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Conserved domains on  [gi|1937369559|ref|NP_114446|]
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inositol monophosphatase 1 [Rattus norvegicus]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108155)

inositol monophosphatase family protein such as inositol monophosphatase, which catalyzes the hydrolysis of several inositol monophosphates and the artificial substrate p-nitrophenyl-phosphate to inorganic phosphate and inositol

CATH:  3.40.190.80
EC:  3.1.3.-
Gene Ontology:  GO:0008934|GO:0006020|GO:0046872
PubMed:  7890024

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-254 8.16e-124

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


:

Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 352.61  E-value: 8.16e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   8 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639     1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSS 166
Cdd:cd01639    78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 167 RkPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLM 246
Cdd:cd01639   158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236


                  ....*...
gi 1937369559 247 SRRIIAAS 254
Cdd:cd01639   237 SGNILAGN 244
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-254 8.16e-124

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 352.61  E-value: 8.16e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   8 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639     1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSS 166
Cdd:cd01639    78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 167 RkPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLM 246
Cdd:cd01639   158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236


                  ....*...
gi 1937369559 247 SRRIIAAS 254
Cdd:cd01639   237 SGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
5-271 2.56e-101

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 296.95  E-value: 2.56e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   5 WQECMDYAVI-LARQAGEMIREALKNKMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVF 81
Cdd:pfam00459   1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  82 TEQ-PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLV 160
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 161 TELGSSRKPETL-RIVLSNMERLcsIPIHGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDV 238
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKL--VRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369559 239 TGGPFDLMSRRIIAASNIALAERIAKELEIIPL 271
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
PLN02553 PLN02553
inositol-phosphate phosphatase
 3-270 2.94e-93

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 276.19  E-value: 2.94e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   3 DPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFT 82
Cdd:PLN02553    5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  83 EQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTE 162
Cdd:PLN02553   84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 163 LGSSRKPETLRIVLSNMERLCSiPIHGIRSVGTAAVNMCLVATGGADAYYEMGI-HCWDMAGAGIIVIEAGGVLLDVTGG 241
Cdd:PLN02553  164 VGTKRDKATVDATTNRINALLY-KVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGG 242

                         250       260
                  ....*....|....*....|....*....
gi 1937369559 242 PFDLMSRRiIAASNIALAERIAKELEIIP 270
Cdd:PLN02553  243 PFDIMSRR-VAASNGHLKDAFVEALRQTE 270
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 6-266 7.87e-81

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 243.98  E-value: 7.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   6 QECMDYAVILARQAGEMIREALKN-KMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQ 84
Cdd:COG0483     1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  85 PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELG 164
Cdd:COG0483    77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 165 SSRKPETLRIVLSNMERLCsipiHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD 244
Cdd:COG0483   157 YLRDDREYLAALAALLPRV----RRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232

                         250       260
                  ....*....|....*....|..
gi 1937369559 245 LMSRRIIAAsNIALAERIAKEL 266
Cdd:COG0483   233 LGSGSLVAA-NPALHDELLALL 253
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 12-267 1.66e-34

histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273949 [Multi-domain]  Cd Length: 251  Bit Score: 125.11  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  12 AVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDP 91
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  92 IDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPET 171
Cdd:TIGR02067  82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 172 LRIVLSNMERLCSipihgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFdLMSRRII 251
Cdd:TIGR02067 162 NRPAFERLRRAAR-----LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAV 235

                         250
                  ....*....|....*.
gi 1937369559 252 AASNIALAERIAKELE 267
Cdd:TIGR02067 236 AAGNAMLHDEALEILN 251
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-254 8.16e-124

IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.


Pssm-ID: 238817 [Multi-domain]  Cd Length: 244  Bit Score: 352.61  E-value: 8.16e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   8 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639     1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSS 166
Cdd:cd01639    78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 167 RkPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLM 246
Cdd:cd01639   158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236


                  ....*...
gi 1937369559 247 SRRIIAAS 254
Cdd:cd01639   237 SGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
5-271 2.56e-101

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 296.95  E-value: 2.56e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   5 WQECMDYAVI-LARQAGEMIREALKNKMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVF 81
Cdd:pfam00459   1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  82 TEQ-PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLV 160
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 161 TELGSSRKPETL-RIVLSNMERLcsIPIHGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDV 238
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKL--VRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1937369559 239 TGGPFDLMSRRIIAASNIALAERIAKELEIIPL 271
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
PLN02553 PLN02553
inositol-phosphate phosphatase
 3-270 2.94e-93

