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Conserved domains on  [gi|1848404389|ref|WP_172690522|]
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inositol monophosphatase family protein [Rhizobium rhizogenes]

Protein Classification

FIG domain-containing protein( domain architecture ID 299)

FIG (FBPase/IMPase/glpX-like) domain-containing protein belongs to a superfamily of metal-dependent phosphatases with various substrates; such as fructose-1,6-bisphosphatase (both the major and the glpX-encoded variant), inositol-monophosphatases and inositol polyphosphatases

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
FIG super family cl00289
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 15-227 3.33e-81

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+.


The actual alignment was detected with superfamily member cd01643:

Pssm-ID: 469707 [Multi-domain]  Cd Length: 242  Bit Score: 243.78  E-value: 3.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGRVWVIDP 94
Cdd:cd01643     1 LSLAEAIAQEAGDRALADFGN--SLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWYWVIDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  95 IDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRASTGFSRFI------ 168
Cdd:cd01643    79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSrasara 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848404389 169 -----SDDLKISFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPILGHLGISNTIDWDR 227
Cdd:cd01643   159 vlrviLRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEE 222
 
Name Accession Description Interval E-value
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 15-227 3.33e-81

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: 243.78  E-value: 3.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGRVWVIDP 94
Cdd:cd01643     1 LSLAEAIAQEAGDRALADFGN--SLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWYWVIDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  95 IDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRASTGFSRFI------ 168
Cdd:cd01643    79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSrasara 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848404389 169 -----SDDLKISFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPILGHLGISNTIDWDR 227
Cdd:cd01643   159 vlrviLRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEE 222
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 12-214 3.68e-66

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: 205.85  E-value: 3.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  12 QDTAAIVEKIARKAGERALDHFRSLSsLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA-SGRVW 90
Cdd:COG0483     1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRdSGYVW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  91 VIDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA--STGFSRFI 168
Cdd:COG0483    80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDAlvATGFPYLR 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1848404389 169 SDDLKI-----------SFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPIL 214
Cdd:COG0483   160 DDREYLaalaallprvrRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIV 216
Inositol_P pfam00459
Inositol monophosphatase family;
12-214 3.60e-45

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 152.50  E-value: 3.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  12 QDTAAIVEKIARKAGERALDHFRSlsSLPVETKGHL---DLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIP----- 83
Cdd:pfam00459   3 EEVLKVAVELAAKAGEILREAFSN--KLTIEEKGKSganDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGdqtel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  84 GASGRVWVIDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRAS-- 161
Cdd:pfam00459  81 TDDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALlv 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848404389 162 TGFSR----------FISDDLKI----SFRFCGAATLSMIEVAMGETDGYVSLGDL-TWDVMAALPIL 214
Cdd:pfam00459 161 TLFGVssrkdtseasFLAKLLKLvrapGVRRVGSAALKLAMVAAGKADAYIEFGRLkPWDHAAGVAIL 228
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 15-229 1.72e-32

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: 118.95  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlSSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIP-GASGRVWVID 93
Cdd:TIGR02067   2 LAFAEDLADAAGETILPFFRA-SLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEeGDAERVWVLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  94 PIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA---STGFSRFISD 170
Cdd:TIGR02067  81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAvlfTTSPDLLDDP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848404389 171 DLKISFRFCGAATL---------SMIEVAMGETDGYVSLGDLTWDVMAALPILGHLGISNTiDWDRID 229
Cdd:TIGR02067 161 GNRPAFERLRRAARltryggdcyAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFT-DWDGKP 227
PLN02553 PLN02553
inositol-phosphate phosphatase
 16-214 2.58e-32

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 119.02  E-value: 2.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRSLSSlpVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA----SGRVWV 91
Cdd:PLN02553   12 EVAVDAAKAAGQIIRKGFYQTKH--VEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGteltDEPTWI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  92 IDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRASTG-------- 163
Cdd:PLN02553   90 VDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLAtevgtkrd 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389 164 -------FSRFISDDLKI-SFRFCGAATLSMIEVAMGETDGYVSLG-DLTWDVMAALPIL 214
Cdd:PLN02553  170 katvdatTNRINALLYKVrSLRMSGSCALNLCGVACGRLDIFYEIGfGGPWDVAAGAVIV 229
 
