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Conserved domains on  [gi|146350804|dbj|BAF62082|]
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inositol-1(or 4)-monophosphatase [Caenorhabditis elegans]

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, ...
 13-263 8.98e-117

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: 335.28  E-value: 8.98e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPT 92
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES---GAAGGLTDEPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  93 WIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQllskgVLCQSLGLH 172
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK-----ELKDALVAT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 173 NRVQFGDRWLDIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSP 252
Cdd:cd01639  153 GFPYDRGDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGP 232

                        250
                 ....*....|.
gi 146350804 253 FDVMSRKVLCA 263
Cdd:cd01639  233 FDLMSGNILAG 243
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 13-263 8.98e-117

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: 335.28  E-value: 8.98e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPT 92
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES---GAAGGLTDEPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  93 WIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQllskgVLCQSLGLH 172
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK-----ELKDALVAT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 173 NRVQFGDRWLDIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSP 252
Cdd:cd01639  153 GFPYDRGDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGP 232

                        250
                 ....*....|.
gi 146350804 253 FDVMSRKVLCA 263
Cdd:cd01639  233 FDLMSGNILAG 243
Inositol_P pfam00459
Inositol monophosphatase family;
17-268 3.72e-91

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 271.14  E-value: 3.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   17 AIELVKKAGTLVRTAFdSPESKVDTKS--SNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWT-DAPTW 93
Cdd:pfam00459   9 AVELAAKAGEILREAF-SNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTdDGPTW 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   94 IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCQSLGLHN 173
Cdd:pfam00459  88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTLFGVSS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  174 RVQFGDR-WLDIAQSNMRNQvmagvrGHRSFGSAAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGS 251
Cdd:pfam00459 168 RKDTSEAsFLAKLLKLVRAP------GVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241

                         250
                  ....*....|....*..
gi 146350804  252 PFDVMSRKVLCAGTAEL 268
Cdd:pfam00459 242 PFDLLAGRVIAANPKVL 258
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 17-276 1.10e-85

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: 256.70  E-value: 1.10e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  17 AIELVKKAGTLVRTAFDSPESKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKiewTDAPTWIID 96
Cdd:COG0483    7 ALRAARAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR---DSGYVWVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCqslglhnrvq 176
Cdd:COG0483   83 PIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVA---------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 177 FGDRWLDIAQSNMRN--QVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFD 254
Cdd:COG0483  153 TGFPYLRDDREYLAAlaALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232

                        250       260
                 ....*....|....*....|..
gi 146350804 255 VMSRKVLcAGTAELGRDLSACL 276
Cdd:COG0483  233 LGSGSLV-AANPALHDELLALL 253
PLN02553 PLN02553
inositol-phosphate phosphatase
 7-277 5.70e-79

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 240.36  E-value: 5.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   7 HEEEQvFVDYAIELVKKAGTLVRTAFDSPEsKVDTKSSnTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIE 86
Cdd:PLN02553   5 DDLEQ-FLEVAVDAAKAAGQIIRKGFYQTK-HVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  87 WTDAPTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLC 166
Cdd:PLN02553  82 LTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 167 QSLGLHNRVQFGDrwldiAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHA-WDVAAPSIIVTEAGGVV 245
Cdd:PLN02553 162 TEVGTKRDKATVD-----ATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAGGLV 236

                        250       260       270
                 ....*....|....*....|....*....|..
gi 146350804 246 TDPTGSPFDVMSRKVLCAGtAELGRDLSACLT 277
Cdd:PLN02553 237 FDPSGGPFDIMSRRVAASN-GHLKDAFVEALR 267
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 17-276 5.22e-39

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: 137.05  E-value: 5.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   17 AIELVKKAGTLVRTAFDSPESKVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPTWIID 96
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKT-PVTEADRAAEEAMRELIAAFFPDHGILGEEF---GHNEEGDAERVWVLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVL-CQSLGLHNRV 175
Cdd:TIGR02067  81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLfTTSPDLLDDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  176 QFGDRWLDIAqsnmrnqvmAGVRGHRSFGSaAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFdV 255
Cdd:TIGR02067 161 GNRPAFERLR---------RAARLTRYGGD-CYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-P 229

                         250       260
                  ....*....|....*....|.
gi 146350804  256 MSRKVLCAGTAELGRDLSACL 276
Cdd:TIGR02067 230 DGGGAVAAGNAMLHDEALEIL 250
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 13-263 8.98e-117