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 276.19  E-value: 2.94e-93
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   3 DPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFT 82
Cdd:PLN02553    5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  83 EQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTE 162
Cdd:PLN02553   84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 163 LGSSRKPETLRIVLSNMERLCSiPIHGIRSVGTAAVNMCLVATGGADAYYEMGI-HCWDMAGAGIIVIEAGGVLLDVTGG 241
Cdd:PLN02553  164 VGTKRDKATVDATTNRINALLY-KVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGG 242

                         250       260
                  ....*....|....*....|....*....
gi 1937369559 242 PFDLMSRRiIAASNIALAERIAKELEIIP 270
Cdd:PLN02553  243 PFDIMSRR-VAASNGHLKDAFVEALRQTE 270
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 6-266 7.87e-81

Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family [Carbohydrate transport and metabolism]; Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family is part of the Pathway/BioSystem: Gluconeogenesis


Pssm-ID: 440251 [Multi-domain]  Cd Length: 255  Bit Score: 243.98  E-value: 7.87e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   6 QECMDYAVILARQAGEMIREALKN-KMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQ 84
Cdd:COG0483     1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  85 PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELG 164
Cdd:COG0483    77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 165 SSRKPETLRIVLSNMERLCsipiHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD 244
Cdd:COG0483   157 YLRDDREYLAALAALLPRV----RRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232

                         250       260
                  ....*....|....*....|..
gi 1937369559 245 LMSRRIIAAsNIALAERIAKEL 266
Cdd:COG0483   233 LGSGSLVAA-NPALHDELLALL 253
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 9-253 1.93e-79

Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.


Pssm-ID: 238815 [Multi-domain]  Cd Length: 238  Bit Score: 239.91  E-value: 1.93e-79
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   9 MDYAVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaAGEKTVFTEQPTWI 88
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  89 IDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRK 168
Cdd:cd01637    79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 169 PEtlrivLSNMERLCsIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD-LMS 247
Cdd:cd01637   159 NR-----AAVLASLV-NRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtLNR 232


                  ....*.
gi 1937369559 248 RRIIAA 253
Cdd:cd01637   233 SGIIAA 238
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 9-238 7.80e-50

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


Pssm-ID: 238814 [Multi-domain]  Cd Length: 184  Bit Score: 162.56  E-value: 7.80e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   9 MDYAVILARQAGEMIREALKNK--MDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPT 86
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFGRElsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  87 WIIDPIDGTTNFVHRFPFVAVSIGfvvnkemefgvVYSCvedkmytgrkgkgafcngqklrvsqqeditksLLVTELGSS 166
Cdd:cd01636    81 WVIDPIDGTKNFINGLPFVAVVIA-----------VYVI--------------------------------LILAEPSHK 117

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1937369559 167 RKPEtlrivlsNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGI--HCWDMAGAGIIVIEAGGVLLDV 238
Cdd:cd01636   118 RVDE-------KKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTDW 184
PLN02737 PLN02737
inositol monophosphatase family protein
 13-262 7.07e-47

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 160.35  E-value: 7.07e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  13 VILARQAG-EMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPTWIIDP 91
Cdd:PLN02737   83 AELAAKTGaEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS---SDYLWCIDP 158

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  92 IDGTTNFVHRFPFVAVSIGFVVNKE------MEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGS 165
Cdd:PLN02737  159 LDGTTNFAHGYPSFAVSVGVLFRGTpaaatvVEFVGGPMCWNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGY 238

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 166 SR-KPETLRIVL----SNMERlcsipihGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTG 240
Cdd:PLN02737  239 EHdDAWATNIELfkefTDVSR-------GVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDG 311

                         250       260
                  ....*....|....*....|..
gi 1937369559 241 GPFDLMSRRIIaASNIALAERI 262
Cdd:PLN02737  312 GKFSVFDRSVL-VSNGVLHPKL 332
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 15-259 9.95e-47

Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate inositol monophosphate or similar substrates.