Name Accession Description Interval E-value
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 15-227 3.33e-81

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: 243.78  E-value: 3.33e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGRVWVIDP 94
Cdd:cd01643     1 LSLAEAIAQEAGDRALADFGN--SLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWYWVIDP 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  95 IDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRASTGFSRFI------ 168
Cdd:cd01643    79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSrasara 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848404389 169 -----SDDLKISFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPILGHLGISNTIDWDR 227
Cdd:cd01643   159 vlrviLRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEE 222
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 12-214 3.68e-66

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: 205.85  E-value: 3.68e-66
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  12 QDTAAIVEKIARKAGERALDHFRSLSsLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA-SGRVW 90
Cdd:COG0483     1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRdSGYVW 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  91 VIDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA--STGFSRFI 168
Cdd:COG0483    80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDAlvATGFPYLR 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1848404389 169 SDDLKI-----------SFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPIL 214
Cdd:COG0483   160 DDREYLaalaallprvrRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIV 216
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 16-214 3.51e-53

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: 172.11  E-value: 3.51e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRSlsSLPVETKGHL-DLVTEADKDVEAFLIGSLREAFPDDGIMGEESGE--IPGASGRVWVI 92
Cdd:cd01637     2 ELALKAVREAGALILEAFGE--ELTVETKKGDgDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGsgNVSDGGRVWVI 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  93 DPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA--STGFSRFISD 170
Cdd:cd01637    80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDAllSTNASMLRSN 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1848404389 171 DLKI---------SFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPIL 214
Cdd:cd01637   160 RAAVlaslvnralGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIV 212
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 17-214 8.28e-51

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: 166.17  E-value: 8.28e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  17 IVEKIARKAGERALDHFRSLSsLPVETKGHL-DLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA-SGRVWVIDP 94
Cdd:cd01639     4 IAIEAARKAGEILLEAYEKLG-LNVEEKGSPvDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLtDEPTWIIDP 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  95 IDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA--STGFSRFISDDL 172
Cdd:cd01639    83 LDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDAlvATGFPYDRGDNF 162

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1848404389 173 K--------------ISFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPIL 214
Cdd:cd01639   163 DrylnnfakllakavRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIV 218
Inositol_P pfam00459
Inositol monophosphatase family;
12-214 3.60e-45

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 152.50  E-value: 3.60e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  12 QDTAAIVEKIARKAGERALDHFRSlsSLPVETKGHL---DLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIP----- 83
Cdd:pfam00459   3 EEVLKVAVELAAKAGEILREAFSN--KLTIEEKGKSganDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGdqtel 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  84 GASGRVWVIDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRAS-- 161
Cdd:pfam00459  81 TDDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALlv 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848404389 162 TGFSR----------FISDDLKI----SFRFCGAATLSMIEVAMGETDGYVSLGDL-TWDVMAALPIL 214
Cdd:pfam00459 161 TLFGVssrkdtseasFLAKLLKLvrapGVRRVGSAALKLAMVAAGKADAYIEFGRLkPWDHAAGVAIL 228
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 16-210 1.90e-42

CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).


Pssm-ID: 238816 [Multi-domain]  Cd Length: 242  Bit Score: 144.68  E-value: 1.90e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA--SGRVWVID 93
Cdd:cd01638     3 ELLIRIAREAGDAILEVYRG--GFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRlgWDRFWLVD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  94 PIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDM------------SRAS 161
Cdd:cd01638    81 PLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPpplqplrvvasrSHPD 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1848404389 162 TGFSRFISDDLKISFRFCGAAtLSMIEVAMGETDGYVSLGDLT-WDVMAA 210
Cdd:cd01638   161 EELEALLAALGVAEVVSIGSS-LKFCLVAEGEADIYPRLGPTMeWDTAAG 209
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 15-214 1.16e-40

