|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-266 |
4.28e-148 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 414.59 E-value: 4.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 1 MHPMLTIAVRAARAAGQTIMRAYTELDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYL 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 81 WIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 161 ARQHTETYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*.
gi 1710358131 241 NIVAGAPKATSLLVKRFRPLLSDALK 266
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALK 266
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-245 |
2.78e-125 |
|
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: 356.08 E-value: 2.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELDRiEVDAKGV-NDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWI 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGL-NVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 83 VDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKAR 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 163 QHTETYMKLFGE-TFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSGN 241
Cdd:cd01639 160 DNFDRYLNNFAKlLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....
gi 1710358131 242 IVAG 245
Cdd:cd01639 240 ILAG 243
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
1.72e-120 |
|
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: 344.14 E-value: 1.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 2 HPMLTIAVRAARAAGQTIMRAYTELDrIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 82 IVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 162 RQHteTYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSGN 241
Cdd:COG0483 160 DDR--EYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*...
gi 1710358131 242 IVAGAPKATSLLVKRFRP 259
Cdd:COG0483 238 LVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-249 |
4.32e-86 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 257.66 E-value: 4.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 1 MHPMLTIAVRAARAAGQTIMRAY-TELDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEE----NGENRGT 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFsNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 76 NQDYLWIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 156 GFPFKARQHTETYMKLFG-ETFSLCADLRRAGSAALDLAYVAAGRVDAFFELG-LKPWDIAAGDLIVREAGGTVTDFSGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKlLKLVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250
....*....|....*.
gi 1710358131 234 HNYLLSGNIVAGAPKA 249
Cdd:pfam00459 242 PFDLLAGRVIAANPKV 257
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-246 |
8.67e-48 |
|
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: 159.01 E-value: 8.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTELDrIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWIVD 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASL-LVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 85 PLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATgfpfkarqh 164
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFT--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 165 TETYM---KLFGETFSLCAD---LRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGhNYLL 238
Cdd:TIGR02067 152 TSPDLlddPGNRPAFERLRRaarLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGK-PAPD 230
|
....*...
gi 1710358131 239 SGNIVAGA 246
Cdd:TIGR02067 231 GGGAVAAG 238
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-266 |
4.28e-148 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 414.59 E-value: 4.28e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 1 MHPMLTIAVRAARAAGQTIMRAYTELDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYL 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 81 WIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 161 ARQHTETYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*.
gi 1710358131 241 NIVAGAPKATSLLVKRFRPLLSDALK 266
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALK 266
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-245 |
2.78e-125 |
|
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: 356.08 E-value: 2.78e-125
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELDRiEVDAKGV-NDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWI 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGL-NVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 83 VDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKAR 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 163 QHTETYMKLFGE-TFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSGN 241
Cdd:cd01639 160 DNFDRYLNNFAKlLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....
gi 1710358131 242 IVAG 245
Cdd:cd01639 240 ILAG 243
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
1.72e-120 |
|
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: 344.14 E-value: 1.72e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 2 HPMLTIAVRAARAAGQTIMRAYTELDrIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 82 IVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 162 RQHteTYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSGN 241
Cdd:COG0483 160 DDR--EYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*...
gi 1710358131 242 IVAGAPKATSLLVKRFRP 259
Cdd:COG0483 238 LVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-249 |
4.32e-86 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 257.66 E-value: 4.32e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 1 MHPMLTIAVRAARAAGQTIMRAY-TELDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEE----NGENRGT 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFsNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 76 NQDYLWIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 156 GFPFKARQHTETYMKLFG-ETFSLCADLRRAGSAALDLAYVAAGRVDAFFELG-LKPWDIAAGDLIVREAGGTVTDFSGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKlLKLVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250
....*....|....*.
gi 1710358131 234 HNYLLSGNIVAGAPKA 249
Cdd:pfam00459 242 PFDLLAGRVIAANPKV 257
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-245 |
5.28e-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: 238.37 E-value: 5.28e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTELDRIEVDaKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGT-NQDYLWIV 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVsDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 84 DPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKARQ 163
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 164 HTETYMKLFGETfslcADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGG-HNYLLSGNI 242
Cdd:cd01637 160 RAAVLASLVNRA----LGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEpLDTLNRSGI 235
|
...