Pssm-ID: 238821 [Multi-domain]  Cd Length: 242  Bit Score: 156.34  E-value: 9.95e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  15 LARQAGEMIREALKNKMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaaGEKTVFTEQPTWIIDPIDG 94
Cdd:cd01643     7 IAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVIDPIDG 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  95 TTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDItKSLLVTELGSSRKPETLRI 174
Cdd:cd01643    82 TTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQL-PDCNVGFNRSSRASARAVL 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 175 VLSNMERLCSipihgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIAAS 254
Cdd:cd01643   161 RVILRRFPGK-----IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYLSAG 235


                  ....*
gi 1937369559 255 NIALA 259
Cdd:cd01643   236 FPTLI 240
PRK10757 PRK10757
inositol-1-monophosphatase;
12-254 1.11e-44

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 151.88  E-value: 1.11e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  12 AVILARQAGEMIREALKNKMDVMI-KSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQPTWIID 90
Cdd:PRK10757    8 AVRAARKAGNLIAKNYETPDAVEAsQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVID 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  91 PIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPE 170
Cdd:PRK10757   85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQH 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 171 T---LRIVlSNMERLCSipihGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 247
Cdd:PRK10757  165 AttyINIV-GKLFTECA----DFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLT 239


                  ....*..
gi 1937369559 248 RRIIAAS 254
Cdd:PRK10757  240 GNIVAGN 246
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 15-255 5.32e-43

3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 147.23  E-value: 5.32e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  15 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 92
Cdd:COG1218    11 IAREAGEAILEIYRADFEVEEKAddSP---VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  93 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFC-----NGQKLRVSQQEDITKSLLVTelgsSR 167
Cdd:COG1218    88 DGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPLRVVA----SR 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 168 ---KPETLRIvlsnMERLcsiPIHGIRSVGtAAVNMCLVATGGADAYYEMGIHC-WDMAGAGIIVIEAGGVLLDVTGGPF 243
Cdd:COG1218   164 shrDEETEAL----LARL---GVAELVSVG-SSLKFCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRVTDLDGKPL 235

                         250
                  ....*....|....*...
gi 1937369559 244 ------DLMSRRIIAASN 255
Cdd:COG1218   236 rynkkeDLLNPGFIASGD 253
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 9-263 9.30e-36

Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol monophosphatases. These enzymes may dephosphorylate fructose-1,6-bisphosphate, inositol monophospate, 3'-phosphoadenosine-5'-phosphate, or similar substrates.


Pssm-ID: 238819 [Multi-domain]  Cd Length: 248  Bit Score: 128.14  E-value: 9.30e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   9 MDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTeqptWI 88
Cdd:cd01641     2 LAFALELADAAGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV----WV 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  89 IDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCN---GQKLRVSQQEDITKSLLVTElgs 165
Cdd:cd01641    77 LDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTT--- 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 166 srKPETLRIVLSN-MERLCSipIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD 244
Cdd:cd01641   154 --DPHFFTPGDRAaFERLAR--AVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLT 229

                         250
                  ....*....|....*....
gi 1937369559 245 LMSRRIIAASNIALAERIA 263
Cdd:cd01641   230 GGSGRVVAAGDAELHEALL 248
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 10-243 3.01e-35

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 126.57  E-value: 3.01e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  10 DYAVILARQAGEMIREALKNKMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEktVFTEQPTWII 89
Cdd:cd01638     3 ELLIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFWLV 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  90 DPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGS--SR 167
Cdd:cd01638    80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASrsHP 159

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369559 168 KPETLRIVLsnmerlcSIPIHGIRSVGTAAvNMCLVATGGADAYYEMGIHC-WDMAgAGIIVI-EAGGVLLDVTGGPF 243
Cdd:cd01638   160 DEELEALLA-------ALGVAEVVSIGSSL-KFCLVAEGEADIYPRLGPTMeWDTA-AGDAVLrAAGGAVSDLDGSPL 228
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 12-267 1.66e-34

histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]


Pssm-ID: 273949 [Multi-domain]  Cd Length: 251  Bit Score: 125.11  E-value: 1.66e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  12 AVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDP 91
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  92 IDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPET 171
Cdd:TIGR02067  82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 172 LRIVLSNMERLCSipihgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFdLMSRRII 251
Cdd:TIGR02067 162 NRPAFERLRRAAR-----LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAV 235

