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Conserved domains on  [gi|504063338|ref|WP_014297332|]
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MULTISPECIES: inositol monophosphatase family protein [Marinitoga]

Protein Classification

inositol monophosphatase family protein( domain architecture ID 10001594)

inositol monophosphatase family protein similar to Thermotoga maritima inositol monophosphatase (I-1-Pase) that catalyzes the dephosphorylation step in the de novo biosynthetic pathway of inositol and is crucial for all inositol-dependent processes

CATH:  3.30.540.10|3.40.190.80
PubMed:  1660408
SCOP:  4002766

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 7-251 2.17e-86

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: 257.47  E-value: 2.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   7 LKDLVFNAGRKLLE-WREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPID 85
Cdd:COG0483    7 ALRAARAAGALILRrFRELDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDPID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  86 GTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNL----RGHTY 161
Cdd:COG0483   86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPylrdDREYL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 162 KFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYI 241
Cdd:COG0483  166 AALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPAL 245

                        250
                 ....*....|
gi 504063338 242 HERLLKIIQG 251
Cdd:COG0483  246 HDELLALLRE 255
 
Name Accession Description Interval E-value
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 7-251 2.17e-86

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: 257.47  E-value: 2.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   7 LKDLVFNAGRKLLE-WREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPID 85
Cdd:COG0483    7 ALRAARAAGALILRrFRELDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDPID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  86 GTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNL----RGHTY 161
Cdd:COG0483   86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPylrdDREYL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 162 KFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYI 241
Cdd:COG0483  166 AALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPAL 245

                        250
                 ....*....|
gi 504063338 242 HERLLKIIQG 251
Cdd:COG0483  246 HDELLALLRE 255
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 4-235 4.96e-78

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: 235.29  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   4 FEYLKDLVFNAGRKLLEWREEEFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY-WVID 82
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRvWVID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  83 PIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGN--LRGHT 160
Cdd:cd01637   81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNAsmLRSNR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504063338 161 YKFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAI 235
Cdd:cd01637  161 AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGI 235
Inositol_P pfam00459
Inositol monophosphatase family;
7-253 1.29e-56

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 181.77  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338    7 LKDLVFNAGRKLLEWREEEFSVNTKS--SKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY----WV 80
Cdd:pfam00459   9 AVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDdgptWI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   81 IDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKK---VIPHWNKDIESSMISLGNLR 157
Cdd:pfam00459  89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPlpvSRAPPLSEALLVTLFGVSSR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  158 GHTYK--FFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNK 232
Cdd:pfam00459 169 KDTSEasFLAKLLklVRAPGVRRVGSAALKLAMVAAGKADAYIEFgRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAG 248

                         250       260
                  ....*....|....*....|..
gi 504063338  233 KAIYSNPY-IHERLLKIIQGVQ 253
Cdd:pfam00459 249 RVIAANPKvLHELLAAALEEII 270
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
80-251 1.09e-41

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 143.12  E-value: 1.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  80 VIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISlgnLRGH 159
Cdd:PRK12676  85 VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVS---IYGY 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 160 TYKFFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISVKGN--SWDVAAGYIIVKEAGGIITDYSGNKATI-FNKKA 234
Cdd:PRK12676 162 RRGKERTVKlgRKVRRVRILGAIALELCYVASGRLDAFVDVRNYlrVTDIAAGKLICEEAGGIVTDEDGNELKLpLNVTE 241

                        170       180
                 ....*....|....*....|..
gi 504063338 235 ----IYSNP-YIHERLLKIIQG 251
Cdd:PRK12676 242 rtnlIAANGeELHKKILELLEG 263
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 13-239 6.11e-39

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: 135.66  E-value: 6.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   13 NAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED---GFDKKPSTKGYWVIDPIDGTVN 89
Cdd:TIGR01331  11 AAGEEILPVYQKELAVAQKADN-SPVTEADRAAHRFILEGLRALTPDIPVLSEEDasiPLTPRQTWQRFWLVDPLDGTKE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   90 FAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYE-----NGKKVIPHWNKDIESSMISLGnlRGH-TYKF 163
Cdd:TIGR01331  90 FINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegdgqALKAPIHVRPWPSGPLLVVIS--RSHaEEKT 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338  164 FRALENNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATiFNKKAIYSNP 239
Cdd:TIGR01331 168 TEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLgPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL-YGKRESFRNP 243
 
