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Conserved domains on  [gi|62719327|ref|NP_599186|]
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serine/threonine-protein phosphatase 4 catalytic subunit [Rattus norvegicus]

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List of domain hits

Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
6-290 0e+00

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: 163658 [Multi-domain]  Cd Length: 285  Bit Score: 642.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:cd07415   1 DLDKWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRVGGDPPDTNYLFLGDYVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYCTDLFDYLPLAALIDNQIFCVHG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGY 245
Cdd:cd07415 161 GLSPSIDTLDQIRAIDRFQEVPHEGPMCDLLWSDPDDIEGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62719327 246 KWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:cd07415 241 QWMFDDKLVTVWSAPNYCYRCGNVASIMELDEHLKRSFKVFEAAP 285
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
6-307 6.18e-164

serine/threonine protein phosphatase 2A; Provisional


:

Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 461.59  E-value: 6.18e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGY 245
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62719327  246 KWHFNETVL-TVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKpVADYFL 307
Cdd:PTZ00239 242 KYWFPDQNLvTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKN-VLPYFL 303
 
Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
6-290 0e+00

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: 163658 [Multi-domain]  Cd Length: 285  Bit Score: 642.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:cd07415   1 DLDKWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRVGGDPPDTNYLFLGDYVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYCTDLFDYLPLAALIDNQIFCVHG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGY 245
Cdd:cd07415 161 GLSPSIDTLDQIRAIDRFQEVPHEGPMCDLLWSDPDDIEGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62719327 246 KWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:cd07415 241 QWMFDDKLVTVWSAPNYCYRCGNVASIMELDEHLKRSFKVFEAAP 285
ApaH COG0639
Diadenosine tetraphosphatase and related serine/threonine protein phosphatases [Signal ...
118-264 9.71e-40

Diadenosine tetraphosphatase and related serine/threonine protein phosphatases [Signal transduction mechanisms]


Pssm-ID: 223712  Cd Length: 155  Bit Score: 138.25  E-value: 9.71e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 118 RQITQVYGFYDECLRKYGSVTVWRY---CTEIFDYLSLSAIIDG-KIFCVHGGLSPSI-QTLDQIRTIDRKQ--EVPHDG 190
Cdd:COG0639   1 MLLTALYGFYDEKLRKYGEELEWLRaagGLETFDSLPLAAVAEGgKLLCHHGGLSPGLdRLLDIIEVLDRLRacEVPHAG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62719327 191 PMCDLLWSDPE--DTTGWGVSPRGAGYLFGsDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAPNYCY 264
Cdd:COG0639  81 HTHDLLWSDPDggDRRIWNPGPRGVPRDGG-DVTAVFGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNYCY 155
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
48-183 3.51e-34

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: 249630  Cd Length: 186  Bit Score: 124.49  E-value: 3.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    48 PVTVCGDIHGQFYDL---KELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVY 124
Cdd:pfam00149   2 RILVIGDLHGGLDDLdllLLLLELLGEPKPDLVLFLGDLVDRGPPSLEVLALLFALKLKAPGPVYLVRGNHDFDSGNSEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   125 GFYDEC------------------------LRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTI 180
Cdd:pfam00149  82 GFYLECaglpyvlgngdvsngtveiiglssLYGKGGGLVWEEFLELLDLLLLAALVDGKILLVHGPLSPSLDSGDDIVLF 161

                  ...
gi 62719327   181 DRK 183
Cdd:pfam00149 162 GEE 164
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
6-307 6.18e-164

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 461.59  E-value: 6.18e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGY 245
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62719327  246 KWHFNETVL-TVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKpVADYFL 307
Cdd:PTZ00239 242 KYWFPDQNLvTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKN-VLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
22-290 1.53e-135

