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Conserved domains on  [gi|1845969936|ref|NP_001370693|]
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Serine/threonine specific protein phosphatases domain-containing protein [Caenorhabditis elegans]

Protein Classification

serine/threonine protein phosphatase( domain architecture ID 12191156)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 50-338 3.13e-95

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: 283.72  E-value: 3.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936   50 FYPEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkVPPEQTYVMLGCYLGRGFAQIECLVFLL 129
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNG-QPPETNYVFLGDYVDRGPFSIEVILLLF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  130 AYKILHPEKVVLLKGHHEESISIEMlkvkewlmaRGIERDVDL---EECMIEMKRACSMMSAAAVIDSKILCMPGGPGPt 206
Cdd:smart00156  80 ALKILYPNRIVLLRGNHESRSMNEI---------YGFYDECKRkygERIYEKFNEAFSWLPLAALINGKILCMHGGLSP- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  207 iREKGLQKLVGLKKgVQAIADKKLLMEASWSVL--LLDDAQKDMHGMPF-FTPQQATDFCKANNLKCIVRGRQMVDEGYL 283
Cdd:smart00156 150 -DLTTLDDIRKLKR-PQEPPDDGLLIDLLWSDPdqPVNGFGPSIRGASYiFGPDAVDEFLKKNNLKLIIRAHQVVDDGYE 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969936  284 NKP-REVVTLISAVAYLDNFRNHAAVLQVDNDkgkvirykmeegEQLSLELVKPGM 338
Cdd:smart00156 228 FFAdGKLVTIFSAPNYCDRFGNKAAVLKVDKD------------LKLTFEQFKPGK 271
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 50-338 3.13e-95

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: 283.72  E-value: 3.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936   50 FYPEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkVPPEQTYVMLGCYLGRGFAQIECLVFLL 129
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNG-QPPETNYVFLGDYVDRGPFSIEVILLLF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  130 AYKILHPEKVVLLKGHHEESISIEMlkvkewlmaRGIERDVDL---EECMIEMKRACSMMSAAAVIDSKILCMPGGPGPt 206
Cdd:smart00156  80 ALKILYPNRIVLLRGNHESRSMNEI---------YGFYDECKRkygERIYEKFNEAFSWLPLAALINGKILCMHGGLSP- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  207 iREKGLQKLVGLKKgVQAIADKKLLMEASWSVL--LLDDAQKDMHGMPF-FTPQQATDFCKANNLKCIVRGRQMVDEGYL 283
Cdd:smart00156 150 -DLTTLDDIRKLKR-PQEPPDDGLLIDLLWSDPdqPVNGFGPSIRGASYiFGPDAVDEFLKKNNLKLIIRAHQVVDDGYE 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969936  284 NKP-REVVTLISAVAYLDNFRNHAAVLQVDNDkgkvirykmeegEQLSLELVKPGM 338
Cdd:smart00156 228 FFAdGKLVTIFSAPNYCDRFGNKAAVLKVDKD------------LKLTFEQFKPGK 271
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 53-314 3.08e-28

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: 111.63  E-value: 3.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  53 EVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkvPPEQT-YVMLGCYLGRGFAQIECLVFLLAY 131
Cdd:cd07416    19 EDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGG--SPANTrYLFLGDYVDRGYFSIECVLYLWAL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 132 KILHPEKVVLLKGHHEESISIEMLKVK-EWLMARGIERdvdLEECMiemkRACSMMSAAAVIDSKILCMPGGPGPTIreK 210
Cdd:cd07416    97 KILYPKTLFLLRGNHECRHLTEYFTFKqECKIKYSERV---YDACM----EAFDCLPLAALMNQQFLCVHGGLSPEL--K 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 211 GLQKLVGLKKgVQAIADKKLLMEASWSVLLLDDAQKDMHGM----------PFFTPQQATDFCKANNLKCIVRGRQMVDE 280
Cdd:cd07416   168 TLDDIRKLDR-FREPPSYGPMCDLLWSDPLEDFGNEKTQEHfvhntvrgcsYFYSYRAVCEFLQKNNLLSIIRAHEAQDA 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1845969936 281 GY----LNKPR---EVVTLISAVAYLDNFRNHAAVLQVDND 314
Cdd:cd07416   247 GYrmyrKSQTTgfpSLITIFSAPNYLDVYNNKAAVLKYENN 287
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 24-312 2.94e-22

