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Conserved domains on  [gi|636795189|dbj|BAO87214|]
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Bis(5'-nucleosyl)-tetraphosphatase, symmetrical [Burkholderia sp. RPE67]

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;
14-284 1.29e-157

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


:

Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 439.60  E-value: 1.29e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  14 APLVFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPK 92
Cdd:PRK00166   2 ATYAIGDIQGCYDELQRLLEKIDFDPAKdTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLLAVAAGIKRNK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  93 KGDTLDDILNAPDAADLIEWVRHKPVAHF--ENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPH 170
Cdd:PRK00166  82 KKDTLDPILEAPDRDELLDWLRHQPLLHVdeELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNEPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 171 RWEDTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVL 249
Cdd:PRK00166 162 RWSPDLTGLERLRYIINAFTRMRFCTPDGRLDFKCKGPPDEAPAGLKPWFEVPGRKTRDYTIVFGHWAALeGLTTPPNII 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 636795189 250 CLDSGCVWGNKLSAVRMtadpAQRVLTQVNCSMKK 284
Cdd:PRK00166 242 ALDTGCVWGGKLTALRL----EDKQIFQVPCLKAK 272
 
Name Accession Description Interval E-value
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
14-284 1.29e-157

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 439.60  E-value: 1.29e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  14 APLVFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPK 92
Cdd:PRK00166   2 ATYAIGDIQGCYDELQRLLEKIDFDPAKdTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLLAVAAGIKRNK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  93 KGDTLDDILNAPDAADLIEWVRHKPVAHF--ENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPH 170
Cdd:PRK00166  82 KKDTLDPILEAPDRDELLDWLRHQPLLHVdeELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNEPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 171 RWEDTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVL 249
Cdd:PRK00166 162 RWSPDLTGLERLRYIINAFTRMRFCTPDGRLDFKCKGPPDEAPAGLKPWFEVPGRKTRDYTIVFGHWAALeGLTTPPNII 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 636795189 250 CLDSGCVWGNKLSAVRMtadpAQRVLTQVNCSMKK 284
Cdd:PRK00166 242 ALDTGCVWGGKLTALRL----EDKQIFQVPCLKAK 272
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 17-266 4.03e-148

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: 415.02  E-value: 4.03e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  17 VFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPKKGD 95
Cdd:cd07422    3 AIGDIQGCYDELQRLLEKINFDPAKdRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLAVAAGIKKLKKKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  96 TLDDILNAPDAADLIEWVRHKPVAHFE--NGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPHRWE 173
Cdd:cd07422   83 TLDEILEAPDRDELLDWLRHQPLLHRDdeLGIVMVHAGIPPQWDIEKALALAREVEAVLRGDNYRDFLANMYGNEPDRWS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 174 DTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAALGLMIRDD-VLCLD 252
Cdd:cd07422  163 DDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAGLRPWFDVPNRKTRDYTIVFGHWAALGGLTRPNnIIALD 242

                        250
                 ....*....|....
gi 636795189 253 SGCVWGNKLSAVRM 266
Cdd:cd07422  243 TGCVWGGKLTALRL 256
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 14-265 5.49e-78

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: 237.86  E-value: 5.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189   14 APLVFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPK 92
Cdd:TIGR00668   2 ATYLIGDLHGCYDELQALLERVEFDPGQdTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189   93 KGDTLDDILNAPDAADLIEWVRHKP--VAHFENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPH 170
Cdd:TIGR00668  82 PKDRLDPLLEAPDADELLNWLRRQPllQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  171 RWEDTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVL 249
Cdd:TIGR00668 162 RWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDAPAPLKPWFAIPGPVYEEYSIAFGHWASLeGEGTPEGIY 241

                         250
                  ....*....|....*.
gi 636795189  250 CLDSGCVWGNKLSAVR 265
Cdd:TIGR00668 242 ALDTGCCWGGRLTCLR 257
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
 103-280 3.58e-72

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


Pssm-ID: 440404  Cd Length: 182  Bit Score: 219.76  E-value: 3.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 103 APDAADLIEWVRHKPVAH---FENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPHRWEDTLTGI 179
Cdd:COG0639    3 DLLRLDLLLLLLRRLLLLlhdLHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYNKPDRWSDDLQGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 180 DRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVLCLDSGCVWG 258
Cdd:COG0639   83 DRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAPPGLKPWFDVPGRRTADYTIVFGHWAALeGLGTPPNIYALDTGCVWG 162