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: 388.11  E-value: 1.53e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327     22 ESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALK 101
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    102 VRYPDRITLIRGNHESRQITQVYGFYDECLRKYGsVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTID 181
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    182 RKQEVPHDGPMCDLLWSDPEDTT-GWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAP 260
Cdd:smart00156 162 RPQEPPDDGLLIDLLWSDPDQPVnGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAP 241
                          250       260       270
                   ....*....|....*....|....*....|
gi 62719327    261 NYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:smart00156 242 NYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
PHA02239 PHA02239
putative protein phosphatase
49-150 5.84e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 39.21  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   49 VTVCGDIHGQFydlKELFRVGGDV-----PETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIrGNHES---RQI 120
Cdd:PHA02239   3 IYVVPDIHGEY---QKLLTIMDKInnerkPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHDDefyNIM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 62719327  121 TQV--YGFYD---------ECLRKYGSVTVWRYCTEIFDYL 150
Cdd:PHA02239  79 ENVdrLSIYDiewlsryciETLNSYGVSTVTLKYSSVEENL 119
Ser/Thr_phosphatase_family_protein TIGR04075
polynucleotide kinase-phosphatase; Members of this protein family are the bacterial ...
48-125 8.98e-03

polynucleotide kinase-phosphatase; Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring. [Transcription, RNA processing]


Pssm-ID: 274963 [Multi-domain]  Cd Length: 851  Bit Score: 36.13  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    48 PVTVCGDIHGQFYDLKEL---------FRVGGDVPETNY------LFMGDFVDRGFYSVETFLLLLALkVRYPDRITlIR 112
Cdd:TIGR04075 181 PFDIIGDVHGCRDELETLleelgyqieRDEGGRGVDVTHpegrkaVFVGDLVDRGPDSPGVLRLVMGM-VAAGTALC-VP 258
                          90       100
                  ....*....|....*....|.
gi 62719327   113 GNHE--------SRQITQVYG 125
Cdd:TIGR04075 259 GNHDvkllralrGRNVKLTHG 279
 
Name Accession Description Interval E-value
MPP_PP2A_PP4_PP6 cd07415
PP2A, PP4, and PP6 phosphoprotein phosphatases, metallophosphatase domain; PP2A-like family of ...
6-290 0e+00

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: 163658 [Multi-domain]  Cd Length: 285  Bit Score: 642.35  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:cd07415   1 DLDKWIEQLKKCELLPESEVKSLCEKAKEILVKESNVQRVRSPVTVCGDIHGQFYDLLELFRVGGDPPDTNYLFLGDYVD 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07415  81 RGYYSVETFLLLLALKVRYPDRITLLRGNHESRQITQVYGFYDECLRKYGNANVWKYCTDLFDYLPLAALIDNQIFCVHG 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGY 245
Cdd:cd07415 161 GLSPSIDTLDQIRAIDRFQEVPHEGPMCDLLWSDPDDIEGWGISPRGAGYLFGQDVVEEFNHNNGLTLICRAHQLVMEGY 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 62719327 246 KWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:cd07415 241 QWMFDDKLVTVWSAPNYCYRCGNVASIMELDEHLKRSFKVFEAAP 285
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
6-289 6.04e-114

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: 163657 [Multi-domain]  Cd Length: 293  Bit Score: 333.95  E-value: 6.04e-114
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   6 DLDRQIEQL---RRCELIK-----ESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNY 77
Cdd:cd07414   1 DIDSIIERLlevRGSRPGKnvqltEAEIRGLCLKSREIFLSQPILLELEAPLKICGDIHGQYYDLLRLFEYGGFPPESNY 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  78 LFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIID 157
Cdd:cd07414  81 LFLGDYVDRGKQSLETICLLLAYKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-NIKLWKTFTDCFNCLPVAAIID 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 158 GKIFCVHGGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPE-DTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCR 236
Cdd:cd07414 160 EKIFCMHGGLSPDLQSMEQIRRIMRPTDVPDQGLLCDLLWSDPDkDVQGWGENDRGVSFTFGKDVVAKFLNKHDLDLICR 239
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 62719327 237 AHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAA 289
Cdd:cd07414 240 AHQVVEDGYEFFAKRQLVTLFSAPNYCGEFDNAGAMMSVDETLMCSFQILKPA 292
MPP_PP2B cd07416
PP2B, metallophosphatase domain; PP2B (calcineurin) is a unique serine/threonine protein ...
10-276 3.65e-99

