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Conserved domains on  [gi|564335854|ref|XP_006232213|]
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inositol monophosphatase 1 isoform X1 [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, ...
 61-307 3.65e-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: 355.69  E-value: 3.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  61 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 139
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 140 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSS 219
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 220 RkPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLM 299
Cdd:cd01639  158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236


                 ....*...
gi 564335854 300 SRRIIAAS 307
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, ...
 61-307 3.65e-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: 355.69  E-value: 3.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  61 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 139
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 140 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSS 219
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 220 RkPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLM 299
Cdd:cd01639  158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236


                 ....*...
gi 564335854 300 SRRIIAAS 307
Cdd:cd01639  237 SGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
58-324 1.10e-101

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 299.65  E-value: 1.10e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854   58 WQECMDYAVI-LARQAGEMIREALKNKMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVF 134
Cdd:pfam00459   1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  135 TEQ-PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLV 213
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  214 TELGSSRKPETL-RIVLSNMERLcsIPIHGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDV 291
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKL--VRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 564335854  292 TGGPFDLMSRRIIAASNIALAERIAKELEIIPL 324
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
PLN02553 PLN02553
inositol-phosphate phosphatase
 56-323 6.61e-93

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 277.34  E-value: 6.61e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  56 DPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFT 135
Cdd:PLN02553   5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 136 EQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTE 215
Cdd:PLN02553  84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 216 LGSSRKPETLRIVLSNMERLCSIpIHGIRSVGTAAVNMCLVATGGADAYYEMGI-HCWDMAGAGIIVIEAGGVLLDVTGG 294
Cdd:PLN02553 164 VGTKRDKATVDATTNRINALLYK-VRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGG 242

                        250       260
                 ....*....|....*....|....*....
gi 564335854 295 PFDLMSRRiIAASNIALAERIAKELEIIP 323
Cdd:PLN02553 243 PFDIMSRR-VAASNGHLKDAFVEALRQTE 270
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 59-319 3.06e-80

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: 244.75  E-value: 3.06e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  59 QECMDYAVILARQAGEMIREALKN-KMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQ 137
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 138 PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELG 217
Cdd:COG0483   77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 218 SSRKPETLRIVLSNMERLCsipiHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD 297
Cdd:COG0483  157 YLRDDREYLAALAALLPRV----RRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232

                        250       260
                 ....*....|....*....|..
gi 564335854 298 LMSRRIIAAsNIALAERIAKEL 319
Cdd:COG0483  233 LGSGSLVAA-NPALHDELLALL 253
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 65-320 5.52e-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: 5.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854   65 AVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDP 144
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  145 IDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPET 224
Cdd:TIGR02067  82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  225 LRIVLSNMERLCSipihgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFdLMSRRII 304
Cdd:TIGR02067 162 NRPAFERLRRAAR-----LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAV 235

                         250
                  ....*....|....*.
gi 564335854  305 AASNIALAERIAKELE 320
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, ...
 61-307 3.65e-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: 355.69  E-value: 3.65e-124
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  61 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 139
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 140 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSS 219
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 220 RkPETLRIVLSNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLM 299
Cdd:cd01639  158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236


                 ....*...
gi 564335854 300 SRRIIAAS 307
Cdd:cd01639  237 SGNILAGN 244
Inositol_P pfam00459
Inositol monophosphatase family;
58-324 1.10e-101

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 299.65  E-value: 1.10e-101
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854   58 WQECMDYAVI-LARQAGEMIREALKNKMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVF 134
Cdd:pfam00459   1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  135 TEQ-PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLV 213
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  214 TELGSSRKPETL-RIVLSNMERLcsIPIHGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDV 291
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKL--VRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238

                         250       260       270
                  ....*....|....*....|....*....|...
gi 564335854  292 TGGPFDLMSRRIIAASNIALAERIAKELEIIPL 324
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
PLN02553 PLN02553
inositol-phosphate phosphatase
 56-323 6.61e-93

