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Conserved domains on  [gi|15829308|ref|NP_308081|]
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diadenosine tetraphosphatase [Escherichia coli O157:H7 str. Sakai]

Protein Classification

diadenosine tetraphosphatase( domain architecture ID 11489501)

diadenosine tetraphosphatase catalyzes the hydrolysis of P1,P4-bis(5'-adenosyl) tetraphosphate to yield ADP

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 1-279 0e+00

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


:

Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 566.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308     1 MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRN 80
Cdd:TIGR00668   1 MATYLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    81 KPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160
Cdd:TIGR00668  81 KPKDRLDPLLEAPDADELLNWLRRQPLLQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   161 NNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGI 240
Cdd:TIGR00668 161 NRWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDAPAPLKPWFAIPGPVYEEYSIAFGHWASLEGEGTPEGI 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 15829308   241 YALDTGCCWGGSLTCLRWEDKQYFVQPSNRHKDLGEGEA 279
Cdd:TIGR00668 241 YALDTGCCWGGRLTCLRWEDKQYFTQPSNRHKDLGEAAA 279
 
Name Accession Description Interval E-value
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 1-279 0e+00

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 566.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308     1 MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRN 80
Cdd:TIGR00668   1 MATYLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    81 KPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160
Cdd:TIGR00668  81 KPKDRLDPLLEAPDADELLNWLRRQPLLQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   161 NNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGI 240
Cdd:TIGR00668 161 NRWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDAPAPLKPWFAIPGPVYEEYSIAFGHWASLEGEGTPEGI 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 15829308   241 YALDTGCCWGGSLTCLRWEDKQYFVQPSNRHKDLGEGEA 279
Cdd:TIGR00668 241 YALDTGCCWGGRLTCLRWEDKQYFTQPSNRHKDLGEAAA 279
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
1-275 0e+00

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 535.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    1 MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRN 80
Cdd:PRK00166   1 MATYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLLAVAAGIKRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   81 KPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160
Cdd:PRK00166  81 KKKDTLDPILEAPDRDELLDWLRHQPLLHVDEELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  161 NNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGI 240
Cdd:PRK00166 161 DRWSPDLTGLERLRYIINAFTRMRFCTPDGRLDFKCKGPPDEAPAGLKPWFEVPGRKTRDYTIVFGHWAALEGLTTPPNI 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15829308  241 YALDTGCCWGGSLTCLRWEDKQYFVQPSNRHKDLG 275
Cdd:PRK00166 241 IALDTGCVWGGKLTALRLEDKQIFQVPCLKAKDPG 275
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 3-259 4.11e-168

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: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 465.48  E-value: 4.11e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   3 TYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKP 82
Cdd:cd07422   1 TYAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLAVAAGIKKLKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  83 KDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNN 162
Cdd:cd07422  81 KDTLDEILEAPDRDELLDWLRHQPLLHRDDELGIVMVHAGIPPQWDIEKALALAREVEAVLRGDNYRDFLANMYGNEPDR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308 163 WSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYA 242
Cdd:cd07422 161 WSDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAGLRPWFDVPNRKTRDYTIVFGHWAALGGLTRPNNIIA 240

                       250
                ....*....|....*..
gi 15829308 243 LDTGCCWGGSLTCLRWE 259
Cdd:cd07422 241 LDTGCVWGGKLTALRLE 257
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
 45-270 4.64e-102

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


Pssm-ID: 440404  Cd Length: 182  Bit Score: 295.65  E-value: 4.64e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  45 SLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQideekklvmahagit 124
Cdd:COG0639   1 SLDLLRLDLLLLLLRRLLLLLHDLHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLY--------------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308 125 pqwdlqtakecardveavlssdsypffldAMYGDMPNNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAP 204
Cdd:COG0639  66 -----------------------------GMYYNKPDRWSDDLQGLDRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAP 116

