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Conserved domains on  [gi|119626160|gb|EAX05755|]
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protein phosphatase, EF-hand calcium binding domain 2, isoform CRA_d [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 122-537 0e+00

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: 599.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 122 PLLPDHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFYKNGLPSPER 201
Cdd:cd07420    1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 202 SYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKVHGKEILRTLQDVFCWLPLA 281
Cdd:cd07420   81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 282 TLIDEKVLILHGGVSDITDLELLDKIERSKIVStmrcktrqksekqmeekrranqkssaqgpipwflpesrslpssplrl 361
Cdd:cd07420  161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 362 gsykaqktsrsssipcsgsldgrelsrqvrssvelelercrqqagllvtgekeepsrsaseadseagelrkpTQEEWRQV 441
Cdd:cd07420  194 ------------------------------------------------------------------------TKTEWQQV 201

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 442 VDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGA 521
Cdd:cd07420  202 VDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGA 281

                        410
                 ....*....|....*.
gi 119626160 522 YVKLGPALTPHIVQYQ 537
Cdd:cd07420  282 YVKLGPQLTPHFVQYQ 297
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 122-537 0e+00

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: 599.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 122 PLLPDHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFYKNGLPSPER 201
Cdd:cd07420    1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 202 SYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKVHGKEILRTLQDVFCWLPLA 281
Cdd:cd07420   81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 282 TLIDEKVLILHGGVSDITDLELLDKIERSKIVStmrcktrqksekqmeekrranqkssaqgpipwflpesrslpssplrl 361
Cdd:cd07420  161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 362 gsykaqktsrsssipcsgsldgrelsrqvrssvelelercrqqagllvtgekeepsrsaseadseagelrkpTQEEWRQV 441
Cdd:cd07420  194 ------------------------------------------------------------------------TKTEWQQV 201

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 442 VDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGA 521
Cdd:cd07420  202 VDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGA 281

                        410
                 ....*....|....*.
gi 119626160 522 YVKLGPALTPHIVQYQ 537
Cdd:cd07420  282 YVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 141-540 5.45e-90

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: 279.10  E-value: 5.45e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   141 LHARYVLNLLYETKKHLVQLPNINRVStcysEEITVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEIL 220
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQP-PETNYVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   221 MILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYkvhGKEILRTLQDVFCWLPLATLIDEKVLILHGGVS-DIT 299
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSpDLT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   300 DLELLDKIERSKIvstmrcktrqksekqmeekrranqkssaqgpipwflpesrslpssplrlgsykaqktsrsssIPCSG 379
Cdd:smart00156 153 TLDDIRKLKRPQE--------------------------------------------------------------PPDDG 170

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   380 sldgrelsrqvrssvelelercrqqagllvtgekeepsrsaseadseagelrkptqeewrQVVDILWSDPMA-QEGCKAN 458
Cdd:smart00156 171 ------------------------------------------------------------LLIDLLWSDPDQpVNGFGPS 190

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   459 tIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQA 538
Cdd:smart00156 191 -IRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKP 269


                   ..
gi 119626160   539 NK 540
Cdd:smart00156 270 GK 271
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 174-512 5.11e-34

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 131.18  E-value: 5.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 174 ITVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFT 253
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFP-PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 254 KEVMNKYKVhgkEILRTLQDVFCWLPLATLIDEKVLILHGGVS-DITDLELLDKIERskivstmrcktrqksekqmeekr 332
Cdd:PTZ00244 133 DDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHGGLSpDLTSLASVNEIER----------------------- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 333 ranqkssaqgpipwflpesrslpssplrlgsykaqktsrsssiPCsgsldgrelsrqvrssvelelercrqqagllvtge 412
Cdd:PTZ00244 187 -------------------------------------------PC----------------------------------- 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 413 kEEPSRSAseadseagelrkptqeewrqVVDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKP 492
Cdd:PTZ00244 189 -DVPDRGI--------------------LCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVME 247

                        330       340
                 ....*....|....*....|
gi 119626160 493 EGYEFCHNRKVLTIFSASNY 512
Cdd:PTZ00244 248 RGYGFFASRQLVTVFSAPNY 267
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 174-284 1.55e-13