Name Accession Description Interval E-value
SuhB COG0483
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ...
 7-251 2.17e-86

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: 257.47  E-value: 2.17e-86
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   7 LKDLVFNAGRKLLE-WREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPID 85
Cdd:COG0483    7 ALRAARAAGALILRrFRELDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDPID 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  86 GTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNL----RGHTY 161
Cdd:COG0483   86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPylrdDREYL 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 162 KFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYI 241
Cdd:COG0483  166 AALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPAL 245

                        250
                 ....*....|
gi 504063338 242 HERLLKIIQG 251
Cdd:COG0483  246 HDELLALLRE 255
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
 4-235 4.96e-78

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: 235.29  E-value: 4.96e-78
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   4 FEYLKDLVFNAGRKLLEWREEEFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY-WVID 82
Cdd:cd01637    1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRvWVID 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  83 PIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGN--LRGHT 160
Cdd:cd01637   81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNAsmLRSNR 160

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504063338 161 YKFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAI 235
Cdd:cd01637  161 AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGI 235
IMPase cd01639
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ...
 4-232 3.58e-71

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: 218.18  E-value: 3.58e-71
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   4 FEYLKDLVFNAGRKLLE-WREEEFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVID 82
Cdd:cd01639    2 LNIAIEAARKAGEILLEaYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWIID 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  83 PIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMIS--LGNLRGHT 160
Cdd:cd01639   82 PLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVAtgFPYDRGDN 161

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338 161 YK-----FFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNK 232
Cdd:cd01639  162 FDrylnnFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSG 238
Inositol_P pfam00459
Inositol monophosphatase family;
7-253 1.29e-56

Inositol monophosphatase family;


Pssm-ID: 459820 [Multi-domain]  Cd Length: 271  Bit Score: 181.77  E-value: 1.29e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338    7 LKDLVFNAGRKLLEWREEEFSVNTKS--SKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY----WV 80
Cdd:pfam00459   9 AVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDdgptWI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   81 IDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKK---VIPHWNKDIESSMISLGNLR 157
Cdd:pfam00459  89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPlpvSRAPPLSEALLVTLFGVSSR 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  158 GHTYK--FFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNK 232
Cdd:pfam00459 169 KDTSEasFLAKLLklVRAPGVRRVGSAALKLAMVAAGKADAYIEFgRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAG 248

                         250       260
                  ....*....|....*....|..
gi 504063338  233 KAIYSNPY-IHERLLKIIQGVQ 253
Cdd:pfam00459 249 RVIAANPKvLHELLAAALEEII 270
Bacterial_IMPase_like_2 cd01643
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ...
 4-220 1.33e-52

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: 170.59  E-value: 1.33e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   4 FEYLKDLVFNAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKkPSTKGYWVIDP 83
Cdd:cd01643    1 LSLAEAIAQEAGDRALADFGNSLSAETKADG-SLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIF-PSSGWYWVIDP 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  84 IDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSmiSLGNLRGHTYKF 163
Cdd:cd01643   79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDC--NVGFNRSSRASA 156

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504063338 164 FRALENNVMR----VRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIIT 220
Cdd:cd01643  157 RAVLRVILRRfpgkIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWT 217
CysQ cd01638
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ...
 5-224 7.32e-45

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: 150.84  E-value: 7.32e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   5 EYLKDLVFNAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKG-YWVIDP 83
Cdd:cd01638    3 ELLIRIAREAGDAILEVYRGGFTVERKEDG-SPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDrFWLVDP 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  84 IDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHW---NKDIESSMISLGnlRGHT 160
Cdd:cd01638   82 LDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLqarPPPLQPLRVVAS--RSHP 159

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338 161 YKFFRALeNNVMRVRLLGTAA--LQIAYVGTGNLDAFISVKG-NSWDVAAGYIIVKEAGGIITDYSG 224
Cdd:cd01638  160 DEELEAL-LAALGVAEVVSIGssLKFCLVAEGEADIYPRLGPtMEWDTAAGDAVLRAAGGAVSDLDG 225
Arch_FBPase_1 cd01515
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ...
 52-249 1.73e-42