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: 335.28  E-value: 8.98e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPT 92
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES---GAAGGLTDEPT 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  93 WIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQllskgVLCQSLGLH 172
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK-----ELKDALVAT 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 173 NRVQFGDRWLDIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSP 252
Cdd:cd01639  153 GFPYDRGDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGP 232

                        250
                 ....*....|.
gi 146350804 253 FDVMSRKVLCA 263
Cdd:cd01639  233 FDLMSGNILAG 243
Inositol_P pfam00459
Inositol monophosphatase family;
17-268 3.72e-91

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 271.14  E-value: 3.72e-91
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   17 AIELVKKAGTLVRTAFdSPESKVDTKS--SNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWT-DAPTW 93
Cdd:pfam00459   9 AVELAAKAGEILREAF-SNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTdDGPTW 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   94 IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCQSLGLHN 173
Cdd:pfam00459  88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTLFGVSS 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  174 RVQFGDR-WLDIAQSNMRNQvmagvrGHRSFGSAAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGS 251
Cdd:pfam00459 168 RKDTSEAsFLAKLLKLVRAP------GVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241

                         250
                  ....*....|....*..
gi 146350804  252 PFDVMSRKVLCAGTAEL 268
Cdd:pfam00459 242 PFDLLAGRVIAANPKVL 258
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 17-276 1.10e-85

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: 256.70  E-value: 1.10e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  17 AIELVKKAGTLVRTAFDSPESKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKiewTDAPTWIID 96
Cdd:COG0483    7 ALRAARAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR---DSGYVWVID 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCqslglhnrvq 176
Cdd:COG0483   83 PIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVA---------- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 177 FGDRWLDIAQSNMRN--QVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFD 254
Cdd:COG0483  153 TGFPYLRDDREYLAAlaALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232

                        250       260
                 ....*....|....*....|..
gi 146350804 255 VMSRKVLcAGTAELGRDLSACL 276
Cdd:COG0483  233 LGSGSLV-AANPALHDELLALL 253
PLN02553 PLN02553
inositol-phosphate phosphatase
 7-277 5.70e-79

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 240.36  E-value: 5.70e-79
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   7 HEEEQvFVDYAIELVKKAGTLVRTAFDSPEsKVDTKSSnTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIE 86
Cdd:PLN02553   5 DDLEQ-FLEVAVDAAKAAGQIIRKGFYQTK-HVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  87 WTDAPTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLC 166
Cdd:PLN02553  82 LTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 167 QSLGLHNRVQFGDrwldiAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHA-WDVAAPSIIVTEAGGVV 245
Cdd:PLN02553 162 TEVGTKRDKATVD-----ATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAGGLV 236

                        250       260       270
                 ....*....|....*....|....*....|..
gi 146350804 246 TDPTGSPFDVMSRKVLCAGtAELGRDLSACLT 277
Cdd:PLN02553 237 FDPSGGPFDIMSRRVAASN-GHLKDAFVEALR 267
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 15-264 4.04e-70

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: 216.41  E-value: 4.04e-70
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  15 DYAIELVKKAGTLVRTAFDSPESkVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvaGGAKIEWTDAPTWI 94
Cdd:cd01637    2 ELALKAVREAGALILEAFGEELT-VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  95 IDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLcqslglhnr 174
Cdd:cd01637   79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALL--------- 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 175 vQFGDRWLDIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFD 254
Cdd:cd01637  150 -STNASMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLD 228

                        250
                 ....*....|
gi 146350804 255 VMSRKVLCAG 264
Cdd:cd01637  229 TLNRSGIIAA 238
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 15-265 4.36e-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: 157.50  E-value: 4.36e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  15 DYAIELVKKAGTLVRTAFDSpESKVDTKSsNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTdaptWI 94
Cdd:cd01643    2 SLAEAIAQEAGDRALADFGN-SLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY----WV 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  95 IDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRAS-KNQLLSKGVLCqslGLHN 173
Cdd:cd01643   76 IDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHpPLQLPDCNVGF---NRSS 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 174 RVQfgdrwLDIAQSNMRNQVMAGVRGhrsFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPF 253
Cdd:cd01643  153 RAS-----ARAVLRVILRRFPGKIRM---LGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPA 224

