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Conserved domains on  [gi|882939027|ref|NP_001297362|]
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inositol monophosphatase 1 isoform 2 [Mus musculus]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10108155)

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-164 5.74e-73

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: 220.87  E-value: 5.74e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   8 CMDYAVILARQAGEMIREALKN-EMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  87 WVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEEsgvLEQLLLIC 164
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKE---LKDALVAT 152
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-164 5.74e-73

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: 220.87  E-value: 5.74e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   8 CMDYAVILARQAGEMIREALKN-EMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  87 WVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEEsgvLEQLLLIC 164
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKE---LKDALVAT 152
Inositol_P pfam00459
Inositol monophosphatase family;
5-154 1.32e-59

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 187.94  E-value: 1.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027    5 WQECMDYAVI-LARQAGEMIREALKNEMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVF 81
Cdd:pfam00459   1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939027   82 TEQ-PTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEES 154
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPL 154
PLN02553 PLN02553
inositol-phosphate phosphatase
 3-155 1.71e-55

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 177.19  E-value: 1.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   3 DPWQECMDYAVILARQAGEMIREALKNEMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFT 82
Cdd:PLN02553   5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939027  83 EQPTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEESG 155
Cdd:PLN02553  84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELG 156
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 6-162 1.12e-48

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: 159.24  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   6 QECMDYAVILARQAGEMIREALKN-EMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESvaaGEKTVFTEQ 84
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  85 PTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEEsgvLEQLLL 162
Cdd:COG0483   77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTD---LEDALV 151
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 15-139 2.74e-20

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: 85.58  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   15 LARQAGEMIREALKNEMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTEQPTWVIDPI 92
Cdd:TIGR01331   8 IARAAGEEILPVYQKELAVAQKAdnSP---VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 882939027   93 DGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGA 139
Cdd:TIGR01331  85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAA 131
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-164 5.74e-73

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: 220.87  E-value: 5.74e-73
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   8 CMDYAVILARQAGEMIREALKN-EMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  87 WVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEEsgvLEQLLLIC 164
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKE---LKDALVAT 152
Inositol_P pfam00459
Inositol monophosphatase family;
5-154 1.32e-59

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 187.94  E-value: 1.32e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027    5 WQECMDYAVI-LARQAGEMIREALKNEMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVF 81
Cdd:pfam00459   1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939027   82 TEQ-PTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEES 154
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPL 154
PLN02553 PLN02553
inositol-phosphate phosphatase
 3-155 1.71e-55

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 177.19  E-value: 1.71e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   3 DPWQECMDYAVILARQAGEMIREALKNEMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFT 82
Cdd:PLN02553   5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939027  83 EQPTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEESG 155
Cdd:PLN02553  84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELG 156
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 9-151 7.15e-52

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: 167.11  E-value: 7.15e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   9 MDYAVILARQAGEMIREALKNEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESvaAGEKTVFTEQPTWV 88
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939027  89 IDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQ 151
Cdd:cd01637   79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKD 141
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 6-162 1.12e-48

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: 159.24  E-value: 1.12e-48
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   6 QECMDYAVILARQAGEMIREALKN-EMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESvaaGEKTVFTEQ 84
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  85 PTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEEsgvLEQLLL 162
Cdd:COG0483   77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTD---LEDALV 151
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 9-113 1.91e-35

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: 123.27  E-value: 1.91e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   9 MDYAVILARQAGEMIREALKNE--MDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTEQPT 86
Cdd:cd01636    1 LEELCRVAKEAGLAILKAFGRElsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80

                         90       100
                 ....*....|....*....|....*..
gi 882939027  87 WVIDPIDGTTNFVHRFPFVAVSIGFLV 113
Cdd:cd01636   81 WVIDPIDGTKNFINGLPFVAVVIAVYV 107
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 15-156 2.65e-30

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: 111.66  E-value: 2.65e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  15 LARQAGEMIREALKNEMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEEsvaaGEKTVFTEQPTWVIDPIDG 94
Cdd:cd01643    7 IAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVIDPIDG 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939027  95 TTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKL--QVSQQEESGV 156
Cdd:cd01643   82 TTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLalHPPLQLPDCN 145
PRK10757 PRK10757
inositol-1-monophosphatase;
12-149 6.21e-25

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 97.96  E-value: 6.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  12 AVILARQAGEMIreALKNEMDVMIKSSPA---DLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESvaaGEKTVFTEQPTWV 88
Cdd:PRK10757   8 AVRAARKAGNLI--AKNYETPDAVEASQKgsnDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWV 82

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882939027  89 IDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVS 149
Cdd:PRK10757  83 IDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGS 143
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 15-157 3.46e-24

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 96.00  E-value: 3.46e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  15 LARQAGEMIREALKNEMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTEQPTWVIDPI 92
Cdd:COG1218   11 IAREAGEAILEIYRADFEVEEKAddSP---VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPL 87

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  93 DGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFC-----NGQKLQVSQQEESGVL 157
Cdd:COG1218   88 DGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPL 157
PLN02737 PLN02737
inositol monophosphatase family protein
 13-163 6.89e-24

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 97.18  E-value: 6.89e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  13 VILARQAG-EMIREALKNEMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTvftEQPTWVIDP 91
Cdd:PLN02737  83 AELAAKTGaEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS---SDYLWCIDP 158

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  92 IDGTTNFVHRFPFVAVSIGFLVNKE------MEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEEsgvLEQLLLI 163
Cdd:PLN02737 159 LDGTTNFAHGYPSFAVSVGVLFRGTpaaatvVEFVGGPMCWNTRTFSASAGGGAFCNGQKIHVSQTDK---VERSLLV 233
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 10-151 3.12e-23