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: 163659 [Multi-domain]  Cd Length: 305  Bit Score: 296.52  E-value: 3.65e-99
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  10 QIEQLRRcELIKESEVKALCA-----KAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFV 84
Cdd:cd07416   2 RIDVLKA-HFMREGRLSEEDAlriitEGAEILRQEPNLLRIEAPVTVCGDIHGQFYDLLKLFEVGGSPANTRYLFLGDYV 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  85 DRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIIDGKIFCVH 164
Cdd:cd07416  81 DRGYFSIECVLYLWALKILYPKTLFLLRGNHECRHLTEYFTFKQECKIKY-SERVYDACMEAFDCLPLAALMNQQFLCVH 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 165 GGLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDP--EDTTGW------GVSPRGAGYLFGSDVVAQFNAANDIDMTCR 236
Cdd:cd07416 160 GGLSPELKTLDDIRKLDRFREPPAFGPMCDLLWSDPleDFGNEKtqehfvHNTVRGCSYFYSYRAVCEFLQKNNLLSIIR 239
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*.
gi 62719327 237 AHQLVMEGYKWHFNE------TVLTVWSAPNYCYRCGNVAAILELD 276
Cdd:cd07416 240 AHEAQDAGYRMYRKSqttgfpSLITIFSAPNYLDVYNNKAAVLKYE 285
MPP_PP5_C cd07417
PP5, C-terminal metallophosphatase domain; Serine/threonine protein phosphatase-5 (PP5) is a ...
31-303 2.25e-93

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: 163660 [Multi-domain]  Cd Length: 316  Bit Score: 282.21  E-value: 2.25e-93
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  31 KAREILVEESNVQRVDSP----VTVCGDIHGQFYDLKELFRVGGDVPETN-YLFMGDFVDRGFYSVETFLLLLALKVRYP 105
Cdd:cd07417  40 QVKELLKKLPSLVEITIPegekITVCGDTHGQFYDLLNIFELNGLPSETNpYLFNGDFVDRGSFSVEVILTLFAFKLLYP 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 106 DRITLIRGNHESRQITQVYGFYDECLRKYGSvTVWRYCTEIFDYLSLSAIIDGKIFCVHGGL-SPSIQTLDQIRTIDRKQ 184
Cdd:cd07417 120 NHFHLNRGNHETDNMNKMYGFEGEVKAKYNE-QMFDLFSEVFNWLPLAHLINGKVLVVHGGLfSDDGVTLDDIRKIDRFR 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 185 EVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAPNYCY 264
Cdd:cd07417 199 QPPDSGLMCELLWSDPQPQPGRSPSKRGVGCQFGPDVTKRFLEENNLEYIIRSHEVKDEGYEVEHDGKCITVFSAPNYCD 278
                       250       260       270       280
                ....*....|....*....|....*....|....*....|
gi 62719327 265 RCGNVAAILELDEH-LQKDFIIFEAAPQetrgiPSKKPVA 303
Cdd:cd07417 279 QMGNKGAFIRITGSdLKPKFTQFEAVPH-----PNVKPMA 313
MPP_Bsu1_C cd07419
Arabidopsis thaliana Bsu1 phosphatase and related proteins, C-terminal metallophosphatase ...
19-285 1.06e-82

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: 163662 [Multi-domain]  Cd Length: 311  Bit Score: 254.64  E-value: 1.06e-82
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  19 LIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELF--------RVGGDVPETNYLFMGDFVDRGFYS 90
Cdd:cd07419  20 FFNWNEILELCDAAEDIFKQEPMVLRLRAPIKIFGDIHGQFGDLMRLFdeygspvtEAAGDIEYIDYLFLGDYVDRGSNS 99
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  91 VETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGS-----VTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:cd07419 100 LETICLLLALKVKYPNQIHLIRGNHEDRDINALFGFREECKERLGEdpndgDSVWRRINRLFEWLPLAAIIEDKILCMHG 179
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 166 GLSPSIQTLDQIRTIDRKQEVPHDGP-MCDLLWSDPEDTTGWGVS------PRGAG--YLFGSDVVAQFNAANDIDMTCR 236
Cdd:cd07419 180 GIGRSINHVSEIEDLKRPLTMEFGEQvVMDLLWSDPTENDSVLGLrpnaidPRGPGliVKFGPDRVHRFLEENDLQMIIR 259
                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*....
gi 62719327 237 AHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILeldeHLQKDFII 285
Cdd:cd07419 260 AHECVMDGFERFAQGKLITLFSATNYCGTAGNAGAIL----VLGRDLTI 304
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
50-275 1.99e-72

