|
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: 594.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 1 MHPMLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 81 WVIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 161 AKQHAASYMKILGKMFTECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 489127879 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
3.23e-133 |
|
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: 376.11 E-value: 3.23e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVI 83
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 84 DPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKAKQ 163
Cdd:cd01639 81 DPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 164 HAASYMKILGKMFT-ECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATGNI 242
Cdd:cd01639 161 NFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNI 240
|
....
gi 489127879 243 VAGN 246
Cdd:cd01639 241 LAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-258 |
7.45e-123 |
|
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: 350.30 E-value: 7.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 2 HPMLTIAVRAARKAGNVIAKHYETPDsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 82 VIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 162 KQHAasYMKILGKMFTECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 489127879 242 IVAGNPRVVKAMLANMR 258
Cdd:COG0483 238 LVAANPALHDELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-255 |
3.56e-86 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 258.04 E-value: 3.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 1 MHPMLTIAVRAARKAGNVIAKHYETP-DSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHA----GE 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGdqteLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 76 DQDVQWVIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 156 GFPFKAKQHAASYMKILGKMF-TECADFRRTGSAALDLAYVAAARVDGYFEIG-LKPWDFAAGELIAREAGALVCDFTGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|..
gi 489127879 234 HNYLATGNIVAGNPRVVKAMLA 255
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLA 263
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-255 |
2.62e-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: 137.05 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVEtSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 85 PLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFP---FKA 161
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdllDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 162 KQHAAsYMKILGKmftecADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATGN 241
Cdd:TIGR02067 161 GNRPA-FERLRRA-----ARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGGA 234
|
250
....*....|....
gi 489127879 242 IVAGNPRVVKAMLA 255
Cdd:TIGR02067 235 VAAGNAMLHDEALE 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: 594.48 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 1 MHPMLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 81 WVIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 161 AKQHAASYMKILGKMFTECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 489127879 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
3.23e-133 |
|
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: 376.11 E-value: 3.23e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVI 83
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 84 DPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKAKQ 163
Cdd:cd01639 81 DPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 164 HAASYMKILGKMFT-ECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATGNI 242
Cdd:cd01639 161 NFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNI 240
|
....
gi 489127879 243 VAGN 246
Cdd:cd01639 241 LAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-258 |
7.45e-123 |
|
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: 350.30 E-value: 7.45e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 2 HPMLTIAVRAARKAGNVIAKHYETPDsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 82 VIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 162 KQHAasYMKILGKMFTECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 489127879 242 IVAGNPRVVKAMLANMR 258
Cdd:COG0483 238 LVAANPALHDELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-255 |
3.56e-86 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 258.04 E-value: 3.56e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 1 MHPMLTIAVRAARKAGNVIAKHYETP-DSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHA----GE 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGdqteLT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 76 DQDVQWVIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 156 GFPFKAKQHAASYMKILGKMF-TECADFRRTGSAALDLAYVAAARVDGYFEIG-LKPWDFAAGELIAREAGALVCDFTGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|..
gi 489127879 234 HNYLATGNIVAGNPRVVKAMLA 255
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLA 263
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-245 |
2.37e-80 |
|
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: 241.83 E-value: 2.37e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVETSqKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHA-GEDQDVQWVI 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGnVSDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 84 DPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKAKQ 163
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 164 HAASYMKILGkmftECADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGG-HNYLATGNI 242
Cdd:cd01637 160 RAAVLASLVN----RALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEpLDTLNRSGI 235
|
...
gi 489127879 243 VAG 245
Cdd:cd01637 236 IAA 238
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-259 |
4.13e-65 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 204.15 E-value: 4.13e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVEtsQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAG--EDQDV-QW 81
Cdd:PLN02553 11 LEVAVDAAKAAGQIIRKGFYQTKHVE--HKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGgtELTDEpTW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 82 VIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKA 161
Cdd:PLN02553 89 IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 162 -KQHAASYMKILGKMFTECADFRRTGSAALDLAYVAAARVDGYFEIGL-KPWDFAAGELIAREAGALVCDFTGGHNYLAT 239
Cdd:PLN02553 169 dKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMS 248
|
250 260
....*....|....*....|
gi 489127879 240 GNIVAGNPRVVKAMLANMRD 259
Cdd:PLN02553 249 RRVAASNGHLKDAFVEALRQ 268
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-252 |
2.42e-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: 2.42e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVETsqKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVqWVID 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAET--KADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY-WVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 85 PLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFPFKAKQH 164
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 165 AAS--YMKILGKMftecadFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTG-GHNYLATGN 241
Cdd:cd01643 158 AVLrvILRRFPGK------IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEePAFLQTKDY 231
|
250
....*....|.