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: 140.47  E-value: 1.16e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGRVWVIDP 94
Cdd:cd01641     2 LAFALELADAAGQITLPYFRT--RLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYVWVLDP 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  95 IDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPL-----PALDMSRASTGFSRFIS 169
Cdd:cd01641    80 IDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLrvracADLAEAVLSTTDPHFFT 159

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1848404389 170 DDLKISF----------RF---CGAATLsmieVAMGETDGYVSLGDLTWDVMAALPIL 214
Cdd:cd01641   160 PGDRAAFerlaravrltRYggdCYAYAL----VASGRVDLVVEAGLKPYDVAALIPII 213
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 16-210 2.80e-34

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 124.12  E-value: 2.80e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGAS----GRVWV 91
Cdd:COG1218     6 EAAIEIAREAGEAILEIYRA--DFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEErkswDRFWL 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  92 IDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGK----------TVPTRLNGQPIKPLPALD--MSR 159
Cdd:COG1218    84 VDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKgqgafketggGERQPIRVRDRPPAEPLRvvASR 163

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1848404389 160 --ASTGFSRFISDDLKISFRFCGAAtLSMIEVAMGETDGYVSLGDlT--WDvMAA 210
Cdd:COG1218   164 shRDEETEALLARLGVAELVSVGSS-LKFCLVAEGEADLYPRLGP-TmeWD-TAA 215
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 15-229 1.72e-32

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: 118.95  E-value: 1.72e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlSSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIP-GASGRVWVID 93
Cdd:TIGR02067   2 LAFAEDLADAAGETILPFFRA-SLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEeGDAERVWVLD 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  94 PIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA---STGFSRFISD 170
Cdd:TIGR02067  81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAvlfTTSPDLLDDP 160

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1848404389 171 DLKISFRFCGAATL---------SMIEVAMGETDGYVSLGDLTWDVMAALPILGHLGISNTiDWDRID 229
Cdd:TIGR02067 161 GNRPAFERLRRAARltryggdcyAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFT-DWDGKP 227
PLN02553 PLN02553
inositol-phosphate phosphatase
 16-214 2.58e-32

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 119.02  E-value: 2.58e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRSLSSlpVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA----SGRVWV 91
Cdd:PLN02553   12 EVAVDAAKAAGQIIRKGFYQTKH--VEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGteltDEPTWI 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  92 IDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRASTG-------- 163
Cdd:PLN02553   90 VDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLAtevgtkrd 169

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389 164 -------FSRFISDDLKI-SFRFCGAATLSMIEVAMGETDGYVSLG-DLTWDVMAALPIL 214
Cdd:PLN02553  170 katvdatTNRINALLYKVrSLRMSGSCALNLCGVACGRLDIFYEIGfGGPWDVAAGAVIV 229
PRK10757 PRK10757
inositol-1-monophosphatase;
17-209 6.20e-30

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 112.98  E-value: 6.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  17 IVEKIARKAGERALDHFRSLSSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGRV-WVIDPI 95
Cdd:PRK10757    7 IAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVqWVIDPL 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  96 DGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPA--LDMSRASTGF--------S 165
Cdd:PRK10757   87 DGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTArdLDGTILATGFpfkakqhaT 166

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1848404389 166 RFISDDLKI-----SFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMA 209
Cdd:PRK10757  167 TYINIVGKLftecaDFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAA 215
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 16-137 2.25e-28

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: 108.94  E-value: 2.25e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRSLSSL-PVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEipgASGRVWVIDP 94
Cdd:cd01517     3 EVAILAVRAAASLTLPVFRNLGAGdVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA---ALGRFWVLDP 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1848404389  95 IDGTFNFVRGGQnWAISIGLYENRRPSFGVIYAPVRDLILVGG 137
Cdd:cd01517    80 IDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLDDGGG 121
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 17-235 5.87e-28

