|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-267 |
0e+00 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 529.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 1 MHPMLNIAIRAARKAGNHIAKNYEMPSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 81 WVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 161 QKQHAAVYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 1327839123 241 NLVAGSPRVVRDILSVMKNELSESLKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
9.78e-130 |
|
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: 367.25 E-value: 9.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAKNYEMPsNIKVTQKG-TNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQWV 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKL-GLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 83 IDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQK 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 163 QHAAVYMNIMTAMFDK-CADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASGN 241
Cdd:cd01639 160 DNFDRYLNNFAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*
gi 1327839123 242 LVAGS 246
Cdd:cd01639 240 ILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
4.44e-125 |
|
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: 356.08 E-value: 4.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 2 HPMLNIAIRAARKAGNHIAKNYEmPSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFR-ELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 82 VIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQ 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 162 KQHAavYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*...
gi 1327839123 242 LVAGSPRVVRDILSVMKN 259
Cdd:COG0483 238 LVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-249 |
6.38e-82 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 246.87 E-value: 6.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 1 MHPMLNIAIRAARKAGNHIAKNYEMPSNIKV-TQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGK---- 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEkGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQtelt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 76 DDDIQWVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 156 GFPFKQKQHAAVYMNIMTAMFDKCA-DFRRTGSAALDLCYVASGRVDAFFEIG-LKPWDFLGGELIMREAGGIMTDFIGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRApGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250
....*....|....*.
gi 1327839123 234 HNYIASGNLVAGSPRV 249
Cdd:pfam00459 242 PFDLLAGRVIAANPKV 257
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-252 |
1.77e-43 |
|
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: 147.84 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEMpSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRA-SLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 85 PLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFP---FKQ 161
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdllDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 162 KQHAAvymniMTAMFDKCAdFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDfIGGHNYIASGN 241
Cdd:TIGR02067 161 GNRPA-----FERLRRAAR-LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTD-WDGKPAPDGGG 233
|
250
....*....|.
gi 1327839123 242 LVAGSPRVVRD 252
Cdd:TIGR02067 234 AVAAGNAMLHD 244
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-267 |
0e+00 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 529.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 1 MHPMLNIAIRAARKAGNHIAKNYEMPSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 81 WVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 161 QKQHAAVYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 1327839123 241 NLVAGSPRVVRDILSVMKNELSESLKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
9.78e-130 |
|
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: 367.25 E-value: 9.78e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAKNYEMPsNIKVTQKG-TNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQWV 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKL-GLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 83 IDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQK 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 163 QHAAVYMNIMTAMFDK-CADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASGN 241
Cdd:cd01639 160 DNFDRYLNNFAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*
gi 1327839123 242 LVAGS 246
Cdd:cd01639 240 ILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
4.44e-125 |
|
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: 356.08 E-value: 4.44e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 2 HPMLNIAIRAARKAGNHIAKNYEmPSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFR-ELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 82 VIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQ 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 162 KQHAavYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*...
gi 1327839123 242 LVAGSPRVVRDILSVMKN 259
Cdd:COG0483 238 LVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-249 |
6.38e-82 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 246.87 E-value: 6.38e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 1 MHPMLNIAIRAARKAGNHIAKNYEMPSNIKV-TQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGK---- 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEkGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQtelt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 76 DDDIQWVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 156 GFPFKQKQHAAVYMNIMTAMFDKCA-DFRRTGSAALDLCYVASGRVDAFFEIG-LKPWDFLGGELIMREAGGIMTDFIGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRApGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250
....*....|....*.
gi 1327839123 234 HNYIASGNLVAGSPRV 249
Cdd:pfam00459 242 PFDLLAGRVIAANPKV 257
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-245 |
7.75e-79 |
|
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: 237.98 E-value: 7.75e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEMPSNIKVTqKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGEL-IGKDDDIQWVI 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSgNVSDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 84 DPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQKQ 163
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 164 HAAVymniMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGG-HNYIASGNL 242
Cdd:cd01637 160 RAAV----LASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEpLDTLNRSGI 235
|
...
gi 1327839123 243 VAG 245
Cdd:cd01637 236 IAA 238
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-247 |
6.54e-66 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 206.08 E-value: 6.54e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEMPSNikVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGK---DDDIQW 81
Cdd:PLN02553 11 LEVAVDAAKAAGQIIRKGFYQTKH--VEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGtelTDEPTW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 82 VIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQ 161
Cdd:PLN02553 89 IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 162 -KQHAAVYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGL-KPWDFLGGELIMREAGGIMTDFIGGHNYIAS 239
Cdd:PLN02553 169 dKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMS 248
|
....*...
