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Conserved domains on  [gi|26105964|gb|AAN78342|]
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TcC31.31 [Trypanosoma cruzi]

Protein Classification

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 ...
271-584 2.29e-98

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 cd07417:

Pssm-ID: 353799  Cd Length: 316  Bit Score: 310.73  E-value: 2.29e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 271 EPITIEVVQRLINDLTDHVLLPYPAAWRVFTDAMSHLNTMPNVVRLSppvgarvsngrINQGSKVVVVGDLHGQLADLLH 350
Cdd:cd07417   9 GKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEIT-----------IPEGEKITVCGDTHGQFYDLLN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 351 ILKECGMPNEGTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQ 430
Cdd:cd07417  78 IFELNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 431 RCFCALPLATIIGKKVFVVHGGLPRRKGVNIEDISRIQRFRQIPmpdysqpeEDEIFQDLLWSDPVEdLQGWRESPRGAG 510
Cdd:cd07417 158 EVFNWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPP--------DSGLMCELLWSDPQP-QPGRGPSKRGVG 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26105964 511 VVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNYDGPETNFGSFAVFVGDNPEPSFHTYQ 584
Cdd:cd07417 229 CQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFE 302
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
271-584 2.29e-98

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  Cd Length: 316  Bit Score: 310.73  E-value: 2.29e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 271 EPITIEVVQRLINDLTDHVLLPYPAAWRVFTDAMSHLNTMPNVVRLSppvgarvsngrINQGSKVVVVGDLHGQLADLLH 350
Cdd:cd07417   9 GKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEIT-----------IPEGEKITVCGDTHGQFYDLLN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 351 ILKECGMPNEGTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQ 430
Cdd:cd07417  78 IFELNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 431 RCFCALPLATIIGKKVFVVHGGLPRRKGVNIEDISRIQRFRQIPmpdysqpeEDEIFQDLLWSDPVEdLQGWRESPRGAG 510
Cdd:cd07417 158 EVFNWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPP--------DSGLMCELLWSDPQP-QPGRGPSKRGVG 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26105964 511 VVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNYDGPETNFGSFAVFVGDNPEPSFHTYQ 584
Cdd:cd07417 229 CQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFE 302
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
307-587 8.81e-85

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547  Cd Length: 271  Bit Score: 272.93  E-value: 8.81e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964    307 LNTMPNVVRLSPPVgarvsngrinqgskvVVVGDLHGQLADLLHILKECGMPNEgTYYIFNGDFVDRGANGVEVLLILFS 386
Cdd:smart00156  17 FRQEPNLVEVSAPV---------------TVCGDIHGQFDDLLRLFDKNGQPPE-TNYVFLGDYVDRGPFSIEVILLLFA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964    387 LMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGLPRRkGVNIEDISR 466
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPD-LTTLDDIRK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964    467 IQRFRQIPmpdysqpeEDEIFQDLLWSDPVEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHD 546
Cdd:smart00156 160 LKRPQEPP--------DDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFAD 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 26105964    547 GKLLTVFSASNYDGPETNFGSFAVfVGDNPEPSFHTYQVAE 587
Cdd:smart00156 232 GKLVTIFSAPNYCDRFGNKAAVLK-VDKDLKLTFEQFKPGK 271
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
333-558 9.91e-49

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 175.00  E-value: 9.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  333 SKVVVVGDLHGQLADLLHILKECG-MPNEGtyYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEY 411
Cdd:PTZ00239  43 APVNVCGDIHGQFYDLQALFKEGGdIPNAN--YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  412 GFDVEVSTKY-DRNVFRLVQRCFCALPLATIIGKKVFVVHGGL-PRRKgvNIEDISRIQRFRQIPmpdysqpeEDEIFQD 489
Cdd:PTZ00239 121 GFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLsPDMR--TIDQIRTIDRKIEIP--------HEGPFCD 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  490 LLWSDPvEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEE-HHDGKLLTVFSASNY 558
Cdd:PTZ00239 191 LMWSDP-EEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNY 259
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
407-558 6.67e-18

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];


