|
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: 587.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 1 MHPMLNIAIRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 161 LKQHSKSYINAIGALFTHCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 504729117 241 NLVAGNPRVVKSILGTIREELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.62e-130 |
|
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.
Pssm-ID: 238817 [Multi-domain] Cd Length: 244 Bit Score: 369.17 E-value: 1.62e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDaVEASQKGS-NDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQWV 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLG-LNVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 83 IDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFKLK 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 163 QHSKSYINAIGALFT-HCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASGN 241
Cdd:cd01639 160 DNFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*
gi 504729117 242 LVAGN 246
Cdd:cd01639 240 ILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
3.71e-124 |
|
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: 353.77 E-value: 3.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 2 HPMLNIAIRAARKAGNLIAKNYETPDaVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 82 VIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFkl 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPY-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 162 KQHSKSYINAIGALFTHCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASGN 241
Cdd:COG0483 158 LRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*...
gi 504729117 242 LVAGNPRVVKSILGTIRE 259
Cdd:COG0483 238 LVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-261 |
1.81e-83 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 251.11 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 1 MHPMLNIAIRAARKAGNLIAKNYETP-DAVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEE----CGELVGE 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 76 DPAVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 156 GFPFKLKQHSKSYINAIGALFTHCA-DFRRTGSAALDLAYVAAGRVDGFFEIG-LKPWDFAGGELLVREAGGIVTDFVGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRApGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|....*...
gi 504729117 234 HNYLASGNLVAGNPRVVKSILGTIREEL 261
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLAAALEEI 269
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-254 |
5.19e-42 |
|
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: 144.37 E-value: 5.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEaSQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFklkqh 164
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPD----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 165 sksyinaigALFT---HCADFRRTGSAALDLAY--------VAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFvGG 233
Cdd:TIGR02067 156 ---------LLDDpgnRPAFERLRRAARLTRYGgdcyaylmVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDW-DG 225
|
250 260
....*....|....*....|..
gi 504729117 234 HNYLASGNLVA-GNPRVVKSIL 254
Cdd:TIGR02067 226 KPAPDGGGAVAaGNAMLHDEAL 247
|
|
| |
|
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: 587.54 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 1 MHPMLNIAIRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 161 LKQHSKSYINAIGALFTHCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 504729117 241 NLVAGNPRVVKSILGTIREELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.62e-130 |
|
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.
Pssm-ID: 238817 [Multi-domain] Cd Length: 244 Bit Score: 369.17 E-value: 1.62e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDaVEASQKGS-NDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQWV 82
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLG-LNVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 83 IDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFKLK 162
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 163 QHSKSYINAIGALFT-HCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASGN 241
Cdd:cd01639 160 DNFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*
gi 504729117 242 LVAGN 246
Cdd:cd01639 240 ILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
3.71e-124 |
|
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: 353.77 E-value: 3.71e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 2 HPMLNIAIRAARKAGNLIAKNYETPDaVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 82 VIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFkl 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPY-- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 162 KQHSKSYINAIGALFTHCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASGN 241
Cdd:COG0483 158 LRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*...
gi 504729117 242 LVAGNPRVVKSILGTIRE 259
Cdd:COG0483 238 LVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-261 |
1.81e-83 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 251.11 E-value: 1.81e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 1 MHPMLNIAIRAARKAGNLIAKNYETP-DAVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEE----CGELVGE 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggakGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 76 DPAVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 156 GFPFKLKQHSKSYINAIGALFTHCA-DFRRTGSAALDLAYVAAGRVDGFFEIG-LKPWDFAGGELLVREAGGIVTDFVGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRApGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|....*...
gi 504729117 234 HNYLASGNLVAGNPRVVKSILGTIREEL 261
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLAAALEEI 269
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-245 |
5.57e-78 |
|
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent metal ions such as Mg++, and many members are inhibited by Li+ (which is thought to displace a bivalent ion in the active site). Substrates include fructose-1,6-bisphosphate, inositol poly- and monophosphates, PAP and PAPS, sedoheptulose-1,7-bisphosphate and probably others.