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: 145.21  E-value: 1.73e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  52 ELTKKFPEIGFLAEEDGFDKKPSTKGYWVI-DPIDGTVNFAKGIPNFCISAA--YVEDDEPLYGVIYAPVMNQLIYAEKG 128
Cdd:cd01515   51 EILKKLGSVNIVSEEIGVIDNGDEPEYTVVlDPLDGTYNAINGIPFYSVSVAvfKIDKSDPYYGYVYNLATGDLYYAIKG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 129 KGVYENGKKVIPHWNKDIESSMISL-GNLRGHTYKFfrALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNS--WDV 205
Cdd:cd01515  131 KGAYLNGKRIKVSDFSSLKSISVSYyIYGKNHDRTF--KICRKVRRVRIFGSVALELCYVASGALDAFVDVRENLrlVDI 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504063338 206 AAGYIIVKEAGGIITDYSGNKATI-FNKKA----IYSNPYIHERLLKII 249
Cdd:cd01515  209 AAGYLIAEEAGGIVTDENGKELKLkLNVTErvniIAANSELHKKLLELL 257
PRK12676 PRK12676
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
80-251 1.09e-41

bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;


Pssm-ID: 183673 [Multi-domain]  Cd Length: 263  Bit Score: 143.12  E-value: 1.09e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  80 VIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISlgnLRGH 159
Cdd:PRK12676  85 VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVS---IYGY 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 160 TYKFFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISVKGN--SWDVAAGYIIVKEAGGIITDYSGNKATI-FNKKA 234
Cdd:PRK12676 162 RRGKERTVKlgRKVRRVRILGAIALELCYVASGRLDAFVDVRNYlrVTDIAAGKLICEEAGGIVTDEDGNELKLpLNVTE 241

                        170       180
                 ....*....|....*....|..
gi 504063338 235 ----IYSNP-YIHERLLKIIQG 251
Cdd:PRK12676 242 rtnlIAANGeELHKKILELLEG 263
PLN02553 PLN02553
inositol-phosphate phosphatase
 36-252 1.26e-39

inositol-phosphate phosphatase


Pssm-ID: 178168 [Multi-domain]  Cd Length: 270  Bit Score: 138.28  E-value: 1.26e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEED--GFDKKPST-KGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYG 112
Cdd:PLN02553  42 DLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaASGGTELTdEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVG 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 113 VIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMIS--LGNLRGH-----TYKFFRALENNVMRVRLLGTAALQIA 185
Cdd:PLN02553 122 VVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLAteVGTKRDKatvdaTTNRINALLYKVRSLRMSGSCALNLC 201

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504063338 186 YVGTGNLDAFISVK-GNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYIHERLLKIIQGV 252
Cdd:PLN02553 202 GVACGRLDIFYEIGfGGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRVAASNGHLKDAFVEALRQT 269
CysQ COG1218
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ...
 2-247 2.10e-39

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


Pssm-ID: 440831 [Multi-domain]  Cd Length: 260  Bit Score: 137.21  E-value: 2.10e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   2 KEFEYLKDLVFNAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED---GFDKKPSTKGY 78
Cdd:COG1218    3 ALLEAAIEIAREAGEAILEIYRADFEVEEKADD-SPVTEADLAAHAIILAGLAALTPDIPVLSEESaaiPYEERKSWDRF 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  79 WVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGK-------KVIPHWNKD----IE 147
Cdd:COG1218   82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGggerqpiRVRDRPPAEplrvVA 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 148 SsmislgnlRGHTYKFFRALENNvmrvrlLGTA-------ALQIAYVGTGNLDAFISVKGNS-WDVAAGYIIVKEAGGII 219
Cdd:COG1218  162 S--------RSHRDEETEALLAR------LGVAelvsvgsSLKFCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRV 227

                        250       260       270
                 ....*....|....*....|....*....|...
gi 504063338 220 TDYSGNKATiFNKKAIYSNPYI-----HERLLK 247
Cdd:COG1218  228 TDLDGKPLR-YNKKEDLLNPGFiasgdHAAILA 259
bisphos_cysQ TIGR01331
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ...
 13-239 6.11e-39