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: 67.24  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160  174 ITVCGDLH--GQLDDLIFIFykNGLPSPERSYVF--NGDFVDRGKDSVEILmiLFAFMLVYPKEFHLNRGNHEDHMVNLr 249
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVL--ELLERLIKYVPVYLVRGNHDFDYGEC- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 119626160  250 ygftkEVMNKYKVHGKEILRTLQDVFCWLPLATLI 284
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
 
Name Accession Description Interval E-value
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 122-537 0e+00

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: 599.78  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 122 PLLPDHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFYKNGLPSPER 201
Cdd:cd07420    1 PLTKTHIDLLIEAFKLKQRLHAKYVLLILREARKSLKQLPNISRVSTSYSKEVTICGDLHGKLDDLLLIFYKNGLPSPEN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 202 SYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKVHGKEILRTLQDVFCWLPLA 281
Cdd:cd07420   81 PYVFNGDFVDRGKRSIEILMILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHGKKILRLLEDVFSWLPLA 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 282 TLIDEKVLILHGGVSDITDLELLDKIERSKIVStmrcktrqksekqmeekrranqkssaqgpipwflpesrslpssplrl 361
Cdd:cd07420  161 TIIDNKVLVVHGGISDSTDLDLLDKIDRHKYVS----------------------------------------------- 193

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 362 gsykaqktsrsssipcsgsldgrelsrqvrssvelelercrqqagllvtgekeepsrsaseadseagelrkpTQEEWRQV 441
Cdd:cd07420  194 ------------------------------------------------------------------------TKTEWQQV 201

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 442 VDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGA 521
Cdd:cd07420  202 VDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNYYEEGSNRGA 281

                        410
                 ....*....|....*.
gi 119626160 522 YVKLGPALTPHIVQYQ 537
Cdd:cd07420  282 YVKLGPQLTPHFVQYQ 297
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 141-540 5.45e-90

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: 279.10  E-value: 5.45e-90
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   141 LHARYVLNLLYETKKHLVQLPNINRVStcysEEITVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEIL 220
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVS----APVTVCGDIHGQFDDLLRLFDKNGQP-PETNYVFLGDYVDRGPFSIEVI 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   221 MILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYkvhGKEILRTLQDVFCWLPLATLIDEKVLILHGGVS-DIT 299
Cdd:smart00156  76 LLLFALKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKY---GERIYEKFNEAFSWLPLAALINGKILCMHGGLSpDLT 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   300 DLELLDKIERSKIvstmrcktrqksekqmeekrranqkssaqgpipwflpesrslpssplrlgsykaqktsrsssIPCSG 379
Cdd:smart00156 153 TLDDIRKLKRPQE--------------------------------------------------------------PPDDG 170

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   380 sldgrelsrqvrssvelelercrqqagllvtgekeepsrsaseadseagelrkptqeewrQVVDILWSDPMA-QEGCKAN 458
Cdd:smart00156 171 ------------------------------------------------------------LLIDLLWSDPDQpVNGFGPS 190

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160   459 tIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQA 538
Cdd:smart00156 191 -IRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAPNYCDRFGNKAAVLKVDKDLKLTFEQFKP 269


                   ..
gi 119626160   539 NK 540
Cdd:smart00156 270 GK 271
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 114-543 1.44e-86

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: 271.82  E-value: 1.44e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 114 YTGPRLSFPLLP-DHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFY 192
Cdd:cd07417    1 YSGPKLEDGKVTlEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEITIPEGEKITVCGDTHGQFYDLLNIFE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 193 KNGLPSPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYkvhGKEILRTLQ 272
Cdd:cd07417   81 LNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKY---NEQMFNLFS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 273 DVFCWLPLATLIDEKVLILHGGvsditdlelldkierskivstmrcktrqksekqmeekrranqkssaqgpipwflpesr 352
Cdd:cd07417  158 EVFNWLPLAHLINGKVLVVHGG---------------------------------------------------------- 179

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 353 sLPSSplrlgsykaqktsrsssipcsgslDGRELSrQVRssvelELERCRQ--QAGLlvtgekeepsrsaseadseagel 430
Cdd:cd07417  180 -LFSD------------------------DGVTLD-DIR-----KIDRFRQppDSGL----------------------- 205

