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Conserved domains on  [gi|1067578912|emb|SBN07304|]
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Myo-inositol-1(Or 4)-monophosphatase [Neisseria gonorrhoeae]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108142)

inositol monophosphatase family protein similar to Bacillus subtilis inositol-1-monophosphatase that catalyzes the hydrolysis of several inositol monophosphates and the artificial substrate p-nitrophenyl-phosphate to inorganic phosphate and inositol

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 2-247 6.15e-81

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: 243.38  E-value: 6.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   2 LHRLQKVVRHIAQTEIMPRFLNTP-SRRKEDGSMLSEADIAAQTAFAAALPLLI-DCPMLGEEMSRQEQSALWEqysgek 79
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELTvETKKGDGDLVTEADLAAEELIVDVLKALFpDDGILGEEGGGSGNVSDGG------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  80 GLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGVEI 159
Cdd:cd01637    75 RVWVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLS-KDTPLNDALLSTNA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 160 KYLRSGKLSSRMSTLAPFGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFWsgeHV 239
Cdd:cd01637   154 SMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLD---TL 230


                  ....*...
gi 1067578912 240 FKRSVVAA 247
Cdd:cd01637   231 NRSGIIAA 238
 
Name Accession Description Interval E-value
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 2-247 6.15e-81

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: 243.38  E-value: 6.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   2 LHRLQKVVRHIAQTEIMPRFLNTP-SRRKEDGSMLSEADIAAQTAFAAALPLLI-DCPMLGEEMSRQEQSALWEqysgek 79
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELTvETKKGDGDLVTEADLAAEELIVDVLKALFpDDGILGEEGGGSGNVSDGG------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  80 GLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGVEI 159
Cdd:cd01637    75 RVWVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLS-KDTPLNDALLSTNA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 160 KYLRSGKLSSRMSTLAPFGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFWsgeHV 239
Cdd:cd01637   154 SMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLD---TL 230


                  ....*...
gi 1067578912 240 FKRSVVAA 247
Cdd:cd01637   231 NRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 1-262 2.48e-74

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: 227.04  E-value: 2.48e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   1 MLHRLQKVVRhIAQTEIMPRFLNTPS--RRKEDGSMLSEADIAAQTAFAAALP-LLIDCPMLGEEMSRQEQSalweqysG 77
Cdd:COG0483     3 LLELALRAAR-AAGALILRRFRELDLevETKGDGDLVTEADRAAEAAIRERLRaAFPDHGILGEESGASEGR-------D 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  78 EKGLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGV 157
Cdd:COG0483    75 SGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVS-ARTDLEDALVAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 158 EIKYLRSGK-LSSRMSTLAP-FGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFws 235
Cdd:COG0483   154 GFPYLRDDReYLAALAALLPrVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPL-- 231

                         250       260
                  ....*....|....*....|....*..
gi 1067578912 236 geHVFKRSVVAAlEPKLFERWVGWIRE 262
Cdd:COG0483   232 --DLGSGSLVAA-NPALHDELLALLRE 255
Inositol_P pfam00459
Inositol monophosphatase family;
82-255 9.45e-49

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 162.13  E-value: 9.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  82 WIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLVDkKLNEAIAGVEIKY 161
Cdd:pfam00459  87 WIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAP-PLSEALLVTLFGV 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 162 lRSGKLSSRMSTLAPF------GTIRSMGSSTLDWCYLACGRYDVYVHGGQ-KLWDYAAGALIFEEAGGRLTTLEGDGFw 234
Cdd:pfam00459 166 -SSRKDTSEASFLAKLlklvraPGVRRVGSAALKLAMVAAGKADAYIEFGRlKPWDHAAGVAILREAGGVVTDADGGPF- 243

                         170       180
                  ....*....|....*....|.
gi 1067578912 235 sgeHVFKRSVVAALEPKLFER 255
Cdd:pfam00459 244 ---DLLAGRVIAANPKVLHEL 261
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 1-230 2.54e-36