Pssm-ID: 238815 [Multi-domain] Cd Length: 238 Bit Score: 235.67 E-value: 5.57e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEASqKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEE-CGELVGEDPAVQWVI 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEgGGSGNVSDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 84 DPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFKLKQ 163
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 164 HSKsyinAIGALFTHCADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGG-HNYLASGNL 242
Cdd:cd01637 160 RAA----VLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEpLDTLNRSGI 235
|
...
gi 504729117 243 VAG 245
Cdd:cd01637 236 IAA 238
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-247 |
3.85e-67 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 209.16 E-value: 3.85e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEasQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEEC-----GELVGEDPAv 79
Cdd:PLN02553 11 LEVAVDAAKAAGQIIRKGFYQTKHVE--HKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaasgGTELTDEPT- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 80 qWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPF 159
Cdd:PLN02553 88 -WIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGT 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 160 KLKQHSKSYI-NAIGALFTHCADFRRTGSAALDLAYVAAGRVDGFFEIGL-KPWDFAGGELLVREAGGIVTDFVGGHNYL 237
Cdd:PLN02553 167 KRDKATVDATtNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDI 246
|
250
....*....|
gi 504729117 238 ASGNLVAGNP 247
Cdd:PLN02553 247 MSRRVAASNG 256
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-243 |
8.74e-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: 187.16 E-value: 8.74e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYEtpDAVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVqWVID 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFG--NSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY-WVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFKLKQH 164
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 165 SKSYINAIGALFThcadFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVT------DFVGGHNYLA 238
Cdd:cd01643 158 AVLRVILRRFPGK----IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTildeepAFLQTKDYLS 233
|
....*
gi 504729117 239 SGNLV 243
Cdd:cd01643 234 AGFPT 238
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-255 |
3.98e-52 |
|
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: 170.13 E-value: 3.98e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEAsqKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGElVGEDPAVQWVID 84
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVET--KADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGN-EGGDAGYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLN---GYRLRSSTARDLEGTVLATGFPFKL 161
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTTDPHFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 162 KQHSKsyiNAIGALFTHCADFrRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGHNYLASGN 241
Cdd:cd01641 159 TPGDR---AAFERLARAVRLT-RYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGR 234
|
250
....*....|....
gi 504729117 242 LVAGNPRVVKSILG 255
Cdd:cd01641 235 VVAAGDAELHEALL 248
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-233 |
4.32e-50 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 168.44 E-value: 4.32e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVeaSQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQWVI 83
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNI--SYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 84 DPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYD----PM--RNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGF 157
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 158 PFklkQHSKSYINAIgALFTH----CADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGG 233
Cdd:PLN02737 237 GY---EHDDAWATNI-ELFKEftdvSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGG 312
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
5-258 |
3.87e-46 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 155.07 E-value: 3.87e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEASQKG-SNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQWVI 83
Cdd:PRK12676 7 LEICDDMAKEVEKAIMPLFGTPDAGETVGMGaDGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 84 DPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDL-EGTVLATGFPFKLK 162
Cdd:PRK12676 87 DPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELnESAVSIYGYRRGKE 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 163 QHSKSYINAigalfthcadfRRT---GSAALDLAYVAAGRVDGFFEIG--LKPWDFAGGELLVREAGGIVTDFVGGH--- 234
Cdd:PRK12676 167 RTVKLGRKV-----------RRVrilGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNElkl 235
|
250 260
....*....|....*....|....*..
gi 504729117 235 --NYLASGNLVAGNPRVV-KSILGTIR 258
Cdd:PRK12676 236 plNVTERTNLIAANGEELhKKILELLE 262
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-257 |
3.22e-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: 152.53 E-value: 3.22e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEASQKG-SNDFVTNVDRDAERLIVEVIRKSYPQhTIIGEECGELV-GEDPAVQW 81
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGaDGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEIGVIDnGDEPEYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 82 VIDPLDGTTNFIKRLPHFAVSIAV--RIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATgFPF 159
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSY-YIY 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 160 KLKQHSKSYInaigalfthCADFRRT---GSAALDLAYVAAGRVDGFFEI--GLKPWDFAGGELLVREAGGIVTDFVGGH 234
Cdd:cd01515 159 GKNHDRTFKI---------CRKVRRVrifGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKE 229
|
250 260
....*....|....*....|....*...