gi 489127879 242 IVAGNPRVVKA 252
Cdd:cd01643 232 LSAGFPTLIAA 242
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-233 |
2.60e-52 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 174.22 E-value: 2.60e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVetSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVI 83
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNI--SYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 84 DPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYD----PM--RNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGF 157
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489127879 158 PFKAKQHAASYMKiLGKMFTE-CADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGG 233
Cdd:PLN02737 237 GYEHDDAWATNIE-LFKEFTDvSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGG 312
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-255 |
5.19e-48 |
|
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: 159.73 E-value: 5.19e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVETsqKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGeDQDVQWVID 84
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVET--KADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGG-DAGYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 85 PLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLN---GYRLRGSTARDLDGTIIATGFPFKA 161
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTTDPHFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 162 KQHA-ASYMKILGKmftecADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATG 240
Cdd:cd01641 159 TPGDrAAFERLARA-----VRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSG 233
|
250
....*....|....*
gi 489127879 241 NIVAGNPRVVKAMLA 255
Cdd:cd01641 234 RVVAAGDAELHEALL 248
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-232 |
8.50e-47 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 156.86 E-value: 8.50e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 1 MHPMLTIAVRAARKAGNVIAKHYETPdsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGE-HAGEDQDV 79
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRAD--FEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAiPYEERKSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 80 Q--WVIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGA-----QLNGYRLRGSTARDLDGTI 152
Cdd:COG1218 79 DrfWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAfketgGGERQPIRVRDRPPAEPLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 153 IATGfpfkaKQHAASYMK-ILGKMftECADFRRTGSaALDLAYVAAARVDGYFEIGlkP---WDFAAGELIAREAGALVC 228
Cdd:COG1218 159 VVAS-----RSHRDEETEaLLARL--GVAELVSVGS-SLKFCLVAEGEADLYPRLG--PtmeWDTAAGQAILEAAGGRVT 228
|
....
gi 489127879 229 DFTG 232
Cdd:COG1218 229 DLDG 232
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-232 |
2.67e-45 |
|
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).
Pssm-ID: 238816 [Multi-domain] Cd Length: 242 Bit Score: 152.38 E-value: 2.67e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVEtsQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQ-DVQWV 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVE--RKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGwDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 83 IDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNG---YRLRGSTARDLDGTIIATGfpf 159
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGrpgAVSLQARPPPLQPLRVVAS--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489127879 160 kaKQHAASYMKILGKMFTECaDFRRTGSaALDLAYVAAARVDGYFEIGLKP-WDFAAGELIAREAGALVCDFTG 232
Cdd:cd01638 156 --RSHPDEELEALLAALGVA-EVVSIGS-SLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-255 |
9.94e-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: 151.38 E-value: 9.94e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKG-SNDFVTNVDKAAEAIIIETIRKSYPQhTIITEESGE-HAGEDQDVQW 81
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGaDGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEIGViDNGDEPEYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 82 VIDPLDGTTNFVKRLPHFAVSIAV--RIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIAtgfpf 159
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVS----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 160 kakqhAASYMKILGKMFTECADFRRT---GSAALDLAYVAAARVDGYFEI--GLKPWDFAAGELIAREAGALVCDFTGGH 234
Cdd:cd01515 155 -----YYIYGKNHDRTFKICRKVRRVrifGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKE 229
|
250 260
....*....|....*....|....*.
gi 489127879 235 -----NYLATGNIVAGNPRVVKAMLA 255
Cdd:cd01515 230 lklklNVTERVNIIAANSELHKKLLE 255
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
5-250 |
1.01e-42 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 146.21 E-value: 1.01e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVETSQKG-SNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVI 83
Cdd:PRK12676 7 LEICDDMAKEVEKAIMPLFGTPDAGETVGMGaDGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 84 DPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFpfkAKQ 163
Cdd:PRK12676 87 DPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSIYG---YRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 164 HAASYMKILGKMftecadfRRT---GSAALDLAYVAAARVDGYFEIG--LKPWDFAAGELIAREAGALVCDFTGGH---- 234
Cdd:PRK12676 164 GKERTVKLGRKV-------RRVrilGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNElklp 236
|
250
....*....|....*..