gi 1710358131 243 VAG 245
Cdd:cd01637 236 IAA 238
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-255 |
5.46e-69 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 214.17 E-value: 5.46e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTELDRIEvdAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGT---NQDYLW 81
Cdd:PLN02553 11 LEVAVDAAKAAGQIIRKGFYQTKHVE--HKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGtelTDEPTW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 82 IVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKA 161
Cdd:PLN02553 89 IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 162 RQHT-ETYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDAFFELGL-KPWDIAAGDLIVREAGGTVTDFSGGHNYLLS 239
Cdd:PLN02553 169 DKATvDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMS 248
|
250
....*....|....*.
gi 1710358131 240 GNIVAGAPKATSLLVK 255
Cdd:PLN02553 249 RRVAASNGHLKDAFVE 264
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-233 |
1.72e-63 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 203.11 E-value: 1.72e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELDRIevDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWIV 83
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNI--SYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 84 DPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPV------RDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGF 157
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVggpmcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1710358131 158 PFKARQHTETYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGG 233
Cdd:PLN02737 237 GYEHDDAWATNIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGG 312
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-245 |
1.70e-59 |
|
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: 188.70 E-value: 1.70e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTelDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYlWIVD 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFG--NSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY-WVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 85 PLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFKA--R 162
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRAsaR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 163 QHTETYMKLFGETFslcadlRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVT------DFSGGHNY 236
Cdd:cd01643 158 AVLRVILRRFPGKI------RMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTildeepAFLQTKDY 231
|
250
....*....|.
gi 1710358131 237 LLSGN--IVAG 245
Cdd:cd01643 232 LSAGFptLIAA 242
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-249 |
4.45e-56 |
|
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: 180.14 E-value: 4.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTEldRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNqDYLWIVD 84
Cdd:cd01641 2 LAFALELADAAGQITLPYFRT--RLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDA-GYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 85 PLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDF---RIRVNNVSDLGGSLVATGFPFKA 161
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAggrPLRVRACADLAEAVLSTTDPHFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 162 RQH-TETYMKLFGETfslcaDLRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGHNYLLSG 240
Cdd:cd01641 159 TPGdRAAFERLARAV-----RLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSG 233
|
....*....
gi 1710358131 241 NIVAGAPKA 249
Cdd:cd01641 234 RVVAAGDAE 242
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-232 |
4.17e-53 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 173.04 E-value: 4.17e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 1 MHPMLTIAVRAARAAGQTIMRAYTelDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGT---NQ 77
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYR--ADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEerkSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 78 DYLWIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDF-----RIRVNNVSDLGGSL 152
Cdd:COG1218 79 DRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGggerqPIRVRDRPPAEPLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 153 VATGfpfkaRQH----TETYMKLFGEtfslcADLRRAGSaALDLAYVAAGRVDAFFELGlkP---WDIAAGDLIVREAGG 225
Cdd:COG1218 159 VVAS-----RSHrdeeTEALLARLGV-----AELVSVGS-SLKFCLVAEGEADLYPRLG--PtmeWDTAAGQAILEAAGG 225
|
....*..
gi 1710358131 226 TVTDFSG 232
Cdd:COG1218 226 RVTDLDG 232
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-246 |
8.67e-48 |
|
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: 159.01 E-value: 8.67e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTELDrIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWIVD 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASL-LVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 85 PLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATgfpfkarqh 164
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFT--------- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 165 TETYM---KLFGETFSLCAD---LRRAGSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGhNYLL 238
Cdd:TIGR02067 152 TSPDLlddPGNRPAFERLRRaarLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGK-PAPD 230
|
....*...
