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Conserved domains on  [gi|498399381|ref|WP_010712689|]
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MULTISPECIES: inositol monophosphatase family protein [Enterococcus]

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 ...
 9-243 5.38e-92

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: 271.11  E-value: 5.38e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   9 QTIQSWLFEAADVIRMNLESELTVQQKNGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSFAGRVWIIDP 88
Cdd:cd01637    2 ELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVIDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  89 IDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMNAYMHGKNIH 168
Cdd:cd01637   82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNRA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498399381 169 -HATEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGREYFIAA 243
Cdd:cd01637  162 aVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSsGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
 
Name Accession Description Interval E-value
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 9-243 5.38e-92

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: 271.11  E-value: 5.38e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   9 QTIQSWLFEAADVIRMNLESELTVQQKNGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSFAGRVWIIDP 88
Cdd:cd01637    2 ELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVIDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  89 IDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMNAYMHGKNIH 168
Cdd:cd01637   82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNRA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498399381 169 -HATEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGREYFIAA 243
Cdd:cd01637  162 aVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSsGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 5-251 9.69e-65

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: 202.38  E-value: 9.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   5 QKFVQTIQSWLFEAADVIRMNLES-ELTVQQKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSfAGRV 83
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETK-GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD-SGYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  84 WIIDPIDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMNAYMH 163
Cdd:COG0483   79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 164 GKNIHHA---TEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGREy 239
Cdd:COG0483  159 RDDREYLaalAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEaGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS- 237

                        250
                 ....*....|..
gi 498399381 240 FIAATPETYDEV 251
Cdd:COG0483  238 LVAANPALHDEL 249
Inositol_P pfam00459
Inositol monophosphatase family;
5-259 6.92e-51

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 167.52  E-value: 6.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381    5 QKFVQTIQSWLFEAADVIRMNLESELTVQQK--NGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEE---KGYNTLKSF 79
Cdd:pfam00459   3 EEVLKVAVELAAKAGEILREAFSNKLTIEEKgkSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggaKGDQTELTD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   80 AGRVWIIDPIDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADG-LWGM 158
Cdd:pfam00459  83 DGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEAlLVTL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  159 NAYMHGKNIHHATEIGQASM-----GVRISGCAGLEIIAMLKGNHHGYL--SNLSPWDYAAGLVLLEEFGFKYSGITGKP 231
Cdd:pfam00459 163 FGVSSRKDTSEASFLAKLLKlvrapGVRRVGSAALKLAMVAAGKADAYIefGRLKPWDHAAGVAILREAGGVVTDADGGP 242

                         250       260
                  ....*....|....*....|....*...
gi 498399381  232 LTFAGREYfIAATPETYDEVFTQYLNES 259
Cdd:pfam00459 243 FDLLAGRV-IAANPKVLHELLAAALEEI 269
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 17-240 8.72e-23

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: 93.67  E-value: 8.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   17 EAADVIRMNLESELTVQQKNGRTDlVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLK--SFAGRVWIIDPIDGTMN 94
Cdd:TIGR01331  11 AAGEEILPVYQKELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTprQTWQRFWLVDPLDGTKE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   95 FVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYR--NNQLLKAPTMKALADGLWGMNAYMHGKNIHHATE 172
Cdd:TIGR01331  90 FINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegDGQALKAPIHVRPWPSGPLLVVISRSHAEEKTTE 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498399381  173 IGQA-SMGVRISGCAGLEIIAMLKGNHHGYLsNLSP---WDYAAGLVLLEEFGFKYSGITGKPLTFAGREYF 240
Cdd:TIGR01331 170 YLANlGYDLRTSGGSSLKFCLVAEGSADIYP-RLGPtgeWDTAAGHAVLAAAGGAIFDLDGSPLLYGKRESF 240
PRK10757 PRK10757
inositol-1-monophosphatase;
17-229 9.28e-23