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829308 205 APLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYALDTGCCWGGSLTCLRWEDKQYFVQPSNR 270
Cdd:COG0639 117 PGLKPWFDVPGRRTADYTIVFGHWAALEGLGTPPNIYALDTGCVWGGKLTALRWEDKQRFQVPCPQ 182
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-74 1.28e-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: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 63.00  E-value: 1.28e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829308     1 MATYLIGDVH--GCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVR--LVLGNHDLHLLAVF 74
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPvyLVRGNHDFDYGECL 78
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 6-171 1.01e-04

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: 42.97  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308      6 IGDVHGCYDELIALLHKVEFTPGKDTLWLtGDLVARGPGSLDV--LRYVKSLGDSVRLVL--GNHDLHLLAVFAGISR-- 79
Cdd:smart00156  33 CGDIHGQFDDLLRLFDKNGQPPETNYVFL-GDYVDRGPFSIEVilLLFALKILYPNRIVLlrGNHESRSMNEIYGFYDec 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308     80 -NKPKDRLTPLLEapdadELLNWLrrqPLLQIDEEKKLVMaHAGITPqwDLQTAKECARDVEAVLSSDSYPFFlDAMYGD 158
Cdd:smart00156 112 kRKYGERIYEKFN-----EAFSWL---PLAALINGKILCM-HGGLSP--DLTTLDDIRKLKRPQEPPDDGLLI-DLLWSD 179

                          170
                   ....*....|....*.
gi 15829308    159 ---MPNNWSPELRGLG 171
Cdd:smart00156 180 pdqPVNGFGPSIRGAS 195
 
Name Accession Description Interval E-value
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 1-279 0e+00

bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate (Ap4A) is a regulatory metabolite of stress conditions. It is hydrolyzed to two ADP by this enzyme. Alternate names include diadenosine-tetraphosphatase and Ap4A hydrolase. [Cellular processes, Adaptations to atypical conditions]


Pssm-ID: 273208 [Multi-domain]  Cd Length: 279  Bit Score: 566.44  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308     1 MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRN 80
Cdd:TIGR00668   1 MATYLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    81 KPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160
Cdd:TIGR00668  81 KPKDRLDPLLEAPDADELLNWLRRQPLLQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   161 NNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGI 240
Cdd:TIGR00668 161 NRWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDAPAPLKPWFAIPGPVYEEYSIAFGHWASLEGEGTPEGI 240

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 15829308   241 YALDTGCCWGGSLTCLRWEDKQYFVQPSNRHKDLGEGEA 279
Cdd:TIGR00668 241 YALDTGCCWGGRLTCLRWEDKQYFTQPSNRHKDLGEAAA 279
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
1-275 0e+00

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 535.90  E-value: 0e+00
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    1 MATYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRN 80
Cdd:PRK00166   1 MATYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLLAVAAGIKRN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   81 KPKDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160
Cdd:PRK00166  81 KKKDTLDPILEAPDRDELLDWLRHQPLLHVDEELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNEP 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  161 NNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGI 240
Cdd:PRK00166 161 DRWSPDLTGLERLRYIINAFTRMRFCTPDGRLDFKCKGPPDEAPAGLKPWFEVPGRKTRDYTIVFGHWAALEGLTTPPNI 240

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15829308  241 YALDTGCCWGGSLTCLRWEDKQYFVQPSNRHKDLG 275
Cdd:PRK00166 241 IALDTGCVWGGKLTALRLEDKQIFQVPCLKAKDPG 275
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 3-259 4.11e-168

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: 277365 [Multi-domain]  Cd Length: 257  Bit Score: 465.48  E-value: 4.11e-168
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   3 TYLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKP 82
Cdd:cd07422   1 TYAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLAVAAGIKKLKK 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  83 KDRLTPLLEAPDADELLNWLRRQPLLQIDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPNN 162
Cdd:cd07422  81 KDTLDEILEAPDRDELLDWLRHQPLLHRDDELGIVMVHAGIPPQWDIEKALALAREVEAVLRGDNYRDFLANMYGNEPDR 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308 163 WSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYA 242
Cdd:cd07422 161 WSDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAGLRPWFDVPNRKTRDYTIVFGHWAALGGLTRPNNIIA 240