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: 129.11  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   1 MLHRLQKVVRHIAQtEIMPrFLNTP--SRRKEDGSMLSEADIAAQTAFAAAL-PLLIDCPMLGEE------MSRQeqsaL 71
Cdd:TIGR01331   1 MLDDVIKIARAAGE-EILP-VYQKElaVAQKADNSPVTEADRAAHRFILEGLrALTPDIPVLSEEdasiplTPRQ----T 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  72 WEQYsgekglWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNG----TRLPLRlVD 147
Cdd:TIGR01331  75 WQRF------WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqaLKAPIH-VR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 148 KKLNEAIAGVEIKYLRSGKLSSRMSTLApFGTIRSMGSStLDWCYLACGRYDVYV-HGGQKLWDYAAGALIFEEAGGRLT 226
Cdd:TIGR01331 148 PWPSGPLLVVISRSHAEEKTTEYLANLG-YDLRTSGGSS-LKFCLVAEGSADIYPrLGPTGEWDTAAGHAVLAAAGGAIF 225


                  ....
gi 1067578912 227 TLEG 230
Cdd:TIGR01331 226 DLDG 229
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
77-231 4.75e-36

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 128.87  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  77 GEKGLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLVdKKLNE---A 153
Cdd:PRK12676   79 GPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKT-SELNEsavS 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 154 IAGVEIKYLRSGKLSS---RMstlapfgtiRSMGSSTLDWCYLACGRYDVYVHGGQKL--WDYAAGALIFEEAGGRLTTL 228
Cdd:PRK12676  158 IYGYRRGKERTVKLGRkvrRV---------RILGAIALELCYVASGRLDAFVDVRNYLrvTDIAAGKLICEEAGGIVTDE 228


                  ...
gi 1067578912 229 EGD 231
Cdd:PRK12676  229 DGN 231
 
Name Accession Description Interval E-value
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 2-247 6.15e-81

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: 243.38  E-value: 6.15e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   2 LHRLQKVVRHIAQTEIMPRFLNTP-SRRKEDGSMLSEADIAAQTAFAAALPLLI-DCPMLGEEMSRQEQSALWEqysgek 79
Cdd:cd01637     1 LELALKAVREAGALILEAFGEELTvETKKGDGDLVTEADLAAEELIVDVLKALFpDDGILGEEGGGSGNVSDGG------ 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  80 GLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGVEI 159
Cdd:cd01637    75 RVWVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLS-KDTPLNDALLSTNA 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 160 KYLRSGKLSSRMSTLAPFGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFWsgeHV 239
Cdd:cd01637   154 SMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLD---TL 230


                  ....*...
gi 1067578912 240 FKRSVVAA 247
Cdd:cd01637   231 NRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 1-262 2.48e-74

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: 227.04  E-value: 2.48e-74
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   1 MLHRLQKVVRhIAQTEIMPRFLNTPS--RRKEDGSMLSEADIAAQTAFAAALP-LLIDCPMLGEEMSRQEQSalweqysG 77
Cdd:COG0483     3 LLELALRAAR-AAGALILRRFRELDLevETKGDGDLVTEADRAAEAAIRERLRaAFPDHGILGEESGASEGR-------D 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  78 EKGLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGV 157
Cdd:COG0483    75 SGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVS-ARTDLEDALVAT 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 158 EIKYLRSGK-LSSRMSTLAP-FGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFws 235
Cdd:COG0483   154 GFPYLRDDReYLAALAALLPrVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPL-- 231

                         250       260
                  ....*....|....*....|....*..
gi 1067578912 236 geHVFKRSVVAAlEPKLFERWVGWIRE 262
Cdd:COG0483   232 --DLGSGSLVAA-NPALHDELLALLRE 255
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 59-247 3.43e-64

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: 200.84  E-value: 3.43e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  59 LGEEMSRQEQSalweqysGEKGLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNG 138
Cdd:cd01639    62 LGEESGAAGGL-------TDEPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNG 134