Pssm-ID: 223712  Cd Length: 155  Bit Score: 81.63  E-value: 6.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 407 MNDEYGFDVEVSTKYDRNVFRLV----QRCFCALPLATII-GKKVFVVHGGLPRRKGVNIEDISRIQRFRQIPMPDYSqp 481
Cdd:COG0639   3 LTALYGFYDEKLRKYGEELEWLRaaggLETFDSLPLAAVAeGGKLLCHHGGLSPGLDRLLDIIEVLDRLRACEVPHAG-- 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26105964 482 eedeIFQDLLWSDP-VEDLQGWRESPRGAGVVFGaDVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNY 558
Cdd:COG0639  81 ----HTHDLLWSDPdGGDRRIWNPGPRGVPRDGG-DVTAVFGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNY 153
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
334-404 3.60e-12

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: 333878 [Multi-domain]  Cd Length: 79  Bit Score: 62.40  E-value: 3.60e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26105964   334 KVVVVGDLH--GQLADLLHILKECGMPNEGTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTlnRGNHEC 404
Cdd:pfam00149   2 RILVIGDLHgpGQLDDLLELLKKLLEEEKPDLVLHAGDLVDRGPWETEVLELLERLIAYVPVYLV--RGNHDL 72
 
Name Accession Description Interval E-value
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
271-584 2.29e-98

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  Cd Length: 316  Bit Score: 310.73  E-value: 2.29e-98
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 271 EPITIEVVQRLINDLTDHVLLPYPAAWRVFTDAMSHLNTMPNVVRLSppvgarvsngrINQGSKVVVVGDLHGQLADLLH 350
Cdd:cd07417   9 GKVTLEFVKEMMEWFKDQKKLHKKYAYQILLQVKEILKKLPSLVEIT-----------IPEGEKITVCGDTHGQFYDLLN 77
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 351 ILKECGMPNEGTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQ 430
Cdd:cd07417  78 IFELNGLPSETNPYLFNGDFVDRGSFSVEVILTLFAFKLLYPNHFHLNRGNHETDNMNKIYGFEGEVKAKYNEQMFNLFS 157
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 431 RCFCALPLATIIGKKVFVVHGGLPRRKGVNIEDISRIQRFRQIPmpdysqpeEDEIFQDLLWSDPVEdLQGWRESPRGAG 510
Cdd:cd07417 158 EVFNWLPLAHLINGKVLVVHGGLFSDDGVTLDDIRKIDRFRQPP--------DSGLMCELLWSDPQP-QPGRGPSKRGVG 228
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 26105964 511 VVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNYDGPETNFGSFAVFVGDNPEPSFHTYQ 584
Cdd:cd07417 229 CQFGPDVTKRFLEENNLDYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCDQMGNKGAFIRFKGSDLKPKFTQFE 302
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
307-587 8.81e-85

Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine phosphatases, that includes PP1, PP2A and PP2B (calcineurin) family members.


Pssm-ID: 197547  Cd Length: 271  Bit Score: 272.93  E-value: 8.81e-85
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964    307 LNTMPNVVRLSPPVgarvsngrinqgskvVVVGDLHGQLADLLHILKECGMPNEgTYYIFNGDFVDRGANGVEVLLILFS 386
Cdd:smart00156  17 FRQEPNLVEVSAPV---------------TVCGDIHGQFDDLLRLFDKNGQPPE-TNYVFLGDYVDRGPFSIEVILLLFA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964    387 LMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGLPRRkGVNIEDISR 466
Cdd:smart00156  81 LKILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYGERIYEKFNEAFSWLPLAALINGKILCMHGGLSPD-LTTLDDIRK 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964    467 IQRFRQIPmpdysqpeEDEIFQDLLWSDPVEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHD 546
Cdd:smart00156 160 LKRPQEPP--------DDGLLIDLLWSDPDQPVNGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFAD 231
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 26105964    547 GKLLTVFSASNYDGPETNFGSFAVfVGDNPEPSFHTYQVAE 587
Cdd:smart00156 232 GKLVTIFSAPNYCDRFGNKAAVLK-VDKDLKLTFEQFKPGK 271
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
302-584 2.82e-81