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: 135.66  E-value: 6.11e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   13 NAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED---GFDKKPSTKGYWVIDPIDGTVN 89
Cdd:TIGR01331  11 AAGEEILPVYQKELAVAQKADN-SPVTEADRAAHRFILEGLRALTPDIPVLSEEDasiPLTPRQTWQRFWLVDPLDGTKE 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   90 FAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYE-----NGKKVIPHWNKDIESSMISLGnlRGH-TYKF 163
Cdd:TIGR01331  90 FINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegdgqALKAPIHVRPWPSGPLLVVIS--RSHaEEKT 167

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338  164 FRALENNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATiFNKKAIYSNP 239
Cdd:TIGR01331 168 TEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLgPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL-YGKRESFRNP 243
PAP_phosphatase cd01517
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ...
 25-250 3.49e-35

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: 126.66  E-value: 3.49e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  25 EFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGfdkkpSTKG-YWVIDPIDGTVNFAKGIPnFCISAAY 103
Cdd:cd01517   25 AGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS-----AALGrFWVLDPIDGTKGFLRGDQ-FAVALAL 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 104 VEDDEPLYGVIYAPVMNQ-------LIYAEKGKGVYENG--------KKVIPHWNKDIESSMISLGnlRGHTYKFFRALE 168
Cdd:cd01517   99 IEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLRPldgsslqpLSVRQLTNAARASFCESVE--SAHSSHRLQAAI 176

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 169 NNVMRVRLLGTAALQIAY--VGTGNLDAFI------SVKGNSWDVAAGYIIVKEAGGIITDYSGN------KATIFNKKA 234
Cdd:cd01517  177 KALGGTPQPVRLDSQAKYaaVARGAADFYLrlplsmSYREKIWDHAAGVLIVEEAGGKVTDADGKpldfgkGRKLLNNGG 256

                        250
                 ....*....|....*..
gi 504063338 235 -IYSNPYIHERLLKIIQ 250
Cdd:cd01517  257 lIAAPGEIHEQVLEALR 273
PRK10757 PRK10757
inositol-1-monophosphatase;
36-250 4.54e-33

inositol-1-monophosphatase;


Pssm-ID: 236753 [Multi-domain]  Cd Length: 267  Bit Score: 121.07  E-value: 4.54e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIY 115
Cdd:PRK10757  38 DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVY 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLG---NLRGHTYKFFRALENNVMRV---RLLGTAALQIAYVGT 189
Cdd:PRK10757 118 DPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGfpfKAKQHATTYINIVGKLFTECadfRRTGSAALDLAYVAA 197

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504063338 190 GNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYIHERLLKIIQ 250
Cdd:PRK10757 198 GRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMR 258
PLN02737 PLN02737
inositol monophosphatase family protein
 36-249 1.33e-31

inositol monophosphatase family protein


Pssm-ID: 215392 [Multi-domain]  Cd Length: 363  Bit Score: 119.13  E-value: 1.33e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIY 115
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVV 190

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APV------MNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNLRGH------TYKFFRALENNVMRVRLLGTAALQ 183
Cdd:PLN02737 191 EFVggpmcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHddawatNIELFKEFTDVSRGVRRLGAAAVD 270

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504063338 184 IAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYIHERLLKII 249
Cdd:PLN02737 271 MCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLVSNGVLHPKLLDRI 336
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
 5-221 3.11e-30

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: 111.33  E-value: 3.11e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   5 EYLKDLVFNAGRKLLEWREEEFSVNTKSSKF--DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKG---YW 79
Cdd:cd01636    2 EELCRVAKEAGLAILKAFGRELSGKVKITKSdnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRdeyTW 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  80 VIDPIDGTVNFAKGIPNFCISAAyveddeplygviyapVMNQLIYAEKGKgvyengkkviphwnkdiessmislgnlRGH 159
Cdd:cd01636   82 VIDPIDGTKNFINGLPFVAVVIA---------------VYVILILAEPSH---------------------------KRV 119

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504063338 160 TYKFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISV--KGNSWDVAAGYIIVKEAGGIITD 221
Cdd:cd01636  120 DEKKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPggKRRAWDVAASAAIVREAGGIMTD 183
pnk PRK14076
bifunctional NADP phosphatase/NAD kinase;
52-249 1.78e-28

bifunctional NADP phosphatase/NAD kinase;