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 277.34  E-value: 6.61e-93
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  56 DPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFT 135
Cdd:PLN02553   5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 136 EQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTE 215
Cdd:PLN02553  84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 216 LGSSRKPETLRIVLSNMERLCSIpIHGIRSVGTAAVNMCLVATGGADAYYEMGI-HCWDMAGAGIIVIEAGGVLLDVTGG 294
Cdd:PLN02553 164 VGTKRDKATVDATTNRINALLYK-VRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGG 242

                        250       260
                 ....*....|....*....|....*....
gi 564335854 295 PFDLMSRRiIAASNIALAERIAKELEIIP 323
Cdd:PLN02553 243 PFDIMSRR-VAASNGHLKDAFVEALRQTE 270
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 59-319 3.06e-80

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: 244.75  E-value: 3.06e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  59 QECMDYAVILARQAGEMIREALKN-KMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQ 137
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 138 PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELG 217
Cdd:COG0483   77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 218 SSRKPETLRIVLSNMERLCsipiHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD 297
Cdd:COG0483  157 YLRDDREYLAALAALLPRV----RRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232

                        250       260
                 ....*....|....*....|..
gi 564335854 298 LMSRRIIAAsNIALAERIAKEL 319
Cdd:COG0483  233 LGSGSLVAA-NPALHDELLALL 253
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 62-306 8.20e-80

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: 242.99  E-value: 8.20e-80
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  62 MDYAVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaAGEKTVFTEQPTWI 141
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 142 IDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRK 221
Cdd:cd01637   79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 222 PEtlrivLSNMERLCsIPIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD-LMS 300
Cdd:cd01637  159 NR-----AAVLASLV-NRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtLNR 232


                 ....*.
gi 564335854 301 RRIIAA 306
Cdd:cd01637  233 SGIIAA 238
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 62-291 3.52e-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: 165.26  E-value: 3.52e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  62 MDYAVILARQAGEMIREALKNK--MDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPT 139
Cdd:cd01636    1 LEELCRVAKEAGLAILKAFGRElsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 140 WIIDPIDGTTNFVHRFPFVAVSIGfvvnkemefgvVYSCvedkmytgrkgkgafcngqklrvsqqeditksLLVTELGSS 219
Cdd:cd01636   81 WVIDPIDGTKNFINGLPFVAVVIA-----------VYVI--------------------------------LILAEPSHK 117

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 564335854 220 RKPEtlrivlsNMERLCSIPIHGIRSVGTAAVNMCLVATGGADAYYEMGI--HCWDMAGAGIIVIEAGGVLLDV 291
Cdd:cd01636  118 RVDE-------KKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTDW 184
PLN02737 PLN02737
inositol monophosphatase family protein
 27-315 5.64e-47

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 162.28  E-value: 5.64e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  27 ARRSSVSEVLRRRMSPTLPKTSGLYTIMADPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKM 106
Cdd:PLN02737  45 LARRPTPAVLSETPNQAKYPRVGAASTGPIPAEELLAVAELAAKTGAEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 107 LMSSIKEKYPYHSFIGEESVAAGEKTvftEQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKE------MEFGVVYSCVE 180
Cdd:PLN02737 124 ILEVVRKNFPDHLILGEEGGVIGDSS---SDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTpaaatvVEFVGGPMCWN 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 181 DKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSR-KPETLRIVL----SNMERlcsipihGIRSVGTAAVNMCL 255
Cdd:PLN02737 201 TRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHdDAWATNIELfkefTDVSR-------GVRRLGAAAVDMCH 273

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 256 VATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIaASNIALAERI 315
Cdd:PLN02737 274 VALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVL-VSNGVLHPKL 332
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 68-312 4.54e-46

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: 4.54e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  68 LARQAGEMIREALKNKMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaaGEKTVFTEQPTWIIDPIDG 147
Cdd:cd01643    7 IAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVIDPIDG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 148 TTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDItKSLLVTELGSSRKPETLRI 227
Cdd:cd01643   82 TTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQL-PDCNVGFNRSSRASARAVL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 228 VLSNMERLCSipihgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIAAS 307
Cdd:cd01643  161 RVILRRFPGK-----IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYLSAG 235