                        250
                 ....*....|..
gi 146350804 254 DVMSRKVLCAGT 265
Cdd:cd01643  225 FLQTKDYLSAGF 236
PRK10757 PRK10757
inositol-1-monophosphatase;
17-250 3.68e-45

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 153.42  E-value: 3.68e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  17 AIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPTWIID 96
Cdd:PRK10757   8 AVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVID 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCQSLglhnrvQ 176
Cdd:PRK10757  85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGF------P 158

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146350804 177 FGDRWLDIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTG 250
Cdd:PRK10757 159 FKAKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTG 232
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 13-268 4.27e-44

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: 150.10  E-value: 4.27e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  13 FVDYAIELVKKAGTLVRTAFDSPeSKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEEsvaGGAkiEWTDAP- 91
Cdd:cd01641    1 DLAFALELADAAGQITLPYFRTR-LQVETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEE---FGN--EGGDAGy 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  92 TWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGF---PIRASKNQLLSKGVLCQS 168
Cdd:cd01641   74 VWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAggrPLRVRACADLAEAVLSTT 153

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 169 ---LGLHNRvqfGDRWLDIAQSnmrnqvmagVRGHRsFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVV 245
Cdd:cd01641  154 dphFFTPGD---RAAFERLARA---------VRLTR-YGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVI 220

                        250       260
                 ....*....|....*....|...
gi 146350804 246 TDPTGSPFDVMSRKVLCAGTAEL 268
Cdd:cd01641  221 TDWDGGPLTGGSGRVVAAGDAEL 243
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 14-253 1.05e-41

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: 143.52  E-value: 1.05e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  14 VDYAIELVKKAGTLVRTAFDSPESkVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDapTW 93
Cdd:cd01638    2 LELLIRIAREAGDAILEVYRGGFT-VERKEDGS-PVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDR--FW 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  94 IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCQSLGLHN 173
Cdd:cd01638   78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRS 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 174 RvqfgdrwldIAQSNMRNQVMAGVRGHRSFGSAAiNMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGSP 252
Cdd:cd01638  158 H---------PDEELEALLAALGVAEVVSIGSSL-KFCLVAEGEADIYPRLGpTMEWDTAAGDAVLRAAGGAVSDLDGSP 227


                 .
gi 146350804 253 F 253
Cdd:cd01638  228 L 228
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 17-276 5.22e-39

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: 137.05  E-value: 5.22e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   17 AIELVKKAGTLVRTAFDSPESKVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPTWIID 96
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKT-PVTEADRAAEEAMRELIAAFFPDHGILGEEF---GHNEEGDAERVWVLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVL-CQSLGLHNRV 175
Cdd:TIGR02067  81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLfTTSPDLLDDP 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  176 QFGDRWLDIAqsnmrnqvmAGVRGHRSFGSaAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFdV 255
Cdd:TIGR02067 161 GNRPAFERLR---------RAARLTRYGGD-CYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-P 229

                         250       260
                  ....*....|....*....|.
gi 146350804  256 MSRKVLCAGTAELGRDLSACL 276
Cdd:TIGR02067 230 DGGGAVAAGNAMLHDEALEIL 250
PLN02737 PLN02737
inositol monophosphatase family protein
 18-266 9.26e-39

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 139.16  E-value: 9.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  18 IELVKKAGT-LVRTAFDSPESkVDTKSSnTDLVTETDQAVEKLLIEGLSERFKGHRFIGEES-VAGGAKIEWTdaptWII 95
Cdd:PLN02737  83 AELAAKTGAeVVMEAVNKPRN-ISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGgVIGDSSSDYL----WCI 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  96 DPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYN----PI--TNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLCQSL 169
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 170 GLhnrvQFGDRWldIAQSNMRNQVMAGVRGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPT 249
Cdd:PLN02737 237 GY----EHDDAW--ATNIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMD 310

                        250
                 ....*....|....*..
gi 146350804 250 GSPFDVMSRKVLCAGTA 266
Cdd:PLN02737 311 GGKFSVFDRSVLVSNGV 327
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 17-254 1.11e-37