Pssm-ID: 237601 [Multi-domain]  Cd Length: 569  Bit Score: 112.90  E-value: 1.78e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  52 ELTKKFPEIGFLAEEDGFDK--KPSTKGYWVIDPIDGTVNFAKGIPNFCISAAY----VEDDEPLYGVIYAPVMNQL--- 122
Cdd:PRK14076  55 NSLEKFCSGILISEEIGFKKigKNKPEYIFVLDPIDGTYNALKDIPIYSASIAIakidGFDKKIKEFIGKNLTINDLevg 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 123 ----------IYAEKGKGVYE--NGKKVIPHWNKDIESSMISLG----NLRGHTYKFFRalENNVMRVRLLGTAALQIAY 186
Cdd:PRK14076 135 vvkniatgdtYYAEKGEGAYLlkKGEKKKIEISNISNLKDASIGlfayGLSLDTLKFIK--DRKVRRIRLFGSIALEMCY 212

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 187 VGTGNLDAFISVKGNS--WDVAAGYIIVKEAGGIITDYSG----NKATIFNKKA-IYSNPYIHERLLKII 249
Cdd:PRK14076 213 VASGALDAFINVNETTrlCDIAAGYVICKEAGGIITNKNGkplnMKLDINEKTSvICSNEILHKKLVGIF 282
his_9_HisN TIGR02067
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ...
 55-250 2.14e-27

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: 105.46  E-value: 2.14e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   55 KKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYEN 134
Cdd:TIGR02067  53 AFFPDHGILGEEFGHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLG 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  135 GKKVIPHWNKDIESSMISLGNLR----GHTYKFFRALENNVmRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYI 210
Cdd:TIGR02067 133 GRRLRVSSCANLSDAVLFTTSPDllddPGNRPAFERLRRAA-RLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIP 211

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 504063338  211 IVKEAGGIITDYSGnKATIFNKKAIYS-NPYIHERLLKIIQ 250
Cdd:TIGR02067 212 VIEEAGGCFTDWDG-KPAPDGGGAVAAgNAMLHDEALEILN 251
Bacterial_IMPase_like_1 cd01641
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ...
 14-246 2.94e-27

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: 105.03  E-value: 2.94e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  14 AGRKLLEWREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDkkPSTKGY-WVIDPIDGTVNFAK 92
Cdd:cd01641   12 AGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNE--GGDAGYvWVLDPIDGTKSFIR 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  93 GIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNK---DIESSMISLGN---LRGHTYKFFRA 166
Cdd:cd01641   89 GLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVRacaDLAEAVLSTTDphfFTPGDRAAFER 168

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 167 LENNVMRVRlLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSN-PYIHERL 245
Cdd:cd01641  169 LARAVRLTR-YGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVVAAGdAELHEAL 247


                 .
gi 504063338 246 L 246
Cdd:cd01641  248 L 248
PRK10931 PRK10931
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
 38-224 5.09e-16

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


Pssm-ID: 182848 [Multi-domain]  Cd Length: 246  Bit Score: 75.11  E-value: 5.09e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  38 VTSLDFRVQDFLYNELTKKFPEIGFLAEED--GFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIY 115
Cdd:PRK10931  37 VTAADIAAHTVIKDGLRTLTPDIPVLSEEDppAWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVY 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APVMNQLIYAEKGKG-VYENGKK-------------VI--PHWNKDIESSMISLGNLR----GHTYKFFRALEnnvmrvr 175
Cdd:PRK10931 117 APVMNVMYSAAEGKAwKEECGVRkqiqvrdarpplvVIsrSHADAELKEYLQQLGEHQttsiGSSLKFCLVAE------- 189

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 504063338 176 llGTAALQIAYVGTgnldafisvkgNSWDVAAGYIIVKEAGGIITDYSG 224
Cdd:PRK10931 190 --GQAQLYPRFGPT-----------NIWDTAAGHAVAIAAGAHVHDWQG 225
PLN02911 PLN02911
inositol-phosphate phosphatase
 53-252 3.28e-15

inositol-phosphate phosphatase


Pssm-ID: 178499 [Multi-domain]  Cd Length: 296  Bit Score: 73.60  E-value: 3.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  53 LTKKFPEIGFLAEEDGFDKKPSTKGY-WVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGV 131
Cdd:PLN02911  85 ILENFPSHAIFGEEHGLRCGEGSSDYvWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRAT 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 132 YENGKKVIPHWNKDIESSMI---SLGNLRGHTYKFFRALENNVmRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAG 208
Cdd:PLN02911 165 TLNGEEISTRSCASLKDAYLyttSPHMFSGDAEDAFARVRDKV-KVPLYGCDCYAYGLLASGHVDLVVESGLKPYDYLAL 243