gi 1327839123 240 GNLVAGSP 247
Cdd:PLN02553 249 RRVAASNG 256
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-245 |
2.22e-58 |
|
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: 186.00 E-value: 2.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEmpSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIqWVID 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFG--NSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY-WVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 85 PLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFPFKQKQH 164
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 165 AAVYMNIMTAmfdKCAdFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMT------DFIGGHNYIA 238
Cdd:cd01643 158 AVLRVILRRF---PGK-IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTildeepAFLQTKDYLS 233
|
....*....
gi 1327839123 239 SGN--LVAG 245
Cdd:cd01643 234 AGFptLIAA 242
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-233 |
3.73e-55 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 181.54 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAKNYEMPSNIkvTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQWVI 83
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNI--SYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 84 DPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYD----PM--RNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGF 157
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1327839123 158 PFKQKQHAAVYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGG 233
Cdd:PLN02737 237 GYEHDDAWATNIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGG 312
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-254 |
8.99e-51 |
|
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: 166.66 E-value: 8.99e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEMPsnIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGElIGKDDDIQWVID 84
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTR--LQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGN-EGGDAGYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 85 PLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLN---GYRIRIDEKRDLDGAIVATGFPFKQ 161
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTTDPHFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 162 KQHAAvymNIMTAMFDKCADFrRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGHNYIASGN 241
Cdd:cd01641 159 TPGDR---AAFERLARAVRLT-RYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGR 234
|
250
....*....|...
gi 1327839123 242 LVAGSPRVVRDIL 254
Cdd:cd01641 235 VVAAGDAELHEAL 247
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-230 |
1.29e-45 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 153.78 E-value: 1.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 1 MHPMLNIAIRAARKAGNHIAKNYEmpSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESgELIGKDDDIQ 80
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYR--ADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEES-AAIPYEERKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 81 ----WVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGA-----QLNGYRIRIDEKRDLDGA 151
Cdd:COG1218 78 wdrfWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAfketgGGERQPIRVRDRPPAEPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 152 IVATGfpfkqKQHAAVYM-NIMTAMfdKCADFRRTGSaALDLCYVASGRVDAFFEIGlkP---WDFLGGELIMREAGGIM 227
Cdd:COG1218 158 RVVAS-----RSHRDEETeALLARL--GVAELVSVGS-SLKFCLVAEGEADLYPRLG--PtmeWDTAAGQAILEAAGGRV 227
|
...
gi 1327839123 228 TDF 230
Cdd:COG1218 228 TDL 230
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-255 |
8.55e-45 |
|
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: 151.76 E-value: 8.55e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAK---NYEMPSNIKVTQKGTNdfVTNVDHESEQLIIEIIRKSYPdHTIITEESGEL-IGKDDDI 79
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPlfgTEDASEVVKIGADGTP--TKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIdNGDEPEY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 80 QWVIDPLDGTTNFTKRLPHFSVSIAV--RVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVAtgf 157
Cdd:cd01515 78 TVVLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVS--- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 158 pfkqkqhAAVYMNIMTAMFDKCADFRRT---GSAALDLCYVASGRVDAFFEI--GLKPWDFLGGELIMREAGGIMTDFIG 232
Cdd:cd01515 155 -------YYIYGKNHDRTFKICRKVRRVrifGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENG 227
|
250 260
....*....|....*....|....*...
gi 1327839123 233 GH-----NYIASGNLVAGSPRVVRDILS 255
Cdd:cd01515 228 KElklklNVTERVNIIAANSELHKKLLE 255
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-252 |
1.77e-43 |
|
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: 147.84 E-value: 1.77e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEMpSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRA-SLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 85 PLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFP---FKQ 161
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdllDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 162 KQHAAvymniMTAMFDKCAdFRRTGSAALDLCYVASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDfIGGHNYIASGN 241
Cdd:TIGR02067 161 GNRPA-----FERLRRAAR-LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTD-WDGKPAPDGGG 233
|
250
....*....|.