gi 489127879 235 -NYLATGNIVAGNPRVV 250
Cdd:PRK12676 237 lNVTERTNLIAANGEEL 253
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-255 |
2.62e-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: 137.05 E-value: 2.62e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVEtSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 85 PLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFP---FKA 161
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdllDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 162 KQHAAsYMKILGKmftecADFRRTGSAALDLAYVAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGHNYLATGN 241
Cdd:TIGR02067 161 GNRPA-FERLRRA-----ARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGGA 234
|
250
....*....|....
gi 489127879 242 IVAGNPRVVKAMLA 255
Cdd:TIGR02067 235 VAAGNAMLHDEALE 248
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
3.32e-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: 129.82 E-value: 3.32e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVETSQKGS-NDFVTNVDKAAEAIIIETIRKSYPQHTIITEESG---EHAGEDQDVQ 80
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSdNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 81 WVIDPLDGTTNFVKRLPHFAVSIAVrikgrtevavvydpmrnelftatrgqgaqLNGYRLRGSTARDLDGTIIatgfpfk 160
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAV-----------------------------YVILILAEPSHKRVDEKKA------- 124
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489127879 161 AKQHAASYMkilgkmftecadFRRTGSAALDLAYVAAARVDGYFEIGLK--PWDFAAGELIAREAGALVCDF 230
Cdd:cd01636 125 ELQLLAVYR------------IRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTDW 184
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-233 |
1.71e-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: 124.49 E-value: 1.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVEtsQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQ--- 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVA--QKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWqrf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 81 WVIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNG--------YRLRGSTARDLDGTI 152
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkapIHVRPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 153 IATgfpfKAKQHAASYMKILGKmftecaDFRRTGSAALDLAYVAAARVDGYFEIG-LKPWDFAAGELIAREAGALVCDFT 231
Cdd:TIGR01331 159 SRS----HAEEKTTEYLANLGY------DLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLD 228
|
..
gi 489127879 232 GG 233
Cdd:TIGR01331 229 GS 230
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-253 |
4.77e-34 |
|
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: 123.96 E-value: 4.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAK-HYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIIteesGEHAGEDQDVQWV 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPvFRNLGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIV----GEEDSAALGRFWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 83 IDPLDGTTNFVKRLPhFAVSIAVRIKGRTEVAVVYDPMRNE-------LFTATRGQGA---QLNGYRLRGSTARDLDGTI 152
Cdd:cd01517 77 LDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAwlrPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 153 IATGFPFKAKQHAASYMKILGKMFTECADFRRTGSAAldlAYVAAARVDGYFEIGL--------KPWDFAAGELIAREAG 224
Cdd:cd01517 156 RASFCESVESAHSSHRLQAAIKALGGTPQPVRLDSQA---KYAAVARGAADFYLRLplsmsyreKIWDHAAGVLIVEEAG 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 489127879 225 ALVCDFTG-------GHNYLATGNIVAGN----PRVVKAM 253
Cdd:cd01517 233 GKVTDADGkpldfgkGRKLLNNGGLIAAPgeihEQVLEAL 272
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-257 |
3.37e-24 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 98.64 E-value: 3.37e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 6 TIAVRAARKAGNVIAKHYETPdsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGE-DQDVQWVID 84
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTK--FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEgSSDYVWVLD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 85 PLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTIIATGFP--FKAK 162
Cdd:PLN02911 116 PIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSPhmFSGD 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 163 QHAAsymkilgkmFTECADFRRTGSAALD-LAY--VAAARVDGYFEIGLKPWDFAAGELIAREAGALVCDFTGGH----- 234
Cdd:PLN02911 196 AEDA---------FARVRDKVKVPLYGCDcYAYglLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKlrwep 266
|
250 260
....*....|....*....|....*..