gi 1710358131 239 SGNIVAGA 246
Cdd:TIGR02067 231 GGGAVAAG 238
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
5-233 |
8.73e-48 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 159.30 E-value: 8.73e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTELDRIEVDAKGV-NDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWIV 83
Cdd:PRK12676 7 LEICDDMAKEVEKAIMPLFGTPDAGETVGMGAdGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 84 DPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFpfkarq 163
Cdd:PRK12676 87 DPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSIYG------ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1710358131 164 htetYMKLFGETFSLCADLRRA---GSAALDLAYVAAGRVDAFFELG--LKPWDIAAGDLIVREAGGTVTDFSGG 233
Cdd:PRK12676 161 ----YRRGKERTVKLGRKVRRVrilGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGN 231
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-232 |
1.65e-47 |
|
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: 158.16 E-value: 1.65e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELdrIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGT-NQDYLWI 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGG--FTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRlGWDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 83 VDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNN---VSDLGGSLVATGfpf 159
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLqarPPPLQPLRVVAS--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1710358131 160 kaRQH----TETYMKLFGEtfslcADLRRAGSaALDLAYVAAGRVDAFFELGLKP-WDIAAGDLIVREAGGTVTDFSG 232
Cdd:cd01638 156 --RSHpdeeLEALLAALGV-----AEVVSIGS-SLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-233 |
5.91e-41 |
|
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: 141.75 E-value: 5.91e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELDRIEVDAKGVN-DFVTSVDKEAEAAIIYQIRKSYPdHSIVGEENGENR-GTNQDYLW 81
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGADgTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIDnGDEPEYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 82 IVDPLDGTNNFVNGVPHFAVSIAMQYKGK--TEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLgGSLVATGFPf 159
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSL-KSISVSYYI- 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1710358131 160 karqhtetYMKLFGETFSLCADLRRA---GSAALDLAYVAAGRVDAFFEL--GLKPWDIAAGDLIVREAGGTVTDFSGG 233
Cdd:cd01515 158 --------YGKNHDRTFKICRKVRRVrifGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGK 228
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-250 |
2.78e-39 |
|
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: 137.83 E-value: 2.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELDRIEVD-AKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTnqdyLWI 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGAGDVVwKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAALGR----FWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 83 VDPLDGTNNFVNGVPhFAVSIAMQYKGKTEVAVVYDPVRDE-------LFSAVRGKGA---KLNDFRIRVNNVSDLGGSL 152
Cdd:cd01517 77 LDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAwlrPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 153 VATGFPFKARQHTETymklfGETFSLCADLRRAGSAALDLAY----VAAGRVDAFFELG------LKPWDIAAGDLIVRE 222
Cdd:cd01517 156 RASFCESVESAHSSH-----RLQAAIKALGGTPQPVRLDSQAkyaaVARGAADFYLRLPlsmsyrEKIWDHAAGVLIVEE 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1710358131 223 AGGTVTDFSG-------GHNYLLSGNIVAgAPKAT 250
Cdd:cd01517 231 AGGKVTDADGkpldfgkGRKLLNNGGLIA-APGEI 264
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-233 |
6.09e-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: 136.04 E-value: 6.09e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTEldRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEEN----GENRGTNQDY 79
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQK--ELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDasipLTPRQTWQRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 80 lWIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLN------DFRIRVNNvSDLGGSLV 153
Cdd:TIGR01331 79 -WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREgdgqalKAPIHVRP-WPSGPLLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 154 ATGfpfkaRQHTETYMKLFGEtfSLCADLRRAGSAALDLAYVAAGRVDAFFELG-LKPWDIAAGDLIVREAGGTVTDFSG 232
Cdd:TIGR01331 157 VIS-----RSHAEEKTTEYLA--NLGYDLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDG 229
|
.