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: 264.66  E-value: 2.82e-81
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 302 DAMSHLNTMPNVVRLSppvgARVSNgrinqgsKVVVVGDLHGQLADLLHILKECGMPNEGTYYIFNGDFVDRGANGVEVL 381
Cdd:cd07420  31 EARKSLKQLPNISRVS----TSYSK-------EVTICGDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFVDRGKRSIEIL 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 382 LILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRN---VFRLVQRCFCALPLATIIGKKVFVVHGGLPRRKG 458
Cdd:cd07420 100 MILFAFVLVYPNAVHLNRGNHEDHIMNLRYGFTKEVMQKYKDHgkkILRLLEDVFSWLPLATIIDNKVLVVHGGISDSTD 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 459 VNIedISRIQRFRQIpmpdySQPEEDEIFQDLLWSDPVEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECL 538
Cdd:cd07420 180 LDL--LDKIDRHKYV-----STKTEWQQVVDILWSDPKATKGCKPNTFRGGGCYFGPDVTSQFLQKHGLSLLIRSHECKP 252
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 26105964 539 RGYEEHHDGKLLTVFSASNYDGPETNFGSFaVFVGDNPEPSFHTYQ 584
Cdd:cd07420 253 EGYEFCHNNKVITIFSASNYYEEGSNRGAY-VKLGPQLTPHFVQYQ 297
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
336-571 6.56e-80

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: 258.07  E-value: 6.56e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 336 VVVGDLHGQLADLLHILKECGMPNEgTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDV 415
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGFPPE-DKYLFLGDYVDRGPDSVEVIDLLLALKILYPDNVFLLRGNHEFMLLNFLYGFYD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 416 EVST----KYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGLPRrkgvNIEDISRIQRFRQIPMPDysqpeeDEIFQDLL 491
Cdd:cd00144  80 ERTLrclrKGGEELWREFNEVFNYLPLAALVDGKILCVHGGLSP----DLTLLDQIRNIRPIENPD------DQLVEDLL 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 492 WSDPVEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNYDGPETNFGSFAVF 571
Cdd:cd00144 150 WSDPDESVGDFESSSRGGGYLFGEDAVDEFLKKNGLKLIVRGHTPVEGGYEFLHGGKLITIFSAPNYCGKGGNKLAALVV 229
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
280-558 7.10e-71

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: 235.94  E-value: 7.10e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 280 RLINDLTDHVLLPYPAAWRVFTDAMSHLNTMPNVVRLSPPVgarvsngrinqgskvVVVGDLHGQLADLLHILKECGMPN 359
Cdd:cd07415   4 QWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPV---------------TVCGDIHGQFYDLLELFRIGGDVP 68
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 360 EgTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKY-DRNVFRLVQRCFCALPL 438
Cdd:cd07415  69 D-TNYLFLGDYVDRGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYgNANVWKYFTDLFDYLPL 147
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 439 ATIIGKKVFVVHGGL-PRRKgvNIEDISRIQRFRQIPmpdysqpeEDEIFQDLLWSDPvEDLQGWRESPRGAGVVFGADV 517
Cdd:cd07415 148 AALIDGQIFCVHGGLsPSIQ--TLDQIRALDRFQEVP--------HEGPMCDLLWSDP-DDREGWGISPRGAGYLFGQDV 216
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 26105964 518 TQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNY 558
Cdd:cd07415 217 VEEFNHNNGLTLICRAHQLVMEGYQWMFNNKLVTVWSAPNY 257
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
290-584 2.50e-57

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: 201.57  E-value: 2.50e-57
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 290 LLPYPAAWRVFTDAMSHLNTMPNVVRLSppvgarvsngrINQGSKVVVVGDLHGQLADLLHILKECGMPNEGTYYIFNGD 369
Cdd:cd07418  34 VLPVNVFDSLVLTAHKILHREPNCVRID-----------VEDVCEVVVVGDVHGQLHDVLFLLEDAGFPDQNRFYVFNGD 102
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 370 FVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYD---RNVFRLVQRCFCALPLATIIGKKV 446
Cdd:cd07418 103 YVDRGAWGLETFLLLLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGdkgKHVYRKCLGCFEGLPLASIIAGRV 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 447 FVVHGGLPR---------RKGVNIEDISRIQRFRQIPM---PDYSQ--------PEE--DEIFQDLLWSDPVEDLQGWRE 504
Cdd:cd07418 183 YTAHGGLFRspslpkrkkQKGKNRRVLLLEPESESLKLgtlDDLMKarrsvldpPGEgsNLIPGDVLWSDPSLTPGLSPN 262
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 505 SPRGAGVVFGADVTQEFLQNNGLELVIRSHE------------ECLRGYEEHHD---GKLLTVFSASNY------DGPET 563
Cdd:cd07418 263 KQRGIGLLWGPDCTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVDHDvesGKLITLFSAPDYpqfqatEERYN 342
                       330       340
                ....*....|....*....|..
gi 26105964 564 NFGSFAVF-VGDNPEPSFHTYQ 584
Cdd:cd07418 343 NKGAYIILqPPDFSDPQFHTFE 364
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
295-558 8.04e-55