gi 489127879 235 --NYLATGNIV--AGNPRVVKAMLANM 257
Cdd:PLN02911 267 spGSLATSFNVvaAGDARLHKQALDIL 293
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
37-226 |
8.70e-21 |
|
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: 88.27 E-value: 8.70e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 37 NDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQWVIDPLDGTTNFVKRLPHFAVSIAV-RIKGRTEVAV 115
Cdd:cd01642 33 GDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALaDPRSKVKAAT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 116 VYDPMRNELFtatrgqgAQLNGYRLRGSTARDL-DGTIIATGFPFKAKQHAASYMKILGKMFTECAD--FRRTGSAALDL 192
Cdd:cd01642 113 LDNFVSGEGG-------LKVYSPPTRFSYISVPkLGPPLVPEVPSKIGIYEGSSRNPEKFLLLSRNGlkFRSLGSAALEL 185
|
170 180 190
....*....|....*....|....*....|....*.
gi 489127879 193 AYVAAARVDGYFEI--GLKPWDFAAGELIAREAGAL 226
Cdd:cd01642 186 AYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLGLH 221
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-232 |
6.02e-20 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 85.90 E-value: 6.02e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQ--W 81
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQryW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 82 VIDPLDGTTNFVKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQG-AQLNGYRLRgSTARDLDGTIIATgfpfk 160
Cdd:PRK10931 81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAwKEECGVRKQ-IQVRDARPPLVVI----- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489127879 161 AKQHAAS----YMKILGKMFTECadfrrTGSaALDLAYVAAARVDGYFEIGlkP---WDFAAGELIAREAGALVCDFTG 232
Cdd:PRK10931 155 SRSHADAelkeYLQQLGEHQTTS-----IGS-SLKFCLVAEGQAQLYPRFG--PtniWDTAAGHAVAIAAGAHVHDWQG 225
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
4-232 |
1.27e-18 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 85.16 E-value: 1.27e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTN-VDKAAEAIIIETIRKsYPQHTIITEESGE-HAGEDQ-DVQ 80
Cdd:PRK14076 5 MLKIALKVAKEIEKKIKPLIGWEKAGEVVKIGADGTPTKrIDLIAENIAINSLEK-FCSGILISEEIGFkKIGKNKpEYI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 81 WVIDPLDGTTNFVKRLPHFAVSIAV-RIKGRT----------------EVAVVYDPMRNELFTATRGQGAQL--NGYRLR 141
Cdd:PRK14076 84 FVLDPIDGTYNALKDIPIYSASIAIaKIDGFDkkikefigknltindlEVGVVKNIATGDTYYAEKGEGAYLlkKGEKKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 142 GSTARDLDGTIIATGFPFKAKQHAASymkilgkMFTECADFRRT---GSAALDLAYVAAARVDGYFEI--GLKPWDFAAG 216
Cdd:PRK14076 164 IEISNISNLKDASIGLFAYGLSLDTL-------KFIKDRKVRRIrlfGSIALEMCYVASGALDAFINVneTTRLCDIAAG 236
|
250
....*....|....*.
gi 489127879 217 ELIAREAGALVCDFTG 232
Cdd:PRK14076 237 YVICKEAGGIITNKNG 252
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
5-232 |
4.65e-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: 67.35 E-value: 4.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 5 LTIAVRAARKAGNVIAKHYETPDSVETSQK-GSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHAGEDQDVQ--- 80
Cdd:cd01640 6 LAVAEKAGGIARDVVKKGRLLILLVEGKTKeGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 81 ------------------------WvIDPLDGTTNFVK-RLPHFAVSIAVRIKGRTEVAVVYDPMRNElftatrgqgaQL 135
Cdd:cd01640 86 ldeeileescpspskdlpeedlgvW-VDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEK----------TA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489127879 136 NGYRLRGSTARDLDGtIIATGFPFKAKQ----------HAASYMKILGKMFTECADFRRTGSAALDLAYVAAARVDGYF- 204
Cdd:cd01640 155 GAGAWLGRTIWGLSG-LGAHSSDFKEREdagkiivstsHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVh 233
|
250 260
....*....|....*....|....*....
gi 489127879 205 -EIGLKPWDFAAGELIAREAGALVCDFTG 232
Cdd:cd01640 234 sTGGIKKWDICAPEAILRALGGDMTDLHG 262
|
|
| |