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 431 rkptqeewrqVVDILWSDPMAQEGcKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSAS 510
Cdd:cd07417  206 ----------MCELLWSDPQPQPG-RGPSKRGVGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAP 274

                        410       420       430
                 ....*....|....*....|....*....|....
gi 119626160 511 NYYEVGSNRGAYVKL-GPALTPHIVQYQAnkVTH 543
Cdd:cd07417  275 NYCDQMGNKGAFIRFkGSDLKPKFTQFEA--VPH 306
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 175-525 1.16e-69

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: 224.56  E-value: 1.16e-69
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 175 TVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTK 254
Cdd:cd00144    1 IVVGDIHGCFDDLLRLLEKLGFP-PEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 255 EVMNK-YKVHGKEILRTLQDVFCWLPLATLIDEKVLILHGGVSDitDLELLDKIERSkivstmrcktrqksekqmeekrr 333
Cdd:cd00144   80 ERTLRcLRKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSP--DLTLLDQIRNI----------------------- 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 334 anqkssaqgpipwflpesrslpssplrlgsykaqktsrsssipcsgsldgrelsrqvrssvelelercrqqagllvtgek 413
Cdd:cd00144      --------------------------------------------------------------------------------

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 414 eepsrsaseadseagelrKPTQEEWRQVV-DILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKP 492
Cdd:cd00144  135 ------------------RPIENPDDQLVeDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVE 196

                        330       340       350
                 ....*....|....*....|....*....|...
gi 119626160 493 EGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKL 525
Cdd:cd00144  197 GGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 149-527 2.59e-51

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: 181.15  E-value: 2.59e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 149 LLYETKKHLVQLPNINRVSTCYSEEITVCGDLHGQLDDLIFIFYKNGLPSPERSYVFNGDFVDRGKDSVEILMILFAFML 228
Cdd:cd07418   43 LVLTAHKILHREPNCVRIDVEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLLSWKV 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 229 VYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKVHGKEILRTLQDVFCWLPLATLIDEKVLILHGGVSDITDLELLDKIE 308
Cdd:cd07418  123 LLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLGCFEGLPLASIIAGRVYTAHGGLFRSPSLPKRKKQK 202

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 309 RSKIVSTMRCktrqksekqmeekrranqkssaqgpipwflPESRSLPssplrLGSYKA-QKTSRSSSIPcsgSLDGREls 387
Cdd:cd07418  203 GKNRRVLLLE------------------------------PESESLK-----LGTLDDlMKARRSVLDP---PGEGSN-- 242

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 388 rqvrssvelelercrqqaglLVTGekeepsrsaseadseagelrkptqeewrqvvDILWSDPMAQEGCKANTIRGGGCYF 467
Cdd:cd07418  243 --------------------LIPG-------------------------------DVLWSDPSLTPGLSPNKQRGIGLLW 271

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 468 GPDVTQQLLQKYNLQFLIRSHEC------KPE------GYEFCHN---RKVLTIFSASNY------YEVGSNRGAYVKLG 526
Cdd:cd07418  272 GPDCTEEFLEKNNLKLIIRSHEGpdarekRPGlagmnkGYTVDHDvesGKLITLFSAPDYpqfqatEERYNNKGAYIILQ 351


                 .
gi 119626160 527 P 527
Cdd:cd07418  352 P 352
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 157-538 1.51e-49

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: 173.54  E-value: 1.51e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 157 LVQLPNINRVSTcyseEITVCGDLHGQLDDLIFIFyKNGLPSPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHL 236
Cdd:cd07415   31 LVKESNVQRVRS----PVTVCGDIHGQFYDLLELF-RIGGDVPDTNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITL 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 237 NRGNHEDHMVNLRYGFTKEVMNKYkvhGKE-ILRTLQDVFCWLPLATLIDEKVLILHGGVS-DITDLELLDKIERskivs 314
Cdd:cd07415  106 LRGNHESRQITQVYGFYDECLRKY---GNAnVWKYFTDLFDYLPLAALIDGQIFCVHGGLSpSIQTLDQIRALDR----- 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 315 tmrcktrqksekQMEekrranqkssaqgpipwflpesrslpssplrlgsykaqktsrsssIPCSGSLdgrelsrqvrssv 394
Cdd:cd07415  178 ------------FQE---------------------------------------------VPHEGPM------------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 395 elelerCrqqagllvtgekeepsrsaseadseagelrkptqeewrqvvDILWSDPMAQEGCKANTiRGGGCYFGPDVTQQ 474
Cdd:cd07415  188 ------C-----------------------------------------DLLWSDPDDREGWGISP-RGAGYLFGQDVVEE 219

