|
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: 591.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 1 MHPMLTIAVRAARKAGNVIAKNYETPDAAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 81 WVIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 161 AKQYATTYINIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 446475610 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.03e-131 |
|
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: 372.25 E-value: 1.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAaEASQKGS-NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWV 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGL-NVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 83 IDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAK 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 163 QYATTYINIIGKLFT-ECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGN 241
Cdd:cd01639 160 DNFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*
gi 446475610 242 IVAGN 246
Cdd:cd01639 240 ILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-258 |
1.15e-122 |
|
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: 349.91 E-value: 1.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 2 HPMLTIAVRAARKAGNVIAKNYETPDAaEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDL-EVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 82 VIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 162 KQYAttYINIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 446475610 242 IVAGNPRVVKAMLANMR 258
Cdd:COG0483 238 LVAANPALHDELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-255 |
5.70e-87 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 259.97 E-value: 5.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 1 MHPMLTIAVRAARKAGNVIAKNYETP-DAAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEH----VGT 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKgdqtELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 76 DQDVQWVIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 156 GFPFKAKQYATTYINIIGKLF-TECADFRRTGSAALDLAYVAAGRVDGFFEIG-LRPWDFAAGELLVREAGGIVSDFTGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|..
gi 446475610 234 HNYMMTGNIVAGNPRVVKAMLA 255
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLA 263
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-255 |
1.43e-39 |
|
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: 137.82 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEaSQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 85 PLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFP--FKAK 162
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdlLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 163 QYATTYINIIGKlftecADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGNI 242
Cdd:TIGR02067 161 GNRPAFERLRRA-----ARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGGAV 235
|
250
....*....|...
gi 446475610 243 VAGNPRVVKAMLA 255
Cdd:TIGR02067 236 AAGNAMLHDEALE 248
|
|
| |
|
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: 591.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 1 MHPMLTIAVRAARKAGNVIAKNYETPDAAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 81 WVIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 161 AKQYATTYINIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 446475610 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.03e-131 |
|
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: 372.25 E-value: 1.03e-131
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAaEASQKGS-NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWV 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGL-NVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 83 IDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAK 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 163 QYATTYINIIGKLFT-ECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGN 241
Cdd:cd01639 160 DNFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*
gi 446475610 242 IVAGN 246
Cdd:cd01639 240 ILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-258 |
1.15e-122 |
|
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: 349.91 E-value: 1.15e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 2 HPMLTIAVRAARKAGNVIAKNYETPDAaEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDL-EVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 82 VIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 162 KQYAttYINIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 446475610 242 IVAGNPRVVKAMLANMR 258
Cdd:COG0483 238 LVAANPALHDELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-255 |
5.70e-87 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 259.97 E-value: 5.70e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 1 MHPMLTIAVRAARKAGNVIAKNYETP-DAAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEH----VGT 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKgdqtELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 76 DQDVQWVIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 156 GFPFKAKQYATTYINIIGKLF-TECADFRRTGSAALDLAYVAAGRVDGFFEIG-LRPWDFAAGELLVREAGGIVSDFTGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|..
gi 446475610 234 HNYMMTGNIVAGNPRVVKAMLA 255
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLA 263
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-245 |
1.50e-77 |
|
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: 234.90 E-value: 1.50e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEASqKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGE-HVGTDQDVQWVI 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGsGNVSDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 84 DPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQ 163
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 164 YAttyiNIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGG-HNYMMTGNI 242
Cdd:cd01637 160 RA----AVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEpLDTLNRSGI 235
|
...
gi 446475610 243 VAG 245
Cdd:cd01637 236 IAA 238
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-259 |
6.17e-69 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 213.78 E-value: 6.17e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVG----TDqDVQ 80
Cdd:PLN02553 11 LEVAVDAAKAAGQIIRKGFYQTKHVE--HKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGgtelTD-EPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 81 WVIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPF- 159
Cdd:PLN02553 88 WIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTk 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 160 --KAKQYATTyiNIIGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGL-RPWDFAAGELLVREAGGIVSDFTGGHNY 236
Cdd:PLN02553 168 rdKATVDATT--NRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFD 245
|
250 260
....*....|....*....|...