                         250
                  ....*....|....*.
gi 1937369559 252 AASNIALAERIAKELE 267
Cdd:TIGR02067 236 AAGNAMLHDEALEILN 251
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 15-244 2.34e-33

3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]


Pssm-ID: 130398 [Multi-domain]  Cd Length: 249  Bit Score: 121.79  E-value: 2.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  15 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 92
Cdd:TIGR01331   8 IARAAGEEILPVYQKELAVAQKAdnSP---VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  93 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAF--CNGQKLR--VSQQEDITKSLLVTELGSSRK 168
Cdd:TIGR01331  85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQALKapIHVRPWPSGPLLVVISRSHAE 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1937369559 169 PETLRIvLSNMERLCSIPihgirsvGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFD 244
Cdd:TIGR01331 165 EKTTEY-LANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-254 8.53e-29

PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 110.48  E-value: 8.53e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559   9 MDYAVILARQAGEMIREALKNKM--DVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAgektvftEQPT 86
Cdd:cd01517     2 LEVAILAVRAAASLTLPVFRNLGagDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGRF 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  87 WIIDPIDGTTNFVHRFPFvAVSIGFVVNKEMEFGVVYSCV-------EDKMYTGRKGKGAFC---NGQKLRVSQQEDITK 156
Cdd:cd01517    75 WVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAWLrplDGSSLQPLSVRQLTN 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 157 SLLVTELGSSRKPETLRIVLSNMERLCSIPihgirsvgtAAVNM------CLVATGGADAY--------YEMGIhcWDMA 222
Cdd:cd01517   154 AARASFCESVESAHSSHRLQAAIKALGGTP---------QPVRLdsqakyAAVARGAADFYlrlplsmsYREKI--WDHA 222

                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1937369559 223 GAGIIVIEAGGVLLDVTGGPFD-------LMSRRIIAAS 254
Cdd:cd01517   223 AGVLIVEEAGGKVTDADGKPLDfgkgrklLNNGGLIAAP 261
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
47-267 5.57e-27

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 105.37  E-value: 5.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  47 DQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCV 126
Cdd:PRK12676   47 DKVAEDIILEVLKPLGRCVNIISEE---LGEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLA 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 127 EDKMYTGRKGKGAFCNGQKLRVSQQEDItKSLLVTELGSSRKPETLRIVLSNMERlcsipihgIRSVGTAAVNMCLVATG 206
Cdd:PRK12676  124 TGDFYEAIPGKGAYLNGKPIKVSKTSEL-NESAVSIYGYRRGKERTVKLGRKVRR--------VRILGAIALELCYVASG 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1937369559 207 GADAYYEMG--IHCWDMAGAGIIVIEAGGVLLDVTGGPFDL-----MSRRIIAASNIALAERIAKELE 267
Cdd:PRK12676  195 RLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvtERTNLIAANGEELHKKILELLE 262
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 19-262 4.43e-26

Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.


Pssm-ID: 238773 [Multi-domain]  Cd Length: 257  Bit Score: 102.84  E-value: 4.43e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  19 AGEMIREALKNKMDVM--------IKSSP-ADLVTVTDQKVEKMLMSSIKEKYPYhSFIGEESvaaGEKtVFTEQPTW-- 87
Cdd:cd01515     5 ARNIAKEIEKAIKPLFgtedasevVKIGAdGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEI---GVI-DNGDEPEYtv 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  88 IIDPIDGTTNFVHRFPFVAVSIGFVVNKE--MEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDItKSLLVTELGS 165
Cdd:cd01515    80 VLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSL-KSISVSYYIY 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 166 SRKPETLRIVLSNMERlcsipihgIRSVGTAAVNMCLVATGGADAYYEM--GIHCWDMAGAGIIVIEAGGVLLDVTGGP- 242
Cdd:cd01515   159 GKNHDRTFKICRKVRR--------VRIFGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKEl 230

                         250       260
                  ....*....|....*....|...
gi 1937369559 243 ---FDLMSRRIIAASNIALAERI 262
Cdd:cd01515   231 klkLNVTERVNIIAANSELHKKL 253
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
51-255 1.43e-20