                 ....*
gi 564335854 308 NIALA 312
Cdd:cd01643  236 FPTLI 240
PRK10757 PRK10757
inositol-1-monophosphatase;
65-307 4.92e-44

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 151.88  E-value: 4.92e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  65 AVILARQAGEMIREALKNKMDVMI-KSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQPTWIID 143
Cdd:PRK10757   8 AVRAARKAGNLIAKNYETPDAVEAsQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 144 PIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPE 223
Cdd:PRK10757  85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQH 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 224 T---LRIVlSNMERLCSipihGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 300
Cdd:PRK10757 165 AttyINIV-GKLFTECA----DFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLT 239


                 ....*..
gi 564335854 301 RRIIAAS 307
Cdd:PRK10757 240 GNIVAGN 246
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 68-308 1.22e-42

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 148.00  E-value: 1.22e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  68 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 145
Cdd:COG1218   11 IAREAGEAILEIYRADFEVEEKAddSP---VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPL 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 146 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFC-----NGQKLRVSQQEDITKSLLVTelgsSR 220
Cdd:COG1218   88 DGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPLRVVA----SR 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 221 ---KPETLRIvlsnMERLcsiPIHGIRSVGtAAVNMCLVATGGADAYYEMGIHC-WDMAGAGIIVIEAGGVLLDVTGGPF 296
Cdd:COG1218  164 shrDEETEAL----LARL---GVAELVSVG-SSLKFCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRVTDLDGKPL 235

                        250
                 ....*....|....*...
gi 564335854 297 ------DLMSRRIIAASN 308
Cdd:COG1218  236 rynkkeDLLNPGFIASGD 253
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 62-316 4.34e-35

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: 127.76  E-value: 4.34e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  62 MDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTeqptWI 141
Cdd:cd01641    2 LAFALELADAAGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV----WV 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 142 IDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCN---GQKLRVSQQEDITKSLLVTElgs 218
Cdd:cd01641   77 LDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTT--- 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 219 srKPETLRIVLSN-MERLCSipIHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD 297
Cdd:cd01641  154 --DPHFFTPGDRAaFERLAR--AVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLT 229

                        250
                 ....*....|....*....
gi 564335854 298 LMSRRIIAASNIALAERIA 316
Cdd:cd01641  230 GGSGRVVAAGDAELHEALL 248
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 63-296 1.48e-34

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: 126.19  E-value: 1.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  63 DYAVILARQAGEMIREALKNKMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEktVFTEQPTWII 142
Cdd:cd01638    3 ELLIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFWLV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 143 DPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGS--SR 220
Cdd:cd01638   80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASrsHP 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564335854 221 KPETLRIVLsnmerlcSIPIHGIRSVGTAAvNMCLVATGGADAYYEMGIHC-WDMAgAGIIVI-EAGGVLLDVTGGPF 296
Cdd:cd01638  160 DEELEALLA-------ALGVAEVVSIGSSL-KFCLVAEGEADIYPRLGPTMeWDTA-AGDAVLrAAGGAVSDLDGSPL 228
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 65-320 5.52e-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: 5.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854   65 AVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDP 144
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  145 IDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTELGSSRKPET 224
Cdd:TIGR02067  82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  225 LRIVLSNMERLCSipihgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFdLMSRRII 304
Cdd:TIGR02067 162 NRPAFERLRRAAR-----LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAV 235

                         250
                  ....*....|....*.
gi 564335854  305 AASNIALAERIAKELE 320
Cdd:TIGR02067 236 AAGNAMLHDEALEILN 251
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 68-297 8.40e-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: 8.40e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854   68 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 145
Cdd:TIGR01331   8 IARAAGEEILPVYQKELAVAQKAdnSP---VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  146 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAF--CNGQKLR--VSQQEDITKSLLVTELGSSRK 221
Cdd:TIGR01331  85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQALKapIHVRPWPSGPLLVVISRSHAE 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 564335854  222 PETLRIvLSNMERLCSIPihgirsvGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFD 297
Cdd:TIGR01331 165 EKTTEY-LANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 62-307 2.61e-28