gi 1710358131 233 G 233
Cdd:TIGR01331 230 S 230
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
3.56e-37 |
|
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: 129.43 E-value: 3.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 5 LTIAVRAARAAGQTIMRAYTELDRIEVDAKGV-NDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENG---ENRGTNQDYL 80
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSdNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 81 WIVDPLDGTNNFVNGVPHFAVSIAmqykgktevavVYDPVRDELFSAVRGKGAKLNDFRIRVnnvsdlggslvatgfpfk 160
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIA-----------VYVILILAEPSHKRVDEKKAELQLLAV------------------ 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1710358131 161 arqhtetymklfgetfslcADLRRAGSAALDLAYVAAGRVDAFFELGLK--PWDIAAGDLIVREAGGTVTDF 230
Cdd:cd01636 132 -------------------YRIRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-234 |
1.60e-36 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 131.00 E-value: 1.60e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 6 TIAVRAARAAGQTIMRAYTEldRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTN-QDYLWIVD 84
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRT--KFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGsSDYVWVLD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 85 PLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATGFPFkarqh 164
Cdd:PLN02911 116 PIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSPH----- 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1710358131 165 tetymkLF-GETFSLCADLRRA------GSAALDLAYVAAGRVDAFFELGLKPWDIAAGDLIVREAGGTVTDFSGGH 234
Cdd:PLN02911 191 ------MFsGDAEDAFARVRDKvkvplyGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRK 261
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-232 |
4.16e-24 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 97.07 E-value: 4.16e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 4 MLTIAVRAARAAGQTIMRAYTELDRIEVDAKGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENG---ENRGTNQDYl 80
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPpawEVRQHWQRY- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 81 WIVDPLDGTNNFVNGVPHFAVSIAMQYKGKTEVAVVYDPVRDELFSAVRGKGAKLNDFRIRVNNVSDLGGSLVATgfpfk 160
Cdd:PRK10931 80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVI----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 161 ARQHT----ETYMKLFGE--TFSLcadlrraGSaALDLAYVAAGRVDAFFELGlkP---WDIAAGDLIVREAGGTVTDFS 231
Cdd:PRK10931 155 SRSHAdaelKEYLQQLGEhqTTSI-------GS-SLKFCLVAEGQAQLYPRFG--PtniWDTAAGHAVAIAAGAHVHDWQ 224
|
.
gi 1710358131 232 G 232
Cdd:PRK10931 225 G 225
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
43-232 |
5.43e-23 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 97.88 E-value: 5.43e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 43 VDKEAEAAIIYQIRKsYPDHSIVGEENGENR-GTNQ-DYLWIVDPLDGTNNFVNGVPHFAVSIAMQY-KGKT-------- 111
Cdd:PRK14076 45 IDLIAENIAINSLEK-FCSGILISEEIGFKKiGKNKpEYIFVLDPIDGTYNALKDIPIYSASIAIAKiDGFDkkikefig 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 112 --------EVAVVYDPVRDELFSAVRGKGAKL----NDFRIRVNNVSDLGGSLVAtGFpfkarqhteTYmKLFGETFSLC 179
Cdd:PRK14076 124 knltindlEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDASIG-LF---------AY-GLSLDTLKFI 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 180 AD-----LRRAGSAALDLAYVAAGRVDAFFEL--GLKPWDIAAGDLIVREAGGTVTDFSG 232
Cdd:PRK14076 193 KDrkvrrIRLFGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNG 252
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
34-224 |
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: 84.81 E-value: 1.31e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 34 KGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENGENRGTNQDYLWIVDPLDGTNNFVNGVPHFAVSIA-MQYKGKTE 112
Cdd:cd01642 30 GAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVAlADPRSKVK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 113 VAVVYDPVRDELFsavrgkgAKLNDFRIRVNNVSDLGGSLVAT-------GFPFKARQHTETYMKLFGETFSlcadLRRA 185
Cdd:cd01642 110 AATLDNFVSGEGG-------LKVYSPPTRFSYISVPKLGPPLVpevpskiGIYEGSSRNPEKFLLLSRNGLK----FRSL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 1710358131 186 GSAALDLAYVAAGRVDAFFEL--GLKPWDIAAGDLIVREAG 224
Cdd:cd01642 179 GSAALELAYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLG 219
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
34-232 |
5.40e-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: 78.52 E-value: 5.40e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 34 KGVNDFVTSVDKEAEAAIIYQIRKSYPDHSIVGEENgeNRGTNQDYLWI----------------------------VDP 85
Cdd:cd01640 36 EGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEED--NEFENQEDESRdvdldeeileescpspskdlpeedlgvwVDP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 86 LDGTNNFVNG-VPHFAVSIAMQYKGKTEVAVVYDP----------VRDELFSAVRGKGAKLNDFRIRVNnvsdlGGSLVA 154
Cdd:cd01640 114 LDATQEYTEGlLEYVTVLIGVAVKGKPIAGVIHQPfyektagagaWLGRTIWGLSGLGAHSSDFKERED-----AGKIIV 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1710358131 155 TgfpfkaRQHTETYMKLFGETFSLCADLRRAGSAALDLAYVAAGRVDA--FFELGLKPWDIAAGDLIVREAGGTVTDFSG 232
Cdd:cd01640 189 S------TSHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAyvHSTGGIKKWDICAPEAILRALGGDMTDLHG 262
|
|
| |