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119626160 475 LLQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALTPHIVQYQA 538
Cdd:cd07415  220 FNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNYCYRCGNVASILELDEHLNRSFKQFEA 283
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 174-521 2.08e-42

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: 154.42  E-value: 2.08e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 174 ITVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFT 253
Cdd:cd07414   52 LKICGDIHGQYYDLLRLFEYGGFP-PESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 254 KEVMNKYKVhgkEILRTLQDVFCWLPLATLIDEKVLILHGGVSdiTDLELLDKIERskivstmrcktrqksekqmeekrr 333
Cdd:cd07414  131 DECKRRYNI---KLWKTFTDCFNCLPVAAIVDEKIFCCHGGLS--PDLQSMEQIRR------------------------ 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 334 anqkssaqgpipwflpesrslpssplrlgsykaqkTSRSSSIPCSGSLdgrelsrqvrssvelelerCrqqagllvtgek 413
Cdd:cd07414  182 -----------------------------------IMRPTDVPDQGLL-------------------C------------ 195

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 414 eepsrsaseadseagelrkptqeewrqvvDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPE 493
Cdd:cd07414  196 -----------------------------DLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVED 246

                        330       340
                 ....*....|....*....|....*...
gi 119626160 494 GYEFCHNRKVLTIFSASNYYEVGSNRGA 521
Cdd:cd07414  247 GYEFFAKRQLVTLFSAPNYCGEFDNAGA 274
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 125-525 7.09e-40

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: 147.84  E-value: 7.09e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 125 PDHaTALVEAFRLKQQLHARYVLNLLYETKKHLVQLPNINRVStcysEEITVCGDLHGQLDDLIFIFYKNGLPSPERsYV 204
Cdd:cd07416    1 PRV-DILKAHFMREGRLSEEDALRIITEGAEILRQEPNLLRIE----APVTVCGDIHGQFYDLLKLFEVGGSPANTR-YL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 205 FNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYkvhGKEILRTLQDVFCWLPLATLI 284
Cdd:cd07416   75 FLGDYVDRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY---SERVYDACMEAFDCLPLAALM 151

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 285 DEKVLILHGGVS-DITDLELLDKIERSKivstmrcktrqksekqmeekrranqKSSAQGPIpwflpesrslpssplrlgs 363
Cdd:cd07416  152 NQQFLCVHGGLSpELKTLDDIRKLDRFR-------------------------EPPSYGPM------------------- 187

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 364 ykaqktsrsssipCsgsldgrelsrqvrssvelelercrqqagllvtgekeepsrsaseadseagelrkptqeewrqvvD 443
Cdd:cd07416  188 -------------C-----------------------------------------------------------------D 189

                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 444 ILWSDPMAQEGCKA-------NTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKPEGYEFCHNRK------VLTIFSAS 510
Cdd:cd07416  190 LLWSDPLEDFGNEKtqehfvhNTVRGCSYFYSYRAVCEFLQKNNLLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAP 269

                        410
                 ....*....|....*
gi 119626160 511 NYYEVGSNRGAYVKL 525
Cdd:cd07416  270 NYLDVYNNKAAVLKY 284
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 174-530 5.98e-37

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: 139.88  E-value: 5.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 174 ITVCGDLHGQLDDLIFIFYKNGLPSPERS-------YVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMV 246
Cdd:cd07419   50 IKIFGDIHGQFGDLMRLFDEYGSPVTEEAgdieyidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADI 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 247 NLRYGFTKEV---MNKYKVHGKEILRTLQDVFCWLPLATLIDEKVLILHGGV-SDITDLELLDKIERskivstmrcktrq 322
Cdd:cd07419  130 NALFGFREECierLGEDIRDGDSVWQRINRLFNWLPLAALIEDKIICVHGGIgRSINHIHQIENLKR------------- 196