                        170       180
                 ....*....|....*....|..
gi 636795189 259 NKLSAVRMTadpaQRVLTQVNC 280
Cdd:COG0639  163 GKLTALRWE----DKQRFQVPC 180
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-110 1.53e-07

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: 49.13  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189   16 LVFGDLQ--GCCDPFERLLKKAAPDPTTPLW-FAGDLINRGPKSLQTLREVIALGSRATV--VLGNHDLNLLSVAAGL-- 88
Cdd:pfam00149   4 LVIGDLHlpGQLDDLLELLKKLLEEGKPDLVlHAGDLVDRGPPSEEVLELLERLIKYVPVylVRGNHDFDYGECLRLYpy 83

                          90       100
                  ....*....|....*....|....
gi 636795189   89 --RKPKKGDTLDDILNAPDAADLI 110
Cdd:pfam00149  84 lgLLARPWKRFLEVFNFLPLAGIL 107
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 13-60 1.82e-03

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: 39.12  E-value: 1.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 636795189    13 SAPL-VFGDLQGCCDPFERLLKKAAPDPTTPLWFAGDLINRGPKSLQTL 60
Cdd:smart00156  27 SAPVtVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVI 75
 
Name Accession Description Interval E-value
apaH PRK00166
symmetrical bis(5'-nucleosyl)-tetraphosphatase;
14-284 1.29e-157

symmetrical bis(5'-nucleosyl)-tetraphosphatase;


Pssm-ID: 234673 [Multi-domain]  Cd Length: 275  Bit Score: 439.60  E-value: 1.29e-157
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  14 APLVFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPK 92
Cdd:PRK00166   2 ATYAIGDIQGCYDELQRLLEKIDFDPAKdTLWLVGDLVNRGPDSLEVLRFVKSLGDSAVTVLGNHDLHLLAVAAGIKRNK 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  93 KGDTLDDILNAPDAADLIEWVRHKPVAHF--ENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPH 170
Cdd:PRK00166  82 KKDTLDPILEAPDRDELLDWLRHQPLLHVdeELGLVMVHAGIPPQWDLATALALAREVEAVLRSDDYRDFLANMYGNEPD 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 171 RWEDTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVL 249
Cdd:PRK00166 162 RWSPDLTGLERLRYIINAFTRMRFCTPDGRLDFKCKGPPDEAPAGLKPWFEVPGRKTRDYTIVFGHWAALeGLTTPPNII 241

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 636795189 250 CLDSGCVWGNKLSAVRMtadpAQRVLTQVNCSMKK 284
Cdd:PRK00166 242 ALDTGCVWGGKLTALRL----EDKQIFQVPCLKAK 272
MPP_ApaH cd07422
Escherichia coli ApaH and related proteins, metallophosphatase domain; ApaH (also known as ...
 17-266 4.03e-148

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: 415.02  E-value: 4.03e-148
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  17 VFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPKKGD 95
Cdd:cd07422    3 AIGDIQGCYDELQRLLEKINFDPAKdRLWLVGDLVNRGPDSLETLRFVKSLGDSAVVVLGNHDLHLLAVAAGIKKLKKKD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  96 TLDDILNAPDAADLIEWVRHKPVAHFE--NGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPHRWE 173
Cdd:cd07422   83 TLDEILEAPDRDELLDWLRHQPLLHRDdeLGIVMVHAGIPPQWDIEKALALAREVEAVLRGDNYRDFLANMYGNEPDRWS 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 174 DTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAALGLMIRDD-VLCLD 252
Cdd:cd07422  163 DDLEGIDRLRYIINAFTRMRFCTPDGRLDFKCKGSPEEAPAGLRPWFDVPNRKTRDYTIVFGHWAALGGLTRPNnIIALD 242

                        250
                 ....*....|....
gi 636795189 253 SGCVWGNKLSAVRM 266
Cdd:cd07422  243 TGCVWGGKLTALRL 256
apaH TIGR00668
bis(5'-nucleosyl)-tetraphosphatase (symmetrical); Diadenosine 5',5"'-P1,P4-tetraphosphate ...
 14-265 5.49e-78