                       250
                ....*....|....*..
gi 15829308 243 LDTGCCWGGSLTCLRWE 259
Cdd:cd07422 241 LDTGCVWGGKLTALRLE 257
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
 45-270 4.64e-102

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


Pssm-ID: 440404  Cd Length: 182  Bit Score: 295.65  E-value: 4.64e-102
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  45 SLDVLRYVKSLGDSVRLVLGNHDLHLLAVFAGISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQideekklvmahagit 124
Cdd:COG0639   1 SLDLLRLDLLLLLLRRLLLLLHDLHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLY--------------- 65

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308 125 pqwdlqtakecardveavlssdsypffldAMYGDMPNNWSPELRGLGRLRFITNAFTRMRFCFPNGQLDMYSKESPEEAP 204
Cdd:COG0639  66 -----------------------------GMYYNKPDRWSDDLQGLDRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAP 116

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829308 205 APLKPWFAIPGPVAEEYSIAFGHWASLEGKGTPEGIYALDTGCCWGGSLTCLRWEDKQYFVQPSNR 270
Cdd:COG0639 117 PGLKPWFDVPGRRTADYTIVFGHWAALEGLGTPPNIYALDTGCVWGGKLTALRWEDKQRFQVPCPQ 182
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 4-258 8.43e-33

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: 120.17  E-value: 8.43e-33
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   4 YLIGDVHGCYDELIALLHKVEFtPGKDTLWLTGDLVARGPGSLDVLRYVKSL----GDSVRLVLGNHDLHLLAVFAGIsR 79
Cdd:cd00144   1 IVVGDIHGCFDDLLRLLEKLGF-PPEDKYLFLGDYVDRGPDSVEVIDLLLALkilyPDNVFLLRGNHEFMLLNFLYGF-Y 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  80 NKPKDRLTPLLEAPDADELLNWLRRQPLLQIDeEKKLVMAHAGITPQWDLQTAKECARDVEavlssdsYPFfldamygdm 159
Cdd:cd00144  79 DERTLRCLRKGGEELWREFNEVFNYLPLAALV-DGKILCVHGGLSPDLTLLDQIRNIRPIE-------NPD--------- 141

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308 160 pnnwspelrglgrlRFITNAFTRMRFCFPNGQLDMYSKESPEEAPAPLKPWFAipgPVAEEYSIAFGHWASLEGKGTPEG 239
Cdd:cd00144 142 --------------DQLVEDLLWSDPDESVGDFESSSRGGGYLFGEDAVDEFL---KKNGLKLIVRGHTPVEGGYEFLHG 204

                       250       260
                ....*....|....*....|....*
gi 15829308 240 --IYALDTGCCW----GGSLTCLRW 258
Cdd:cd00144 205 gkLITIFSAPNYcgkgGNKLAALVV 229
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 6-270 6.63e-21

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: 88.73  E-value: 6.63e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   6 IGDVHGCYDELIALLHKVEFT---------PGKDTLWLTGDLVARGPGSLDVLRYVKSLGDS--VRLVLGNHDLHLLAVF 74
Cdd:cd07423   3 IGDVHGCYDELVELLEKLGYQkkeeglyvhPEGRKLVFLGDLVDRGPDSIDVLRLVMNMVKAgkALYVPGNHCNKLYRYL 82