gi 446475610 237 MMTGNIVAGNPRVVKAMLANMRD 259
Cdd:PLN02553 246 IMSRRVAASNGHLKDAFVEALRQ 268
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-252 |
7.74e-57 |
|
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: 182.15 E-value: 7.74e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVqWVID 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAE--TKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY-WVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 85 PLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKAKQY 164
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 165 ATTYINII---GKlftecadFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTG-GHNYMMTG 240
Cdd:cd01643 158 AVLRVILRrfpGK-------IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEePAFLQTKD 230
|
250
....*....|..
gi 446475610 241 NIVAGNPRVVKA 252
Cdd:cd01643 231 YLSAGFPTLIAA 242
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-233 |
2.19e-52 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 174.22 E-value: 2.19e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPdaAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVI 83
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKP--RNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 84 DPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYD----PM--RNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGF 157
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446475610 158 PFKAKQYATTYINIIgKLFTE-CADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGG 233
Cdd:PLN02737 237 GYEHDDAWATNIELF-KEFTDvSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGG 312
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
5-233 |
5.64e-46 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 154.68 E-value: 5.64e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEASQKG-SNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVI 83
Cdd:PRK12676 7 LEICDDMAKEVEKAIMPLFGTPDAGETVGMGaDGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 84 DPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFpfkakq 163
Cdd:PRK12676 87 DPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSIYG------ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446475610 164 YATTYINIIGKlfteCADFRRT---GSAALDLAYVAAGRVDGFFEIG--LRPWDFAAGELLVREAGGIVSDFTGG 233
Cdd:PRK12676 161 YRRGKERTVKL----GRKVRRVrilGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGN 231
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-255 |
6.29e-46 |
|
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: 154.33 E-value: 6.29e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEAsqKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHvGTDQDVQWVID 84
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVET--KADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNE-GGDAGYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 85 PLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLN---GYRLRGSTARDLDGTILATGFPFKA 161
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTTDPHFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 162 KQYATtyiNIIGKLFTECADFrRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGN 241
Cdd:cd01641 159 TPGDR---AAFERLARAVRLT-RYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGR 234
|
250
....*....|....
gi 446475610 242 IVAGNPRVVKAMLA 255
Cdd:cd01641 235 VVAAGDAELHEALL 248
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-255 |
2.71e-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: 152.92 E-value: 2.71e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAAEASQKG-SNDFVTNVDKAAEAVIIDTIRKSYPQhTIITEESGE-HVGTDQDVQW 81
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGaDGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEIGViDNGDEPEYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 82 VIDPLDGTTNFIKRLPHFSVSIAV--HIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILAtgfpf 159
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVS----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 160 kakqyATTYINIIGKLFTECADFRRT---GSAALDLAYVAAGRVDGFFEI--GLRPWDFAAGELLVREAGGIVSDFTGGH 234
Cdd:cd01515 155 -----YYIYGKNHDRTFKICRKVRRVrifGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKE 229
|
250 260
....*....|....*....|....*.
gi 446475610 235 -----NYMMTGNIVAGNPRVVKAMLA 255
Cdd:cd01515 230 lklklNVTERVNIIAANSELHKKLLE 255
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-232 |
3.15e-44 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 150.31 E-value: 3.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 1 MHPMLTIAVRAARKAGNVIAKNYETPdaAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESgEHVGTDQDVQ 80
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRAD--FEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEES-AAIPYEERKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 81 ----WVIDPLDGTTNFIKRLPHFSVSIA-VHiKGRTEVAVVYDPMRNELFTATRGQGA-----QLNGYRLRGSTARDLDG 150
Cdd:COG1218 78 wdrfWLVDPLDGTKEFIKRNGEFTVNIAlIE-DGRPVLGVVYAPALGRLYYAAKGQGAfketgGGERQPIRVRDRPPAEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 151 TILATGFPFKAKQYAttyiNIIGKLftECADFRRTGSaALDLAYVAAGRVDGFFEIGlrP---WDFAAGELLVREAGGIV 227
Cdd:COG1218 157 LRVVASRSHRDEETE----ALLARL--GVAELVSVGS-SLKFCLVAEGEADLYPRLG--PtmeWDTAAGQAILEAAGGRV 227
|
....*
gi 446475610 228 SDFTG 232
Cdd:COG1218 228 TDLDG 232
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-232 |
7.76e-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: 143.52 E-value: 7.76e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAAEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQ-DVQWV 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVE--RKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGwDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 83 IDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNG--YRLRGSTARDLDGTILATGFPFK 160
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGrpGAVSLQARPPPLQPLRVVASRSH 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446475610 161 AKQYATTYINIIGKlftecADFRRTGSaALDLAYVAAGRVDGFFEIGLRP-WDFAAGELLVREAGGIVSDFTG 232
Cdd:cd01638 159 PDEELEALLAALGV-----AEVVSIGS-SLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-255 |
1.43e-39 |
|
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: 137.82 E-value: 1.43e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEaSQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 85 PLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFP--FKAK 162
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdlLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 163 QYATTYINIIGKlftecADFRRTGSAALDLAYVAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNYMMTGNI 242
Cdd:TIGR02067 161 GNRPAFERLRRA-----ARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGGAV 235
|
250
....*....|...