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 133.75  E-value: 1.11e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  17 AIELVKKAGTLVRTAFDSPeSKVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTWIID 96
Cdd:COG1218    8 AIEIAREAGEAILEIYRAD-FEVEEKADDS-PVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGF-----PIRASKNQLLSKGVLCQSlgl 171
Cdd:COG1218   86 PLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGggerqPIRVRDRPPAEPLRVVAS--- 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 172 hnRVQFGDRWLDIAQSnmrnqvmAGVRGHRSFGSaAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTG 250
Cdd:COG1218  163 --RSHRDEETEALLAR-------LGVAELVSVGS-SLKFCLVAEGEADLYPRLGpTMEWDTAAGQAILEAAGGRVTDLDG 232


                 ....
gi 146350804 251 SPFD 254
Cdd:COG1218  233 KPLR 236
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
9-255 3.18e-36

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 130.03  E-value: 3.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   9 EEQVFVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTE-TDQAVEKLLIEGLSERFKGHRFIGEES-VAGGAKIE 86
Cdd:PRK12676   2 SIMEWLEICDDMAKEVEKAIMPLFGTPDAGETVGMGADGTPTKlIDKVAEDIILEVLKPLGRCVNIISEELgEIVGNGPE 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  87 WTdaptWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGvlC 166
Cdd:PRK12676  82 YT----VVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNES--A 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 167 QSL-GLHNRVqfgDRWLDIAQSnmrnqvmagVRGHRSFGSAAINMVMVAQGSCDGYVEYG--IHAWDVAAPSIIVTEAGG 243
Cdd:PRK12676 156 VSIyGYRRGK---ERTVKLGRK---------VRRVRILGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGG 223

                        250
                 ....*....|..
gi 146350804 244 VVTDPTGSPFDV 255
Cdd:PRK12676 224 IVTDEDGNELKL 235
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 15-247 3.96e-36

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: 127.51  E-value: 3.96e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  15 DYAIELVKKAGTLVRTAFDSPES-KVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTW 93
Cdd:cd01636    2 EELCRVAKEAGLAILKAFGRELSgKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  94 IIDPIDGTTNFVHRIPMIAICVGLAikkqiragivynpITNELYlaqlgkgafknGFPIRASKNQLLSKGVLCqslglhn 173
Cdd:cd01636   82 VIDPIDGTKNFINGLPFVAVVIAVY-------------VILILA-----------EPSHKRVDEKKAELQLLA------- 130

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 146350804 174 rvqfgdrwldiaqsnmrnqvmagVRGHRSFGSAAINMVMVAQGSCDGYVEYGI--HAWDVAAPSIIVTEAGGVVTD 247
Cdd:cd01636  131 -----------------------VYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTD 183
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 15-254 6.92e-34

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: 124.35  E-value: 6.92e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  15 DYAIELVKKAGTLVRTAFDS-PESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAggakiewTDAPTW 93
Cdd:cd01517    3 EVAILAVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA-------ALGRFW 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  94 IIDPIDGTTNFVhRIPMIAICVGLAIKKQIRAGIVYNPITNE-------LYLAQLGKGAFkngfpIRASKNQLLSKGVLC 166
Cdd:cd01517   76 VLDPIDGTKGFL-RGDQFAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAW-----LRPLDGSSLQPLSVR 149

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 167 QSLGLHNRVQFGdrwlDIAQSNMRNQVMAGVRgHRSFGSAAINM------VMVAQGSCDGY------VEYGIHAWDVAAP 234
Cdd:cd01517  150 QLTNAARASFCE----SVESAHSSHRLQAAIK-ALGGTPQPVRLdsqakyAAVARGAADFYlrlplsMSYREKIWDHAAG 224

                        250       260
                 ....*....|....*....|
gi 146350804 235 SIIVTEAGGVVTDPTGSPFD 254
Cdd:cd01517  225 VLIVEEAGGKVTDADGKPLD 244
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 18-254 1.81e-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: 122.56  E-value: 1.81e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   18 IELVKKAGTLVRTAFDSpESKVDTKSSNTDlVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTWIIDP 97
Cdd:TIGR01331   6 IKIARAAGEEILPVYQK-ELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDP 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   98 IDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGfpirasknqllskgvlcqsLGLHNRVQF 177
Cdd:TIGR01331  84 LDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREG-------------------DGQALKAPI 144

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  178 GDRWLD-------IAQSNMRNQVMAGVRG----HRSFGSAAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVV 245
Cdd:TIGR01331 145 HVRPWPsgpllvvISRSHAEEKTTEYLANlgydLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAI 224