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  75 AGisRNKpkdRLT------------PLLEAPDA--DELLNWLRRQPLLQIDEEKKLVMAHAGITPqwDLQtakecARDVE 140
Cdd:cd07423  83 KG--RNV---QLAhglettveeleaLSKEERPEfrERFAEFLESLPSHLVLDGGRLVVAHAGIKE--EMI-----GRGSK 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308 141 AVLSsdsypFfldAMYGDmpnnwspelrglgrlrfITnaftrmrfcfpnGQLDMYSKesPEEapaplKPWfaipgpvAEE 220
Cdd:cd07423 151 RVRD-----F---CLYGD-----------------TT------------GETDEDGL--PVR-----RDW-------AKD 179

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 15829308 221 YS----IAFGHWASLEgkgtPEGI---YALDTGCCWGGSLTCLRWEDKQyFVQ-PSNR 270
Cdd:cd07423 180 YRgkalVVYGHTPVPE----PRWLnntINIDTGCVFGGKLTALRYPEME-LVSvPAKQ 232
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 1-123 2.19e-16

bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 76.67  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    1 MATYLIGDVHGCYDELIALLHKVEFT--------PGKDTLWLTGDLVARGPGSLDVLRYVKSLGD--SVRLVLGNHDLHL 70
Cdd:PRK13625   1 MKYDIIGDIHGCYQEFQALTEKLGYNwssglpvhPDQRKLAFVGDLTDRGPHSLRMIEIVWELVEkkAAYYVPGNHCNKL 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829308   71 LAVFAGisRNKpkdRLTPLLEAPDAD-ELL-----NWLRRQ--------PLLQIDEEKKLVMAHAGI 123
Cdd:PRK13625  81 YRFFLG--RNV---TIAHGLETTVAEyEALpshkqNMIKEKfitlyeqaPLYHILDEGRLVVAHAGI 142
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 4-80 6.40e-13

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: 66.19  E-value: 6.40e-13
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15829308   4 YLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSlgDSVRLVLGNHDLHLLAVFAGISRN 80
Cdd:cd07424   4 FVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQ--PWFHAVQGNHEQMAIDALRGGDDV 78
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 1-74 1.28e-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: 459691 [Multi-domain]  Cd Length: 114  Bit Score: 63.00  E-value: 1.28e-12
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829308     1 MATYLIGDVH--GCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGDSVR--LVLGNHDLHLLAVF 74
Cdd:pfam00149   1 MRILVIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYVPvyLVRGNHDFDYGECL 78
PRK09968 PRK09968
protein-serine/threonine phosphatase;
4-145 7.01e-10

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 57.60  E-value: 7.01e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    4 YLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYV-KSLGDSVRlvlGNHDLHLLAVFAG------ 76
Cdd:PRK09968  18 WVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLLnQPWFISVK---GNHEAMALDAFETgdgnmw 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15829308   77 -ISRNKPKDRLTPLLEAPDADELLNWLRRQPLLQI-DEEKKLVMAHAGItPQWDLQTAKECARD-----VEAVLSS 145
Cdd:PRK09968  95 lASGGDWFFDLNDSEQQEATDLLLKFHHLPHIIEItNDNIKYVIAHADY-PGDEYDFGKEIAESellwpVDRVQKS 169
PHA02239 PHA02239
putative protein phosphatase
 1-79 1.04e-09

putative protein phosphatase


Pssm-ID: 107154 [Multi-domain]  Cd Length: 235  Bit Score: 57.31  E-value: 1.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    1 MATYLIGDVHGCYDELIALLHKV--EFTPgKDTLWLTGDLVARGPGSLDVLRYVKSL---GDSVRLVLGNHDLHLLAVFA 75
Cdd:PHA02239   1 MAIYVVPDIHGEYQKLLTIMDKInnERKP-EETIVFLGDYVDRGKRSKDVVNYIFDLmsnDDNVVTLLGNHDDEFYNIME 79


                 ....
gi 15829308   76 GISR 79
Cdd:PHA02239  80 NVDR 83
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 5-72 1.31e-09

