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Conserved domains on  [gi|71993073|ref|NP_496359|]
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Serine/threonine specific protein phosphatases domain-containing protein [Caenorhabditis elegans]

Protein Classification

metallophosphoesterase family protein( domain architecture ID 46112)

metallophosphoesterase family protein may contain an active site consisting of two metal ions (usually manganese, iron, or zinc)

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
MPP_superfamily super family cl13995
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 334-595 1.15e-40

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.


The actual alignment was detected with superfamily member smart00156:

Pssm-ID: 472684 [Multi-domain]  Cd Length: 271  Bit Score: 148.90  E-value: 1.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    334 LELLCLFEETAFKmaEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSLK 413
Cdd:smart00156   6 ILELLREVKEIFR--QEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRG-PFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    414 CRFPKHVFILRGEPETSP------------FRMSTRLHPVITRAvqscikrmCTHMPFAAIIGKSVLAVYSGFSPMIREK 481
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSmneiygfydeckRKYGERIYEKFNEA--------FSWLPLAALINGKILCMHGGLSPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    482 GHIHHLFRPVTAEHmNAVERHIIFNQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNR 561
Cdd:smart00156 155 DDIRKLKRPQEPPD-DGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK 233

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 71993073    562 LINLWSAPGYGSDF---GAILSISKDLVITPILMEKQ 595
Cdd:smart00156 234 LVTIFSAPNYCDRFgnkAAVLKVDKDLKLTFEQFKPG 270
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 334-595 1.15e-40

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: 148.90  E-value: 1.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    334 LELLCLFEETAFKmaEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSLK 413
Cdd:smart00156   6 ILELLREVKEIFR--QEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRG-PFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    414 CRFPKHVFILRGEPETSP------------FRMSTRLHPVITRAvqscikrmCTHMPFAAIIGKSVLAVYSGFSPMIREK 481
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSmneiygfydeckRKYGERIYEKFNEA--------FSWLPLAALINGKILCMHGGLSPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    482 GHIHHLFRPVTAEHmNAVERHIIFNQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNR 561
Cdd:smart00156 155 DDIRKLKRPQEPPD-DGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK 233

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 71993073    562 LINLWSAPGYGSDF---GAILSISKDLVITPILMEKQ 595
Cdd:smart00156 234 LVTIFSAPNYCDRFgnkAAVLKVDKDLKLTFEQFKPG 270
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 361-581 2.28e-28

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: 113.23  E-value: 2.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 361 TVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSLKCRFPKHVFILRGEPETS---------- 430
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRG-PDSVEVIDLLLALKILYPDNVFLLRGNHEFMllnflygfyd 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 431 --PFRMSTRLHPVITRAVQSCIKrmctHMPFAAIIGKSVLAVYSGFSPMIREKGHIHHLFRPVTAEhmNAVERHIIFNQP 508
Cdd:cd00144  80 erTLRCLRKGGEELWREFNEVFN----YLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIENPD--DQLVEDLLWSDP 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71993073 509 SNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNRLINLWSAPGYGSDFGAILSI 581
Cdd:cd00144 154 DESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAA 226
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 350-588 5.74e-23

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 100.12  E-value: 5.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  350 EPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGESgSVECLALICSLKCRFPKHVFILRGEPET 429
Cdd:PTZ00480  51 QPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQ-SLETICLLLAYKIKYPENFFLLRGNHEC 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  430 SPFRMSTRLHPVITRAVQSCIKRMCTH----MPFAAIIGKSVLAVYSGFSPMIREKGHIHHLFRPVTAEHMNAVeRHIIF 505
Cdd:PTZ00480 130 ASINRIYGFYDECKRRYTIKLWKTFTDcfncLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLL-CDLLW 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  506 NQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNRLINLWSAPGYGSDF---GAILSIS 582
Cdd:PTZ00480 209 SDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFdnaGSMMTID 288


                 ....*.
gi 71993073  583 KDLVIT 588
Cdd:PTZ00480 289 ESLMCS 294
 
Name Accession Description Interval E-value
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 334-595 1.15e-40

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: 148.90  E-value: 1.15e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    334 LELLCLFEETAFKmaEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSLK 413
Cdd:smart00156   6 ILELLREVKEIFR--QEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRG-PFSIEVILLLFALK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    414 CRFPKHVFILRGEPETSP------------FRMSTRLHPVITRAvqscikrmCTHMPFAAIIGKSVLAVYSGFSPMIREK 481
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSmneiygfydeckRKYGERIYEKFNEA--------FSWLPLAALINGKILCMHGGLSPDLTTL 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073    482 GHIHHLFRPVTAEHmNAVERHIIFNQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNR 561
Cdd:smart00156 155 DDIRKLKRPQEPPD-DGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGK 233