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 323 ksekqmeekrranqkssaqgPIPwflpesrSLPSSPLrlgsykaqktsrsssipcsgsldgrelsrqvrssvelelercr 402
Cdd:cd07419  197 --------------------PIT-------MEAGSPV------------------------------------------- 206

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 403 qqagllvtgekeepsrsaseadseagelrkptqeewrqVVDILWSDPM---AQEGCKANTI--RGGGCY--FGPDVTQQL 475
Cdd:cd07419  207 --------------------------------------VMDLLWSDPTendSVLGLRPNAIdpRGTGLIvkFGPDRVMEF 248

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119626160 476 LQKYNLQFLIRSHECKPEGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPALT 530
Cdd:cd07419  249 LEENDLQMIIRAHECVMDGFERFAQGHLITLFSATNYCGTAGNAGAILVLGRDLV 303
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 174-512 5.11e-34

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 131.18  E-value: 5.11e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 174 ITVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFT 253
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFP-PYSNYLFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 254 KEVMNKYKVhgkEILRTLQDVFCWLPLATLIDEKVLILHGGVS-DITDLELLDKIERskivstmrcktrqksekqmeekr 332
Cdd:PTZ00244 133 DDVKRRYNI---KLFKAFTDVFNTMPVCCVISEKIICMHGGLSpDLTSLASVNEIER----------------------- 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 333 ranqkssaqgpipwflpesrslpssplrlgsykaqktsrsssiPCsgsldgrelsrqvrssvelelercrqqagllvtge 412
Cdd:PTZ00244 187 -------------------------------------------PC----------------------------------- 188

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 413 kEEPSRSAseadseagelrkptqeewrqVVDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKP 492
Cdd:PTZ00244 189 -DVPDRGI--------------------LCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVME 247

                        330       340
                 ....*....|....*....|
gi 119626160 493 EGYEFCHNRKVLTIFSASNY 512
Cdd:PTZ00244 248 RGYGFFASRQLVTVFSAPNY 267
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 174-529 1.46e-32

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 127.85  E-value: 1.46e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 174 ITVCGDLHGQLDDLIFIFYKNGLPsPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLNRGNHEDHMVNLRYGFT 253
Cdd:PTZ00480  61 LKICGDVHGQYFDLLRLFEYGGYP-PESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFY 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 254 KEVMNKYKVhgkEILRTLQDVFCWLPLATLIDEKVLILHGGVS-DITDLELLDKIerskivstmrcktrqksekqmeekr 332
Cdd:PTZ00480 140 DECKRRYTI---KLWKTFTDCFNCLPVAALIDEKILCMHGGLSpELSNLEQIRRI------------------------- 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 333 ranqkssaqgpipwflpesrslpssplrlgsykaqktSRSSSIPCSGSLdgrelsrqvrssvelelercrqqagllvtge 412
Cdd:PTZ00480 192 -------------------------------------MRPTDVPDTGLL------------------------------- 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 413 keepsrsaseadseagelrkptqeewrqvVDILWSDPMAQEGCKANTIRGGGCYFGPDVTQQLLQKYNLQFLIRSHECKP 492
Cdd:PTZ00480 204 -----------------------------CDLLWSDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVE 254

                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 119626160 493 EGYEFCHNRKVLTIFSASNYYEVGSNRGAYVKLGPAL 529
Cdd:PTZ00480 255 DGYEFFSKRQLVTLFSAPNYCGEFDNAGSMMTIDESL 291
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 147-309 7.98e-28

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 113.76  E-value: 7.98e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 147 LNLLYETKKH-LVQLPNINRVSTcyseEITVCGDLHGQLDDLIFIFYKNGlPSPERSYVFNGDFVDRGKDSVEILMILFA 225
Cdd:PTZ00239  21 LKLICERAKEiFLEESNVQPVRA----PVNVCGDIHGQFYDLQALFKEGG-DIPNANYIFIGDFVDRGYNSVETMEYLLC 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 226 FMLVYPKEFHLNRGNHEDHMVNLRYGFTKEVMNKYKvhGKEILRTLQDVFCWLPLATLIDEKVLILHGGVS-DITDLELL 304
Cdd:PTZ00239  96 LKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYG--NSNPWRLFMDVFDCLPLAALIEGQILCVHGGLSpDMRTIDQI 173


