKYFTDLFDYLPLAALIDGQIFCVHGGL--S 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 204 PVLPkrttrgkknrrvvllepepssmklgTLDELMQARRsVLDPPWEGsnlIPGDVLWSDPSMTPGLSPNeQRGIGLLWG 283
Cdd:cd07415 164 PSIQ-------------------------TLDQIRALDR-FQEVPHEG---PMCDLLWSDPDDREGWGIS-PRGAGYLFG 213

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 284 PDCTEDFLKKYELKLIIRSHEgpdarekrtgLggMDNGYTIDHNvesGKLITIFSAPDYPQfqateeRYKNKGAyiILQA 363
Cdd:cd07415 214 QDVVEEFNHNNGLTLICRAHQ----------L--VMEGYQWMFN---NKLVTVWSAPNYCY------RCGNVAS--ILEL 270

                       330
                ....*....|....
gi 42570616 364 PDFSDPQFHSFEAV 377
Cdd:cd07415 271 DEHLNRSFKQFEAA 284
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 57-361 2.65e-61

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: 200.33  E-value: 2.65e-61
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  57 AHKILHKERNCVHIDDldSVSN-VVVVGDIHGQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLM 135
Cdd:cd07420  32 ARKSLKQLPNISRVST--SYSKeVTICGDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFVDRGKRSIEILMILFAFVLVY 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 136 PDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKGKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSPVLP--KRTTRG 213
Cdd:cd07420 110 PNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGISDSTDLDllDKIDRH 189

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 214 KknrrvvllepepssMKlGTLDELMQarrsVLdppwegsnlipgDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKK 293
Cdd:cd07420 190 K--------------YV-STKTEWQQ----VV------------DILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQK 238

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 42570616 294 YELKLIIRSHEGPdarekrtglggmDNGYTIDHNvesGKLITIFSAPDYpqfqatEERYKNKGAYIIL 361
Cdd:cd07420 239 HGLSLLIRSHECK------------PEGYEFCHN---NKVITIFSASNY------YEEGSNRGAYVKL 285
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 53-357 4.68e-53

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: 179.04  E-value: 4.68e-53
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  53 LVLTAHKILHKERNCVHIDDldsvsNVVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLETFLVLLSWK 132
Cdd:cd07416  24 IITEGAEILRQEPNLLRIEA-----PVTVCGDIHGQFYDLLKLFEVGGSPANTR-YLFLGDYVDRGYFSIECVLYLWALK 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 133 VLMPDRVYLLRGNHESKYCTSMYGFEKEVLTKYGDKgkhVYRKCLGCFEGLPLASIISGRVYTAHGGLfrSPvlpkrttr 212
Cdd:cd07416  98 ILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSER---VYDACMEAFDCLPLAALMNQQFLCVHGGL--SP-------- 164

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 213 gkknrrvvllepepssmKLGTLDELMQARRsVLDPPWEGSNLipgDVLWSDP-------SMTPGLSPNEQRGIGLLWGPD 285
Cdd:cd07416 165 -----------------ELKTLDDIRKLDR-FREPPSYGPMC---DLLWSDPledfgneKTQEHFVHNTVRGCSYFYSYR 223

                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 42570616 286 CTEDFLKKYELKLIIRSHEgpdarekrtglgGMDNGYTIDHNVESG---KLITIFSAPDYPqfqateERYKNKGA 357
Cdd:cd07416 224 AVCEFLQKNNLLSIIRAHE------------AQDAGYRMYRKSQTTgfpSLITIFSAPNYL------DVYNNKAA 280
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 81-342 8.50e-45

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: 157.12  E-value: 8.50e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  81 VVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKE 160
Cdd:cd07414  54 ICGDIHGQYYDLLRLFEYGGFPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE 132

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 161 VLTKYGDKgkhVYRKCLGCFEGLPLASIISGRVYTAHGGLfrSPVLpkrttrgkknrrvvllepepSSMKlgtldelmQA 240
Cdd:cd07414 133 CKRRYNIK---LWKTFTDCFNCLPVAAIVDEKIFCCHGGL--SPDL--------------------QSME--------QI 179

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 241 RRSV--LDPPWEGsnlIPGDVLWSDPSM-TPGLSPNEqRGIGLLWGPDCTEDFLKKYELKLIIRSHEgpdarekrtglgG 317
Cdd:cd07414 180 RRIMrpTDVPDQG---LLCDLLWSDPDKdVQGWGEND-RGVSFTFGADVVAKFLHKHDLDLICRAHQ------------V 243

                       250       260
                ....*....|....*....|....*
gi 42570616 318 MDNGYTIdhnVESGKLITIFSAPDY 342
Cdd:cd07414 244 VEDGYEF---FAKRQLVTLFSAPNY 265
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 81-361 6.23e-44