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: 237.86  E-value: 5.49e-78
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189   14 APLVFGDLQGCCDPFERLLKKAAPDPTT-PLWFAGDLINRGPKSLQTLREVIALGSRATVVLGNHDLNLLSVAAGLRKPK 92
Cdd:TIGR00668   2 ATYLIGDLHGCYDELQALLERVEFDPGQdTLWLTGDLVARGPGSLEVLRYVKSLGDAVRLVLGNHDLHLLAVFAGISRNK 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189   93 KGDTLDDILNAPDAADLIEWVRHKP--VAHFENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPH 170
Cdd:TIGR00668  82 PKDRLDPLLEAPDADELLNWLRRQPllQHDEEKKLVMAHAGITPQWDLQTAKECARDVEAVLSSDSYPFFLDAMYGDMPN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  171 RWEDTLTGIDRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVL 249
Cdd:TIGR00668 162 RWSPELQGLARLRFIINAFTRMRFCFPNGQLDMYSKESPEDAPAPLKPWFAIPGPVYEEYSIAFGHWASLeGEGTPEGIY 241

                         250
                  ....*....|....*.
gi 636795189  250 CLDSGCVWGNKLSAVR 265
Cdd:TIGR00668 242 ALDTGCCWGGRLTCLR 257
ApaH COG0639
Diadenosine tetraphosphatase ApaH/serine/threonine protein phosphatase, PP2A family [Signal ...
 103-280 3.58e-72

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


Pssm-ID: 440404  Cd Length: 182  Bit Score: 219.76  E-value: 3.58e-72
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 103 APDAADLIEWVRHKPVAH---FENGILMVHAGVVPQWDATMTMELAHELEQALRGPNWKETLASLYGNEPHRWEDTLTGI 179
Cdd:COG0639    3 DLLRLDLLLLLLRRLLLLlhdLHLLAHAGHAGQWPLWDALTALLEAEDVERLLNWLRLLPLLYGMYYNKPDRWSDDLQGL 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 180 DRLRVIYNALTRIRFCTREGAMEFANNGGPDAAPPGYMPWFDVPERRTRDVTIVFGHWAAL-GLMIRDDVLCLDSGCVWG 258
Cdd:COG0639   83 DRLRFIINAFTRMRFCTPDGRLDFKCKEPPETAPPGLKPWFDVPGRRTADYTIVFGHWAALeGLGTPPNIYALDTGCVWG 162

                        170       180
                 ....*....|....*....|..
gi 636795189 259 NKLSAVRMTadpaQRVLTQVNC 280
Cdd:COG0639  163 GKLTALRWE----DKQRFQVPC 180
MPP_PPP_family cd00144
phosphoprotein phosphatases of the metallophosphatase superfamily, metallophosphatase domain; ...
 17-266 4.43e-23

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: 94.36  E-value: 4.43e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  17 VFGDLQGCCDPFERLLKKAAPDPTTPLWFAGDLINRGPKSLQTLREVIAL----GSRATVVLGNHDLNLLSVAAGLRKPK 92
Cdd:cd00144    2 VVGDIHGCFDDLLRLLEKLGFPPEDKYLFLGDYVDRGPDSVEVIDLLLALkilyPDNVFLLRGNHEFMLLNFLYGFYDER 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  93 KGDTLDDiLNAPDAADLIEWVRHKPV-AHFENGILMVHAGVVPQWdatmtmELAHELEQALRGPNWKETLAslygnephr 171
Cdd:cd00144   82 TLRCLRK-GGEELWREFNEVFNYLPLaALVDGKILCVHGGLSPDL------TLLDQIRNIRPIENPDDQLV--------- 145

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189 172 wedtltgidrlrviyNALTRIRFCTREGamEFANNGGPDAAPPGYmPWFDVPERRTRDVTIVFGHWAALGL---MIRDDV 248
Cdd:cd00144  146 ---------------EDLLWSDPDESVG--DFESSSRGGGYLFGE-DAVDEFLKKNGLKLIVRGHTPVEGGyefLHGGKL 207