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: 163613 [Multi-domain]  Cd Length: 225  Bit Score: 225.41  E-value: 1.99e-72
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  50 TVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRyPDRITLIRGNHESRQITQVYGFYDE 129
Cdd:cd00144   1 YVIGDIHGCLDDLLRLLEKIGFPPNDKLIFLGDYVDRGPDSVEVIDLLLALKIL-PDNVILLRGNHEDMLLNFLYGFYDE 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 130 C--------LRKYGSVTVWRYCTEIFDYLSLSAIID-GKIFCVHGGLSPSIQTLDQIrtidrkQEVPHDGPMCDLLWSDP 200
Cdd:cd00144  80 DewiggtlrLLKKLGEDLWEEFNDVFFYLPLAALIEtKKVLCVHGGLSPGLPLEEQI------KEEPEDQLPEDLLWSDP 153
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62719327 201 EDTTGWGVSPRGAGylfGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAPNYCYRCGNVAAILEL 275
Cdd:cd00144 154 LELPGGFGSSRRGG---GPDAVEWFLKKNGLKLIVRGHTPVEEGYEFGHDGNLITIDSGCNYCGGGGNKLAALVL 225
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
6-284 1.48e-51

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: 163663 [Multi-domain]  Cd Length: 321  Bit Score: 174.11  E-value: 1.48e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDS----PVTVCGDIHGQFYDLKELFRVGG-DVPETNYLFM 80
Cdd:cd07420   6 HIDALIEAFKEKQLLHAKYVLLILREARKVLKQLPNISRVSTsiskQVTICGDLHGKLDDLFLIFYKNGlPSPENPYVFN 85
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  81 GDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYG--SVTVWRYCTEIFDYLSLSAIIDG 158
Cdd:cd07420  86 GDFVDRGKRSIEILIILFAFFLVYPNEVHLNRGNHEDHIMNLRYGFTKEVMSKYKlhGKKILRLLEDVFSWLPLATIIDN 165
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 159 KIFCVHGGLSpSIQTLDQIRTIDR----------------KQEVPHDGPMC-----------DLLWSDPEDTTG-WGVSP 210
Cdd:cd07420 166 KILVVHGGIS-DSTDLDLLDKIDRhkyvsvlrpplrkgmeELTGEEEDPSEpldktewrqilDILWSDPKAQKGcKPNTF 244
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 62719327 211 RGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAPNYcYRCG-NVAAILELDEHLQKDFI 284
Cdd:cd07420 245 RGGGCYFGPDVTSKVLQKHGLSLLIRSHECKPEGYEFCHNNKVITIFSASNY-YEEGsNRGAYIKLGPDLTPHFV 318
MPP_PP7 cd07418
PP7, metallophosphatase domain; PP7 is a plant phosphoprotein phosphatase that is highly ...
23-288 1.88e-47

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: 164.97  E-value: 1.88e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  23 SEVKALCAKAREILVEESNVQRVD----SPVTVCGDIHGQFYDLKELFRVGGdVPETN--YLFMGDFVDRGFYSVETFLL 96
Cdd:cd07418  38 NVFDSLVLTAHKILHREPNCVRIDvedvCEVVVVGDVHGQLHDVLFLLEDAG-FPDQNrfYVFNGDYVDRGAWGLETFLL 116
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  97 LLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSV--TVWRYCTEIFDYLSLSAIIDGKIFCVHGGL------- 167
Cdd:cd07418 117 LLSWKVLLPDRVYLLRGNHESKFCTSMYGFEQEVLTKYGDKgkHVYRKCLGCFEGLPLASIIAGRVYTAHGGLfrspslp 196
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 168 --------------------SPSIQTLDQIRTIDRK-QEVPHDGPMC---DLLWSDPEDTTgwGVSP---RGAGYLFGSD 220
Cdd:cd07418 197 krkkqkgknrrvlllepeseSLKLGTLDDLMKARRSvLDPPGEGSNLipgDVLWSDPSLTP--GLSPnkqRGIGLLWGPD 274
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 221 VVAQFNAANDIDMTCRAHQ------------LVMEGYKWHFNETV---LTVWSAPNYCY------RCGNVAA--ILELDE 277
Cdd:cd07418 275 CTEEFLEKNNLKLIIRSHEgpdarekrpglaGMNKGYTVDHDVESgklITLFSAPDYPQfqateeRYNNKGAyiILQPPD 354
                       330
                ....*....|.
gi 62719327 278 HLQKDFIIFEA 288
Cdd:cd07418 355 FSDPQFHTFEA 365
ApaH COG0639
Diadenosine tetraphosphatase and related serine/threonine protein phosphatases [Signal ...
118-264 9.71e-40