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 139 TRLPLRLVdKKLNEAIAGVEIKYLRSGKLSSRMSTLA-----PFGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAA 213
Cdd:cd01639   135 RRIRVSGR-KELKDALVATGFPYDRGDNFDRYLNNFAkllakAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAA 213

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1067578912 214 GALIFEEAGGRLTTLEGDGFWsgehVFKRSVVAA 247
Cdd:cd01639   214 GALIVREAGGLVTDFDGGPFD----LMSGNILAG 243
Inositol_P pfam00459
Inositol monophosphatase family;
82-255 9.45e-49

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 162.13  E-value: 9.45e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  82 WIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLVDkKLNEAIAGVEIKY 161
Cdd:pfam00459  87 WIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAP-PLSEALLVTLFGV 165

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 162 lRSGKLSSRMSTLAPF------GTIRSMGSSTLDWCYLACGRYDVYVHGGQ-KLWDYAAGALIFEEAGGRLTTLEGDGFw 234
Cdd:pfam00459 166 -SSRKDTSEASFLAKLlklvraPGVRRVGSAALKLAMVAAGKADAYIEFGRlKPWDHAAGVAILREAGGVVTDADGGPF- 243

                         170       180
                  ....*....|....*....|.
gi 1067578912 235 sgeHVFKRSVVAALEPKLFER 255
Cdd:pfam00459 244 ---DLLAGRVIAANPKVLHEL 261
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 7-234 7.36e-45

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: 151.33  E-value: 7.36e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   7 KVVRHIAQtEIMPR----FLNT-PSRRKEDGSMLSEADIAAQTAFAAAL----PlliDCPMLGEEMSRQEQSALWeqysg 77
Cdd:cd01643     2 SLAEAIAQ-EAGDRaladFGNSlSAETKADGSLVTAADRWVEQLIRARLaaqfP---DDGVLGEEGGGIFPSSGW----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  78 ekgLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGV 157
Cdd:cd01643    73 ---YWVIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALH-PPLQLPDCNVGF 148

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1067578912 158 EIKYLRSGKLSSRMSTLAPFGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFW 234
Cdd:cd01643   149 NRSSRASARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAF 225
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 2-230 2.50e-44

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 150.31  E-value: 2.50e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   2 LHRLQKVVRHIAQ---TEIMP-RFLNTPSRRKEDGSMLSEADIAAQTAFAAALPLLI-DCPMLGEEMSrqeqSALWEQYS 76
Cdd:COG1218     1 LEALLEAAIEIAReagEAILEiYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTpDIPVLSEESA----AIPYEERK 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  77 GEKGLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFL---NGTRLPLRLVDKKLNEA 153
Cdd:COG1218    77 SWDRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgGGERQPIRVRDRPPAEP 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578912 154 IAGVEIKYLRSGKLSSRMSTLaPFGTIRSMGSStLDWCYLACGRYDVYVH-GGQKLWDYAAGALIFEEAGGRLTTLEG 230
Cdd:COG1218   157 LRVVASRSHRDEETEALLARL-GVAELVSVGSS-LKFCLVAEGEADLYPRlGPTMEWDTAAGQAILEAAGGRVTDLDG 232
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 9-230 2.00e-42

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: 144.68  E-value: 2.00e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   9 VRHIAQT---EIMPRFLN-TPSRRKEDGSMLSEADIAAQTAFAAAL-PLLIDCPMLGEEMSRQEQSALWEQYsgekglWI 83
Cdd:cd01638     5 LIRIAREagdAILEVYRGgFTVERKEDGSPVTAADLAANAFIVEGLaALRPDIPVLSEESADDPLRLGWDRF------WL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  84 VDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLvdkkLNEAIAGVEIKYLR 163
Cdd:cd01638    79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSL----QARPPPLQPLRVVA 154

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1067578912 164 S----GKLSSRMSTLAPFGTIRSMGSStLDWCYLACGRYDVYVH-GGQKLWDYAAGALIFEEAGGRLTTLEG 230
Cdd:cd01638   155 SrshpDEELEALLAALGVAEVVSIGSS-LKFCLVAEGEADIYPRlGPTMEWDTAAGDAVLRAAGGAVSDLDG 225
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 1-230 2.54e-36