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 93.72  E-value: 9.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESELTVQ--QKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGyntlkSFAGR----VWIIDPID 90
Cdd:PRK10757  14 KAGNLIAKNYETPDAVEasQK-GSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESG-----ELEGEdqdvQWVIDPLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  91 GTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALaDGLWGMNAYMHgKNIHHA 170
Cdd:PRK10757  88 GTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDL-DGTILATGFPF-KAKQHA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498399381 171 T-------EIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITG 229
Cdd:PRK10757 166 TtyinivgKLFTECADFRRTGSAALDLAYVAAGRVDGFFEiGLKPWDFAAGELLVREAGGIVSDFTG 232
 
Name Accession Description Interval E-value
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 9-243 5.38e-92

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: 271.11  E-value: 5.38e-92
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   9 QTIQSWLFEAADVIRMNLESELTVQQKNGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSFAGRVWIIDP 88
Cdd:cd01637    2 ELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVIDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  89 IDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMNAYMHGKNIH 168
Cdd:cd01637   82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNRA 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498399381 169 -HATEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGREYFIAA 243
Cdd:cd01637  162 aVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSsGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 5-251 9.69e-65

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: 202.38  E-value: 9.69e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   5 QKFVQTIQSWLFEAADVIRMNLES-ELTVQQKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSfAGRV 83
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETK-GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD-SGYV 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  84 WIIDPIDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMNAYMH 163
Cdd:COG0483   79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 164 GKNIHHA---TEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGREy 239
Cdd:COG0483  159 RDDREYLaalAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEaGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS- 237

                        250
                 ....*....|..
gi 498399381 240 FIAATPETYDEV 251
Cdd:COG0483  238 LVAANPALHDEL 249
Inositol_P pfam00459
Inositol monophosphatase family;
5-259 6.92e-51

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 167.52  E-value: 6.92e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381    5 QKFVQTIQSWLFEAADVIRMNLESELTVQQK--NGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEE---KGYNTLKSF 79
Cdd:pfam00459   3 EEVLKVAVELAAKAGEILREAFSNKLTIEEKgkSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggaKGDQTELTD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   80 AGRVWIIDPIDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADG-LWGM 158
Cdd:pfam00459  83 DGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEAlLVTL 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  159 NAYMHGKNIHHATEIGQASM-----GVRISGCAGLEIIAMLKGNHHGYL--SNLSPWDYAAGLVLLEEFGFKYSGITGKP 231
Cdd:pfam00459 163 FGVSSRKDTSEASFLAKLLKlvrapGVRRVGSAALKLAMVAAGKADAYIefGRLKPWDHAAGVAILREAGGVVTDADGGP 242

                         250       260
                  ....*....|....*....|....*...
gi 498399381  232 LTFAGREYfIAATPETYDEVFTQYLNES 259
Cdd:pfam00459 243 FDLLAGRV-IAANPKVLHELLAAALEEI 269
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 17-245 1.82e-48

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: 160.40  E-value: 1.82e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLES-ELTVQQKNGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEkGYNTLKSFAGRVWIIDPIDGTMNF 95
Cdd:cd01639   11 KAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEE-SGAAGGLTDEPTWIIDPLDGTTNF 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  96 VMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMN-AYMHGKNIHHATE-- 172
Cdd:cd01639   90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGfPYDRGDNFDRYLNnf 169

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498399381 173 ---IGQASMGVRISGCAGLEI--IAMlkGNHHGY-LSNLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGREyfIAATP 245
Cdd:cd01639  170 aklLAKAVRGVRRLGSAALDLayVAA--GRLDGYwERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN--ILAGN 244
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 17-242 1.62e-29

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: 111.16  E-value: 1.62e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESELTVQQKNGRTdLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSFAGRVWIIDPIDGTMNFV 96
Cdd:cd01638   11 EAGDAILEVYRGGFTVERKEDGS-PVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDRFWLVDPLDGTREFI 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  97 MERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLkAPTMKALADGLWGMNAYM---HGKNIHHAtEI 173
Cdd:cd01638   90 KGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPG-AVSLQARPPPLQPLRVVAsrsHPDEELEA-LL 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498399381 174 GQASMGVRISGCAGLEIIAMLKGNHHGYLSnLSP---WDYAAGLVLLEEFGFKYSGITGKPLTFaGREYFIA 242
Cdd:cd01638  168 AALGVAEVVSIGSSLKFCLVAEGEADIYPR-LGPtmeWDTAAGDAVLRAAGGAVSDLDGSPLTY-NREDFLN 237
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 9-221 2.55e-28