Diadenosine tetraphosphatase and related serine/threonine protein phosphatases [Signal transduction mechanisms]


Pssm-ID: 223712  Cd Length: 155  Bit Score: 138.25  E-value: 9.71e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 118 RQITQVYGFYDECLRKYGSVTVWRY---CTEIFDYLSLSAIIDG-KIFCVHGGLSPSI-QTLDQIRTIDRKQ--EVPHDG 190
Cdd:COG0639   1 MLLTALYGFYDEKLRKYGEELEWLRaagGLETFDSLPLAAVAEGgKLLCHHGGLSPGLdRLLDIIEVLDRLRacEVPHAG 80
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62719327 191 PMCDLLWSDPE--DTTGWGVSPRGAGYLFGsDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAPNYCY 264
Cdd:COG0639  81 HTHDLLWSDPDggDRRIWNPGPRGVPRDGG-DVTAVFGIVHTPKLIERAHVLYDIDTGAVFGGGLLTAFSAPNYCY 155
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
48-183 3.51e-34

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: 249630  Cd Length: 186  Bit Score: 124.49  E-value: 3.51e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    48 PVTVCGDIHGQFYDL---KELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVY 124
Cdd:pfam00149   2 RILVIGDLHGGLDDLdllLLLLELLGEPKPDLVLFLGDLVDRGPPSLEVLALLFALKLKAPGPVYLVRGNHDFDSGNSEL 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   125 GFYDEC------------------------LRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTI 180
Cdd:pfam00149  82 GFYLECaglpyvlgngdvsngtveiiglssLYGKGGGLVWEEFLELLDLLLLAALVDGKILLVHGPLSPSLDSGDDIVLF 161

                  ...
gi 62719327   181 DRK 183
Cdd:pfam00149 162 GEE 164
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
53-169 3.79e-06

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: 163668  Cd Length: 208  Bit Score: 45.70  E-value: 3.79e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  53 GDIHGQFYDLKELFRVGGDVPE-------TNYLFM-GDFVDRGFYSVETFLLLLALKV---RYPDRITLIRGNHESRQI- 120
Cdd:cd07425   4 GDLHGDLDAFREILKGAGVIDSndhwiggSTHLVQlGDIFDRGPDVIEILWLLYKLEQeaaKAGGKVHFLLGNHELMNLc 83
                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 62719327 121 ----------TQVYGFYDECLRKYgsvtvWRYCTEIFDYLS---LSAIIDGKIFcVHGGLSP 169
Cdd:cd07425  84 gdfryvhpkyFNEFGGLAMRRREL-----FSPGGELGRWLRskpVIVKVNDTLF-VHGGLGP 139
MPP_Rhilphs cd07421
Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ ...
49-116 1.19e-05