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: 107.15  E-value: 5.87e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  17 IVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGRV----WVI 92
Cdd:TIGR01331   4 DVIKIARAAGEEILPVYQK--ELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTwqrfWLV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  93 DPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVG-------------GKTVPTRLNGQPIKPLPALDMSR 159
Cdd:TIGR01331  82 DPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFAtagkaakregdgqALKAPIHVRPWPSGPLLVVISRS 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1848404389 160 ASTGFSRFISDDLKISFRFCGAATLSMIEVAMGETDGYVSLG-DLTWDVMAALPILGHLGiSNTIDWDRIDLSSKLR 235
Cdd:TIGR01331 162 HAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAG-GAIFDLDGSPLLYGKR 237
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 15-219 4.28e-26

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: 100.54  E-value: 4.28e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHF-RSLSSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEI----PGASGRV 89
Cdd:cd01636     1 LEELCRVAKEAGLAILKAFgRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAeevmGRRDEYT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  90 WVIDPIDGTFNFVRGGQNWAISIGLYenrrpsfgviyapvrdlilvggktVPTRLNGQPIKPLP---ALDMSRASTGFSR 166
Cdd:cd01636    81 WVIDPIDGTKNFINGLPFVAVVIAVY------------------------VILILAEPSHKRVDekkAELQLLAVYRIRI 136

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1848404389 167 FisddlkisfrfcGAATLSMIEVAMGETDGYVSLGDLT--WDVMAALPILGHLGI 219
Cdd:cd01636   137 V------------GSAVAKMCLVALGLADIYYEPGGKRraWDVAASAAIVREAGG 179
PLN02911 PLN02911
inositol-phosphate phosphatase
 15-225 9.13e-22

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 91.70  E-value: 9.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  15 AAIVEKIARKAGERALDHFRSlsSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESG-EIP-GASGRVWVI 92
Cdd:PLN02911   37 VDVAHKLADAAGEVTRKYFRT--KFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGlRCGeGSSDYVWVL 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  93 DPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKPLPALDMSRA---STGFSRFIS 169
Cdd:PLN02911  115 DPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAylyTTSPHMFSG 194

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848404389 170 DDLKISFRFCGAATLSMIE--------VAMGETDGYVSLGDLTWDVMAALPILGHLGISNTiDW 225
Cdd:PLN02911  195 DAEDAFARVRDKVKVPLYGcdcyayglLASGHVDLVVESGLKPYDYLALVPVVEGAGGVIT-DW 257
PLN02737 PLN02737
inositol monophosphatase family protein
 16-218 1.51e-20

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 89.47  E-value: 1.51e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGE---RALDHFRSLSSlpvetKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGA-SGRVWV 91
Cdd:PLN02737   81 AVAELAAKTGAEvvmEAVNKPRNISY-----KGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSsSDYLWC 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  92 IDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYApvrdliLVGG-KTVPTRL-----------NGQPIKPLPALDMSR 159
Cdd:PLN02737  156 IDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVE------FVGGpMCWNTRTfsasagggafcNGQKIHVSQTDKVER 229

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1848404389 160 A--STGFSRFISD-------------DLKISFRFCGAATLSMIEVAMGETDGYVSLGDLTWDVMAALPILGHLG 218
Cdd:PLN02737  230 SllVTGFGYEHDDawatnielfkeftDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAG 303
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
74-200 8.35e-13

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 66.47  E-value: 8.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  74 IMGEESGEIPGaSGRVW--VIDPIDGTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLILVGGKTVPTRLNGQPIKP 151
Cdd:PRK12676   67 IISEELGEIVG-NGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKV 145

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1848404389 152 -----LPALDMSraSTGFSRFISDDLKIS-----FRFCGAATLSMIEVAMGETDGYVSL 200
Cdd:PRK12676  146 sktseLNESAVS--IYGYRRGKERTVKLGrkvrrVRILGAIALELCYVASGRLDAFVDV 202
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 13-128 1.42e-11

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: 63.35  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  13 DTAAIVEKIARKAGERALDHFRSLSSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGE----------- 81
Cdd:TIGR01330   7 DVATQAVRLASLLTKKVQSELISHKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSglseadftlgr 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  82 --------------------------------------IPGASGRVWVIDPIDGTFNFVRGGQnWAISIGLYENRRPSFG 123
Cdd:TIGR01330  87 vnelvnetlvyaknykkddqfplksledvlqiidfgnyEGGRKGRHWVLDPIDGTKGFLRGDQ-YAVCLALIENGKVVLG 165


                  ....*
gi 1848404389 124 VIYAP 128
Cdd:TIGR01330 166 VIGCP 170
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 16-219 5.73e-11

IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.