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: 192.14  E-value: 8.04e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 295 AAWRVFTDAMSHLNTMPNVVRLSPPVgarvsngrinqgskvVVVGDLHGQLADLLHILkECGMPNEGTYYIFNGDFVDRG 374
Cdd:cd07416  20 DALRIITEGAEILRQEPNLLRIEAPV---------------TVCGDIHGQFYDLLKLF-EVGGSPANTRYLFLGDYVDRG 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 375 ANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGL- 453
Cdd:cd07416  84 YFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKYSERVYDACMEAFDCLPLAALMNQQFLCVHGGLs 163
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 454 PRRKgvNIEDISRIQRFRQIPMpdySQPeedeiFQDLLWSDPVEDLQGWRESP-------RGAGVVFGADVTQEFLQNNG 526
Cdd:cd07416 164 PELK--TLDDIRKLDRFREPPS---YGP-----MCDLLWSDPLEDFGNEKTQEhfvhntvRGCSYFYSYRAVCEFLQKNN 233
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 26105964 527 LELVIRSHEECLRGYEEHHDGK------LLTVFSASNY 558
Cdd:cd07416 234 LLSIIRAHEAQDAGYRMYRKSQttgfpsLITIFSAPNY 271
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
311-568 9.22e-55

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: 191.78  E-value: 9.22e-55
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 311 PNVVRLSPPVGarvsngrinqgskvvVVGDLHGQLADLLHILKECGMPNEgTYYIFNGDFVDRGANGVEVLLILFSLMLA 390
Cdd:cd07414  43 PILLELEAPLK---------------ICGDIHGQYYDLLRLFEYGGFPPE-SNYLFLGDYVDRGKQSLETICLLLAYKIK 106
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 391 CPKYVTLNRGNHECDYMNDEYGFDVEVSTKYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGL-PRRKgvNIEDISRIQR 469
Cdd:cd07414 107 YPENFFLLRGNHECASINRIYGFYDECKRRYNIKLWKTFTDCFNCLPVAAIVDEKIFCCHGGLsPDLQ--SMEQIRRIMR 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 470 FRQIPmpdysqpeEDEIFQDLLWSDPVEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKL 549
Cdd:cd07414 185 PTDVP--------DQGLLCDLLWSDPDKDVQGWGENDRGVSFTFGADVVAKFLHKHDLDLICRAHQVVEDGYEFFAKRQL 256
                       250
                ....*....|....*....
gi 26105964 550 LTVFSASNYDGPETNFGSF 568
Cdd:cd07414 257 VTLFSAPNYCGEFDNAGAM 275
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
337-567 1.36e-51

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: 183.41  E-value: 1.36e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 337 VVGDLHGQLADLLHILKECGMPNEG-----TY--YIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMND 409
Cdd:cd07419  52 IFGDIHGQFGDLMRLFDEYGSPVTEeagdiEYidYLFLGDYVDRGSHSLETICLLLALKVKYPNQIHLIRGNHEAADINA 131
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 410 EYGFDVEVSTKY------DRNVFRLVQRCFCALPLATIIGKKVFVVHGGLPRRkgVN-IEDISRIQRfrQIPMPDYSQpe 482
Cdd:cd07419 132 LFGFREECIERLgedirdGDSVWQRINRLFNWLPLAALIEDKIICVHGGIGRS--INhIHQIENLKR--PITMEAGSP-- 205
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 483 edeIFQDLLWSDPVED--LQGWRES---PRGAG--VVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSA 555
Cdd:cd07419 206 ---VVMDLLWSDPTENdsVLGLRPNaidPRGTGliVKFGPDRVMEFLEENDLQMIIRAHECVMDGFERFAQGHLITLFSA 282
                       250
                ....*....|..
gi 26105964 556 SNYDGPETNFGS 567
Cdd:cd07419 283 TNYCGTAGNAGA 294
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
333-558 9.91e-49