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: 129.11  E-value: 2.54e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   1 MLHRLQKVVRHIAQtEIMPrFLNTP--SRRKEDGSMLSEADIAAQTAFAAAL-PLLIDCPMLGEE------MSRQeqsaL 71
Cdd:TIGR01331   1 MLDDVIKIARAAGE-EILP-VYQKElaVAQKADNSPVTEADRAAHRFILEGLrALTPDIPVLSEEdasiplTPRQ----T 74

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  72 WEQYsgekglWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNG----TRLPLRlVD 147
Cdd:TIGR01331  75 WQRF------WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqaLKAPIH-VR 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 148 KKLNEAIAGVEIKYLRSGKLSSRMSTLApFGTIRSMGSStLDWCYLACGRYDVYV-HGGQKLWDYAAGALIFEEAGGRLT 226
Cdd:TIGR01331 148 PWPSGPLLVVISRSHAEEKTTEYLANLG-YDLRTSGGSS-LKFCLVAEGSADIYPrLGPTGEWDTAAGHAVLAAAGGAIF 225


                  ....
gi 1067578912 227 TLEG 230
Cdd:TIGR01331 226 DLDG 229
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
77-231 4.75e-36

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 128.87  E-value: 4.75e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  77 GEKGLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLVdKKLNE---A 153
Cdd:PRK12676   79 GPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKT-SELNEsavS 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 154 IAGVEIKYLRSGKLSS---RMstlapfgtiRSMGSSTLDWCYLACGRYDVYVHGGQKL--WDYAAGALIFEEAGGRLTTL 228
Cdd:PRK12676  158 IYGYRRGKERTVKLGRkvrRV---------RILGAIALELCYVASGRLDAFVDVRNYLrvTDIAAGKLICEEAGGIVTDE 228


                  ...
gi 1067578912 229 EGD 231
Cdd:PRK12676  229 DGN 231
PLN02553 PLN02553
inositol-phosphate phosphatase
 82-247 1.91e-35

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 127.50  E-value: 1.91e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  82 WIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLVDkKLNEAIAGVEIKY 161
Cdd:PLN02553   88 WIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQS-ELGKALLATEVGT 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 162 LRSGKLSSRM-----STLAPFGTIRSMGSSTLDWCYLACGRYDVYVH---GGQklWDYAAGALIFEEAGGRLTTLEGDGF 233
Cdd:PLN02553  167 KRDKATVDATtnrinALLYKVRSLRMSGSCALNLCGVACGRLDIFYEigfGGP--WDVAAGAVIVKEAGGLVFDPSGGPF 244

                         170
                  ....*....|....
gi 1067578912 234 wsgeHVFKRSVVAA 247
Cdd:PLN02553  245 ----DIMSRRVAAS 254
PRK10757 PRK10757
inositol-1-monophosphatase;
82-262 3.36e-34

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 124.15  E-value: 3.36e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  82 WIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPlRLVDKKLNEAIAGVEIKY 161
Cdd:PRK10757   81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLR-GSTARDLDGTILATGFPF 159

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 162 LRSGKLSSRMSTLAPFGT----IRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGdgfwsGE 237
Cdd:PRK10757  160 KAKQHATTYINIVGKLFTecadFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTG-----GH 234

                         170       180
                  ....*....|....*....|....*
gi 1067578912 238 HVFKRSVVAALEPKLFERWVGWIRE 262
Cdd:PRK10757  235 NYMLTGNIVAGNPRVVKAMLANMRD 259
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 83-254 8.75e-32

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: 117.48  E-value: 8.75e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  83 IVDPIDGTNNFVNGLPHFAVSVAFVRNGRAEL--GVIYNPVSGECFYAERGQGAFLNGTRLPLRlVDKKLNEAIAGVeik 160
Cdd:cd01515    80 VLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPyyGYVYNLATGDLYYAIKGKGAYLNGKRIKVS-DFSSLKSISVSY--- 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 161 YLRSGKLSSRMSTLAPFGTIRSMGSSTLDWCYLACGRYDVY--VHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFWSGEH 238
Cdd:cd01515   156 YIYGKNHDRTFKICRKVRRVRIFGSVALELCYVASGALDAFvdVRENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKLN 235