                 ....*
gi 119626160 305 DKIER 309
Cdd:PTZ00239 174 RTIDR 178
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 174-284 1.55e-13

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: 67.24  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160  174 ITVCGDLH--GQLDDLIFIFykNGLPSPERSYVF--NGDFVDRGKDSVEILmiLFAFMLVYPKEFHLNRGNHEDHMVNLr 249
Cdd:pfam00149   3 ILVIGDLHlpGQLDDLLELL--KKLLEEGKPDLVlhAGDLVDRGPPSEEVL--ELLERLIKYVPVYLVRGNHDFDYGEC- 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 119626160  250 ygftkEVMNKYKVHGKEILRTLQDVFCWLPLATLI 284
Cdd:pfam00149  78 -----LRLYPYLGLLARPWKRFLEVFNFLPLAGIL 107
PHA02239 PHA02239
putative protein phosphatase
 174-248 2.01e-06

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 49.22  E-value: 2.01e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 119626160 174 ITVCGDLHGQLDDLIFIFYK-NGLPSPERSYVFNGDFVDRGKDSVEILMILFAFMLVYPKEFHLnRGNHEDHMVNL 248
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKiNNERKPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTL-LGNHDDEFYNI 77
PPP5 pfam08321
PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine ...
 104-162 2.15e-06

PPP5 TPR repeat region; This region is specific to the PPP5 subfamily of serine/threonine phosphatases and contains TPR repeats.


Pssm-ID: 462427  Cd Length: 92  Bit Score: 45.93  E-value: 2.15e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160  104 DYESIEVPDSYTGPRLSF-PLLPDHATALVEAFRLKQQLHARYVLNLLYETKKHLVQLPN 162
Cdd:pfam08321  30 DLESIVVEDSYDGPRLEDeKITLEFVKDMIERFKKGKKLHKKYAYQILLKVKEILKKEPS 89
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 174-292 1.18e-05

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: 46.54  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 174 ITVCGDLHGQLDDLififyKNGLPS----PERSYVFN-GDFVDRGKDSVEILMILfafmlvypKE--FHLNRGNHEDHMV 246
Cdd:cd07424    3 DFVVGDIHGHFQRL-----QRALDAvgfdPARDRLISvGDLVDRGPESLEVLELL--------KQpwFHAVQGNHEQMAI 69

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119626160 247 NlryGFTKEVMNKYKVHG--------KEILRTLQDVFCWLPLATLI---DEKVLILH 292
Cdd:cd07424   70 D---ALRGGDDVMWRANGggwffdlpDEEAKVLLEKLHHLPIAIEVesrNGKVGIVH 123
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 176-242 5.32e-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: 43.41  E-value: 5.32e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 119626160 176 VCGDLHGQLDDLIFIFYKNGLPSPERSYV-FNGDFVDRGKDSVEILMILFAFMLvYPKEFHLNRGNHE 242
Cdd:cd00838    2 VISDIHGNLEALEAVLEAALAKAEKPDLViCLGDLVDYGPDPEEVELKALRLLL-AGIPVYVVPGNHD 68
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 178-296 2.38e-04

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: 42.67  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119626160 178 GDLHGQLDDLIFIFYKNGLPSPERSYVFN-------GDFVDRGKDSVEilmILFAFMLVYPK------EFHLNRGNHEdh 244
Cdd:cd07425    4 GDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIE---ILKLLEKLKRQarkaggKVILLLGNHE-- 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119626160 245 MVNL----RY-------GFTKEVMNKYKVHGKEilrtlQDVFCWLP--LATLIDEKVLILHGGVS 296
Cdd:cd07425   79 LMNLcgdfRYvhprglnEFGGVAKRRYALLSDG-----GYIGRYLRthPVVLVVNDILFVHGGLG 138
 
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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