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: 277358 [Multi-domain]  Cd Length: 222  Bit Score: 56.79  E-value: 1.31e-09
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15829308   5 LIGDVHGCYDELIALLHKVEFT--------PGKDTLWLtGDLVARGPGSLDVLRYVKSLGD--SVRLVLGNHDLHLLA 72
Cdd:cd07413   3 LIGDVHGCAHTLDRLLDLLGYRlqggvwrhPRRQALFV-GDLIDRGPRIREVLHRVHAMVDagEALCVMGNHEFNALA 79
MPP_RdgC cd07420
Drosophila melanogaster RdgC and related proteins, metallophosphatase domain; RdgC (retinal ...
 7-171 3.07e-09

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: 56.65  E-value: 3.07e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   7 GDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSL----GDSVRLVLGNHDLHLLAVFAGISR--- 79
Cdd:cd07420  57 GDLHGKLDDLLLIFYKNGLPSPENPYVFNGDFVDRGKRSIEILMILFAFvlvyPNAVHLNRGNHEDHIMNLRYGFTKevm 136

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  80 NKPKDRLTPLLEApdADELLNWLrrqPLLQIDEEKKLVmAHAGITPQWDLQTAKECARDvEAVLSSDSYPFFLDAMYGD- 158
Cdd:cd07420 137 QKYKDHGKKILRL--LEDVFSWL---PLATIIDNKVLV-VHGGISDSTDLDLLDKIDRH-KYVSTKTEWQQVVDILWSDp 209

                       170
                ....*....|....*
gi 15829308 159 MPNN--WSPELRGLG 171
Cdd:cd07420 210 KATKgcKPNTFRGGG 224
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
5-141 1.28e-08

Predicted phosphodiesterase, calcineurin family [General function prediction only];


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 53.38  E-value: 1.28e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   5 LIGDVHGCYDELIALLHKVEfTPGKDTLWLTGDLVARGPGSLDVLRYVKSLGdsVRLVLGNHDlhllavfagisrnkpkd 84
Cdd:COG0622   4 VISDTHGNLPALEAVLEDLE-REGVDLIVHLGDLVGYGPDPPEVLDLLRELP--IVAVRGNHD----------------- 63

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829308  85 rltplleapdaDELLNWLRRQPLLQI--DEEKKLVMAHAG----ITPQWDLQTAKECARDVEA 141
Cdd:COG0622  64 -----------GAVLRGLRSLPETLRleLEGVRILLVHGSpneyLLPDTPAERLRALAAEGDA 115
pphA PRK11439
protein-serine/threonine phosphatase;
4-67 3.04e-08

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 52.84  E-value: 3.04e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15829308    4 YLIGDVHGCYDELIALLHKVEFTPGKDTLWLTGDLVARGPGSLDVLRYVKSlgDSVRLVLGNHD 67
Cdd:PRK11439  20 WLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLLEE--HWVRAVRGNHE 81
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 6-128 1.16e-07

Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, eukaryotic, and archeal proteins orthologous to the Shewanella cold-active protein-tyrosine phosphatase, CAPTPase. CAPTPase is an uncharacterized protein that belongs to the Shelph (Shewanella-like phosphatase) family of PPP (phosphoprotein phosphatases). The PPP family is one of two known protein phosphatase families specific for serine and threonine. In addition to Shelps, the PPP family also includes: PP1, PP2A, PP2B (calcineurin), PP4, PP5, PP6, PP7, Bsu1, RdgC, PrpE, PrpA/PrpB, and ApA4 hydrolase. The PPP catalytic domain is defined by three conserved motifs (-GDXHG-, -GDXVDRG- and -GNHE-). The PPP enzyme family is ancient with members found in all eukaryotes, and in most bacterial and archeal genomes. Dephosphorylation of phosphoserines and phosphothreonines on target proteins plays a central role in the regulation of many cellular processes. PPPs belong to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.