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 95.50  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  24 KIDYVKLISKIWTyIREYTPdGPRPQFYPEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkVP 103
Cdd:PTZ00480    8 EIDVDNIIERLLS-VRGSKP-GKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGG-YP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 104 PEQTYVMLGCYLGRGFAQIECLVFLLAYKILHPEKVVLLKGHHE-ESISIEMLKVKEWLMARGIERDVDLEECMiemkra 182
Cdd:PTZ00480   85 PESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHEcASINRIYGFYDECKRRYTIKLWKTFTDCF------ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 183 cSMMSAAAVIDSKILCMPGGPGPTIreKGLQKLVGLKKGVQaIADKKLLMEASWSvllldDAQKDMHGMP--------FF 254
Cdd:PTZ00480  159 -NCLPVAALIDEKILCMHGGLSPEL--SNLEQIRRIMRPTD-VPDTGLLCDLLWS-----DPDKDVQGWAdnergvsyVF 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1845969936 255 TPQQATDFCKANNLKCIVRGRQMVDEGY-LNKPREVVTLISAVAYLDNFRNHAAVLQVD 312
Cdd:PTZ00480  230 SQEIVQVFLKKHELDLICRAHQVVEDGYeFFSKRQLVTLFSAPNYCGEFDNAGSMMTID 288
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 50-338 3.13e-95

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: 283.72  E-value: 3.13e-95
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936   50 FYPEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkVPPEQTYVMLGCYLGRGFAQIECLVFLL 129
Cdd:smart00156   1 LYKEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNG-QPPETNYVFLGDYVDRGPFSIEVILLLF 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  130 AYKILHPEKVVLLKGHHEESISIEMlkvkewlmaRGIERDVDL---EECMIEMKRACSMMSAAAVIDSKILCMPGGPGPt 206
Cdd:smart00156  80 ALKILYPNRIVLLRGNHESRSMNEI---------YGFYDECKRkygERIYEKFNEAFSWLPLAALINGKILCMHGGLSP- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  207 iREKGLQKLVGLKKgVQAIADKKLLMEASWSVL--LLDDAQKDMHGMPF-FTPQQATDFCKANNLKCIVRGRQMVDEGYL 283
Cdd:smart00156 150 -DLTTLDDIRKLKR-PQEPPDDGLLIDLLWSDPdqPVNGFGPSIRGASYiFGPDAVDEFLKKNNLKLIIRAHQVVDDGYE 227

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969936  284 NKP-REVVTLISAVAYLDNFRNHAAVLQVDNDkgkvirykmeegEQLSLELVKPGM 338
Cdd:smart00156 228 FFAdGKLVTIFSAPNYCDRFGNKAAVLKVDKD------------LKLTFEQFKPGK 271
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 53-314 3.08e-28

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: 111.63  E-value: 3.08e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  53 EVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkvPPEQT-YVMLGCYLGRGFAQIECLVFLLAY 131
Cdd:cd07416    19 EDALRIITEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGG--SPANTrYLFLGDYVDRGYFSIECVLYLWAL 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 132 KILHPEKVVLLKGHHEESISIEMLKVK-EWLMARGIERdvdLEECMiemkRACSMMSAAAVIDSKILCMPGGPGPTIreK 210
Cdd:cd07416    97 KILYPKTLFLLRGNHECRHLTEYFTFKqECKIKYSERV---YDACM----EAFDCLPLAALMNQQFLCVHGGLSPEL--K 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 211 GLQKLVGLKKgVQAIADKKLLMEASWSVLLLDDAQKDMHGM----------PFFTPQQATDFCKANNLKCIVRGRQMVDE 280
Cdd:cd07416   168 TLDDIRKLDR-FREPPSYGPMCDLLWSDPLEDFGNEKTQEHfvhntvrgcsYFYSYRAVCEFLQKNNLLSIIRAHEAQDA 246