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: 2.61e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  62 MDYAVILARQAGEMIREALKNKM--DVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAgektvftEQPT 139
Cdd:cd01517    2 LEVAILAVRAAASLTLPVFRNLGagDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGRF 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 140 WIIDPIDGTTNFVHRFPFvAVSIGFVVNKEMEFGVVYSCV-------EDKMYTGRKGKGAFC---NGQKLRVSQQEDITK 209
Cdd:cd01517   75 WVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAWLrplDGSSLQPLSVRQLTN 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 210 SLLVTELGSSRKPETLRIVLSNMERLCSIPihgirsvgtAAVNM------CLVATGGADAY--------YEMGIhcWDMA 275
Cdd:cd01517  154 AARASFCESVESAHSSHRLQAAIKALGGTP---------QPVRLdsqakyAAVARGAADFYlrlplsmsYREKI--WDHA 222

                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 564335854 276 GAGIIVIEAGGVLLDVTGGPFD-------LMSRRIIAAS 307
Cdd:cd01517  223 AGVLIVEEAGGKVTDADGKPLDfgkgrklLNNGGLIAAP 261
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
100-320 7.24e-27

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 106.53  E-value: 7.24e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 100 DQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCV 179
Cdd:PRK12676  47 DKVAEDIILEVLKPLGRCVNIISEE---LGEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLA 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 180 EDKMYTGRKGKGAFCNGQKLRVSQQEDItKSLLVTELGSSRKPETLRIVLSNMERlcsipihgIRSVGTAAVNMCLVATG 259
Cdd:PRK12676 124 TGDFYEAIPGKGAYLNGKPIKVSKTSEL-NESAVSIYGYRRGKERTVKLGRKVRR--------VRILGAIALELCYVASG 194

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 564335854 260 GADAYYEMG--IHCWDMAGAGIIVIEAGGVLLDVTGGPFDL-----MSRRIIAASNIALAERIAKELE 320
Cdd:PRK12676 195 RLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvtERTNLIAANGEELHKKILELLE 262
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 72-315 3.28e-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: 104.38  E-value: 3.28e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  72 AGEMIREALKNKMDVM--------IKSSP-ADLVTVTDQKVEKMLMSSIKEKYPYhSFIGEESvaaGEKtVFTEQPTW-- 140
Cdd:cd01515    5 ARNIAKEIEKAIKPLFgtedasevVKIGAdGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEI---GVI-DNGDEPEYtv 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 141 IIDPIDGTTNFVHRFPFVAVSIGFVVNKE--MEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDItKSLLVTELGS 218
Cdd:cd01515   80 VLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSL-KSISVSYYIY 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 219 SRKPETLRIVLSNMERlcsipihgIRSVGTAAVNMCLVATGGADAYYEM--GIHCWDMAGAGIIVIEAGGVLLDVTGGP- 295
Cdd:cd01515  159 GKNHDRTFKICRKVRR--------VRIFGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKEl 230

                        250       260
                 ....*....|....*....|...
gi 564335854 296 ---FDLMSRRIIAASNIALAERI 315
Cdd:cd01515  231 klkLNVTERVNIIAANSELHKKL 253
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
104-315 5.55e-21

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 93.64  E-value: 5.55e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 104 EKMLMSSIkEKYPYHSFIGEEsvaAGEKTVFTEQPTWI--IDPIDGTTNFVHRFPFVAVSIG-------------FVVN- 167
Cdd:PRK14076  50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIAiakidgfdkkikeFIGKn 125

