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Conserved domains on  [gi|221625507|ref|NP_001138351|]
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inositol monophosphatase 1 isoform 3 [Homo sapiens]

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; it belongs to a family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. Inositol 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. Also similar to some bacterial members of the inositol monophosphatase family classified as SuhB-like; Escherichia 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

EC:  3.1.3.-
Gene Ontology:  GO:0008934|GO:0006020|GO:0046855|GO:0046872

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 1.12e-78

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: 235.12  E-value: 1.12e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   8 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 86
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221625507  87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEgsgVLEQQLLIC 164
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK---ELKDALVAT 152
 
Name Accession Description Interval E-value
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 8-164 1.12e-78

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: 235.12  E-value: 1.12e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   8 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 86
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221625507  87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEgsgVLEQQLLIC 164
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK---ELKDALVAT 152
Inositol_P pfam00459
Inositol monophosphatase family;
5-152 3.20e-64

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 199.11  E-value: 3.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507    5 WQECMDY-AVTLARQAGEVVCEAIKNEMNVMLKS--SPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSIL 81
Cdd:pfam00459   1 DLEEVLKvAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221625507   82 TDN-PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQE 152
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAP 152
PLN02553 PLN02553
inositol-phosphate phosphatase
 3-152 2.60e-58

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 184.12  E-value: 2.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   3 DPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILT 82
Cdd:PLN02553   5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  83 DNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQE 152
Cdd:PLN02553  84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQS 153
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 6-150 1.15e-49

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: 161.55  E-value: 1.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   6 QECMDYAVTLARQAGEVVCEAIKN-EMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltDN 84
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221625507  85 PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQ 150
Cdd:COG0483   77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSA 142
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 15-139 8.00e-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: 84.04  E-value: 8.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   15 LARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPI 92
Cdd:TIGR01331   8 IARAAGEEILPVYQKELAVAQKAdnSPV---TEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 221625507   93 DGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGA 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 1.12e-78

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: 235.12  E-value: 1.12e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   8 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 86
Cdd:cd01639    1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 221625507  87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEgsgVLEQQLLIC 164
Cdd:cd01639   78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRK---ELKDALVAT 152
Inositol_P pfam00459
Inositol monophosphatase family;
5-152 3.20e-64

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 199.11  E-value: 3.20e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507    5 WQECMDY-AVTLARQAGEVVCEAIKNEMNVMLKS--SPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSIL 81
Cdd:pfam00459   1 DLEEVLKvAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221625507   82 TDN-PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQE 152
Cdd:pfam00459  81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAP 152
PLN02553 PLN02553
inositol-phosphate phosphatase
 3-152 2.60e-58

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 184.12  E-value: 2.60e-58
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   3 DPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILT 82
Cdd:PLN02553   5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  83 DNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQE 152
Cdd:PLN02553  84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQS 153
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 9-151 2.35e-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: 167.88  E-value: 2.35e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   9 MDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaAGEKSILTDNPTWI 88
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221625507  89 IDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQ 151
Cdd:cd01637   79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKD 141
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 6-150 1.15e-49

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: 161.55  E-value: 1.15e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   6 QECMDYAVTLARQAGEVVCEAIKN-EMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltDN 84
Cdd:COG0483    1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SG 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221625507  85 PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQ 150
Cdd:COG0483   77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSA 142
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 9-113 8.24e-40

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: 134.06  E-value: 8.24e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   9 MDYAVTLARQAGEVVCEAIKNEMNVML--KSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPT 86
Cdd:cd01636    1 LEELCRVAKEAGLAILKAFGRELSGKVkiTKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80

                         90       100
                 ....*....|....*....|....*..
gi 221625507  87 WIIDPIDGTTNFVHRFPFVAVSIGFAV 113
Cdd:cd01636   81 WVIDPIDGTKNFINGLPFVAVVIAVYV 107
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 10-150 3.39e-29

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: 3.39e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  10 DYAVTLARQAGEVVCEAIKNEMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEEsvaaGEKSILTDNPTWII 89
Cdd:cd01643    2 SLAEAIAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVI 76

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 221625507  90 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQ 150
Cdd:cd01643   77 DPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHP 137
PRK10757 PRK10757
inositol-1-monophosphatase;
12-149 7.25e-28

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 105.66  E-value: 7.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  12 AVTLARQAGEVVCEAIKNEMNVML--KSSPvDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaaGEKSILTDNPTWII 89
Cdd:PRK10757   8 AVRAARKAGNLIAKNYETPDAVEAsqKGSN-DFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVI 83

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  90 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVS 149
Cdd:PRK10757  84 DPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGS 143
PLN02737 PLN02737
inositol monophosphatase family protein
 4-163 1.27e-27

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 106.81  E-value: 1.27e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   4 PWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltD 83
Cdd:PLN02737  75 PAEELLAVAELAAKTGAEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS---S 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  84 NPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKM------YTARKGKGAFCNGQKLQVSQQEGsgvL 157
Cdd:PLN02737 151 DYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPMcwntrtFSASAGGGAFCNGQKIHVSQTDK---V 227


                 ....*.
gi 221625507 158 EQQLLI 163
Cdd:PLN02737 228 ERSLLV 233
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 10-151 5.21e-25

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: 97.30  E-value: 5.21e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  10 DYAVTLARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksILTDNPTW 87
Cdd:cd01638    3 ELLIRIAREAGDAILEVYRGGFTVERKEdgSPV---TAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFW 77