                         170       180
                  ....*....|....*....|
gi 1067578912 239 VFKR-SVVAA---LEPKLFE 254
Cdd:cd01515   236 VTERvNIIAAnseLHKKLLE 255
PLN02737 PLN02737
inositol monophosphatase family protein
 81-255 2.78e-30

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 116.05  E-value: 2.78e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  81 LWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSG------ECFYAERGQGAFLNGTRLPLRLVDKkLNEAI 154
Cdd:PLN02737  153 LWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGpmcwntRTFSASAGGGAFCNGQKIHVSQTDK-VERSL 231

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 155 AGVEIKYLRSGKLSSRMSTLAPFGTI----RSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEG 230
Cdd:PLN02737  232 LVTGFGYEHDDAWATNIELFKEFTDVsrgvRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDG 311

                         170       180
                  ....*....|....*....|....*...
gi 1067578912 231 DGFwsgeHVFKRSVVA---ALEPKLFER 255
Cdd:PLN02737  312 GKF----SVFDRSVLVsngVLHPKLLDR 335
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 16-230 4.19e-30

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: 113.12  E-value: 4.19e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  16 EIMPRF-LNTPSRRKEDGSMLSEADiaaqTAFAAALPLLI--DCP---MLGEEMSRQEQSalweqySGEkgLWIVDPIDG 89
Cdd:cd01641    15 ITLPYFrTRLQVETKADFSPVTEAD----RAAEAAMRELIaaAFPdhgILGEEFGNEGGD------AGY--VWVLDPIDG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  90 TNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTR-LPLRLVD-KKLNEAIAGVEIKYLRSGKL 167
Cdd:cd01641    83 TKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGgRPLRVRAcADLAEAVLSTTDPHFFTPGD 162

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1067578912 168 SSRMSTLApfGTIRSM--GSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEG 230
Cdd:cd01641   163 RAAFERLA--RAVRLTryGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDG 225
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-230 5.99e-29

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


Pssm-ID: 238775 [Multi-domain]  Cd Length: 274  Bit Score: 110.48  E-value: 5.99e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912   9 VRHIAQTEIMPRFLN----TPSRRKEDGSMLSEADIAAQTAFAAALP-LLIDCPMLGEEMSrqeqSALweqysgekGL-W 82
Cdd:cd01517     8 AVRAAASLTLPVFRNlgagDVVWKKSDKSPVTVADYGAQALITAALArLFPSDPIVGEEDS----AAL--------GRfW 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  83 IVDPIDGTNNFVNGLPhFAVSVAFVRNGRAELGVIYNPVS-------GECFYAERGQGAFL----NGTRLPLRLV---DK 148
Cdd:cd01517    76 VLDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLplddgggGDLFSAVRGQGAWLrpldGSSLQPLSVRqltNA 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 149 KLNEAIAGVEIKYLRSGKLSSRMSTLAPFGTIRSMgsSTLDWCYLACGRYDVYVH----GGQKL--WDYAAGALIFEEAG 222
Cdd:cd01517   155 ARASFCESVESAHSSHRLQAAIKALGGTPQPVRLD--SQAKYAAVARGAADFYLRlplsMSYREkiWDHAAGVLIVEEAG 232


                  ....*...
gi 1067578912 223 GRLTTLEG 230
Cdd:cd01517   233 GKVTDADG 240
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 12-252 5.18e-26

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: 102.38  E-value: 5.18e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  12 IAQTEIMPRF--LNTPSRRKEDGSMLSEADiaaqtafaaalpllidcpmLGEEMSRQEQSA--------LWEQYSGEKGL 81
Cdd:TIGR02067  11 AAGETILPFFraSLLVVDKKSDKTPVTEAD-------------------RAAEEAMRELIAaffpdhgiLGEEFGHNEEG 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  82 -----WIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLNGTRLPLRLVdKKLNEA-IA 155
Cdd:TIGR02067  72 daervWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSC-ANLSDAvLF 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 156 GVEIKYLRSGKLSSRMSTLAPFGTIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDYAAGALIFEEAGGRLTTLEGDGFWS 235
Cdd:TIGR02067 151 TTSPDLLDDPGNRPAFERLRRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPD 230