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1845969936 281 GY----LNKPR---EVVTLISAVAYLDNFRNHAAVLQVDND 314
Cdd:cd07416   247 GYrmyrKSQTTgfpSLITIFSAPNYLDVYNNKAAVLKYENN 287
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 39-314 1.30e-27

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: 109.35  E-value: 1.30e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  39 REYTPDGPRP----QFYPEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkVPPEQTYVMLGCY 114
Cdd:cd07414     8 RLLEVRGSRPgknvQLTEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGG-FPPESNYLFLGDY 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 115 LGRGFAQIECLVFLLAYKILHPEKVVLLKGHHEeSISIEML-----------KVKEWLMArgierdVDLEECMiemkrac 183
Cdd:cd07414    87 VDRGKQSLETICLLLAYKIKYPENFFLLRGNHE-CASINRIygfydeckrryNIKLWKTF------TDCFNCL------- 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 184 smmSAAAVIDSKILCMPGGPGPTIreKGLQKLVGLKKGVQaIADKKLLMEASWSvllldDAQKDM-------HGMPF-FT 255
Cdd:cd07414   153 ---PVAAIVDEKIFCCHGGLSPDL--QSMEQIRRIMRPTD-VPDQGLLCDLLWS-----DPDKDVqgwgendRGVSFtFG 221

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1845969936 256 PQQATDFCKANNLKCIVRGRQMVDEGY--LNKpREVVTLISAVAYLDNFRNHAAVLQVDND 314
Cdd:cd07414   222 ADVVAKFLHKHDLDLICRAHQVVEDGYefFAK-RQLVTLFSAPNYCGEFDNAGAMMSVDET 281
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 52-314 2.21e-27

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: 108.83  E-value: 2.21e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  52 PEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKKvPPEQTYVMLGCYLGRGFAQIECLVFLLAY 131
Cdd:cd07415    17 ESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGD-VPDTNYLFLGDYVDRGYYSVETFLLLLAL 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 132 KILHPEKVVLLKGHHEesisiemlkvkewlmARGIERDVDL-EECMieMK-------RACS----MMSAAAVIDSKILCM 199
Cdd:cd07415    96 KVRYPDRITLLRGNHE---------------SRQITQVYGFyDECL--RKygnanvwKYFTdlfdYLPLAALIDGQIFCV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 200 PGGPGPTIreKGLQKLVGLKKgVQAIADKKLLMEASWSvllldDAQKDMHGMP-------FFTPQQATDFCKANNLKCIV 272
Cdd:cd07415   159 HGGLSPSI--QTLDQIRALDR-FQEVPHEGPMCDLLWS-----DPDDREGWGIsprgagyLFGQDVVEEFNHNNGLTLIC 230

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1845969936 273 RGRQMVDEGY---LNkpREVVTLISAVAYLDNFRNHAAVLQVDND 314
Cdd:cd07415   231 RAHQLVMEGYqwmFN--NKLVTVWSAPNYCYRCGNVASILELDEH 273
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 95-311 1.83e-26

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: 104.76  E-value: 1.83e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  95 LMSLAKKV--PPEQTYVMLGCYLGRGFAQIECLVFLLAYKILHPEKVVLLKGHHEESISIEMLKVKEWLMARGIERDVDL 172
Cdd:cd00144    13 LLRLLEKLgfPPEDKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYDERTLRCLRKGGEE 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 173 EEcmIEMKRACSMMSAAAVIDSKILCMPGGPGPTIREKGLQKLVGLKKgvqaIADKKLLMEASWSVLLLDDAQKDM---H 249
Cdd:cd00144    93 LW--REFNEVFNYLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIE----NPDDQLVEDLLWSDPDESVGDFESssrG 166

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1845969936 250 GMPFFTPQQATDFCKANNLKCIVRGRQMVDEGY-LNKPREVVTLISAVAYLDNFRNHAAVLQV 311
Cdd:cd00144   167 GGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYeFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 64-314 8.77e-25