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: 93.06  E-value: 3.12e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  10 DYAVILARQAGEMIREALKNEMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEktVFTEQPTWVI 89
Cdd:cd01638    3 ELLIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFWLV 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882939027  90 DPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQ 151
Cdd:cd01638   80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQ 141
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 9-149 6.99e-21

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: 86.92  E-value: 6.99e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   9 MDYAVILARQAGEMIREALKNEMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTeqptWV 88
Cdd:cd01641    2 LAFALELADAAGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV----WV 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939027  89 IDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCN---GQKLQVS 149
Cdd:cd01641   77 LDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVR 140
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 15-139 2.74e-20

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: 85.58  E-value: 2.74e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   15 LARQAGEMIREALKNEMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVFTEQPTWVIDPI 92
Cdd:TIGR01331   8 IARAAGEEILPVYQKELAVAQKAdnSP---VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 882939027   93 DGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGA 139
Cdd:TIGR01331  85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAA 131
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-140 2.79e-19

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: 83.13  E-value: 2.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   9 MDYAVILARQAGEmiREALK-----NEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAgektvftE 83
Cdd:cd01517    1 ELEVAILAVRAAA--SLTLPvfrnlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------L 71

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939027  84 QPTWVIDPIDGTTNFVHRFPFvAVSIGFLVNKEMEFGIVYSCV-------EDKMYTGRKGKGAF 140
Cdd:cd01517   72 GRFWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAW 134
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 12-154 2.79e-19

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: 82.74  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027   12 AVILARQAGEMIREALKNEMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEEsvaAGEKTVFTEQPTWVIDP 91
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 882939027   92 IDGTTNFVHRFPFVAVSIGfLVNKEME-FGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEES 154
Cdd:TIGR02067  82 IDGTKSFIRGVPVWGTLIA-LVEGGMPvLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANL 144
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
44-153 7.61e-19

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 81.88  E-value: 7.61e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  44 TVT---DQKVEKMLMSSIKEKYPCHSFIGEEsvaAGEKTVFTEQPTWVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFG 120
Cdd:PRK12676  41 TPTkliDKVAEDIILEVLKPLGRCVNIISEE---LGEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYG 117

                         90       100       110
                 ....*....|....*....|....*....|...
gi 882939027 121 IVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEE 153
Cdd:PRK12676 118 YVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSE 150
PLN02911 PLN02911
inositol-phosphate phosphatase
 10-148 3.80e-16

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 74.76  E-value: 3.80e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  10 DYAVILARQAGEMIREALKNEMDVMIK--SSPadlVTVTDQKVEKMLMSSIKEKYPCHSFIGEE-SVAAGEKtvFTEQpT 86
Cdd:PLN02911  38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSP---VTIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEG--SSDY-V 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 882939027  87 WVIDPIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQV 148
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEIST 173
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 19-153 5.49e-15

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: 71.25  E-value: 5.49e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  19 AGEMIREALKNEMDVM--------IKSSP-ADLVTVTDQKVEKMLMSSIKEKYPChSFIGEESvaaGEKtVFTEQPTW-- 87
Cdd:cd01515    5 ARNIAKEIEKAIKPLFgtedasevVKIGAdGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEI---GVI-DNGDEPEYtv 79

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 882939027  88 VIDPIDGTTNFVHRFPFVAVSIGFLVNKE--MEFGIVYSCVEDKMYTGRKGKGAFCNGQKLQVSQQEE 153
Cdd:cd01515   80 VLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSS 147
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 15-148 9.57e-10

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 56.62  E-value: 9.57e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  15 LARQAGEMIREALKNE--MDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEKTVfTEQPTWVID 90
Cdd:PRK10931   8 LARNAGDAIMQVYDGTkpLDVASKAddSP---VTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVD 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  91 PIDGTTNFVHRFPFVAVSIGFLVNKEMEFGIVYSCVEDKMYTGRKGKgAF--CNGQKLQV 148
Cdd:PRK10931  84 PLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI 142
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
51-149 2.04e-08

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 53.58  E-value: 2.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  51 EKMLMSSIkEKYPCHSFIGEEsvaAGEKTVFTEQPTW--VIDPIDGTTNFVHRFPFVAVSIG-------------FLVN- 114
Cdd:PRK14076  50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYifVLDPIDGTYNALKDIPIYSASIAiakidgfdkkikeFIGKn 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 882939027 115 ---KEMEFGIVYSCVEDKMYTGRKGKGAF----CNGQKLQVS 149
Cdd:PRK14076 126 ltiNDLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEIS 167
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 41-111 2.64e-05

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: 43.59  E-value: 2.64e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 882939027  41 DLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESvaaGEKTVFTEQPTWVIDPIDGTTNFVHRFPFVAVSIGF 111
Cdd:cd01642   34 DVTRVADLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVAL 101
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 12-123 2.92e-05

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: 43.85  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 882939027  12 AVILARQAGEMIREALKNE--MDVMI----KSSPADLVTVTDQKVEKMLMSSIKEKYPCHSFIGEESVAAGEK------- 78
Cdd:cd01640    5 LLAVAEKAGGIARDVVKKGrlLILLVegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQedesrdv 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 882939027  79 ---TVFTEQPT--------------WvIDPIDGTTNFVH-RFPFVAVSIGFLVNKEMEFGIVY 123
Cdd:cd01640   85 dldEEILEESCpspskdlpeedlgvW-VDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIH 146
 
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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