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 168 ---KEMEFGVVYSCVEDKMYTGRKGKGAF----CNGQKLRVSQQEDITK-SLLVTELGSSRkpETLRIVLSNMERLcsip 239
Cdd:PRK14076 126 ltiNDLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDaSIGLFAYGLSL--DTLKFIKDRKVRR---- 199

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 240 ihgIRSVGTAAVNMCLVATGGADAYYEM--GIHCWDMAGAGIIVIEAGGVLLDVTGGP----FDLMSRRIIAASNIALAE 313
Cdd:PRK14076 200 ---IRLFGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHK 276


                 ..
gi 564335854 314 RI 315
Cdd:PRK14076 277 KL 278
PLN02911 PLN02911
inositol-phosphate phosphatase
 63-296 9.23e-17

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 79.38  E-value: 9.23e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  63 DYAVILARQAGEMIREALKNKMDVMIK--SSPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEE-SVAAGEKtvFTEQpT 139
Cdd:PLN02911  38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSP---VTIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEG--SSDY-V 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 140 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEDITKSLLVTEL--- 216
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSphm 191

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 217 --GSSRKPetlrivLSNMERLCSIPIHGIRSVGTAavnmcLVATGGADAYYEMGIHCWDMAgAGIIVIE-AGGVLLDVTG 293
Cdd:PLN02911 192 fsGDAEDA------FARVRDKVKVPLYGCDCYAYG-----LLASGHVDLVVESGLKPYDYL-ALVPVVEgAGGVITDWKG 259


                 ...
gi 564335854 294 GPF 296
Cdd:PLN02911 260 RKL 262
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 68-301 7.22e-15

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 73.19  E-value: 7.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  68 LARQAGEMIREALKNK--MDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVfTEQPTWIID 143
Cdd:PRK10931   8 LARNAGDAIMQVYDGTkpLDVASKAddSP---VTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVD 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 144 PIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKgAF--CNGQKLRVsQQEDITKSLLVteLGSSRK 221
Cdd:PRK10931  84 PLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI-QVRDARPPLVV--ISRSHA 159

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 222 PETLRivlsnmERLCSIPIHGIRSVGTaAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 300
Cdd:PRK10931 160 DAELK------EYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTP 232


                 .
gi 564335854 301 R 301
Cdd:PRK10931 233 R 233
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 94-264 2.53e-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: 2.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  94 DLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGF-----VVNK 168
Cdd:cd01642   34 DVTRVADLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALadprsKVKA 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 169 EMEFGVVYSCVEDKMYTGRKGKGaFCNGQKLRVSQQEDItKSLLVTELGSSRKPETLRIVLSNMERlcsipihgIRSVGT 248
Cdd:cd01642  111 ATLDNFVSGEGGLKVYSPPTRFS-YISVPKLGPPLVPEV-PSKIGIYEGSSRNPEKFLLLSRNGLK--------FRSLGS 180

                        170
                 ....*....|....*.
gi 564335854 249 AAVNMCLVATGGADAY 264
Cdd:cd01642  181 AALELAYTCEGSFVLF 196
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 65-298 5.41e-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: 47.32  E-value: 5.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854  65 AVILARQAGEMIREALKN----KMDVMIK--SSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEK------- 131
Cdd:cd01640    5 LLAVAEKAGGIARDVVKKgrllILLVEGKtkEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQedesrdv 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 132 ---TVFTEQPT--------------WIiDPIDGTTNFVH-RFPFVAVSIGFVVNKEMEFGVV----YSCVEDK------M 183
Cdd:cd01640   85 dldEEILEESCpspskdlpeedlgvWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIhqpfYEKTAGAgawlgrT 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564335854 184 YTGRKGKGAFCNGqklrVSQQEDITKSLLVTELGSSRKPETLRIVLSNMErlcsipihgIRSVGTAAVNMCLVATGGADA 263
Cdd:cd01640  164 IWGLSGLGAHSSD----FKEREDAGKIIVSTSHSHSVKEVQLITAGNKDE---------VLRAGGAGYKVLQVLEGLADA 230

                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 564335854 264 YY--EMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDL 298
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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