Rhilph phosphatases, metallophosphatase domain; Rhilphs (Rhizobiales/ Rhodobacterales/ Rhodospirillaceae-like phosphatases) are a phylogenetically distinct group of PPP (phosphoprotein phosphatases), found only in land plants. They are named for their close relationship to to PPP phosphatases from alpha-Proteobacteria, including Rhizobiales, Rhodobacterales and Rhodospirillaceae. The PPP (phosphoprotein phosphatase) family, to which the Rhilphs belong, 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: 163664  Cd Length: 304  Bit Score: 44.80  E-value: 1.19e-05
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62719327  49 VTVC-GDIHGQFYDLKELFR-----VGGDVPETNY-LFMGDFVDRGFYSVETFLLLLALKVRYPD-RITLIRGNHE 116
Cdd:cd07421   3 VVICvGDIHGYISKLNNLWLnlqsaLGPSDFASALvIFLGDYCDRGPETRKVIDFLISLPEKHPKqRHVFLCGNHD 78
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
51-116 2.21e-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: 163667 [Multi-domain]  Cd Length: 207  Bit Score: 43.41  E-value: 2.21e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 62719327  51 VCGDIHGQFYDL-KELFRVGGDvPETNYLF-MGDFVDRGFYSVETFLLLlalkvRYPdRITLIRGNHE 116
Cdd:cd07424   5 VVGDIHGHYSLLqKALDAVGFD-PARDRLIsVGDLIDRGPESLACLELL-----LEP-WFHAVRGNHE 65
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
51-116 9.89e-05

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


Pssm-ID: 163614  Cd Length: 131  Bit Score: 40.36  E-value: 9.89e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 62719327  51 VCGDIHGQFYDLKELFRVGgDVPETNY---LFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIRGNHE 116
Cdd:cd00838   2 VISDIHGNLEALEAVLEAA-LAAAEKPdfvLVLGDLVGDGPDPEEVLAAALALLLLLGIPVYVVPGNHD 69
MPP_PrpE cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
48-172 8.64e-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. 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: 163666 [Multi-domain]  Cd Length: 234  Bit Score: 38.79  E-value: 8.64e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  48 PVTVCGDIHGQFYDLKELF--------RVGGDVPETN--YLFMGDFVDRGFYSVETFLLLLAL----KVRYpdritlIRG 113
Cdd:cd07423   2 PFDIIGDVHGCYDELEELLeklgyrikRVGTVTHPEGrrAVFVGDLVDRGPDSPEVLRLVMSMvaagAALC------VPG 75
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327 114 NHES--------RQITQVYGFyDECLRKYG--SVTVWRYCTEIFDYLSLSAIID-GKIFCVHGGLSPSIQ 172
Cdd:cd07423  76 NHDNklyrklqgRNVKITHGL-EETVAQLEaeSEEFKEEVIEFYESLPSHLVLDeGKLVVAHAGIKEEMI 144
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
53-116 2.91e-03

Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as symmetrically cleaving Ap4A hydrolase and bis(5'nucleosyl)-tetraphosphatase) is a bacterial member of the PPP (phosphoprotein phosphatase) family of serine/threonine phosphatases that hydrolyzes the nucleotide-signaling molecule diadenosine tetraphosphate (Ap(4)A) into two ADP and also hydrolyzes Ap(5)A, Gp(4)G, and other extending compounds. Null mutations in apaH result in high intracellular levels of Ap(4)A which correlate with multiple phenotypes, including a decreased expression of catabolite-repressible genes, a reduction in the expression of flagellar operons, and an increased sensitivity to UV and heat. Ap4A hydrolase is important in responding to heat shock and oxidative stress via regulating the concentration of Ap4A in bacteria. Ap4A hydrolase is also thought to play a role in siderophore production, but the mechanism by which ApaH interacts with siderophore pathways in unknown. The PPP (phosphoprotein phosphatase) family, to which ApaH 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, and PrpA/PrpB. 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: 163665 [Multi-domain]  Cd Length: 257  Bit Score: 37.10  E-value: 2.91e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 62719327  53 GDIHGQFYDLKELF-RVGGDvPETNYL-FMGDFVDRGFYSVETFLLLLALKvrypDRITLIRGNHE 116
Cdd:cd07422   5 GDIQGCYDELQRLLeKINFD-PAKDRLwLVGDLVNRGPDSLETLRFVKSLG----DSAKTVLGNHD 65
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
53-87 7.98e-03

Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an uncharacterized protein from Pseudomonas aeruginosa with a metallophosphatase domain that belongs to the phosphoprotein phosphatase (PPP) family. 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: 163656  Cd Length: 222  Bit Score: 35.72  E-value: 7.98e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 62719327  53 GDIHGQFYDLKEL-----FRVGGDV---PETNYLFMGDFVDRG 87
Cdd:cd07413   5 GDIHGHAEKLVVLlhklgYQELSGVyrhPERQVVFLGDLIDRG 47
PTZ00239 PTZ00239
serine/threonine protein phosphatase 2A; Provisional
6-307 6.18e-164

serine/threonine protein phosphatase 2A; Provisional


Pssm-ID: 173488 [Multi-domain]  Cd Length: 303  Bit Score: 461.59  E-value: 6.18e-164
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    6 DLDRQIEQLRRCELIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVD 85
Cdd:PTZ00239   2 DIDRHIATLLNGGCLPERDLKLICERAKEIFLEESNVQPVRAPVNVCGDIHGQFYDLQALFKEGGDIPNANYIFIGDFVD 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   86 RGFYSVETFLLLLALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYGSVTVWRYCTEIFDYLSLSAIIDGKIFCVHG 165
Cdd:PTZ00239  82 RGYNSVETMEYLLCLKVKYPGNITLLRGNHESRQCTQVYGFYEEILRKYGNSNPWRLFMDVFDCLPLAALIEGQILCVHG 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  166 GLSPSIQTLDQIRTIDRKQEVPHDGPMCDLLWSDPEDTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGY 245
Cdd:PTZ00239 162 GLSPDMRTIDQIRTIDRKIEIPHEGPFCDLMWSDPEEVEYWAVNSRGAGYLFGAKVTKEFCRLNDLTLICRAHQLVMEGY 241
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 62719327  246 KWHFNETVL-TVWSAPNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKpVADYFL 307
Cdd:PTZ00239 242 KYWFPDQNLvTVWSAPNYCYRCGNIASILCLDENLQQTWKTFKEVPESAKSINPKN-VLPYFL 303
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
22-290 1.53e-135

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: 388.11  E-value: 1.53e-135
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327     22 ESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLALK 101
Cdd:smart00156   3 KEEILELLREVKEIFRQEPNLVEVSAPVTVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVILLLFALK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    102 VRYPDRITLIRGNHESRQITQVYGFYDECLRKYGsVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRTID 181
Cdd:smart00156  83 ILYPNRIVLLRGNHESRSMNEIYGFYDECKRKYG-ERIYEKFNEAFSWLPLAALINGKILCMHGGLSPDLTTLDDIRKLK 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    182 RKQEVPHDGPMCDLLWSDPEDTT-GWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWSAP 260
Cdd:smart00156 162 RPQEPPDDGLLIDLLWSDPDQPVnGFGPSIRGASYIFGPDAVDEFLKKNNLKLIIRAHQVVDDGYEFFADGKLVTIFSAP 241
                          250       260       270
                   ....*....|....*....|....*....|
gi 62719327    261 NYCYRCGNVAAILELDEHLQKDFIIFEAAP 290
Cdd:smart00156 242 NYCDRFGNKAAVLKVDKDLKLTFEQFKPGK 271
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
20-307 3.51e-95

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 286.94  E-value: 3.51e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   20 IKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLLA 99
Cdd:PTZ00480  32 LTEAEVRGLCIKARDIFISQPILLELEAPLKICGDVHGQYFDLLRLFEYGGYPPESNYLFLGDYVDRGKQSLETICLLLA 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  100 LKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIRT 179
Cdd:PTZ00480 112 YKIKYPENFFLLRGNHECASINRIYGFYDECKRRY-TIKLWKTFTDCFNCLPVAALIDEKILCMHGGLSPELSNLEQIRR 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  180 IDRKQEVPHDGPMCDLLWSDPE-DTTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVWS 258
Cdd:PTZ00480 191 IMRPTDVPDTGLLCDLLWSDPDkDVQGWADNERGVSYVFSQEIVQVFLKKHELDLICRAHQVVEDGYEFFSKRQLVTLFS 270
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 62719327  259 APNYCYRCGNVAAILELDEHLQKDFIIFEAAPQETRGIPSKKPVADYFL 307
Cdd:PTZ00480 271 APNYCGEFDNAGSMMTIDESLMCSFQILKPAEQGQGASQQNKPGSAKFV 319
PTZ00244 PTZ00244
serine/threonine-protein phosphatase PP1; Provisional
19-289 4.90e-83