Pssm-ID: 277368 [Multi-domain]  Cd Length: 209  Bit Score: 51.15  E-value: 1.16e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   6 IGDVHGCYDELIALLHK-------VEFTPGKDTLWLTGDLVARGPGSLDVLRY-------VKSLGDSVRLVLGNH----- 66
Cdd:cd07425   3 IGDLHGDLDRLRTILKLagvidsnDRWIGGDTVVVQTGDILDRGDDEIEILKLleklkrqARKAGGKVILLLGNHelmnl 82

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  67 --DLH-----LLAVFAGisRNKPKDRLTplleaPDADELLNWLRRQPL-LQIDEekkLVMAHAGITPQWD 128
Cdd:cd07425  83 cgDFRyvhprGLNEFGG--VAKRRYALL-----SDGGYIGRYLRTHPVvLVVND---ILFVHGGLGPLWS 142
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-70 3.21e-07

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: 48.42  E-value: 3.21e-07
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   5 LIGDVHGCYDELIALLHKVEFTPGK-DTLWLTGDLVARGPGSLDVLRYV---KSLGDSVRLVLGNHDLHL 70
Cdd:cd00838   2 VISDIHGNLEALEAVLEAALAKAEKpDLVICLGDLVDYGPDPEEVELKAlrlLLAGIPVYVVPGNHDILV 71
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
6-121 1.82e-05

Predicted phosphoesterase, related to the Icc protein [General function prediction only];


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 44.62  E-value: 1.82e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   6 IGDVHGCYDELIALLHKVEFTPGkDTLWLTGDLVARGPGS--LDVLRYVKSLGDSVRLVLGNHDLHLLA----------- 72
Cdd:COG2129   5 VSDLHGNFDLLEKLLELARAEDA-DLVILAGDLTDFGTAEeaREVLEELAALGVPVLAVPGNHDDPEVLdaleesgvhnl 83

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 15829308  73 ----------VFAGISRNKPKDRLTPLLEapDADELLNWLRRqpllQIDEEKKLVMAHA 121
Cdd:COG2129  84 hgrvveigglRIAGLGGSRPTPFGTPYEY--TEEEIEERLAK----LREKDVDILLTHA 136
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 6-171 1.01e-04

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: 42.97  E-value: 1.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308      6 IGDVHGCYDELIALLHKVEFTPGKDTLWLtGDLVARGPGSLDV--LRYVKSLGDSVRLVL--GNHDLHLLAVFAGISR-- 79
Cdd:smart00156  33 CGDIHGQFDDLLRLFDKNGQPPETNYVFL-GDYVDRGPFSIEVilLLFALKILYPNRIVLlrGNHESRSMNEIYGFYDec 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308     80 -NKPKDRLTPLLEapdadELLNWLrrqPLLQIDEEKKLVMaHAGITPqwDLQTAKECARDVEAVLSSDSYPFFlDAMYGD 158
Cdd:smart00156 112 kRKYGERIYEKFN-----EAFSWL---PLAALINGKILCM-HGGLSP--DLTTLDDIRKLKRPQEPPDDGLLI-DLLWSD 179

                          170
                   ....*....|....*.
gi 15829308    159 ---MPNNWSPELRGLG 171
Cdd:smart00156 180 pdqPVNGFGPSIRGAS 195
CpdA COG1409
3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];
6-143 8.97e-04

3',5'-cyclic AMP phosphodiesterase CpdA [Signal transduction mechanisms];


Pssm-ID: 441019 [Multi-domain]  Cd Length: 234  Bit Score: 39.67  E-value: 8.97e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   6 IGDVH-------GCYDELIALLHKVEfTPGKDTLWLTGDLVARG-PGSLDVLR-YVKSLGDSVRLVLGNHDL--HLLAVF 74
Cdd:COG1409   6 ISDLHlgapdgsDTAEVLAAALADIN-APRPDFVVVTGDLTDDGePEEYAAAReILARLGVPVYVVPGNHDIraAMAEAY 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  75 AGISRNKPKDRLTPLLEAPDA------------------DELLNWLRRQpLLQIDEEKKLVMAHAGI--TPQWDLQTAKE 134
Cdd:COG1409  85 REYFGDLPPGGLYYSFDYGGVrfigldsnvpgrssgelgPEQLAWLEEE-LAAAPAKPVIVFLHHPPysTGSGSDRIGLR 163