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 71993073    562 LINLWSAPGYGSDF---GAILSISKDLVITPILMEKQ 595
Cdd:smart00156 234 LVTIFSAPNYCDRFgnkAAVLKVDKDLKLTFEQFKPG 270
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 361-581 2.28e-28

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: 113.23  E-value: 2.28e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 361 TVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSLKCRFPKHVFILRGEPETS---------- 430
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRG-PDSVEVIDLLLALKILYPDNVFLLRGNHEFMllnflygfyd 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 431 --PFRMSTRLHPVITRAVQSCIKrmctHMPFAAIIGKSVLAVYSGFSPMIREKGHIHHLFRPVTAEhmNAVERHIIFNQP 508
Cdd:cd00144  80 erTLRCLRKGGEELWREFNEVFN----YLPLAALVDGKILCVHGGLSPDLTLLDQIRNIRPIENPD--DQLVEDLLWSDP 153

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 71993073 509 SNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNRLINLWSAPGYGSDFGAILSI 581
Cdd:cd00144 154 DESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAA 226
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
 328-592 1.02e-27

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: 113.69  E-value: 1.02e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 328 QYPFTALELLCLFEETAFKMAEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRI--------LFLGGILDSGe 399
Cdd:cd07419  18 RFFFDCQEIAELCDEAERIFRQEPSVLRLRAPIKIFGDIHGQFGDLMRLFDEYGSPVTEEAgdieyidyLFLGDYVDRG- 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 400 SGSVECLALICSLKCRFPKHVFILRGEPETSP------FRMS--TRLHPVITRAVqSC---IKRMCTHMPFAAIIGKSVL 468
Cdd:cd07419  97 SHSLETICLLLALKVKYPNQIHLIRGNHEAADinalfgFREEciERLGEDIRDGD-SVwqrINRLFNWLPLAALIEDKII 175

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 469 AVYSGFSPMIREKGHIHHLFRPVTAEHMNAVERHIIFNQP--SNRVRMYRPN---PNTEGDW--FGKQAVKRACKATRCN 541
Cdd:cd07419 176 CVHGGIGRSINHIHQIENLKRPITMEAGSPVVMDLLWSDPteNDSVLGLRPNaidPRGTGLIvkFGPDRVMEFLEENDLQ 255

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....
gi 71993073 542 VMIRGQSYVPYGYLPCWNNRLINLWSAPGY---GSDFGAILSISKDLVITPILM 592
Cdd:cd07419 256 MIIRAHECVMDGFERFAQGHLITLFSATNYcgtAGNAGAILVLGRDLVVVPKLI 309
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
 347-585 2.00e-24

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: 103.43  E-value: 2.00e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 347 MAEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSLKCRFPKHVFILRGE 426
Cdd:cd07415  31 LVKESNVQRVRSPVTVCGDIHGQFYDLLELFRIGGDVPDTNYLFLGDYVDRG-YYSVETFLLLLALKVRYPDRITLLRGN 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 427 PETspfRMSTRLHPVITRAVQ----SCIKRMCT----HMPFAAIIGKSVLAVYSGFSPMIRekghihhlfrpvTAEHMNA 498
Cdd:cd07415 110 HES---RQITQVYGFYDECLRkygnANVWKYFTdlfdYLPLAALIDGQIFCVHGGLSPSIQ------------TLDQIRA 174

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 499 VERH-----------IIFNQPSNRVRmYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNRLINLWS 567
Cdd:cd07415 175 LDRFqevphegpmcdLLWSDPDDREG-WGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWS 253

                       250       260
                ....*....|....*....|.
gi 71993073 568 APGYGSDFG---AILSISKDL 585
Cdd:cd07415 254 APNYCYRCGnvaSILELDEHL 274
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 334-586 5.23e-23

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: 99.34  E-value: 5.23e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 334 LELLCLFEETAFKmaEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGESgSVECLALICSLK 413
Cdd:cd07414  28 IRGLCLKSREIFL--SQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNYLFLGDYVDRGKQ-SLETICLLLAYK 104