gi 446475610 243 VAGNPRVVKAMLA 255
Cdd:TIGR02067 236 AAGNAMLHDEALE 248
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
3.67e-36 |
|
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: 127.12 E-value: 3.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNY--ETPDAAEASqKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESG---EHVGTDQDV 79
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFgrELSGKVKIT-KSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeEVMGRRDEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 80 QWVIDPLDGTTNFIKRLPHFSVSIAVhikgrtevavvydpmrnelftatrgqgaqlngYRLRGSTARDLDGTILATGFPF 159
Cdd:cd01636 80 TWVIDPIDGTKNFINGLPFVAVVIAV--------------------------------YVILILAEPSHKRVDEKKAELQ 127
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446475610 160 KAKQYAttyiniigklftecadFRRTGSAALDLAYVAAGRVDGFFEIG--LRPWDFAAGELLVREAGGIVSDF 230
Cdd:cd01636 128 LLAVYR----------------IRIVGSAVAKMCLVALGLADIYYEPGgkRRAWDVAASAAIVREAGGIMTDW 184
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-233 |
1.68e-35 |
|
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: 127.18 E-value: 1.68e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAAEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQ--- 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVA--QKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWqrf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 81 WVIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNG--------YRLRGSTARDLDGTI 152
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkapIHVRPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 153 LATgfpfKAKQYATTYINIIGKLFTECadfrrtGSAALDLAYVAAGRVDGFFEIG-LRPWDFAAGELLVREAGGIVSDFT 231
Cdd:TIGR01331 159 SRS----HAEEKTTEYLANLGYDLRTS------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLD 228
|
..
gi 446475610 232 GG 233
Cdd:TIGR01331 229 GS 230
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-232 |
9.38e-33 |
|
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: 120.88 E-value: 9.38e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAAEASQ-KGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTdqdvQWV 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGAGDVVWkKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAALGR----FWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 83 IDPLDGTTNFIKRLPhFSVSIAVHIKGRTEVAVVYDPMRNE-------LFTATRGQGA---QLNGYRLRGSTARDLDGTI 152
Cdd:cd01517 77 LDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAwlrPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 153 LATGFPFKAKQYATTYINIIGKLFTECADFRRTGSAAlDLAYVAAGRVDGFFEIG------LRPWDFAAGELLVREAGGI 226
Cdd:cd01517 156 RASFCESVESAHSSHRLQAAIKALGGTPQPVRLDSQA-KYAAVARGAADFYLRLPlsmsyrEKIWDHAAGVLIVEEAGGK 234
|
....*.
gi 446475610 227 VSDFTG 232
Cdd:cd01517 235 VTDADG 240
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-257 |
1.11e-24 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 99.79 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 6 TIAVRAARKAGNVIAKNYETPdaAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGT-DQDVQWVID 84
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTK--FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEgSSDYVWVLD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 85 PLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDgtilatgfpfKAKQY 164
Cdd:PLN02911 116 PIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLK----------DAYLY 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 165 ATTYINIIG---KLFTECADFRRTGSAALD-LAY--VAAGRVDGFFEIGLRPWDFAAGELLVREAGGIVSDFTGGHNY-- 236
Cdd:PLN02911 186 TTSPHMFSGdaeDAFARVRDKVKVPLYGCDcYAYglLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKLRwe 265
|
250 260
....*....|....*....|....*...