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: 108.19  E-value: 2.55e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   9 QTIQSWLFEAADVIRMNLESELTVQQKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEkgYNTLKSFAGRVWIIDP 88
Cdd:cd01643    2 SLAEAIAQEAGDRALADFGNSLSAETK-ADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE--GGGIFPSSGWYWVIDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  89 IDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGMNAYMHgknIH 168
Cdd:cd01643   79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSR---AS 155

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 498399381 169 HATEIGQASM----GVRISGCAGLEIIAMLKGNHHGYLSNL-SPWDYAAGLVLLEEFG 221
Cdd:cd01643  156 ARAVLRVILRrfpgKIRMLGSASLNLASVAAGQTLGYVEATpKIWDIAAAWVILREAG 213
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 17-243 1.60e-25

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 101.01  E-value: 1.60e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIrMNL-ESELTVQQKNGRTdLVTNMDEQTQEFLMNKIQTNFPEDQILGEE---KGYNTLKSfAGRVWIIDPIDGT 92
Cdd:COG1218   14 EAGEAI-LEIyRADFEVEEKADDS-PVTEADLAAHAIILAGLAALTPDIPVLSEEsaaIPYEERKS-WDRFWLVDPLDGT 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  93 MNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNN-----------QLLKAPTMKALAD---GLWGM 158
Cdd:COG1218   91 KEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerqpirvrDRPPAEPLRVVASrshRDEET 170

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 159 NAYMHGKNIHHATEIGqasmgvrisgcAGLEIIAMLKGNHHGYLSnLSP---WDYAAGLVLLEEFGFKYSGITGKPLTFA 235
Cdd:COG1218  171 EALLARLGVAELVSVG-----------SSLKFCLVAEGEADLYPR-LGPtmeWDTAAGQAILEAAGGRVTDLDGKPLRYN 238

                        250
                 ....*....|...
gi 498399381 236 GRE-----YFIAA 243
Cdd:COG1218  239 KKEdllnpGFIAS 251
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 17-252 6.56e-25

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: 99.69  E-value: 6.56e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESELT---VQQKNGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGyntlkSFAGRVWIIDPIDGTM 93
Cdd:cd01517   10 RAAASLTLPVFRNLGagdVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS-----AALGRFWVLDPIDGTK 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  94 NFVmeR-ENFCIMLAVYEDGIGKLGFIYDVMREELYWGG-------KGLGVY----RNNQLLKA----PTMKALADGLWG 157
Cdd:cd01517   85 GFL--RgDQFAVALALIEDGEVVLGVIGCPNLPLDDGGGgdlfsavRGQGAWlrplDGSSLQPLsvrqLTNAARASFCES 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 158 MNAYmhgkNIHHATEIGQASMGVRISGCA---GLEIIAMLKGNHHGYL-------SNLSPWDYAAGLVLLEEFGFKYSGI 227
Cdd:cd01517  163 VESA----HSSHRLQAAIKALGGTPQPVRldsQAKYAAVARGAADFYLrlplsmsYREKIWDHAAGVLIVEEAGGKVTDA 238

                        250       260       270
                 ....*....|....*....|....*....|.
gi 498399381 228 TGKPLTFA-GREY-----FIAATPETYDEVF 252
Cdd:cd01517  239 DGKPLDFGkGRKLlnnggLIAAPGEIHEQVL 269
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 17-240 8.72e-23

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: 93.67  E-value: 8.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   17 EAADVIRMNLESELTVQQKNGRTDlVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLK--SFAGRVWIIDPIDGTMN 94
Cdd:TIGR01331  11 AAGEEILPVYQKELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTprQTWQRFWLVDPLDGTKE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   95 FVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYR--NNQLLKAPTMKALADGLWGMNAYMHGKNIHHATE 172
Cdd:TIGR01331  90 FINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegDGQALKAPIHVRPWPSGPLLVVISRSHAEEKTTE 169

