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Conserved domains on  [gi|1538640045|ref|WP_125559884|]
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MULTISPECIES: symmetrical bis(5'-nucleosyl)-tetraphosphatase [Pseudoalteromonas]

Protein Classification

diadenosine tetraphosphatase( domain architecture ID 11478265)

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 PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
1-263 2.89e-113

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


:

Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 326.74  E-value: 2.89e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   1 MANYVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLIcNVLLG-KT 79
Cdd:PRK00166    1 MATYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLL-AVAAGiKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  80 PNPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKE 159
Cdd:PRK00166   80 NKKKDTLDPILEAPDRDELLDWLRHQPLLHVDEELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 160 PRLL---LDTDEQSRFntIVNVFTRMRFLTSQWHLDFDNKGTLDDAGE-LRPWFTHPRFQSEANRYLFGHWAALQGITKV 235
Cdd:PRK00166  160 PDRWspdLTGLERLRY--IINAFTRMRFCTPDGRLDFKCKGPPDEAPAgLKPWFEVPGRKTRDYTIVFGHWAALEGLTTP 237

                         250       260
                  ....*....|....*....|....*...
gi 1538640045 236 PNVTALDTGCVWGGPMTLLDLDANEQIS 263
Cdd:PRK00166  238 PNIIALDTGCVWGGKLTALRLEDKQIFQ 265
 
Name Accession Description Interval E-value
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
1-263 2.89e-113

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 326.74  E-value: 2.89e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   1 MANYVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLIcNVLLG-KT 79
Cdd:PRK00166    1 MATYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLL-AVAAGiKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  80 PNPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKE 159
Cdd:PRK00166   80 NKKKDTLDPILEAPDRDELLDWLRHQPLLHVDEELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 160 PRLL---LDTDEQSRFntIVNVFTRMRFLTSQWHLDFDNKGTLDDAGE-LRPWFTHPRFQSEANRYLFGHWAALQGITKV 235
Cdd:PRK00166  160 PDRWspdLTGLERLRY--IINAFTRMRFCTPDGRLDFKCKGPPDEAPAgLKPWFEVPGRKTRDYTIVFGHWAALEGLTTP 237

                         250       260
                  ....*....|....*....|....*...
gi 1538640045 236 PNVTALDTGCVWGGPMTLLDLDANEQIS 263
Cdd:PRK00166  238 PNIIALDTGCVWGGKLTALRLEDKQIFQ 265
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 4-257 2.45e-99

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: 290.60  E-value: 2.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   4 YVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLICNVLLGKTPNPK 83
Cdd:cd07422     2 YAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLAVAAGIKKLKKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  84 DKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKEP-RL 162
Cdd:cd07422    82 DTLDEILEAPDRDELLDWLRHQPLLHRDDELGIVMVHAGIPPQWDIEKALALAREVEAVLRGDNYRDFLANMYGNEPdRW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 163 LLDTDEQSRFNTIVNVFTRMRFLTSQWHLDFDNKGTLDDAGE-LRPWFTHPRFQSEANRYLFGHWAALQGITKVPNVTAL 241
Cdd:cd07422   162 SDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAgLRPWFDVPNRKTRDYTIVFGHWAALGGLTRPNNIIAL 241

                         250
                  ....*....|....*.
gi 1538640045 242 DTGCVWGGPMTLLDLD 257
Cdd:cd07422   242 DTGCVWGGKLTALRLE 257
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 1-254 8.89e-74

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: 226.69  E-value: 8.89e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   1 MANYVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLICNVLLGKTP 80
Cdd:TIGR00668   1 MATYLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  81 NPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKEP 160
Cdd:TIGR00668  81 KPKDRLDPLLEAPDADELLNWLRRQPLLQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 161 -RLLLDTDEQSRFNTIVNVFTRMRFLTSQWHLDFDNKGTLDDA-GELRPWFTHPRFQSEANRYLFGHWAALQGITKVPNV 238
Cdd:TIGR00668 161 nRWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDApAPLKPWFAIPGPVYEEYSIAFGHWASLEGEGTPEGI 240