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: 102.13  E-value: 8.77e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  64 EVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKKVPPEQT-------YVMLGCYLGRGFAQIECLVFLLAYKILHP 136
Cdd:cd07419    35 RIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEAgdieyidYLFLGDYVDRGSHSLETICLLLALKVKYP 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 137 EKVVLLKGHHEESISIEMLKVKEWLMARGIERDVDLEECMIEMKRACSMMSAAAVIDSKILCMPGGPGPTIREkgLQKLV 216
Cdd:cd07419   115 NQIHLIRGNHEAADINALFGFREECIERLGEDIRDGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRSINH--IHQIE 192

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 217 GLKKGVQAIADKKLLMEASWS-------VLLLDDAQKDMHGMPF---FTPQQATDFCKANNLKCIVRGRQMVDEGYLNKP 286
Cdd:cd07419   193 NLKRPITMEAGSPVVMDLLWSdptendsVLGLRPNAIDPRGTGLivkFGPDRVMEFLEENDLQMIIRAHECVMDGFERFA 272

                         250       260
                  ....*....|....*....|....*....
gi 1845969936 287 R-EVVTLISAVAYLDNFRNHAAVLQVDND 314
Cdd:cd07419   273 QgHLITLFSATNYCGTAGNAGAILVLGRD 301
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 24-312 2.94e-22

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 95.50  E-value: 2.94e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  24 KIDYVKLISKIWTyIREYTPdGPRPQFYPEVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKkVP 103
Cdd:PTZ00480    8 EIDVDNIIERLLS-VRGSKP-GKNVNLTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGG-YP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 104 PEQTYVMLGCYLGRGFAQIECLVFLLAYKILHPEKVVLLKGHHE-ESISIEMLKVKEWLMARGIERDVDLEECMiemkra 182
Cdd:PTZ00480   85 PESNYLFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHEcASINRIYGFYDECKRRYTIKLWKTFTDCF------ 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 183 cSMMSAAAVIDSKILCMPGGPGPTIreKGLQKLVGLKKGVQaIADKKLLMEASWSvllldDAQKDMHGMP--------FF 254
Cdd:PTZ00480  159 -NCLPVAALIDEKILCMHGGLSPEL--SNLEQIRRIMRPTD-VPDTGLLCDLLWS-----DPDKDVQGWAdnergvsyVF 229

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1845969936 255 TPQQATDFCKANNLKCIVRGRQMVDEGY-LNKPREVVTLISAVAYLDNFRNHAAVLQVD 312
Cdd:PTZ00480  230 SQEIVQVFLKKHELDLICRAHQVVEDGYeFFSKRQLVTLFSAPNYCGEFDNAGSMMTID 288
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 53-313 8.13e-20

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 88.04  E-value: 8.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  53 EVLKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEgdsMISLMSLAKKV--PPEQTYVMLGCYLGRGFAQIECLVFLLA 130
Cdd:PTZ00244   28 EDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQ---YYDLLRIFEKCgfPPYSNYLFLGDYVDRGKHSVETITLQFC 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 131 YKILHPEKVVLLKGHHEESISIEMLkvkewlmarGIERDVDlEECMIEMKRACS----MMSAAAVIDSKILCMPGGPGPT 206
Cdd:PTZ00244  105 YKIVYPENFFLLRGNHECASINKMY---------GFFDDVK-RRYNIKLFKAFTdvfnTMPVCCVISEKIICMHGGLSPD 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 207 IREkgLQKLVGLKKGVQaIADKKLLMEASWSvllldDAQKDMHGMP--------FFTPQQATDFCKANNLKCIVRGRQMV 278
Cdd:PTZ00244  175 LTS--LASVNEIERPCD-VPDRGILCDLLWA-----DPEDEVRGFLesdrgvsyLFGEDIVNDFLDMVDMDLIVRAHQVM 246

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1845969936 279 DEGY-LNKPREVVTLISAVAYLDNFRNHAAVLQVDN 313
Cdd:PTZ00244  247 ERGYgFFASRQLVTVFSAPNYCGEFDNDAAVMNIDD 282
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 55-314 2.52e-16