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498399381  173 IGQA-SMGVRISGCAGLEIIAMLKGNHHGYLsNLSP---WDYAAGLVLLEEFGFKYSGITGKPLTFAGREYF 240
Cdd:TIGR01331 170 YLANlGYDLRTSGGSSLKFCLVAEGSADIYP-RLGPtgeWDTAAGHAVLAAAGGAIFDLDGSPLLYGKRESF 240
PRK10757 PRK10757
inositol-1-monophosphatase;
17-229 9.28e-23

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 93.72  E-value: 9.28e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESELTVQ--QKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGyntlkSFAGR----VWIIDPID 90
Cdd:PRK10757  14 KAGNLIAKNYETPDAVEasQK-GSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESG-----ELEGEdqdvQWVIDPLD 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  91 GTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALaDGLWGMNAYMHgKNIHHA 170
Cdd:PRK10757  88 GTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDL-DGTILATGFPF-KAKQHA 165

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498399381 171 T-------EIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITG 229
Cdd:PRK10757 166 TtyinivgKLFTECADFRRTGSAALDLAYVAAGRVDGFFEiGLKPWDFAAGELLVREAGGIVSDFTG 232
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 18-251 3.62e-20

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: 86.59  E-value: 3.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   18 AADVIRMNLESELTVQQKNGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSfAGRVWIIDPIDGTMNFVM 97
Cdd:TIGR02067  12 AGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGD-AERVWVLDPIDGTKSFIR 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   98 ERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADglwgmnAY-MHGKNIHHATEIGQA 176
Cdd:TIGR02067  91 GVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSD------AVlFTTSPDLLDDPGNRP 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  177 SMGVRISGCAgleiIAMLKGNHHGYL------------SNLSPWDYAAGLVLLEEFGFKYSGITGKPLTFAGrEYFIAAT 244
Cdd:TIGR02067 165 AFERLRRAAR----LTRYGGDCYAYLmvaggavdivvePGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGG-GAVAAGN 239


                  ....*..
gi 498399381  245 PETYDEV 251
Cdd:TIGR02067 240 AMLHDEA 246
PLN02737 PLN02737
inositol monophosphatase family protein
 19-233 2.62e-19

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 86.01  E-value: 2.62e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  19 ADVIRMNLESELTVQQKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGY--NTLKSFagrVWIIDPIDGTMNFV 96
Cdd:PLN02737  91 AEVVMEAVNKPRNISYK-GLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVigDSSSDY---LWCIDPLDGTTNFA 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  97 MERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGK------GLGVYRNNQLLKAPTMKALADGLWGMNA-YMH----GK 165
Cdd:PLN02737 167 HGYPSFAVSVGVLFRGTPAAATVVEFVGGPMCWNTRtfsasaGGGAFCNGQKIHVSQTDKVERSLLVTGFgYEHddawAT 246

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498399381 166 NIHHATEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS-NLSPWDYAAGLVLLEEFGFKYSGITGKPLT 233
Cdd:PLN02737 247 NIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEyRLKPWDMAAGVLIVEEAGGTVTRMDGGKFS 315
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 17-245 3.02e-19

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: 83.84  E-value: 3.02e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESELTVQQKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSfaGRVWIIDPIDGTMNFV 96
Cdd:cd01641   11 AAGQITLPYFRTRLQVETK-ADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDA--GYVWVLDPIDGTKSFI 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  97 MERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQL---LKAPTMKALADglwgmnAYMHGKNIHHATEi 173
Cdd:cd01641   88 RGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGgrpLRVRACADLAE------AVLSTTDPHFFTP- 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 174 GQASMGVRISGCAGLeiiAMLKGNHHGYLS------------NLSPWDYAAGLVLLEEFGFKYSGITGKPLTfAGREYFI 241
Cdd:cd01641  161 GDRAAFERLARAVRL---TRYGGDCYAYALvasgrvdlvveaGLKPYDVAALIPIIEGAGGVITDWDGGPLT-GGSGRVV 236


                 ....
gi 498399381 242 AATP 245
Cdd:cd01641  237 AAGD 240
PLN02553 PLN02553
inositol-phosphate phosphatase
 18-260 3.15e-19