                         250
                  ....*....|....*.
gi 1538640045 239 TALDTGCVWGGPMTLL 254
Cdd:TIGR00668 241 YALDTGCCWGGRLTCL 256
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
 102-263 4.72e-39

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


Pssm-ID: 440404  Cd Length: 182  Bit Score: 134.25  E-value: 4.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 102 LRRQPLCVYLDNYRTFI-SHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKEP-----------RLlldtdeq 169
Cdd:COG0639    13 LLRRLLLLLHDLHLLAHaGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYNKPdrwsddlqgldRL------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 170 sRFntIVNVFTRMRFLTSQWHLDFDNKGTLDDA-GELRPWFTHPRFQSEANRYLFGHWAALQGITKVPNVTALDTGCVWG 248
Cdd:COG0639    86 -RF--IINAFTRMRFCTPDGRLDFKCKEPPETApPGLKPWFDVPGRRTADYTIVFGHWAALEGLGTPPNIYALDTGCVWG 162

                         170
                  ....*....|....*
gi 1538640045 249 GPMTLLDLDANEQIS 263
Cdd:COG0639   163 GKLTALRWEDKQRFQ 177
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 5-69 6.81e-08

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: 49.90  E-value: 6.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538640045   5 VVGDLQ--GCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDC--VTITLGNHDLH 69
Cdd:pfam00149   5 VIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYvpVYLVRGNHDFD 73
 
Name Accession Description Interval E-value
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
1-263 2.89e-113

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 326.74  E-value: 2.89e-113
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   1 MANYVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLIcNVLLG-KT 79
Cdd:PRK00166    1 MATYAIGDIQGCYDELQRLLEKIDFDPAKDTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLL-AVAAGiKR 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  80 PNPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKE 159
Cdd:PRK00166   80 NKKKDTLDPILEAPDRDELLDWLRHQPLLHVDEELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNE 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 160 PRLL---LDTDEQSRFntIVNVFTRMRFLTSQWHLDFDNKGTLDDAGE-LRPWFTHPRFQSEANRYLFGHWAALQGITKV 235
Cdd:PRK00166  160 PDRWspdLTGLERLRY--IINAFTRMRFCTPDGRLDFKCKGPPDEAPAgLKPWFEVPGRKTRDYTIVFGHWAALEGLTTP 237

                         250       260
                  ....*....|....*....|....*...
gi 1538640045 236 PNVTALDTGCVWGGPMTLLDLDANEQIS 263
Cdd:PRK00166  238 PNIIALDTGCVWGGKLTALRLEDKQIFQ 265
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 4-257 2.45e-99

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: 290.60  E-value: 2.45e-99
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   4 YVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLICNVLLGKTPNPK 83
Cdd:cd07422     2 YAIGDIQGCYDELQRLLEKINFDPAKDRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLAVAAGIKKLKKK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  84 DKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKEP-RL 162
Cdd:cd07422    82 DTLDEILEAPDRDELLDWLRHQPLLHRDDELGIVMVHAGIPPQWDIEKALALAREVEAVLRGDNYRDFLANMYGNEPdRW 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 163 LLDTDEQSRFNTIVNVFTRMRFLTSQWHLDFDNKGTLDDAGE-LRPWFTHPRFQSEANRYLFGHWAALQGITKVPNVTAL 241
Cdd:cd07422   162 SDDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAgLRPWFDVPNRKTRDYTIVFGHWAALGGLTRPNNIIAL 241

                         250
                  ....*....|....*.
gi 1538640045 242 DTGCVWGGPMTLLDLD 257
Cdd:cd07422   242 DTGCVWGGKLTALRLE 257
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 1-254 8.89e-74