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 414 CRFPKHVFILRGEPETSPF------------RMSTRLHPVITravqSCIKrmCthMPFAAIIGKSVLAVYSGFSPMIREK 481
Cdd:cd07414 105 IKYPENFFLLRGNHECASInriygfydeckrRYNIKLWKTFT----DCFN--C--LPVAAIVDEKIFCCHGGLSPDLQSM 176

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 482 GHIHHLFRPVTAEHMNAVeRHIIFNQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNR 561
Cdd:cd07414 177 EQIRRIMRPTDVPDQGLL-CDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQ 255

                       250       260
                ....*....|....*....|....*...
gi 71993073 562 LINLWSAPGYGSDF---GAILSISKDLV 586
Cdd:cd07414 256 LVTLFSAPNYCGEFdnaGAMMSVDETLM 283
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 350-588 5.74e-23

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 100.12  E-value: 5.74e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  350 EPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGESgSVECLALICSLKCRFPKHVFILRGEPET 429
Cdd:PTZ00480  51 QPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQ-SLETICLLLAYKIKYPENFFLLRGNHEC 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  430 SPFRMSTRLHPVITRAVQSCIKRMCTH----MPFAAIIGKSVLAVYSGFSPMIREKGHIHHLFRPVTAEHMNAVeRHIIF 505
Cdd:PTZ00480 130 ASINRIYGFYDECKRRYTIKLWKTFTDcfncLPVAALIDEKILCMHGGLSPELSNLEQIRRIMRPTDVPDTGLL-CDLLW 208

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  506 NQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNRLINLWSAPGYGSDF---GAILSIS 582
Cdd:PTZ00480 209 SDPDKDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFdnaGSMMTID 288


                 ....*.
gi 71993073  583 KDLVIT 588
Cdd:PTZ00480 289 ESLMCS 294
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
 334-581 2.52e-20

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 91.80  E-value: 2.52e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  334 LELLClfEETAFKMAEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGESgSVECLALICSLK 413
Cdd:PTZ00239  21 LKLIC--ERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVDRGYN-SVETMEYLLCLK 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  414 CRFPKHVFILRGEPETSPFRMSTRLHPVITRAV-QSCIKRMCT----HMPFAAIIGKSVLAVYSGFSPMIREKGHIHHLF 488
Cdd:PTZ00239  98 VKYPGNITLLRGNHESRQCTQVYGFYEEILRKYgNSNPWRLFMdvfdCLPLAALIEGQILCVHGGLSPDMRTIDQIRTID 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  489 RPVTAEHMNAVeRHIIFNQPSNrVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYlPCW--NNRLINLW 566
Cdd:PTZ00239 178 RKIEIPHEGPF-CDLMWSDPEE-VEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY-KYWfpDQNLVTVW 254

                        250
                 ....*....|....*
gi 71993073  567 SAPGYGSDFGAILSI 581
Cdd:PTZ00239 255 SAPNYCYRCGNIASI 269
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
 333-489 1.73e-19

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: 89.29  E-value: 1.73e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 333 ALELLclfEETAFKMAEEPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGeSGSVECLALICSL 412
Cdd:cd07416  21 ALRII---TEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYVDRG-YFSIECVLYLWAL 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 413 KCRFPKHVFILRGEPE----TSPF--------RMSTRLHPVITRAVQScikrmcthMPFAAIIGKSVLAVYSGFSPMIRE 480
Cdd:cd07416  97 KILYPKTLFLLRGNHEcrhlTEYFtfkqeckiKYSERVYDACMEAFDC--------LPLAALMNQQFLCVHGGLSPELKT 168


                ....*....
gi 71993073 481 KGHIHHLFR 489
Cdd:cd07416 169 LDDIRKLDR 177
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
 350-585 3.11e-18

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 85.34  E-value: 3.11e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  350 EPSLLQIEADITVIGDIRGRYADLHRWLQLTGWPPHNRILFLGGILDSGESgSVECLALICSLKCRFPKHVFILRGEPET 429
Cdd:PTZ00244  44 QPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKH-SVETITLQFCYKIVYPENFFLLRGNHEC 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  430 SPF------------RMSTRLHPVITRAVQScikrmcthMPFAAIIGKSVLAVYSGFSPMIREKGHIHHLFRPVTAEHmN 497
Cdd:PTZ00244 123 ASInkmygffddvkrRYNIKLFKAFTDVFNT--------MPVCCVISEKIICMHGGLSPDLTSLASVNEIERPCDVPD-R 193