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 84.36  E-value: 3.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  18 AADVIRMNLESELTVQQKnGRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEkgynTLKSFAG------RVWIIDPIDG 91
Cdd:PLN02553  21 AGQIIRKGFYQTKHVEHK-GQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEE----TTAASGGteltdePTWIVDPLDG 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  92 TMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGLWGmnaymhgknihhaT 171
Cdd:PLN02553  96 TTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLA-------------T 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 172 EIG--------QASMG-----------VRISG-CA-GLEIIAMlkgnhhGYLSNL------SPWDYAAGLVLLEEFGFKY 224
Cdd:PLN02553 163 EVGtkrdkatvDATTNrinallykvrsLRMSGsCAlNLCGVAC------GRLDIFyeigfgGPWDVAAGAVIVKEAGGLV 236

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 498399381 225 SGITGKPLTFAGREyfIAATPETYDEVFTQYLNESE 260
Cdd:PLN02553 237 FDPSGGPFDIMSRR--VAASNGHLKDAFVEALRQTE 270
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 17-109 5.62e-15

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: 70.88  E-value: 5.62e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESELTVQQKNGRT--DLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKGY--NTLKSFAGRVWIIDPIDGT 92
Cdd:cd01636   10 EAGLAILKAFGRELSGKVKITKSdnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVaeEVMGRRDEYTWVIDPIDGT 89

                         90
                 ....*....|....*..
gi 498399381  93 MNFVMERENFCIMLAVY 109
Cdd:cd01636   90 KNFINGLPFVAVVIAVY 106
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
85-246 1.93e-14

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 71.09  E-value: 1.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  85 IIDPIDGTMNFVMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADGlwGMNAYMHG 164
Cdd:PRK12676  85 VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNES--AVSIYGYR 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 165 KNIHHATEIGQASMGVRISGCAGLEIIAMLKGNHHGYL---SNLSPWDYAAGLVLLEEFGFKYSGITGKPLTF----AGR 237
Cdd:PRK12676 163 RGKERTVKLGRKVRRVRILGAIALELCYVASGRLDAFVdvrNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvTER 242


                 ....*....
gi 498399381 238 EYFIAATPE 246
Cdd:PRK12676 243 TNLIAANGE 251
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 17-234 1.99e-14

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: 71.20  E-value: 1.99e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  17 EAADVIRMNLESE----LTVQQKN--GRTDLVTNMDEQTQEFLMNKIQTNFPEDQILGEEKG------------------ 72
Cdd:cd01640   11 KAGGIARDVVKKGrlliLLVEGKTkeGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNefenqedesrdvdldeei 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  73 --------YNTLKSFAGRVWIiDPIDGTMNFVmERENFCI--MLAVYEDGIGKLGFIY----------DVMREELYWGGK 132
Cdd:cd01640   91 leescpspSKDLPEEDLGVWV-DPLDATQEYT-EGLLEYVtvLIGVAVKGKPIAGVIHqpfyektagaGAWLGRTIWGLS 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 133 GLGVYRNNQLLKAPTMKALadglwgMNAYMHGKNIHHATEIGQASMGVRISGCAGLEIIAMLKGNHHGYL---SNLSPWD 209
Cdd:cd01640  169 GLGAHSSDFKEREDAGKII------VSTSHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVhstGGIKKWD 242

                        250       260
                 ....*....|....*....|....*
gi 498399381 210 YAAGLVLLEEFGFKYSGITGKPLTF 234
Cdd:cd01640  243 ICAPEAILRALGGDMTDLHGEPLSY 267
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 66-251 3.63e-13

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: 67.40  E-value: 3.63e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  66 ILGEEKGYNTLKSFAGRVWIIDPIDGTMNFVMERENFCIMLAV-YEDGIGKL-GFIYDVMREELYWGGKGLGVYRNNQLL 143
Cdd:cd01515   61 IVSEEIGVIDNGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVfKIDKSDPYyGYVYNLATGDLYYAIKGKGAYLNGKRI 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 144 KAPTMKALADGLWGmnAYMHGKNIHHATEIGQASMGVRISGCAGLEIIAMLKGNHHGYLS---NLSPWDYAAGLVLLEEF 220
Cdd:cd01515  141 KVSDFSSLKSISVS--YYIYGKNHDRTFKICRKVRRVRIFGSVALELCYVASGALDAFVDvreNLRLVDIAAGYLIAEEA 218