                        250       260
                 ....*....|....*....|..
gi 636795189 249 LCLDSGCVW----GNKLSAVRM 266
Cdd:cd00144  208 ITIFSAPNYcgkgGNKLAALVV 229
MPP_PA3087 cd07413
Pseudomonas aeruginosa PA3087 and related proteins, metallophosphatase domain; PA3087 is an ...
 17-155 4.81e-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: 55.25  E-value: 4.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  17 VFGDLQGCCDPFERLLKKAAPDPTTPLW--------FAGDLINRGPKSLQTLREVIAL--GSRATVVLGNHDLNLL--SV 84
Cdd:cd07413    3 LIGDVHGCAHTLDRLLDLLGYRLQGGVWrhprrqalFVGDLIDRGPRIREVLHRVHAMvdAGEALCVMGNHEFNALawHT 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  85 AAGLRKPKKGD-------------TLDDiLNAPDAADLIEWVRHKPVAHFENGILMVHAGvvpqWDatmtmelahelEQA 151
Cdd:cd07413   83 PAPPGSGRQYVrehspknarqhkaTLDQ-FEGHDWRDFLGWFQTLPLFLDLGRFRVVHAC----WD-----------ERL 146


                 ....
gi 636795189 152 LRGP 155
Cdd:cd07413  147 LKGP 150
MPP_Prp_like cd07423
Bacillus subtilis PrpE and related proteins, metallophosphatase domain; PrpE (protein ...
 19-82 3.73e-08

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: 52.90  E-value: 3.73e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636795189  19 GDLQGCCDPFERLLKKA------APDPTTP----LWFAGDLINRGPKSLQTLREVIAL--GSRATVVLGNHDLNLL 82
Cdd:cd07423    4 GDVHGCYDELVELLEKLgyqkkeEGLYVHPegrkLVFLGDLVDRGPDSIDVLRLVMNMvkAGKALYVPGNHCNKLY 79
Metallophos pfam00149
Calcineurin-like phosphoesterase; This family includes a diverse range of phosphoesterases, ...
 16-110 1.53e-07

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: 49.13  E-value: 1.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189   16 LVFGDLQ--GCCDPFERLLKKAAPDPTTPLW-FAGDLINRGPKSLQTLREVIALGSRATV--VLGNHDLNLLSVAAGL-- 88
Cdd:pfam00149   4 LVIGDLHlpGQLDDLLELLKKLLEEGKPDLVlHAGDLVDRGPPSEEVLELLERLIKYVPVylVRGNHDFDYGECLRLYpy 83

                          90       100
                  ....*....|....*....|....
gi 636795189   89 --RKPKKGDTLDDILNAPDAADLI 110
Cdd:pfam00149  84 lgLLARPWKRFLEVFNFLPLAGIL 107
PRK13625 PRK13625
bis(5'-nucleosyl)-tetraphosphatase PrpE; Provisional
 17-77 2.67e-07

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


Pssm-ID: 184187 [Multi-domain]  Cd Length: 245  Bit Score: 50.47  E-value: 2.67e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 636795189  17 VFGDLQGCCDPFERLLKKAA----------PDPTTpLWFAGDLINRGPKSLQTLREVIALGSRATV--VLGNH 77
Cdd:PRK13625   5 IIGDIHGCYQEFQALTEKLGynwssglpvhPDQRK-LAFVGDLTDRGPHSLRMIEIVWELVEKKAAyyVPGNH 76
MPP_superfamily cd00838
metallophosphatase superfamily, metallophosphatase domain; Metallophosphatases (MPPs), also ...
 16-121 3.41e-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: 3.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  16 LVFGDLQGCCDPFERLLKKAAPDPTTP--LWFAGDLINRGPKSLQTLREVIALGSRAT---VVLGNHDLNLLSvaAGLRK 90
Cdd:cd00838    1 LVISDIHGNLEALEAVLEAALAKAEKPdlVICLGDLVDYGPDPEEVELKALRLLLAGIpvyVVPGNHDILVTH--GPPYD 78