Pssm-ID: 238818 [Multi-domain]  Cd Length: 293  Bit Score: 61.18  E-value: 5.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  16 AIVEKIARKAGERALDHFRS--LSSLPVE---TKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEESGE--------- 81
Cdd:cd01640     3 RSLLAVAEKAGGIARDVVKKgrLLILLVEgktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEfenqedesr 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  82 -------------------IPGASGRVWvIDPIDGTFNFVRGG-QNWAISIGLYENRRPSFGVIYAP----------VRD 131
Cdd:cd01640    83 dvdldeeileescpspskdLPEEDLGVW-VDPLDATQEYTEGLlEYVTVLIGVAVKGKPIAGVIHQPfyektagagaWLG 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389 132 LILVGGKTVPTR-LNGQPIKPLPALDMSRASTGF---SRFISDDLKISFRFCGAATLSMIEVAMGETDGYV--SLGDLTW 205
Cdd:cd01640   162 RTIWGLSGLGAHsSDFKEREDAGKIIVSTSHSHSvkeVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVhsTGGIKKW 241

                         250
                  ....*....|....
gi 1848404389 206 DVMAALPILGHLGI 219
Cdd:cd01640   242 DICAPEAILRALGG 255
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 20-133 2.14e-10

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 59.32  E-value: 2.14e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  20 KIARKAGERALDHFRSLSSLPVETKGHLDLVTEADKDVEAFLIGSLREAFPDDGIMGEE---SGEIPGASGRVWVIDPID 96
Cdd:PRK10931    7 QLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEdppAWEVRQHWQRYWLVDPLD 86

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1848404389  97 GTFNFVRGGQNWAISIGLYENRRPSFGVIYAPVRDLI 133
Cdd:PRK10931   87 GTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVM 123
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 48-211 3.32e-10

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: 58.61  E-value: 3.32e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  48 DLVTEADKDVEAFLIGSLREAFPDDGIMGEESGEIPGASGR-VWVIDPIDGTFNFVRGGQNWAISIGLYENRRPS----- 121
Cdd:cd01642    34 DVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEyIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVkaatl 113

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389 122 FGVIYAPVRDLILVGGKT-VPTRLNGQPIKPLPALDMSRAST-GFSRFISDDLKIS-----FRFCGAATLSMIEVAMGET 194
Cdd:cd01642   114 DNFVSGEGGLKVYSPPTRfSYISVPKLGPPLVPEVPSKIGIYeGSSRNPEKFLLLSrnglkFRSLGSAALELAYTCEGSF 193

                         170
                  ....*....|....*....
gi 1848404389 195 DGYVSLGDLT--WDVMAAL 211
Cdd:cd01642   194 VLFLDLRGKLrnFDVAAAL 212
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 53-200 2.31e-08

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: 53.54  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389  53 ADKDVEAFLIGSLREAFPDDgIMGEESGEI--PGASGRVWVIDPIDGTFNFVRGGQNWAISIGLYENRR--PSFGVIYAP 128
Cdd:cd01515    41 IDKVAEDAAIEILKKLGSVN-IVSEEIGVIdnGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNL 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1848404389 129 VRDLILVGGKTVPTRLNGQPIKPLPALDMSRASTGFS----RFISDDLKIS----FRFCGAATLSMIEVAMGETDGYVSL 200
Cdd:cd01515   120 ATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYiygkNHDRTFKICRkvrrVRIFGSVALELCYVASGALDAFVDV 199
 
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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