                ....*....
gi 15829308 135 CARDVEAVL 143
Cdd:COG1409 164 NAEELLALL 172
MPP_PP1_PPKL cd07414
PP1, PPKL (PP1 and kelch-like) enzymes, and related proteins, metallophosphatase domain; PP1 ...
 7-137 1.66e-03

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: 39.25  E-value: 1.66e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308   7 GDVHGCYDELIALLHKVEFTPGKDTLWLtGDLVARGPGSLDV----LRYVKSLGDSVRLVLGNHDlhllavFAGISR--- 79
Cdd:cd07414  56 GDIHGQYYDLLRLFEYGGFPPESNYLFL-GDYVDRGKQSLETicllLAYKIKYPENFFLLRGNHE------CASINRiyg 128

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308  80 --NKPKDRLTPLLEAPDADeLLNWLrrqPLLQIDEEKKLVMaHAGITPqwDLQTAKECAR 137
Cdd:cd07414 129 fyDECKRRYNIKLWKTFTD-CFNCL---PVAAIVDEKIFCC-HGGLSP--DLQSMEQIRR 181
MPP_NostocDevT-like cd07397
Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative ...
 6-67 2.46e-03

Nostoc DevT and similar proteins, metallophosphatase domain; DevT (Alr4674) is a putative protein phosphatase from Nostoc PCC 7120 (Anabaena PCC 7120). DevT mutants form mature heterocysts, but they are unable to fix N(2) and must be supplied with a source of combined nitrogen in order to survive. Anabaena DevT shows homology to phosphatases of the PPP family and displays a Mn(2+)-dependent phosphatase activity. DevT is constitutively expressed in both vegetative cells and heterocysts, and is not regulated by NtcA. The heterocyst regulator HetR may exert a certain inhibition on the expression of devT. Under diazotrophic growth conditions, DevT protein accumulates specifically in mature heterocysts. The role that DevT plays in a late essential step of heterocyst differentiation is still unknown. 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: 277342 [Multi-domain]  Cd Length: 245  Bit Score: 38.43  E-value: 2.46e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15829308   6 IGDVHGCYDEL-IALLHKVeftpGKDTLWLTGDLvarGPGSLDVLRYVKSLGDSVRLVLGNHD 67
Cdd:cd07397   6 VGDVHGQWDAEdERALRLL----QPDLVLFVGDF---GNENVQLVRRIASLDLPKAVILGNHD 61
PTZ00480 PTZ00480
serine/threonine-protein phosphatase; Provisional
 5-126 4.62e-03

serine/threonine-protein phosphatase; Provisional


Pssm-ID: 185658 [Multi-domain]  Cd Length: 320  Bit Score: 38.10  E-value: 4.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15829308    5 LIGDVHGCYDELIALLHKVEFTPGKDTLWLtGDLVARGPGSLD----VLRYVKSLGDSVRLVLGNHDLHLLAVFAGIsRN 80
Cdd:PTZ00480  63 ICGDVHGQYFDLLRLFEYGGYPPESNYLFL-GDYVDRGKQSLEticlLLAYKIKYPENFFLLRGNHECASINRIYGF-YD 140

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 15829308   81 KPKDRLTPLLEAPDADeLLNWLrrqPLLQIDEEKKLVMaHAGITPQ 126
Cdd:PTZ00480 141 ECKRRYTIKLWKTFTD-CFNCL---PVAALIDEKILCM-HGGLSPE 181
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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