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 78.32  E-value: 2.52e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  55 LKKLLQKSCEVLKQDEMVVKVTGPAVIFGPVYGEGDSMISLMSLAKKVPpEQTYVMLGCYLGRGFAQIECLVFLLAYKIL 134
Cdd:PTZ00239   21 LKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIP-NANYIFIGDFVDRGYNSVETMEYLLCLKVK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 135 HPEKVVLLKGHHE-----------ESISIEMLKVKEWLMArgierdVDLEECmiemkracsmMSAAAVIDSKILCMPGGP 203
Cdd:PTZ00239  100 YPGNITLLRGNHEsrqctqvygfyEEILRKYGNSNPWRLF------MDVFDC----------LPLAALIEGQILCVHGGL 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 204 GPTIREkgLQKLVGLKKGVQaIADKKLLMEASWS-VLLLDDAQKDMHGMPF-FTPQQATDFCKANNLKCIVRGRQMVDEG 281
Cdd:PTZ00239  164 SPDMRT--IDQIRTIDRKIE-IPHEGPFCDLMWSdPEEVEYWAVNSRGAGYlFGAKVTKEFCRLNDLTLICRAHQLVMEG 240

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1845969936 282 YLN--KPREVVTLISAVAYLDNFRNHAAVLQVDND 314
Cdd:PTZ00239  241 YKYwfPDQNLVTVWSAPNYCYRCGNIASILCLDEN 275
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 54-280 1.82e-12

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: 67.52  E-value: 1.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  54 VLKKLLQKSCEVLKQDEMVVKVT----GPAVIFGPVYGEGDSMISLMSLAKKVPPEQTYVMLGCYLGRGFAQIECLVFLL 129
Cdd:cd07418    39 VFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGDYVDRGAWGLETFLLLL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 130 AYKILHPEKVVLLKGHHEESISIEMLKVKEWLMARGIERDVDLEECMIEmkrACSMMSAAAVIDSKILCMPGG------- 202
Cdd:cd07418   119 SWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKGKHVYRKCLG---CFEGLPLASIIAGRVYTAHGGlfrspsl 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 203 PGPTIREKGLQKLVGL--KKGVQAIADKKLLMEAS-------------------WSVLLLDDA--QKDMHGMPF-FTPQQ 258
Cdd:cd07418   196 PKRKKQKGKNRRVLLLepESESLKLGTLDDLMKARrsvldppgegsnlipgdvlWSDPSLTPGlsPNKQRGIGLlWGPDC 275

                         250       260
                  ....*....|....*....|..
gi 1845969936 259 ATDFCKANNLKCIVRGRQMVDE 280
Cdd:cd07418   276 TEEFLEKNNLKLIIRSHEGPDA 297
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 55-317 5.44e-12

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: 65.74  E-value: 5.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936  55 LKKLLQKSC---------EVLKQDEMVVKVTGPA----VIFGPVYGEGDSMISLMSLAKKVPPEQTYVMLGCYLGRGFAQ 121
Cdd:cd07417    25 DQKKLHKKYayqillqvkEILKKLPSLVEITIPEgekiTVCGDTHGQFYDLLNIFELNGLPSETNPYLFNGDFVDRGSFS 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 122 IECLVFLLAYKILHPEKVVLLKGHHEesiSIEMLKVkewlmaRGIERDV--DLEECMIEM-KRACSMMSAAAVIDSKILC 198
Cdd:cd07417   105 VEVILTLFAFKLLYPNHFHLNRGNHE---TDNMNKI------YGFEGEVkaKYNEQMFNLfSEVFNWLPLAHLINGKVLV 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1845969936 199 MPGG----PGPTIREkgLQKlvgLKKGVQaIADKKLLMEASWSvllldDAQKDMHGMP-------FFTPQQATDFCKANN 267
Cdd:cd07417   176 VHGGlfsdDGVTLDD--IRK---IDRFRQ-PPDSGLMCELLWS-----DPQPQPGRGPskrgvgcQFGPDVTKRFLEENN 244

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1845969936 268 LKCIVRGRQMVDEGYlnkprEV------VTLISAVAYLDNFRNHAAVLQVDNDKGK 317
Cdd:cd07417   245 LDYIIRSHEVKDEGY-----EVehdgkcITVFSAPNYCDQMGNKGAFIRFKGSDLK 295
 
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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