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: 155.29  E-value: 6.23e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  81 VVGDIHGQLHDLLFLLKDTGFPCQNRC-------YVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTS 153
Cdd:cd07419  52 IFGDIHGQFGDLMRLFDEYGSPVTEEAgdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINA 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 154 MYGFEKEVLTKYGDK---GKHVYRKCLGCFEGLPLASIISGRVYTAHGGLFRSpvlpkrttrgkknrrvvllepepssmk 230
Cdd:cd07419 132 LFGFREECIERLGEDirdGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRS--------------------------- 184

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 231 LGTLDELMQARRSVLDPPwegSNLIPGDVLWSDPSMT---PGLSPN--EQRGIGLL--WGPDCTEDFLKKYELKLIIRSH 303
Cdd:cd07419 185 INHIHQIENLKRPITMEA---GSPVVMDLLWSDPTENdsvLGLRPNaiDPRGTGLIvkFGPDRVMEFLEENDLQMIIRAH 261

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 42570616 304 EGPdarekrtglggMDnGYTidhNVESGKLITIFSAPDYPQfqateeRYKNKGAYIIL 361
Cdd:cd07419 262 ECV-----------MD-GFE---RFAQGHLITLFSATNYCG------TAGNAGAILVL 298
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 79-386 2.35e-39

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 143.03  E-value: 2.35e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616   79 VVVVGDIHGQLHDLLFLLKDTG-FPCQNrcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGF 157
Cdd:PTZ00239  45 VNVCGDIHGQFYDLQALFKEGGdIPNAN--YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGF 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  158 EKEVLTKYGDKGKhvYRKCLGCFEGLPLASIISGRVYTAHGGLfrspvlpkrttrgkknrrvvllepepsSMKLGTLDEL 237
Cdd:PTZ00239 123 YEEILRKYGNSNP--WRLFMDVFDCLPLAALIEGQILCVHGGL---------------------------SPDMRTIDQI 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  238 MQARRSVlDPPWEGSNLipgDVLWSDPSMTPGLSPNeQRGIGLLWGPDCTEDFLKKYELKLIIRSHEgpdarekrtglgG 317
Cdd:PTZ00239 174 RTIDRKI-EIPHEGPFC---DLMWSDPEEVEYWAVN-SRGAGYLFGAKVTKEFCRLNDLTLICRAHQ------------L 236

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42570616  318 MDNGYtiDHNVESGKLITIFSAPDYPqfqateerYKNKGAYIILQAPDFSDPQFHSFEAVKPRPKAHPY 386
Cdd:PTZ00239 237 VMEGY--KYWFPDQNLVTVWSAPNYC--------YRCGNIASILCLDENLQQTWKTFKEVPESAKSINP 295
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 79-342 6.21e-35

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 130.80  E-value: 6.21e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616   79 VVVVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFE 158
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFPPYSN-YLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  159 KEVLTKYGDKgkhVYRKCLGCFEGLPLASIISGRVYTAHGGLfrspvlpkrttrgkknrrvvllepEPSSMKLGTLDELM 238
Cdd:PTZ00244 133 DDVKRRYNIK---LFKAFTDVFNTMPVCCVISEKIICMHGGL------------------------SPDLTSLASVNEIE 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  239 QArrsvLDPPWEGsnlIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEgpdarekrtglgGM 318
Cdd:PTZ00244 186 RP----CDVPDRG---ILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQ------------VM 246

                        250       260
                 ....*....|....*....|....
gi 42570616  319 DNGYTIdhnVESGKLITIFSAPDY 342
Cdd:PTZ00244 247 ERGYGF---FASRQLVTVFSAPNY 267
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 81-342 8.94e-34

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 128.24  E-value: 8.94e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616   81 VVGDIHGQLHDLLFLLKDTGFPCQNRcYVFNGDYVDRGAWGLETFLVLLSWKVLMPDRVYLLRGNHESKYCTSMYGFEKE 160
Cdd:PTZ00480  63 ICGDVHGQYFDLLRLFEYGGYPPESN-YLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  161 VLTKYGDKgkhVYRKCLGCFEGLPLASIISGRVYTAHGGlfrspvlpkrttrgkknrrvvlLEPEpssmklgtLDELMQA 240
Cdd:PTZ00480 142 CKRRYTIK---LWKTFTDCFNCLPVAALIDEKILCMHGG----------------------LSPE--------LSNLEQI 188

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  241 RRsVLDPPWEGSNLIPGDVLWSDPSMTPGLSPNEQRGIGLLWGPDCTEDFLKKYELKLIIRSHEgpdarekrtglgGMDN 320
Cdd:PTZ00480 189 RR-IMRPTDVPDTGLLCDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQ------------VVED 255