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 90.94  E-value: 1.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  51 EKMLMSSIkEKYPYHSFIGEEsvaAGEKTVFTEQPTWI--IDPIDGTTNFVHRFPFVAVSIG-------------FVVN- 114
Cdd:PRK14076   50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIAiakidgfdkkikeFIGKn 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 115 ---KEMEFGVVYSCVEDKMYTGRKGKGAF----CNGQKLRVSQQEDITK-SLLVTELGSSRkpETLRIVLSNMERLcsip 186
Cdd:PRK14076  126 ltiNDLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDaSIGLFAYGLSL--DTLKFIKDRKVRR---- 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1937369559 187 ihgIRSVGTAAVNMCLVATGGADAYYEM--GIHCWDMAGAGIIVIEAGGVLLDVTGGP----FDLMSRRIIAASN 255
Cdd:PRK14076  200 ---IRLFGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSN 271
PLN02911 PLN02911
inositol-phosphate phosphatase
 10-243 4.28e-17

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 79.38  E-value: 4.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  10 DYAVILARQAGEMIREALKNKMDVMIK--SSPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEE-SVAAGEKtvFTEQpT 86
Cdd:PLN02911   38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSP---VTIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEG--SSDY-V 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTEL--- 163
Cdd:PLN02911  112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSphm 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 164 --GSSRKPetlrivLSNMERLCSIPIHGIRSVGTAavnmcLVATGGADAYYEMGIHCWDMAgAGIIVIE-AGGVLLDVTG 240
Cdd:PLN02911  192 fsGDAEDA------FARVRDKVKVPLYGCDCYAYG-----LLASGHVDLVVESGLKPYDYL-ALVPVVEgAGGVITDWKG 259


                  ...
gi 1937369559 241 GPF 243
Cdd:PLN02911  260 RKL 262
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 15-248 3.74e-15

adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 73.19  E-value: 3.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  15 LARQAGEMIREALKNK--MDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVfTEQPTWIID 90
Cdd:PRK10931    8 LARNAGDAIMQVYDGTkpLDVASKAddSP---VTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVD 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  91 PIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKgAF--CNGQKLRVsQQEDITKSLLVteLGSSRK 168
Cdd:PRK10931   84 PLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI-QVRDARPPLVV--ISRSHA 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 169 PETLRivlsnmERLCSIPIHGIRSVGTaAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 247
Cdd:PRK10931  160 DAELK------EYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTP 232


                  .
gi 1937369559 248 R 248
Cdd:PRK10931  233 R 233
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 41-211 1.59e-07

Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.


Pssm-ID: 238820 [Multi-domain]  Cd Length: 244  Bit Score: 50.91  E-value: 1.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  41 DLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGF-----VVNK 115
Cdd:cd01642    34 DVTRVADLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALadprsKVKA 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 116 EMEFGVVYSCVEDKMYTGRKGKGaFCNGQKLRVSQQEDITKSLLVTElGSSRKPETLRIVLSNMERlcsipihgIRSVGT 195
Cdd:cd01642   111 ATLDNFVSGEGGLKVYSPPTRFS-YISVPKLGPPLVPEVPSKIGIYE-GSSRNPEKFLLLSRNGLK--------FRSLGS 180

                         170
                  ....*....|....*.
gi 1937369559 196 AAVNMCLVATGGADAY 211
Cdd:cd01642   181 AALELAYTCEGSFVLF 196
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 12-245 9.79e-06

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 46.16  E-value: 9.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  12 AVILARQAGEMIREALKN----KMDVMIK--SSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEK------- 78
Cdd:cd01640     5 LLAVAEKAGGIARDVVKKgrllILLVEGKtkEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQedesrdv 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559  79 ---TVFTEQPT--------------WIiDPIDGTTNFVH-RFPFVAVSIGFVVNKEMEFGVV----YSCVEDK------M 130
Cdd:cd01640    85 dldEEILEESCpspskdlpeedlgvWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIhqpfYEKTAGAgawlgrT 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1937369559 131 YTGRKGKGAFCNGqklrVSQQEDITKSLLVTELGSSRKPETLRIVLSNMErlcsipihgIRSVGTAAVNMCLVATGGADA 210
Cdd:cd01640   164 IWGLSGLGAHSSD----FKEREDAGKIIVSTSHSHSVKEVQLITAGNKDE---------VLRAGGAGYKVLQVLEGLADA 230

                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1937369559 211 YY--EMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDL 245
Cdd:cd01640   231 YVhsTGGIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
 
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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