gi 446475610 237 -------MMTGNIVAGNPRVVKAMLANM 257
Cdd:PLN02911 266 pspgslaTSFNVVAAGDARLHKQALDIL 293
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
37-224 |
1.09e-22 |
|
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: 93.28 E-value: 1.09e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 37 NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQWVIDPLDGTTNFIKRLPHFSVSIAVHIKG-RTEVAV 115
Cdd:cd01642 33 GDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRsKVKAAT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 116 VYDPMRNELFtatrgqgAQLNGYRLRGSTARDL-DGTILATGFPFKAKQYATTYINIIGKLFTECAD--FRRTGSAALDL 192
Cdd:cd01642 113 LDNFVSGEGG-------LKVYSPPTRFSYISVPkLGPPLVPEVPSKIGIYEGSSRNPEKFLLLSRNGlkFRSLGSAALEL 185
|
170 180 190
....*....|....*....|....*....|....
gi 446475610 193 AYVAAGRVDGFFEI--GLRPWDFAAGELLVREAG 224
Cdd:cd01642 186 AYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLG 219
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
4-232 |
2.01e-20 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 90.17 E-value: 2.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAAEASQKGSNDFVTN-VDKAAEAVIIDTIRKsYPQHTIITEESGE-HVGTDQ-DVQ 80
Cdd:PRK14076 5 MLKIALKVAKEIEKKIKPLIGWEKAGEVVKIGADGTPTKrIDLIAENIAINSLEK-FCSGILISEEIGFkKIGKNKpEYI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 81 WVIDPLDGTTNFIKRLPHFSVSIAV-HIKGRT----------------EVAVVYDPMRNELFTATRGQGAQL----NGYR 139
Cdd:PRK14076 84 FVLDPIDGTYNALKDIPIYSASIAIaKIDGFDkkikefigknltindlEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 140 LRGSTARDL-DGTIlaTGFpfkAKQYATTYINiigklFTECADFRRT---GSAALDLAYVAAGRVDGFFEI--GLRPWDF 213
Cdd:PRK14076 164 IEISNISNLkDASI--GLF---AYGLSLDTLK-----FIKDRKVRRIrlfGSIALEMCYVASGALDAFINVneTTRLCDI 233
|
250
....*....|....*....
gi 446475610 214 AAGELLVREAGGIVSDFTG 232
Cdd:PRK14076 234 AAGYVICKEAGGIITNKNG 252
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-131 |
8.46e-18 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 80.12 E-value: 8.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 4 MLTIAVRAARKAGNVIAKNYETPDAAEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGEHVGTDQDVQ--W 81
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQryW 80
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 446475610 82 VIDPLDGTTNFIKRLPHFSVSIAVHIKGRTEVAVVYDPMRNELFTATRGQ 131
Cdd:PRK10931 81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK 130
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
5-232 |
6.97e-13 |
|
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: 66.96 E-value: 6.97e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 5 LTIAVRAARKAGNVIAKNYETPDAAEASQK-GSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESG------------- 70
Cdd:cd01640 6 LAVAEKAGGIARDVVKKGRLLILLVEGKTKeGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNefenqedesrdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 71 ------EHVGTDQDVQ--------WvIDPLDGTTNFIK-RLPHFSVSIAVHIKGRTEVAVVYDPMRNElftatrgqgaQL 135
Cdd:cd01640 86 ldeeilEESCPSPSKDlpeedlgvW-VDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEK----------TA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446475610 136 NGYRLRGSTARDLDGtILATGFPFKAKQYATTYI----------NIIGKLFTECADFRRTGSAALDLAYVAAGRVDG--F 203
Cdd:cd01640 155 GAGAWLGRTIWGLSG-LGAHSSDFKEREDAGKIIvstshshsvkEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAyvH 233
|
250 260
....*....|....*....|....*....
gi 446475610 204 FEIGLRPWDFAAGELLVREAGGIVSDFTG 232
Cdd:cd01640 234 STGGIKKWDICAPEAILRALGGDMTDLHG 262
|
|
| |