                        250       260
                 ....*....|....*....|..
gi 42570616  321 GYTIdhnVESGKLITIFSAPDY 342
Cdd:PTZ00480 256 GYEF---FSKRQLVTLFSAPNY 274
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 79-191 6.12e-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: 73.40  E-value: 6.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616    79 VVVVGDIH--GQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKVLMPdrVYLLRGNHESKYCtsmyg 156
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVP--VYLVRGNHDFDYG----- 75

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 42570616   157 fEKEVLTKYGDKGKHVYRKCLGCFEGLPLASIISG 191
Cdd:pfam00149  76 -ECLRLYPYLGLLARPWKRFLEVFNFLPLAGILSG 109
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 81-219 2.60e-06

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


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 48.28  E-value: 2.60e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  81 VVGDIHGQLHDLLFLLKDTGF----------PcQNRCYVFNGDYVDRGAWGLETflVLLSWKVLMPDRVYLLRGNHESKY 150
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGYqkkeeglyvhP-EGRKLVFLGDLVDRGPDSIDV--LRLVMNMVKAGKALYVPGNHCNKL 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616 151 C--------TSMYGFEKEV--LTKYG-DKGKHVYRKCLGCFEGLPLASIIS-GRVYTAHGGLfrspvlpKRTTRGKKNRR 218
Cdd:cd07423  79 YrylkgrnvQLAHGLETTVeeLEALSkEERPEFRERFAEFLESLPSHLVLDgGRLVVAHAGI-------KEEMIGRGSKR 151


                .
gi 42570616 219 V 219
Cdd:cd07423 152 V 152
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 81-219 1.22e-05

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 46.24  E-value: 1.22e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616   81 VVGDIHGQLHDLLFLLK------DTGFPC--QNRCYVFNGDYVDRGAWGLETFLVLlsWKVLMPDRVYLLRGNHeskyCT 152
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEklgynwSSGLPVhpDQRKLAFVGDLTDRGPHSLRMIEIV--WELVEKKAAYYVPGNH----CN 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  153 SMYGF-----------------EKEVLTKygDKGKHVYRKCLGCFEGLPLASII-SGRVYTAHGGLfrspvlpKRTTRGK 214
Cdd:PRK13625  79 KLYRFflgrnvtiahglettvaEYEALPS--HKQNMIKEKFITLYEQAPLYHILdEGRLVVAHAGI-------RQDYIGR 149


                 ....*
gi 42570616  215 KNRRV 219
Cdd:PRK13625 150 QDKKV 154
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 80-147 5.93e-05

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 42.64  E-value: 5.93e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42570616  80 VVVGDIHGQLHDLLFLLKD-TGFPCQNRCYVFNGDYVDRGAWGLETFLVLLSWKvLMPDRVYLLRGNHE 147
Cdd:cd00838   1 LVISDIHGNLEALEAVLEAaLAKAEKPDLVICLGDLVDYGPDPEEVELKALRLL-LAGIPVYVVPGNHD 68
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 81-147 1.58e-03

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: 39.61  E-value: 1.58e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  81 VVGDIHGQLHDLLFLLKDTGF-PCQNRCYVFnGDYVDRGAWGLETfLVLLS--WkvlmpdrVYLLRGNHE 147
Cdd:cd07424   5 VVGDIHGHFQRLQRALDAVGFdPARDRLISV-GDLVDRGPESLEV-LELLKqpW-------FHAVQGNHE 65
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 80-206 2.60e-03

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: 38.82  E-value: 2.60e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 42570616  80 VVVGDIHGQLHDLLFLLKDTGFPCQNRCYVFN-------GDYVDRGAWGLETFLVLLSWKVLMPD---RVYLLRGNHES- 148
Cdd:cd07425   1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEILKLLEKLKRQARKaggKVILLLGNHELm 80

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 42570616 149 ------KYCTS-----MYGFEKeVLTKYGDKGKHVYRKclgcFEGLPLASIISGRVYtAHGGLfrSPVL 206
Cdd:cd07425  81 nlcgdfRYVHPrglneFGGVAK-RRYALLSDGGYIGRY----LRTHPVVLVVNDILF-VHGGL--GPLW 141
pphA PRK11439
protein-serine/threonine phosphatase;
78-147 8.65e-03

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 37.44  E-value: 8.65e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 42570616   78 NVVVVGDIHGQLHDLLFLLKDTGFPCQNRCYVFNGDYVDRGAWGLETfLVLL--SWkvlmpdrVYLLRGNHE 147
Cdd:PRK11439  18 HIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRC-LQLLeeHW-------VRAVRGNHE 81
 
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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