gi 1327839123 242 LVAGSPRVVRD 252
Cdd:TIGR02067 234 AVAAGNAMLHD 244
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
13-259 |
4.64e-43 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 147.36 E-value: 4.64e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 13 RKAGNHIAKNYE---MP--------SNIKVTQKGTndfVTN-VDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQ 80
Cdd:PRK12676 7 LEICDDMAKEVEkaiMPlfgtpdagETVGMGADGT---PTKlIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 81 WVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLD-GAIVATGFPF 159
Cdd:PRK12676 84 VVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNeSAVSIYGYRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 160 KqkqhaavYMNIMtamfDKCADFRRT---GSAALDLCYVASGRVDAFFEIG--LKPWDFLGGELIMREAGGIMTDFIGGH 234
Cdd:PRK12676 164 G-------KERTV----KLGRKVRRVrilGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNE 232
|
250 260 270
....*....|....*....|....*....|.
gi 1327839123 235 -----NYIASGNLVAGSPRVV-RDILSVMKN 259
Cdd:PRK12676 233 lklplNVTERTNLIAANGEELhKKILELLEG 263
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-232 |
2.86e-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: 2.86e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAKNYEmpSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDD-DIQWV 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYR--GGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGwDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 83 IDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKR---DLDGAIVATGfpf 159
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQArppPLQPLRVVAS--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1327839123 160 kQKQHAAVYMNIMTAMFDkcADFRRTGSaALDLCYVASGRVDAFFEIGLKP-WDFLGGELIMREAGGIMTDFIG 232
Cdd:cd01638 156 -RSHPDEELEALLAALGV--AEVVSIGS-SLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
5.16e-39 |
|
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.
Pssm-ID: 238814 [Multi-domain] Cd Length: 184 Bit Score: 134.44 E-value: 5.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 5 LNIAIRAARKAGNHIAKNYEMPSNIKVTQKG-TNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELI---GKDDDIQ 80
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKsDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEevmGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 81 WVIDPLDGTTNFTKRLPHFSVSIAVrvkgrtevavvydpmrnelfsavrgqgaqlngYRIRIDEKRDLDGAIVATGFpfk 160
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAV--------------------------------YVILILAEPSHKRVDEKKAE--- 125
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327839123 161 qKQHAAVYMnimtamfdkcadFRRTGSAALDLCYVASGRVDAFFEIGLK--PWDFLGGELIMREAGGIMTDF 230
Cdd:cd01636 126 -LQLLAVYR------------IRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTDW 184
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-233 |
7.23e-34 |
|
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: 122.94 E-value: 7.23e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAKNYEMPsnIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQ--- 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKE--LAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWqrf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 81 WVIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAqlngyrirideKRDLDGAIVATGFPFK 160
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAA-----------KREGDGQALKAPIHVR 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 161 QKQHAAVYMNIMTAMFDK---------CADFRRTGSAALDLCYVASGRVDAFFEIG-LKPWDFLGGELIMREAGGIMTDF 230
Cdd:TIGR01331 148 PWPSGPLLVVISRSHAEEktteylanlGYDLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDL 227
|
...
gi 1327839123 231 IGG 233
Cdd:TIGR01331 228 DGS 230
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-232 |
2.17e-31 |
|
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: 117.03 E-value: 2.17e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAK-NYEMPSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGEligkDDDIQWV 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPvFRNLGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA----ALGRFWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 83 IDPLDGTTNFTKRLPhFSVSIAVRVKGRTEVAVVYDPMRNE-------LFSAVRGQGA---QLNGYRIRIDEKRDLDGAI 152
Cdd:cd01517 77 LDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAwlrPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 153 VATGFPFKQKQHaavymniMTAMFDKCADFR--RTGSAALDL----CYVASGRVDAFFEIG------LKPWDFLGGELIM 220
Cdd:cd01517 156 RASFCESVESAH-------SSHRLQAAIKALggTPQPVRLDSqakyAAVARGAADFYLRLPlsmsyrEKIWDHAAGVLIV 228
|
250
....*....|..
gi 1327839123 221 REAGGIMTDFIG 232
Cdd:cd01517 229 EEAGGKVTDADG 240
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
7-257 |
5.09e-26 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 103.26 E-value: 5.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 7 IAIRAARKAGNHIAKNYEMPsnIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESG-ELIGKDDDIQWVIDP 85
Cdd:PLN02911 39 VAHKLADAAGEVTRKYFRTK--FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGlRCGEGSSDYVWVLDP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 86 LDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQGAQLNGYRIRIDEKRDLDGAIVATGFP--FKQKQ 163
Cdd:PLN02911 117 IDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSPhmFSGDA 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 164 HAAvymnimtamFDKCADFRRTGSAALDlCY----VASGRVDAFFEIGLKPWDFLGGELIMREAGGIMTDFIGGH----- 234
Cdd:PLN02911 197 EDA---------FARVRDKVKVPLYGCD-CYayglLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKlrwep 266
|
250 260
....*....|....*....|....*..