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: 226.69  E-value: 8.89e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   1 MANYVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDCVTITLGNHDLHLICNVLLGKTP 80
Cdd:TIGR00668   1 MATYLIGDLHGCYDELQALLERVEFDPGQDTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRN 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  81 NPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKEP 160
Cdd:TIGR00668  81 KPKDRLDPLLEAPDADELLNWLRRQPLLQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 161 -RLLLDTDEQSRFNTIVNVFTRMRFLTSQWHLDFDNKGTLDDA-GELRPWFTHPRFQSEANRYLFGHWAALQGITKVPNV 238
Cdd:TIGR00668 161 nRWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDApAPLKPWFAIPGPVYEEYSIAFGHWASLEGEGTPEGI 240

                         250
                  ....*....|....*.
gi 1538640045 239 TALDTGCVWGGPMTLL 254
Cdd:TIGR00668 241 YALDTGCCWGGRLTCL 256
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
 102-263 4.72e-39

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


Pssm-ID: 440404  Cd Length: 182  Bit Score: 134.25  E-value: 4.72e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 102 LRRQPLCVYLDNYRTFI-SHAGIHPDWEIEQALSLGRWAQQKYQGDEASQFLPAMYGKEP-----------RLlldtdeq 169
Cdd:COG0639    13 LLRRLLLLLHDLHLLAHaGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYNKPdrwsddlqgldRL------- 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045 170 sRFntIVNVFTRMRFLTSQWHLDFDNKGTLDDA-GELRPWFTHPRFQSEANRYLFGHWAALQGITKVPNVTALDTGCVWG 248
Cdd:COG0639    86 -RF--IINAFTRMRFCTPDGRLDFKCKEPPETApPGLKPWFDVPGRRTADYTIVFGHWAALEGLGTPPNIYALDTGCVWG 162

                         170
                  ....*....|....*
gi 1538640045 249 GPMTLLDLDANEQIS 263
Cdd:COG0639   163 GKLTALRWEDKQRFQ 177
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 4-147 5.62e-21

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: 88.20  E-value: 5.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   4 YVVGDLQGCFAPLKQLLQEVAFNPaRDHLYLVGDIVARGPDSLGCLDFVFRHQDC----VTITLGNHDLHLIcNVLLGKT 79
Cdd:cd00144     1 IVVGDIHGCFDDLLRLLEKLGFPP-EDKYLFLGDYVDRGPDSVEVIDLLLALKILypdnVFLLRGNHEFMLL-NFLYGFY 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538640045  80 PNPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNyRTFISHAGIHPDWEIEQALSLGRWAQQKYQGDE 147
Cdd:cd00144    79 DERTLRCLRKGGEELWREFNEVFNYLPLAALVDG-KILCVHGGLSPDLTLLDQIRNIRPIENPDDQLV 145
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 4-71 2.27e-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: 66.96  E-value: 2.27e-13
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1538640045   4 YVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQdcVTITLGNHDLHLI 71
Cdd:cd07424     4 FVVGDIHGHFQRLQRALDAVGFDPARDRLISVGDLVDRGPESLEVLELLKQPW--FHAVQGNHEQMAI 69
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 5-123 3.21e-11

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: 61.38  E-value: 3.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   5 VVGDLQGCFAPLKQLLQEVAFNPARDHLY---------LVGDIVARGPDSLGCLDFVFRHQD-----CVTitlGNHDlHL 70
Cdd:cd07423     2 IIGDVHGCYDELVELLEKLGYQKKEEGLYvhpegrklvFLGDLVDRGPDSIDVLRLVMNMVKagkalYVP---GNHC-NK 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1538640045  71 ICNVLLGKTPNPKDKLDA-LYQHPQLPN---------YLAFLRRQPLCVYLDNYRTFISHAGI 123
Cdd:cd07423    78 LYRYLKGRNVQLAHGLETtVEELEALSKeerpefrerFAEFLESLPSHLVLDGGRLVVAHAGI 140
pphA PRK11439
protein-serine/threonine phosphatase;
4-67 4.55e-11

protein-serine/threonine phosphatase;