                         250
                  ....*....|....*..
gi 1067578912 236 GEhvfkrSVVAALEPKL 252
Cdd:TIGR02067 231 GG-----GAVAAGNAML 242
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
83-258 9.43e-22

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 94.02  E-value: 9.43e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  83 IVDPIDGTNNFVNGLPHFAVSVAFVR-----------NGRA------ELGVIYNPVSGECFYAERGQGAFL--NGTRLPL 143
Cdd:PRK14076   85 VLDPIDGTYNALKDIPIYSASIAIAKidgfdkkikefIGKNltindlEVGVVKNIATGDTYYAEKGEGAYLlkKGEKKKI 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 144 RLVDKK-LNEAIAGVEIKYLrSGKLSSRMSTlAPFGTIRSMGSSTLDWCYLACGRYDVY--VHGGQKLWDYAAGALIFEE 220
Cdd:PRK14076  165 EISNISnLKDASIGLFAYGL-SLDTLKFIKD-RKVRRIRLFGSIALEMCYVASGALDAFinVNETTRLCDIAAGYVICKE 242

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1067578912 221 AGGRLTTLEGDGFWSGEHVFKRSVVAALEPKLFERWVG 258
Cdd:PRK14076  243 AGGIITNKNGKPLNMKLDINEKTSVICSNEILHKKLVG 280
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 54-228 2.71e-18

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: 80.13  E-value: 2.71e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  54 IDCPMLGEEmsrqeQSALWEQYSGEKGL-WIVDPIDGTNNFVNGLPHFAVSVAfvrngraelgvIYNPVSGECFYAergq 132
Cdd:cd01636    57 PDVKIVGEE-----SGVAEEVMGRRDEYtWVIDPIDGTKNFINGLPFVAVVIA-----------VYVILILAEPSH---- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 133 gaflngtrlpLRLVDKKLneaiagveikylrsgklssRMSTLAPfGTIRSMGSSTLDWCYLACGRYDVY--VHGGQKLWD 210
Cdd:cd01636   117 ----------KRVDEKKA-------------------ELQLLAV-YRIRIVGSAVAKMCLVALGLADIYyePGGKRRAWD 166

                         170
                  ....*....|....*...
gi 1067578912 211 YAAGALIFEEAGGRLTTL 228
Cdd:cd01636   167 VAASAAIVREAGGIMTDW 184
PLN02911 PLN02911
inositol-phosphate phosphatase
 60-252 1.09e-17

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 80.53  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  60 GEE--MSRQEQSALWeqysgekgLWIVDPIDGTNNFVNGLPHFAVSVAFVRNGRAELGVIYNPVSGECFYAERGQGAFLN 137
Cdd:PLN02911   96 GEEhgLRCGEGSSDY--------VWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLN 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 138 GTRLPLRLVdKKLNEAIAGVEIKYLRSGKlssrmsTLAPFGTIRSMGSSTL---DwCY----LACGRYDVYVHGGQKLWD 210
Cdd:PLN02911  168 GEEISTRSC-ASLKDAYLYTTSPHMFSGD------AEDAFARVRDKVKVPLygcD-CYayglLASGHVDLVVESGLKPYD 239

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1067578912 211 YAAGALIFEEAGGRLTTLEGDGF-W---SGEHVFKRSVVAALEPKL 252
Cdd:PLN02911  240 YLALVPVVEGAGGVITDWKGRKLrWepsPGSLATSFNVVAAGDARL 285
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 28-230 9.33e-17