gi 504729117 235 -----NYLASGNLVAGNPRVVKSILGTI 257
Cdd:cd01515 230 lklklNVTERVNIIAANSELHKKLLELL 257
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-230 |
1.54e-44 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 151.08 E-value: 1.54e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 1 MHPMLNIAIRAARKAGNLIAKNYETPdaVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQ 80
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRAD--FEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 81 ---WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGA-----QLNGYRLRSSTARDLEG-T 151
Cdd:COG1218 79 drfWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAfketgGGERQPIRVRDRPPAEPlR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 152 VLAtgfpfklkqhSKS--------YINAIGalfthCADFRRTGSaALDLAYVAAGRVDGFFEIGlkP---WDFAGGELLV 220
Cdd:COG1218 159 VVA----------SRShrdeeteaLLARLG-----VAELVSVGS-SLKFCLVAEGEADLYPRLG--PtmeWDTAAGQAIL 220
|
250
....*....|
gi 504729117 221 REAGGIVTDF 230
Cdd:COG1218 221 EAAGGRVTDL 230
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-232 |
1.37e-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: 145.45 E-value: 1.37e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEasQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQ-WV 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVE--RKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDRfWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 83 IDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNG----YRLRSSTARDLEGTVLATgfp 158
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGrpgaVSLQARPPPLQPLRVVAS--- 155
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504729117 159 fklKQHSKSYINAIGALFTHCaDFRRTGSaALDLAYVAAGRVDGFFEIGLKP-WDFAGGELLVREAGGIVTDFVG 232
Cdd:cd01638 156 ---RSHPDEELEALLAALGVA-EVVSIGS-SLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-254 |
5.19e-42 |
|
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: 144.37 E-value: 5.19e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEaSQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPFklkqh 164
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPD----- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 165 sksyinaigALFT---HCADFRRTGSAALDLAY--------VAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFvGG 233
Cdd:TIGR02067 156 ---------LLDDpgnRPAFERLRRAARLTRYGgdcyaylmVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDW-DG 225
|
250 260
....*....|....*....|..
gi 504729117 234 HNYLASGNLVA-GNPRVVKSIL 254
Cdd:TIGR02067 226 KPAPDGGGAVAaGNAMLHDEAL 247
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-259 |
2.99e-36 |
|
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: 129.74 E-value: 2.99e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEASQ-KGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGedPAvqWV 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGAGDVVWkKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAALG--RF--WV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 83 IDPLDGTTNFIKRLPhFAVSIAVRIKGRTEVAVVYDPMRNE-------LFTATRGQGA---QLNGYRLRSSTARDLEGTV 152
Cdd:cd01517 77 LDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAwlrPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 153 LATGFPFKLKQHSKSYINAIGALFTHCADFRRTGSAAlDLAYVAAGRVDGFFEIG------LKPWDFAGGELLVREAGGI 226
Cdd:cd01517 156 RASFCESVESAHSSHRLQAAIKALGGTPQPVRLDSQA-KYAAVARGAADFYLRLPlsmsyrEKIWDHAAGVLIVEEAGGK 234
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 504729117 227 VTDFVG-------GHNYLASGNLVAGNPRVVKSILGTIRE 259
Cdd:cd01517 235 VTDADGkpldfgkGRKLLNNGGLIAAPGEIHEQVLEALRE 274
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-233 |
1.30e-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: 127.57 E-value: 1.30e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEasQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQ--- 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVA--QKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWqrf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNG--------YRLRSSTARDLEGTV 152
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkapIHVRPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 153 LATGFPFKLkqhsKSYINAIGALFTHCadfrrtGSAALDLAYVAAGRVDGFFEIG-LKPWDFAGGELLVREAGGIVTDFV 231
Cdd:TIGR01331 159 SRSHAEEKT----TEYLANLGYDLRTS------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLD 228
|
..