                  ....*....
gi 146350804  246 TDPTGSPFD 254
Cdd:TIGR01331 225 FDLDGSPLL 233
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 22-272 4.86e-31

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: 116.32  E-value: 4.86e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  22 KKAGTLVRTAFDSPESKVdtkssnTDLVTEtDQAVEKLlieglsERFKGHRFIGEES--VAGGAKIEWTdaptWIIDPID 99
Cdd:cd01515   23 EDASEVVKIGADGTPTKL------IDKVAE-DAAIEIL------KKLGSVNIVSEEIgvIDNGDEPEYT----VVLDPLD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 100 GTTNFVHRIPMIAICVGLAIKKQIRA--GIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKgvlcQSLGLHNRVQF 177
Cdd:cd01515   86 GTYNAINGIPFYSVSVAVFKIDKSDPyyGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKS----ISVSYYIYGKN 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 178 GDRWLDIAQSnmrnqvmagVRGHRSFGSAAINMVMVAQGSCDGYV---EYgIHAWDVAAPSIIVTEAGGVVTDPTGSP-- 252
Cdd:cd01515  162 HDRTFKICRK---------VRRVRIFGSVALELCYVASGALDAFVdvrEN-LRLVDIAAGYLIAEEAGGIVTDENGKElk 231

                        250       260
                 ....*....|....*....|..
gi 146350804 253 --FDVMSRKVLCAGTAELGRDL 272
Cdd:cd01515  232 lkLNVTERVNIIAANSELHKKL 253
PLN02911 PLN02911
inositol-phosphate phosphatase
 13-268 6.82e-18

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 81.69  E-value: 6.82e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  13 FVDYAIELVKKAGTLVRTAFDSP---ESKVDTKSsntdlVTETDQAVEKLLIEGLSERFKGHRFIGEES--VAGGAKIEW 87
Cdd:PLN02911  36 FVDVAHKLADAAGEVTRKYFRTKfeiIDKEDLSP-----VTIADRAAEEAMRSIILENFPSHAIFGEEHglRCGEGSSDY 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  88 TdaptWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQLLSKGVLcQ 167
Cdd:PLN02911 111 V----WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYL-Y 185

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 168 SLGLHnrvQF-GDRwlDIAQSNMRNQVMAGVRGHRSFGSAainmvMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVT 246
Cdd:PLN02911 186 TTSPH---MFsGDA--EDAFARVRDKVKVPLYGCDCYAYG-----LLASGHVDLVVESGLKPYDYLALVPVVEGAGGVIT 255

                        250       260       270
                 ....*....|....*....|....*....|
gi 146350804 247 DPTGSPF------DVMSRK--VLCAGTAEL 268
Cdd:PLN02911 256 DWKGRKLrwepspGSLATSfnVVAAGDARL 285
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
23-272 1.07e-17

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 82.85  E-value: 1.07e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  23 KAGTLVRTAFDSpeskvdTKSSNTDLVTEtDQAVEKLlieglsERFKGHRFIGEESvagGAKIEWTDAPTWI--IDPIDG 100
Cdd:PRK14076  28 KAGEVVKIGADG------TPTKRIDLIAE-NIAINSL------EKFCSGILISEEI---GFKKIGKNKPEYIfvLDPIDG 91

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 101 TTNFVHRIPMIAICVGLA-IKKQIRA----------------GIVYNPITNELYLAQLGKGAF----KNGFPIRASKNQL 159
Cdd:PRK14076  92 TYNALKDIPIYSASIAIAkIDGFDKKikefigknltindlevGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISN 171

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 160 LSK---GVLCQSLGLHNRVQFGDRwldiaqsnmrnqvmaGVRGHRSFGSAAINMVMVAQGSCDGY--VEYGIHAWDVAAP 234
Cdd:PRK14076 172 LKDasiGLFAYGLSLDTLKFIKDR---------------KVRRIRLFGSIALEMCYVASGALDAFinVNETTRLCDIAAG 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 146350804 235 SIIVTEAGGVVTDPTGSP----FDVMSRKVLCAGTAELGRDL 272
Cdd:PRK14076 237 YVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKKL 278
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 13-233 1.12e-12