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 504063338 209 YIIVKEAGGIITDYSGNK----------ATIFNKKAIySNPYIHERLLKIIQGV 252
Cdd:PLN02911 244 VPVVEGAGGVITDWKGRKlrwepspgslATSFNVVAA-GDARLHKQALDILEWQ 296
IPPase cd01640
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ...
 30-226 1.02e-12

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: 66.19  E-value: 1.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  30 TKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED-------------GFDK--------------KPSTKGYWvID 82
Cdd:cd01640   34 TKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDnefenqedesrdvDLDEeileescpspskdlPEEDLGVW-VD 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  83 PIDGTVNFAKGIPNFC-ISAAYVEDDEPLYGVIYAP----------VMNQLIYAEKGKGVY-------ENGKKVIPHWnk 144
Cdd:cd01640  113 PLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQPfyektagagaWLGRTIWGLSGLGAHssdfkerEDAGKIIVST-- 190

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 145 dIESSMISLgnlrgHTYKFFRaLENNVMRVRLLGTAALQIAyvgTGNLDAFISVKGNS--WDVAAGYIIVKEAGGIITDY 222
Cdd:cd01640  191 -SHSHSVKE-----VQLITAG-NKDEVLRAGGAGYKVLQVL---EGLADAYVHSTGGIkkWDICAPEAILRALGGDMTDL 260


                 ....
gi 504063338 223 SGNK 226
Cdd:cd01640  261 HGEP 264
Arch_FBPase_2 cd01642
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ...
 36-216 1.66e-11

Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.


Pssm-ID: 238820 [Multi-domain]  Cd Length: 244  Bit Score: 62.47  E-value: 1.66e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPlygvIY 115
Cdd:cd01642   34 DVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSK----VK 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APVMNQLIYAEKGKGVY-ENGKKVIPHWNKDIESSMISLGNLRGHTYK------FFRALENNVMRVRLLGTAALQIAYVG 188
Cdd:cd01642  110 AATLDNFVSGEGGLKVYsPPTRFSYISVPKLGPPLVPEVPSKIGIYEGssrnpeKFLLLSRNGLKFRSLGSAALELAYTC 189

                        170       180       190
                 ....*....|....*....|....*....|
gi 504063338 189 TGNLDAFISVKGN--SWDVAAGYIIVKEAG 216
Cdd:cd01642  190 EGSFVLFLDLRGKlrNFDVAAALGACKRLG 219
bisphos_HAL2 TIGR01330
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ...
 23-224 1.09e-10

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: 60.65  E-value: 1.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   23 EEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED----------------------------GFDKKPS 74
Cdd:TIGR01330  30 HKDSTVITKDDK-SPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDssglseadftlgrvnelvnetlvyaknyKKDDQFP 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338   75 TKG--------------------YWVIDPIDGTVNFAKGiPNFCISAAYVEDDEPLYGVIYAPVM--------------- 119
Cdd:TIGR01330 109 LKSledvlqiidfgnyeggrkgrHWVLDPIDGTKGFLRG-DQYAVCLALIENGKVVLGVIGCPNLplssygaqnlkgses 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338  120 -NQLIYAEKGKGVY--------ENGKKVIPHWNKDIESSMISLGNLRGHTYKFFRALENNVMRVRLLGT---AALQIAYV 187
Cdd:TIGR01330 188 kGCIFRAVRGSGAFmyslssdaESPTKVHVSSVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLrldSQAKYAAL 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 504063338  188 GTGNLDAFI------SVKGNSWDVAAGYIIVKEAGGIITDYSG 224
Cdd:TIGR01330 268 ARGDADVYLrlpiklSYQEKIWDHAAGNVIVEEAGGIVTDAMG 310
 
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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