gi 1327839123 235 --NYIASGNLV--AGSPRVVRDILSVM 257
Cdd:PLN02911 267 spGSLATSFNVvaAGDARLHKQALDIL 293
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
43-229 |
9.40e-23 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 97.11 E-value: 9.40e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 43 VDHESEQLIIEIIRKsYPDHTIITEESGEL-IGKDD-DIQWVIDPLDGTTNFTKRLPHFSVSIAV-RVKGRT-------- 111
Cdd:PRK14076 45 IDLIAENIAINSLEK-FCSGILISEEIGFKkIGKNKpEYIFVLDPIDGTYNALKDIPIYSASIAIaKIDGFDkkikefig 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 112 --------EVAVVYDPMRNELFSAVRGQGAQL----NGYRIRIDEKRDLDGAIVAtGFpfkqkqhaAVYMNIMTAMFDKC 179
Cdd:PRK14076 124 knltindlEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDASIG-LF--------AYGLSLDTLKFIKD 194
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 1327839123 180 ADFRRT---GSAALDLCYVASGRVDAFFEI--GLKPWDFLGGELIMREAGGIMTD 229
Cdd:PRK14076 195 RKVRRIrlfGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITN 249
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
2-209 |
1.31e-19 |
|
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: 85.19 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 2 HPMLNIAIRAARKAGNHIAKNYEmpsniKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQW 81
Cdd:cd01642 3 EVLEKITKEIILLLNEKNRQGLV-----KLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 82 VIDPLDGTTNFTKRLPHFSVSIAV-RVKGRTEVAVVYDPMRNELFSAVRGQ---GAQLNGYRIRIDEKRDLDGAIVATgf 157
Cdd:cd01642 78 VLDPLDGSTNYLSGIPFYSVSVALaDPRSKVKAATLDNFVSGEGGLKVYSPptrFSYISVPKLGPPLVPEVPSKIGIY-- 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 1327839123 158 pfkqkqhAAVYMNIMTAMFDKCAD--FRRTGSAALDLCYVASGRVDAFFEIGLK 209
Cdd:cd01642 156 -------EGSSRNPEKFLLLSRNGlkFRSLGSAALELAYTCEGSFVLFLDLRGK 202
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
4-229 |
1.16e-17 |
|
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: 80.44 E-value: 1.16e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHI------AKNYEMPSNIKvTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGElIGKDD 77
Cdd:cd01640 1 LLRSLLAVAEKAGGIArdvvkkGRLLILLVEGK-TKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNE-FENQE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 78 DIQWV---------------------------IDPLDGTTNFTK-RLPHFSVSIAVRVKGRTEVAVVYDP--MRNELFSA 127
Cdd:cd01640 79 DESRDvdldeeileescpspskdlpeedlgvwVDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPfyEKTAGAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 128 VRGQ---GAQLNGYRIRIDEKRDLDGAIVATgfpfkqKQHAAVYMNIMTAMFDKCADFRRTGSAALDLCYVASGRVDA-- 202
Cdd:cd01640 159 WLGRtiwGLSGLGAHSSDFKEREDAGKIIVS------TSHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAyv 232
|
250 260
....*....|....*....|....*..
gi 1327839123 203 FFEIGLKPWDFLGGELIMREAGGIMTD 229
Cdd:cd01640 233 HSTGGIKKWDICAPEAILRALGGDMTD 259
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-142 |
2.07e-16 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 76.27 E-value: 2.07e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327839123 4 MLNIAIRAARKAGNHIAKNYEMPSNIKVTQKGTNDFVTNVDHESEQLIIEIIRKSYPDHTIITEESGELIGKDDDIQ--W 81
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQryW 80
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1327839123 82 VIDPLDGTTNFTKRLPHFSVSIAVRVKGRTEVAVVYDPMRNELFSAVRGQG-AQLNGYRIRI 142
Cdd:PRK10931 81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAwKEECGVRKQI 142
|
|
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