                         90       100       110
                 ....*....|....*....|....*....|.
gi 636795189  91 PKKGDTLDDILNAPDAADLIEwvRHKPVAHF 121
Cdd:cd00838   79 PLDEGSPGEDPGSEALLELLD--KYGPDLVL 107
YfcE COG0622
Predicted phosphodiesterase, calcineurin family [General function prediction only];
16-128 2.88e-06

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


Pssm-ID: 440387 [Multi-domain]  Cd Length: 183  Bit Score: 46.83  E-value: 2.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  16 LVFGDLQGCCDPFERLLKKAAPDPTTPLWFAGDLINRGPKSLQTLREVIALGSRAtvVLGNHDLNLLSVAAGLrkPKK-- 93
Cdd:COG0622    3 AVISDTHGNLPALEAVLEDLEREGVDLIVHLGDLVGYGPDPPEVLDLLRELPIVA--VRGNHDGAVLRGLRSL--PETlr 78

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 636795189  94 ------------GDTLDDILNAPDAADLIEWVR------------HKPVAHFENGILMV 128
Cdd:COG0622   79 lelegvrillvhGSPNEYLLPDTPAERLRALAAegdadvvvcghtHIPFVRRVGGVLLV 137
MPP_PrpA_PrpB cd07424
PrpA and PrpB, metallophosphatase domain; PrpA and PrpB are bacterial type I serine/threonine ...
 16-130 7.38e-05

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


Pssm-ID: 277367 [Multi-domain]  Cd Length: 201  Bit Score: 42.69  E-value: 7.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  16 LVFGDLQGCCDPFERLLKKAAPDPTTPLWFA-GDLINRGPKSLQTLREVIALGSRAtvVLGNHDLNLLSVAAGLR----K 90
Cdd:cd07424    4 FVVGDIHGHFQRLQRALDAVGFDPARDRLISvGDLVDRGPESLEVLELLKQPWFHA--VQGNHEQMAIDALRGGDdvmwR 81

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 636795189  91 PKKGDTLDDiLNAPDAADLIEWVRHKPVA---HFENGIL-MVHA 130
Cdd:cd07424   82 ANGGGWFFD-LPDEEAKVLLEKLHHLPIAievESRNGKVgIVHA 124
MPP_Shelphs cd07425
Shewanella-like phosphatases, metallophosphatase domain; This family includes bacterial, ...
 16-149 5.86e-04

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: 39.97  E-value: 5.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636795189  16 LVFGDLQGCCDPFERLLKKAAPDPTTPLWFA--------GDLINRGPKSLQTL-------REVIALGSRATVVLGNHDLn 80
Cdd:cd07425    1 VAIGDLHGDLDRLRTILKLAGVIDSNDRWIGgdtvvvqtGDILDRGDDEIEILklleklkRQARKAGGKVILLLGNHEL- 79

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 636795189  81 lLSVAAGLRKPKKGD-----TLDDILNA--PDAADLIEWVRHKPVAHFENGILMVHAGVVPQWDATMTMELAHELE 149
Cdd:cd07425   80 -MNLCGDFRYVHPRGlnefgGVAKRRYAllSDGGYIGRYLRTHPVVLVVNDILFVHGGLGPLWSRGYSLETKNGAC 154
PP2Ac smart00156
Protein phosphatase 2A homologues, catalytic domain; Large family of serine/threonine ...
 13-60 1.82e-03

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: 39.12  E-value: 1.82e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 636795189    13 SAPL-VFGDLQGCCDPFERLLKKAAPDPTTPLWFAGDLINRGPKSLQTL 60
Cdd:smart00156  27 SAPVtVCGDIHGQFDDLLRLFDKNGQPPETNYVFLGDYVDRGPFSIEVI 75
COG2129 COG2129
Predicted phosphoesterase, related to the Icc protein [General function prediction only];
16-78 9.36e-03

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


Pssm-ID: 441732 [Multi-domain]  Cd Length: 211  Bit Score: 36.53  E-value: 9.36e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636795189  16 LVFGDLQGCCDPFERLLKKAAPDPTTPLWFAGDLINRGPksLQTLREVIALGSRATV----VLGNHD 78
Cdd:COG2129    3 LAVSDLHGNFDLLEKLLELARAEDADLVILAGDLTDFGT--AEEAREVLEELAALGVpvlaVPGNHD 67
 
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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