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221625507  88 IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQ 151
Cdd:cd01638   78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQ 141
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 12-157 3.77e-24

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 95.61  E-value: 3.77e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  12 AVTLARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWII 89
Cdd:COG1218    8 AIEIAREAGEAILEIYRADFEVEEKAddSPV---TEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLV 84

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221625507  90 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFC-----NGQKLQVSQQEGSGVL 157
Cdd:COG1218   85 DPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPL 157
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 9-140 6.51e-24

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: 95.07  E-value: 6.51e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   9 MDYAVTLARQAGEVVCEAIKNEMN---VMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAgeksiltDNP 85
Cdd:cd01517    1 ELEVAILAVRAAASLTLPVFRNLGagdVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGR 73

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221625507  86 TWIIDPIDGTTNFVHRFPFvAVSIGFAVNKKIEFGVVYSCV-------EGKMYTARKGKGAF 140
Cdd:cd01517   74 FWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAW 134
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
47-151 5.62e-22

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 89.97  E-value: 5.62e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  47 DQKVEKMLISSIKEKYPSHSFIGEEsvaAGEksILTDNPTW--IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYS 124
Cdd:PRK12676  47 DKVAEDIILEVLKPLGRCVNIISEE---LGE--IVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYN 121

                         90       100
                 ....*....|....*....|....*..
gi 221625507 125 CVEGKMYTARKGKGAFCNGQKLQVSQQ 151
Cdd:PRK12676 122 LATGDFYEAIPGKGAYLNGKPIKVSKT 148
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 15-139 8.00e-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: 84.04  E-value: 8.00e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   15 LARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPI 92
Cdd:TIGR01331   8 IARAAGEEILPVYQKELAVAQKAdnSPV---TEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 221625507   93 DGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGA 139
Cdd:TIGR01331  85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAA 131
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 9-149 4.69e-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: 81.92  E-value: 4.69e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   9 MDYAVTLARQAGEVVCEAIKNEMNVMLK--SSPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTdnpt 86
Cdd:cd01641    2 LAFALELADAAGQITLPYFRTRLQVETKadFSPV---TEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV---- 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 221625507  87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCN---GQKLQVS 149
Cdd:cd01641   75 WVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVR 140
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 12-152 1.81e-18

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: 80.43  E-value: 1.81e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507   12 AVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaagEKSILTDNP-TWIID 90
Cdd:TIGR02067   5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEF----GHNEEGDAErVWVLD 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221625507   91 PIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQE 152
Cdd:TIGR02067  81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCA 142
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 47-152 1.11e-16

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: 75.49  E-value: 1.11e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  47 DQKVEKMLISSIKeKYPSHSFIGEESvaaGEKSIlTDNPTW--IIDPIDGTTNFVHRFPFVAVSIGFAVNKK--IEFGVV 122
Cdd:cd01515   42 DKVAEDAAIEILK-KLGSVNIVSEEI---GVIDN-GDEPEYtvVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYV 116

                         90       100       110
                 ....*....|....*....|....*....|
gi 221625507 123 YSCVEGKMYTARKGKGAFCNGQKLQVSQQE 152
Cdd:cd01515  117 YNLATGDLYYAIKGKGAYLNGKRIKVSDFS 146
PLN02911 PLN02911
inositol-phosphate phosphatase
 10-148 1.77e-12

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 64.36  E-value: 1.77e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  10 DYAVTLARQAGEVVCEAIKNEMNVMLK--SSPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEE-SVAAGEKSiltDNPT 86
Cdd:PLN02911  38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSPV---TIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEGS---SDYV 111

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 221625507  87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQV 148
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEIST 173
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
51-149 2.11e-12

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 64.75  E-value: 2.11e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  51 EKMLISSIkEKYPSHSFIGEEsvaAGEKSILTDNPTWI--IDPIDGTTNFVHRFPFVAVSIGFA--------------VN 114
Cdd:PRK14076  50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIAIAkidgfdkkikefigKN 125

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 221625507 115 KKI---EFGVVYSCVEGKMYTARKGKGAF----CNGQKLQVS 149
Cdd:PRK14076 126 LTIndlEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEIS 167
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 15-148 1.80e-10

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 58.17  E-value: 1.80e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  15 LARQAGEVVCEAIKNE--MNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEEsvaageksiltDNPTW--- 87
Cdd:PRK10931   8 LARNAGDAIMQVYDGTkpLDVASKAddSPV---TAADIAAHTVIKDGLRTLTPDIPVLSEE-----------DPPAWevr 73

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  88 -------IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKgAF--CNGQKLQV 148
Cdd:PRK10931  74 qhwqrywLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI 142
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 12-123 6.05e-07

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: 48.47  E-value: 6.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  12 AVTLARQAGEVVCEAIKNEMNVML------KSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGE-------- 77
Cdd:cd01640    5 LLAVAEKAGGIARDVVKKGRLLILlvegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENqedesrdv 84

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221625507  78 -----------KSILTDNP-----TWIiDPIDGTTNFVH-RFPFVAVSIGFAVNKKIEFGVVY 123
Cdd:cd01640   85 dldeeileescPSPSKDLPeedlgVWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIH 146
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 47-129 3.99e-06

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: 45.90  E-value: 3.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625507  47 DQKVEKMLISSIKEKYPSHSFIGEESvaaGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFA-VNKKIEFGVVYSC 125
Cdd:cd01642   40 DLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALAdPRSKVKAATLDNF 116


                 ....
gi 221625507 126 VEGK 129
Cdd:cd01642  117 VSGE 120
 
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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