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: 66.32  E-value: 1.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEES--VAGGAkiewtDA 90
Cdd:cd01642    1 MLEVLEKITKEIILLLNEKNRQGLVKLIRGAGG-DVTRVADLKAEEIILKLLREEGVFGQIISEESgeIRKGS-----GE 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  91 PTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQ-------------IRAGIVYNPITNELYLAQLGKGAfkngFPIRASKN 157
Cdd:cd01642   75 YIAVLDPLDGSTNYLSGIPFYSVSVALADPRSkvkaatldnfvsgEGGLKVYSPPTRFSYISVPKLGP----PLVPEVPS 150

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 146350804 158 QLLskgvlcqslglhnRVQFGDRWLDIAQSNMRNQVMAgvrghRSFGSAAINMVMVAQGSCDGY--VEYGIHAWDVAA 233
Cdd:cd01642  151 KIG-------------IYEGSSRNPEKFLLLSRNGLKF-----RSLGSAALELAYTCEGSFVLFldLRGKLRNFDVAA 210
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 17-254 1.42e-11

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: 63.50  E-value: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  17 AIELVKKAGTLVRTAFDSPE-----SKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAP 91
Cdd:cd01640    5 LLAVAEKAGGIARDVVKKGRllillVEGKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDV 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  92 ------------------------TWIiDPIDGTTNFVH-RIPMIAICVGLAIKKQIRAGIVYNPITNEL---------- 136
Cdd:cd01640   85 dldeeileescpspskdlpeedlgVWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEKTagagawlgrt 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 137 --YLAQLGKGAFKN------GFPIRASKNQLLSKGVLCQSLGLHNRVQFgdrwldiaqsnmrnqvmagvrghrsFGSAAI 208
Cdd:cd01640  164 iwGLSGLGAHSSDFkeredaGKIIVSTSHSHSVKEVQLITAGNKDEVLR-------------------------AGGAGY 218

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 146350804 209 NMVMVAQGSCDGYV--EYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFD 254
Cdd:cd01640  219 KVLQVLEGLADAYVhsTGGIKKWDICAPEAILRALGGDMTDLHGEPLS 266
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 93-254 1.07e-10

3'(2'),5'-bisphosphate nucleotidase, HAL2 family; 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 plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.


Pssm-ID: 273558 [Multi-domain]  Cd Length: 353  Bit Score: 61.42  E-value: 1.07e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804   93 WIIDPIDGTTNFVhRIPMIAICVGLAIKKQIRAGIVYNP-ITNELYLAQLGKGAFKNGFPIRASKNQllskGVLCQSlgL 171
Cdd:TIGR01330 133 WVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIGCPnLPLSSYGAQNLKGSESKGCIFRAVRGS----GAFMYS--L 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  172 HNRVQfgdRWLDIAQSNMRNQVMAGV-----RGHRSFG-SAAINMVM-----------------VAQGSCDGYVEYGIHA 228
Cdd:TIGR01330 206 SSDAE---SPTKVHVSSVKDTKDAIFcegveKGHSSHDeQTAIANKLgisksplrldsqakyaaLARGDADVYLRLPIKL 282

                         170       180       190
                  ....*....|....*....|....*....|..
gi 146350804  229 ------WDVAAPSIIVTEAGGVVTDPTGSPFD 254
Cdd:TIGR01330 283 syqekiWDHAAGNVIVEEAGGIVTDAMGKPLD 314
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 18-259 2.87e-08

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 53.54  E-value: 2.87e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  18 IELVKKAGTLVRTAFDSPES-KVDTKSSNTDlVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGgakieWTDAPTW--- 93
Cdd:PRK10931   6 CQLARNAGDAIMQVYDGTKPlDVASKADDSP-VTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPA-----WEVRQHWqry 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804  94 -IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKgAFK--NG--FPI-------------RAS 155
Cdd:PRK10931  80 wLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGvrKQIqvrdarpplvvisRSH 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350804 156 KNQLLsKGVLCQsLGLHNRVqfgdrwldiaqsnmrnqvmagvrghrSFGSaAINMVMVAQGSCDGYVEYG-IHAWDVAAP 234
Cdd:PRK10931 159 ADAEL-KEYLQQ-LGEHQTT--------------------------SIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAG 209

                        250       260
                 ....*....|....*....|....*
gi 146350804 235 SIIVTEAGGVVTDPTGSPFDVMSRK 259
Cdd:PRK10931 210 HAVAIAAGAHVHDWQGKTLDYTPRE 234
 
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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