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 498399381 221 GFKYSGITGKPLTF----AGREYFIAATPETYDEV 251
Cdd:cd01515  219 GGIVTDENGKELKLklnvTERVNIIAANSELHKKL 253
PLN02911 PLN02911
inositol-phosphate phosphatase
 18-168 3.25e-11

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 62.04  E-value: 3.25e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  18 AADVIRMNLESELTVQQKNgrtDL--VTNMDEQTQEFLMNKIQTNFPEDQILGEEKGYNTLKSFAGRVWIIDPIDGTMNF 95
Cdd:PLN02911  47 AGEVTRKYFRTKFEIIDKE---DLspVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDYVWVLDPIDGTKSF 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498399381  96 VMERENFCIMLAVYEDGIGKLGFIYDVMREELYWGGKGLGVYRNNQLLKAPTMKALADglwgmnAYMHGKNIH 168
Cdd:PLN02911 124 ITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKD------AYLYTTSPH 190
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 26-237 2.20e-07

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: 51.02  E-value: 2.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   26 LESELTVQQKNGRTDlVTNMDEQTQEFLMNKIQTNFPEDQILGEE--------------------------KGYNTLKSF 79
Cdd:TIGR01330  29 SHKDSTVITKDDKSP-VTVGDYGAQAIVINVLKSNFPDDPIVGEEdssglseadftlgrvnelvnetlvyaKNYKKDDQF 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381   80 A---------------------GRVWIIDPIDGTMNFVmERENFCIMLAVYEDGIGKLGFI----YDVMREE-------- 126
Cdd:TIGR01330 108 PlksledvlqiidfgnyeggrkGRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIgcpnLPLSSYGaqnlkgse 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  127 ----LYWGGKGLGVYRNN-------------QLLKAPTMKALADGLWGMNAyMHGKNIHHATEIGQASMGVRISGCAGLE 189
Cdd:TIGR01330 187 skgcIFRAVRGSGAFMYSlssdaesptkvhvSSVKDTKDAIFCEGVEKGHS-SHDEQTAIANKLGISKSPLRLDSQAKYA 265

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 498399381  190 IIAMLKGNHHGYLSNLSP-----WDYAAGLVLLEEFGFKYSGITGKPLTFA-GR 237
Cdd:TIGR01330 266 ALARGDADVYLRLPIKLSyqekiWDHAAGNVIVEEAGGIVTDAMGKPLDFGkGR 319
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
56-232 1.87e-04

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 42.41  E-value: 1.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  56 KIQTNFPEDQILGEEKGYNTLKSFAGR-VWIIDPIDGTMNFVMERENFCIMLAV---------YEDGIGK--------LG 117
Cdd:PRK14076  55 NSLEKFCSGILISEEIGFKKIGKNKPEyIFVLDPIDGTYNALKDIPIYSASIAIakidgfdkkIKEFIGKnltindleVG 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381 118 FIYDVMREELYWGGKGLGVY----RNNQLLKAPTMKALADGLWGMNAYMHGKNIHHATEIGQASMgVRISGCAGLEIIAM 193
Cdd:PRK14076 135 VVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDASIGLFAYGLSLDTLKFIKDRKVRR-IRLFGSIALEMCYV 213

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 498399381 194 LKGNHHGYLS---NLSPWDYAAGLVLLEEFGFKYSGITGKPL 232
Cdd:PRK14076 214 ASGALDAFINvneTTRLCDIAAGYVICKEAGGIITNKNGKPL 255
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 42-133 8.65e-04

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 39.68  E-value: 8.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498399381  42 VTNMDEQTQEFLMNKIQTNFPEDQILGEE--KGYNTLKSFAgRVWIIDPIDGTMNFVMERENFCIMLAVYEDGIGKLGFI 119
Cdd:PRK10931  37 VTAADIAAHTVIKDGLRTLTPDIPVLSEEdpPAWEVRQHWQ-RYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVV 115

                         90
                 ....*....|....
gi 498399381 120 YDVMREELYWGGKG 133
Cdd:PRK10931 116 YAPVMNVMYSAAEG 129
 
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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