serine/threonine-protein phosphatase PP1; Provisional


Pssm-ID: 140271 [Multi-domain]  Cd Length: 294  Bit Score: 254.83  E-value: 4.90e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   19 LIKESEVKALCAKAREILVEESNVQRVDSPVTVCGDIHGQFYDLKELFRVGGDVPETNYLFMGDFVDRGFYSVETFLLLL 98
Cdd:PTZ00244  24 LIREEDIRAVLTEVREIFMSQPMLLEIRPPVRVCGDTHGQYYDLLRIFEKCGFPPYSNYLFLGDYVDRGKHSVETITLQF 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   99 ALKVRYPDRITLIRGNHESRQITQVYGFYDECLRKYgSVTVWRYCTEIFDYLSLSAIIDGKIFCVHGGLSPSIQTLDQIR 178
Cdd:PTZ00244 104 CYKIVYPENFFLLRGNHECASINKMYGFFDDVKRRY-NIKLFKAFTDVFNTMPVCCVISEKIICMHGGLSPDLTSLASVN 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327  179 TIDRKQEVPHDGPMCDLLWSDPED-TTGWGVSPRGAGYLFGSDVVAQFNAANDIDMTCRAHQLVMEGYKWHFNETVLTVW 257
Cdd:PTZ00244 183 EIERPCDVPDRGILCDLLWADPEDeVRGFLESDRGVSYLFGEDIVNDFLDMVDMDLIVRAHQVMERGYGFFASRQLVTVF 262
                        250       260       270
                 ....*....|....*....|....*....|..
gi 62719327  258 SAPNYCYRCGNVAAILELDEHLQKDFIIFEAA 289
Cdd:PTZ00244 263 SAPNYCGEFDNDAAVMNIDDKLQCSFLIIPAR 294
PHA02239 PHA02239
putative protein phosphatase
49-150 5.84e-04

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 39.21  E-value: 5.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327   49 VTVCGDIHGQFydlKELFRVGGDV-----PETNYLFMGDFVDRGFYSVETFLLLLALKVRYPDRITLIrGNHES---RQI 120
Cdd:PHA02239   3 IYVVPDIHGEY---QKLLTIMDKInnerkPEETIVFLGDYVDRGKRSKDVVNYIFDLMSNDDNVVTLL-GNHDDefyNIM 78
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 62719327  121 TQV--YGFYD---------ECLRKYGSVTVWRYCTEIFDYL 150
Cdd:PHA02239  79 ENVdrLSIYDiewlsryciETLNSYGVSTVTLKYSSVEENL 119
Ser/Thr_phosphatase_family_protein TIGR04075
polynucleotide kinase-phosphatase; Members of this protein family are the bacterial ...
48-125 8.98e-03

polynucleotide kinase-phosphatase; Members of this protein family are the bacterial polynucleotide kinase-phosphatase (Pnkp) whose genes occur paired with genes for the 3' terminal RNA ribose 2'-O-methyltransferase Hen1. All members of the seed alignment belong to a cassette with the Hen1. The pair acts in bacterial RNA repair. This enzyme performs end-healing reactions on broken RNA, preparing from the RNA ligase to close the break. The working hypothesis is that the combination of Pnkp (RNA repair) and Hen1 (RNA modification) serves to first repair RNA damage from ribotoxins and then perform a modification that prevents the damage from recurring. [Transcription, RNA processing]


Pssm-ID: 274963 [Multi-domain]  Cd Length: 851  Bit Score: 36.13  E-value: 8.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 62719327    48 PVTVCGDIHGQFYDLKEL---------FRVGGDVPETNY------LFMGDFVDRGFYSVETFLLLLALkVRYPDRITlIR 112
Cdd:TIGR04075 181 PFDIIGDVHGCRDELETLleelgyqieRDEGGRGVDVTHpegrkaVFVGDLVDRGPDSPGVLRLVMGM-VAAGTALC-VP 258
                          90       100
                  ....*....|....*....|.
gi 62719327   113 GNHE--------SRQITQVYG 125
Cdd:TIGR04075 259 GNHDvkllralrGRNVKLTHG 279
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.13
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • 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 et al. (2009), "CDD: specific functional annotation with the Conserved Domain Database.", Nucleic Acids Res.37(D)205-10.
  • 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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