Pssm-ID: 236911 [Multi-domain]  Cd Length: 218  Bit Score: 60.93  E-value: 4.55e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538640045   4 YVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVfrHQDCVTITLGNHD 67
Cdd:PRK11439   20 WLVGDIHGCFEQLMRKLRHCRFDPWRDLLISVGDLIDRGPQSLRCLQLL--EEHWVRAVRGNHE 81
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 1-126 3.37e-08

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 52.78  E-value: 3.37e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   1 MANYVVGDLQGCFAPLKQLLQEVAFN--------PARDHLYLVGDIVARGPDSLGCLDFVFR--HQDCVTITLGNHdlhl 70
Cdd:PRK13625    1 MKYDIIGDIHGCYQEFQALTEKLGYNwssglpvhPDQRKLAFVGDLTDRGPHSLRMIEIVWElvEKKAAYYVPGNH---- 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045  71 iCNVL----LGKTPNPKDKLD-ALYQHPQLP-NYLAFLRRQ--------PLCVYLDNYRTFISHAGIHPD 126
Cdd:PRK13625   77 -CNKLyrffLGRNVTIAHGLEtTVAEYEALPsHKQNMIKEKfitlyeqaPLYHILDEGRLVVAHAGIRQD 145
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 5-69 6.81e-08

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: 49.90  E-value: 6.81e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1538640045   5 VVGDLQ--GCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDC--VTITLGNHDLH 69
Cdd:pfam00149   5 VIGDLHlpGQLDDLLELLKKLLEEGKPDLVLHAGDLVDRGPPSEEVLELLERLIKYvpVYLVRGNHDFD 73
PRK09968 PRK09968
protein-serine/threonine phosphatase;
4-67 6.57e-06

protein-serine/threonine phosphatase;


Pssm-ID: 182173  Cd Length: 218  Bit Score: 46.04  E-value: 6.57e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1538640045   4 YVVGDLQGCFAPLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVfrHQDCVTITLGNHD 67
Cdd:PRK09968   18 WVVGDIHGEYQLLQSRLHQLSFCPETDLLISVGDNIDRGPESLNVLRLL--NQPWFISVKGNHE 79
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
5-71 3.05e-05

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 43.37  E-value: 3.05e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538640045   5 VVGDLQGCFAPLKQLLQEVAFNPArDHLYLVGDIVARGPDSLGCLDFVFRHqdCVTITLGNHDLHLI 71
Cdd:COG0622     4 VISDTHGNLPALEAVLEDLEREGV-DLIVHLGDLVGYGPDPPEVLDLLREL--PIVAVRGNHDGAVL 67
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 5-70 3.81e-04

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


Pssm-ID: 277317 [Multi-domain]  Cd Length: 130  Bit Score: 39.56  E-value: 3.81e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   5 VVGDLQGCF-APLKQLLQEVAFNPARDHLYLVGDIVARGPDSLGCLDFVFRHQDC---VTITLGNHDLHL 70
Cdd:cd00838     2 VISDIHGNLeALEAVLEAALAKAEKPDLVICLGDLVDYGPDPEEVELKALRLLLAgipVYVVPGNHDILV 71
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 4-127 5.42e-03

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: 37.28  E-value: 5.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1538640045   4 YVVGDLQGCFAPLKQLLQ---------EVAFNpaRDHLYLVGDIVARGPDSLGCLDFVFRHQ-------DCVTITLGNHD 67
Cdd:cd07425     1 VAIGDLHGDLDRLRTILKlagvidsndRWIGG--DTVVVQTGDILDRGDDEIEILKLLEKLKrqarkagGKVILLLGNHE 78

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1538640045  68 LhlicNVLLGKTPNPKDKLDALYQHPQLPNYLAFLRRQPLCVYLDNYRTFI-------SHAGIHPDW 127
Cdd:cd07425    79 L----MNLCGDFRYVHPRGLNEFGGVAKRRYALLSDGGYIGRYLRTHPVVLvvndilfVHGGLGPLW 141
 
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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