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 77.04  E-value: 9.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  28 RKEDGSMLSEADIAAQTAFAAALPLLI-DCPMLGEE-----MSRQEqsalWEQYsgekglWIVDPIDGTNNFVNGLPHFA 101
Cdd:PRK10931   30 SKADDSPVTAADIAAHTVIKDGLRTLTpDIPVLSEEdppawEVRQH----WQRY------WLVDPLDGTKEFIKRNGEFT 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 102 VSVAFVRNGRAELGVIYNPVSGECFYAERGQgAFL--NGTRLPLRLVDKKLNEAIAGveikylRS---GKLSSRMSTLAP 176
Cdd:PRK10931  100 VNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGVRKQIQVRDARPPLVVIS------RShadAELKEYLQQLGE 172

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1067578912 177 FGTIrSMGSStLDWCYLACGRYDVYVH-GGQKLWDYAAGALIFEEAGGRLTTLEG 230
Cdd:PRK10931  173 HQTT-SIGSS-LKFCLVAEGQAQLYPRfGPTNIWDTAAGHAVAIAAGAHVHDWQG 225
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 77-230 1.07e-16

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: 78.37  E-value: 1.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  77 GEKG-LWIVDPIDGTNNFVNGlPHFAVSVAFVRNGRAELGVIYNP---VSGEC-------------FYAERGQGAFL--- 136
Cdd:TIGR01330 127 GRKGrHWVLDPIDGTKGFLRG-DQYAVCLALIENGKVVLGVIGCPnlpLSSYGaqnlkgseskgciFRAVRGSGAFMysl 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 137 -NGTRLPLRL--------VDKKLNEAIAGVEIKYLRSGKLSSRMSTLAPFGTIRSMGSstldWCYLACGRYDVYV---HG 204
Cdd:TIGR01330 206 sSDAESPTKVhvssvkdtKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLRLDSQAK----YAALARGDADVYLrlpIK 281

                         170       180
                  ....*....|....*....|....*....
gi 1067578912 205 G---QKLWDYAAGALIFEEAGGRLTTLEG 230
Cdd:TIGR01330 282 LsyqEKIWDHAAGNVIVEEAGGIVTDAMG 310
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 67-218 4.52e-11

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: 61.31  E-value: 4.52e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  67 EQSALWEQYSGEKGLwIVDPIDGTNNFVNGLPHFAVSVAFVR-NGRAELGVIYNPVSGECF---YAERGQGAFLNGTRLP 142
Cdd:cd01642    63 EESGEIRKGSGEYIA-VLDPLDGSTNYLSGIPFYSVSVALADpRSKVKAATLDNFVSGEGGlkvYSPPTRFSYISVPKLG 141

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1067578912 143 LRLVdkklnEAIAGVEIKYLRSGKLSSRMSTLAPFG-TIRSMGSSTLDWCYLACGRYDVYVHGGQKLWDY-AAGALIF 218
Cdd:cd01642   142 PPLV-----PEVPSKIGIYEGSSRNPEKFLLLSRNGlKFRSLGSAALELAYTCEGSFVLFLDLRGKLRNFdVAAALGA 214
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 80-231 2.55e-10

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: 59.64  E-value: 2.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912  80 GLWIvDPIDGTNNFVNG-LPHFAVSVAFVRNGRAELGVIYNP----------VSGECFYAERGQGAF--LNGTRLPLRLV 146
Cdd:cd01640   108 GVWV-DPLDATQEYTEGlLEYVTVLIGVAVKGKPIAGVIHQPfyektagagaWLGRTIWGLSGLGAHssDFKEREDAGKI 186

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1067578912 147 ---------DKKLNEAIAGVEIKYLRSGKlssrmstlAPFGTIRsmgsstldwcyLACGRYDVYVH--GGQKLWDYAAGA 215
Cdd:cd01640   187 ivstshshsVKEVQLITAGNKDEVLRAGG--------AGYKVLQ-----------VLEGLADAYVHstGGIKKWDICAPE 247

                         170
                  ....*....|....*.
gi 1067578912 216 LIFEEAGGRLTTLEGD 231
Cdd:cd01640   248 AILRALGGDMTDLHGE 263
 
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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