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073  498 AVERHIIFNQPSNRVRMYRPNPNTEGDWFGKQAVKRACKATRCNVMIRGQSYVPYGYLPCWNNRLINLWSAPGYGSDF-- 575
Cdd:PTZ00244 194 GILCDLLWADPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFdn 273

                        250
                 ....*....|.
gi 71993073  576 -GAILSISKDL 585
Cdd:PTZ00244 274 dAAVMNIDDKL 284
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
 347-571 1.06e-13

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: 72.29  E-value: 1.06e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 347 MAEEPSLLQIE----ADITVIGDIRGRYADLHRWLQLTGWP-PHNRILFLGGILDSGeSGSVECLALICSLKCRFPKHVF 421
Cdd:cd07417  45 LKKLPSLVEITipegEKITVCGDTHGQFYDLLNIFELNGLPsETNPYLFNGDFVDRG-SFSVEVILTLFAFKLLYPNHFH 123

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 422 ILRGEPET-SPFRM-----------STRLHPVITRAVQScikrmcthMPFAAIIGKSVLAVYSG-FSpmirEKGhihhlf 488
Cdd:cd07417 124 LNRGNHETdNMNKIygfegevkakyNEQMFNLFSEVFNW--------LPLAHLINGKVLVVHGGlFS----DDG------ 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 489 rpVTAEHMNAVERhiiFNQPSNRVRMYR-----PNPNTE--------GDWFGKQAVKRACKATRCNVMIRGQSYVPYGYL 555
Cdd:cd07417 186 --VTLDDIRKIDR---FRQPPDSGLMCEllwsdPQPQPGrgpskrgvGCQFGPDVTKRFLEENNLDYIIRSHEVKDEGYE 260

                       250
                ....*....|....*.
gi 71993073 556 PCWNNRLINLWSAPGY 571
Cdd:cd07417 261 VEHDGKCITVFSAPNY 276
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 336-586 6.60e-11

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: 63.58  E-value: 6.60e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 336 LLCLFEeTAFKMAEEPSLLQIEA----DITVIGDIRGRYADLHRWLQLTGWP-PHNRILFLGGILDSGESgSVECLALIC 410
Cdd:cd07420  26 LLILRE-ARKSLKQLPNISRVSTsyskEVTICGDLHGKLDDLLLIFYKNGLPsPENPYVFNGDFVDRGKR-SIEILMILF 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 411 SLKCRFPKHVFILRGEPETspFRMSTRL---------HPVITRAVQSCIKRMCTHMPFAAIIGKSVLAVYSGFSpmirEK 481
Cdd:cd07420 104 AFVLVYPNAVHLNRGNHED--HIMNLRYgftkevmqkYKDHGKKILRLLEDVFSWLPLATIIDNKVLVVHGGIS----DS 177

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 482 GHIHHLFRpvtaehmnaVERHIIFNQPSNRVRMY-------RPN----PNT---EGDWFGKQAVKRACKATRCNVMIRGQ 547
Cdd:cd07420 178 TDLDLLDK---------IDRHKYVSTKTEWQQVVdilwsdpKATkgckPNTfrgGGCYFGPDVTSQFLQKHGLSLLIRSH 248

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 71993073 548 SYVPYGYLPCWNNRLINLWSAPGY---GSDFGAILSISKDLV 586
Cdd:cd07420 249 ECKPEGYEFCHNNKVITIFSASNYyeeGSNRGAYVKLGPQLT 290
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
 330-473 1.14e-08

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: 57.50  E-value: 1.14e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 71993073 330 PFTALELLCLFEETAFKmaEEPSLLQIEAD----ITVIGDIRGRYADLHRWLQLTGWPPHNRI-LFLGGILDSGESGsVE 404
Cdd:cd07418  36 PVNVFDSLVLTAHKILH--REPNCVRIDVEdvceVVVVGDVHGQLHDVLFLLEDAGFPDQNRFyVFNGDYVDRGAWG-LE 112

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 71993073 405 CLALICSLKCRFPKHVFILRGEPETspfRMSTRLH----PVIT------RAVQSCIKRMCTHMPFAAIIGKSVLAVYSG 473
Cdd:cd07418 113 TFLLLLSWKVLLPDRVYLLRGNHES---KFCTSMYgfeqEVLTkygdkgKHVYRKCLGCFEGLPLASIIAGRVYTAHGG 188
 
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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