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 175.00  E-value: 9.91e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  333 SKVVVVGDLHGQLADLLHILKECG-MPNEGtyYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEY 411
Cdd:PTZ00239  43 APVNVCGDIHGQFYDLQALFKEGGdIPNAN--YIFIGDFVDRGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVY 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  412 GFDVEVSTKY-DRNVFRLVQRCFCALPLATIIGKKVFVVHGGL-PRRKgvNIEDISRIQRFRQIPmpdysqpeEDEIFQD 489
Cdd:PTZ00239 121 GFYEEILRKYgNSNPWRLFMDVFDCLPLAALIEGQILCVHGGLsPDMR--TIDQIRTIDRKIEIP--------HEGPFCD 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  490 LLWSDPvEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEE-HHDGKLLTVFSASNY 558
Cdd:PTZ00239 191 LMWSDP-EEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGYKYwFPDQNLVTVWSAPNY 259
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
337-567 1.43e-45

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 166.37  E-value: 1.43e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  337 VVGDLHGQLADLLHILKECGMPNEGTYyIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFDVE 416
Cdd:PTZ00480  63 ICGDVHGQYFDLLRLFEYGGYPPESNY-LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDE 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  417 VSTKYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGLPRRKGvNIEDISRIQRFRQIPmpdysqpeEDEIFQDLLWSDPV 496
Cdd:PTZ00480 142 CKRRYTIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELS-NLEQIRRIMRPTDVP--------DTGLLCDLLWSDPD 212
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26105964  497 EDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNYDGPETNFGS 567
Cdd:PTZ00480 213 KDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFSAPNYCGEFDNAGS 283
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
335-564 2.83e-45

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 164.69  E-value: 2.83e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  335 VVVVGDLHGQLADLLHILKECGMPNEGTYyIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLNRGNHECDYMNDEYGFD 414
Cdd:PTZ00244  54 VRVCGDTHGQYYDLLRIFEKCGFPPYSNY-LFLGDYVDRGKHSVETITLQFCYKIVYPENFFLLRGNHECASINKMYGFF 132
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  415 VEVSTKYDRNVFRLVQRCFCALPLATIIGKKVFVVHGGLprrkGVNIEDISRIQRF-RQIPMPDYSqpeedeIFQDLLWS 493
Cdd:PTZ00244 133 DDVKRRYNIKLFKAFTDVFNTMPVCCVISEKIICMHGGL----SPDLTSLASVNEIeRPCDVPDRG------ILCDLLWA 202
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 26105964  494 DPVEDLQGWRESPRGAGVVFGADVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNYDGPETN 564
Cdd:PTZ00244 203 DPEDEVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVFSAPNYCGEFDN 273
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
407-558 6.67e-18

Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal transduction mechanisms];


Pssm-ID: 223712  Cd Length: 155  Bit Score: 81.63  E-value: 6.67e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 407 MNDEYGFDVEVSTKYDRNVFRLV----QRCFCALPLATII-GKKVFVVHGGLPRRKGVNIEDISRIQRFRQIPMPDYSqp 481
Cdd:COG0639   3 LTALYGFYDEKLRKYGEELEWLRaaggLETFDSLPLAAVAeGGKLLCHHGGLSPGLDRLLDIIEVLDRLRACEVPHAG-- 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26105964 482 eedeIFQDLLWSDP-VEDLQGWRESPRGAGVVFGaDVTQEFLQNNGLELVIRSHEECLRGYEEHHDGKLLTVFSASNY 558
Cdd:COG0639  81 ----HTHDLLWSDPdGGDRRIWNPGPRGVPRDGG-DVTAVFGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNY 153
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
334-404 3.60e-12

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: 333878 [Multi-domain]  Cd Length: 79  Bit Score: 62.40  E-value: 3.60e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 26105964   334 KVVVVGDLH--GQLADLLHILKECGMPNEGTYYIFNGDFVDRGANGVEVLLILFSLMLACPKYVTlnRGNHEC 404
Cdd:pfam00149   2 RILVIGDLHgpGQLDDLLELLKKLLEEEKPDLVLHAGDLVDRGPWETEVLELLERLIAYVPVYLV--RGNHDL 72
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
336-403 1.34e-05

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  Cd Length: 209  Bit Score: 46.91  E-value: 1.34e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26105964 336 VVVGDLHGQLADLLHILKECGMPNEGTYYIFN-------GDFVDRGANGVEVLLILFSL----MLACPKYVTLNrGNHE 403
Cdd:cd07425   1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGGdtvvvqtGDILDRGDDEIEILKLLEKLkrqaRKAGGKVILLL-GNHE 78
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
337-454 4.26e-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: 45.38  E-value: 4.26e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 337 VVGDLHGQLADLLHILKECGMPNEGTYYIFNGDFVDRGANGVEVLlilfsLMLACPkYVTLNRGNHECDYMNDEYGFDVE 416
Cdd:cd07424   5 VVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVL-----ELLKQP-WFHAVQGNHEQMAIDALRGGDDV 78
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 26105964 417 VSTKY--------DRNVFRLVQRCFCALPLATII---GKKVFVVHGGLP 454
Cdd:cd07424  79 MWRANgggwffdlPDEEAKVLLEKLHHLPIAIEVesrNGKVGIVHADYP 127
PHA02239 PHA02239
putative protein phosphatase
335-421 1.96e-04

putative protein phosphatase


Pssm-ID: 107154  Cd Length: 235  Bit Score: 43.83  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964  335 VVVVGDLHGQLADLLHILKECG---MPNEGTyyIFNGDFVDRGANGVEVLLILFSLMLACPKYVTLnRGNHECDYMN--- 408
Cdd:PHA02239   3 IYVVPDIHGEYQKLLTIMDKINnerKPEETI--VFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTL-LGNHDDEFYNime 79
                         90
                 ....*....|....*.
gi 26105964  409 --DEYG-FDVEVSTKY 421
Cdd:PHA02239  80 nvDRLSiYDIEWLSRY 95
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
337-456 4.98e-04

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


Pssm-ID: 277366 [Multi-domain]  Cd Length: 235  Bit Score: 42.50  E-value: 4.98e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 26105964 337 VVGDLHGQLADLLHILKECG--MPNEGTYY-------IFNGDFVDRGANGVEVLLILFSLMLA-CPKYVTlnrGNHE--- 403
Cdd:cd07423   2 IIGDVHGCYDELVELLEKLGyqKKEEGLYVhpegrklVFLGDLVDRGPDSIDVLRLVMNMVKAgKALYVP---GNHCnkl 78
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 26105964 404 CDYMNdeyGFDVEVS-------------TKYDRNVFR-LVQRCFCALPLATII-GKKVFVVHGGLPRR 456
Cdd:cd07423  79 YRYLK---GRNVQLAhglettveelealSKEERPEFReRFAEFLESLPSHLVLdGGRLVVAHAGIKEE 143
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
336-403 6.36e-04

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: 40.71  E-value: 6.36e-04
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26105964 336 VVVGDLHGQLADLLHILKECGMPNEG-TYYIFNGDFVDRGANGVEVLLILFSLmLACPKYVTLNRGNHE 403
Cdd:cd00838   1 LVISDIHGNLEALEAVLEAALAKAEKpDLVICLGDLVDYGPDPEEVELKALRL-LLAGIPVYVVPGNHD 68
pphA PRK11439
serine/threonine protein phosphatase 1; Provisional
328-403 1.12e-03

serine/threonine protein phosphatase 1; Provisional


Pssm-ID: 236911  Cd Length: 218  Bit Score: 41.29  E-value: 1.12e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 26105964  328 RINqGSK---VVVVGDLHGQLADLLHILKECGMPNEGTYYIFNGDFVDRGANGVEVLLILFSlmlacpKYVTLNRGNHE 403
Cdd:PRK11439  10 RIA-GHQwrhIWLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEE------HWVRAVRGNHE 81
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.17
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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