gi 504729117 232 GG 233
Cdd:TIGR01331 229 GS 230
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
1.91e-35 |
|
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: 125.20 E-value: 1.91e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 5 LNIAIRAARKAGNLIAKNYETPDAVEASQKGS-NDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECG---ELVGEDPAVQ 80
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSdNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 81 WVIDPLDGTTNFIKRLPHFAVSIAVrikgrtevavvydpmrnelftatrgqgaqlngYRLRSSTARDLEGTVLATGFPFK 160
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAV--------------------------------YVILILAEPSHKRVDEKKAELQL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 504729117 161 LKQHSksyinaigalfthcadFRRTGSAALDLAYVAAGRVDGFFEIGLK--PWDFAGGELLVREAGGIVTDF 230
Cdd:cd01636 129 LAVYR----------------IRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
7-257 |
1.57e-26 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 104.80 E-value: 1.57e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 7 IAIRAARKAGNLIAKNYETPdaVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPA-VQWVIDP 85
Cdd:PLN02911 39 VAHKLADAAGEVTRKYFRTK--FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSdYVWVLDP 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRSSTARDLEGTVLATGFPfklkqHS 165
Cdd:PLN02911 117 IDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSP-----HM 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 166 KSYINAigALFTHCADFRRTGSAALD-LAY--VAAGRVDGFFEIGLKPWDFAGGELLVREAGGIVTDFVGGH-------N 235
Cdd:PLN02911 192 FSGDAE--DAFARVRDKVKVPLYGCDcYAYglLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKlrwepspG 269
|
250 260
....*....|....*....|....
gi 504729117 236 YLASGNLV--AGNPRVVKSILGTI 257
Cdd:PLN02911 270 SLATSFNVvaAGDARLHKQALDIL 293
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
4-229 |
5.23e-22 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 94.79 E-value: 5.23e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEASQKGSNDFVTN-VDRDAERLIVEVIRKsYPQHTIIGEECGEL-VGED-PAVQ 80
Cdd:PRK14076 5 MLKIALKVAKEIEKKIKPLIGWEKAGEVVKIGADGTPTKrIDLIAENIAINSLEK-FCSGILISEEIGFKkIGKNkPEYI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 81 WVIDPLDGTTNFIKRLPHFAVSIAV-RIKGRT----------------EVAVVYDPMRNELFTATRGQGAQL----NGYR 139
Cdd:PRK14076 84 FVLDPIDGTYNALKDIPIYSASIAIaKIDGFDkkikefigknltindlEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 140 LRSSTARDLEGTVLAtGFPFKLKQHSKSYINAigalfthcADFRRT---GSAALDLAYVAAGRVDGFFEI--GLKPWDFA 214
Cdd:PRK14076 164 IEISNISNLKDASIG-LFAYGLSLDTLKFIKD--------RKVRRIrlfGSIALEMCYVASGALDAFINVneTTRLCDIA 234
|
250
....*....|....*
gi 504729117 215 GGELLVREAGGIVTD 229
Cdd:PRK14076 235 AGYVICKEAGGIITN 249
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
4-224 |
3.74e-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: 89.04 E-value: 3.74e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIaknYETPDA--VEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEECGELVGEDPAVQW 81
Cdd:cd01642 1 MLEVLEKITKEIILLL---NEKNRQglVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 82 VIDPLDGTTNFIKRLPHFAVSIAV-RIKGRTEVAVVYDPMRNELFtatrgqgAQLNGYRLRSSTARDLE-GTVLATGFPF 159
Cdd:cd01642 78 VLDPLDGSTNYLSGIPFYSVSVALaDPRSKVKAATLDNFVSGEGG-------LKVYSPPTRFSYISVPKlGPPLVPEVPS 150
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 504729117 160 KLKQHSKSYINAIGALFTHCAD--FRRTGSAALDLAYVAAGRVDGFFEI--GLKPWDFAGGELLVREAG 224
Cdd:cd01642 151 KIGIYEGSSRNPEKFLLLSRNGlkFRSLGSAALELAYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLG 219
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-131 |
2.94e-16 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 75.88 E-value: 2.94e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDRDAERLIVEVIRKSYPQHTIIGEEcgelvgeDPAV---- 79
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEE-------DPPAwevr 73
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 504729117 80 -----QWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQ 131
Cdd:PRK10931 74 qhwqrYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK 130
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
4-267 |
3.49e-14 |
|
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: 70.81 E-value: 3.49e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 4 MLNIAIRAARKAGNLIAKNYETPDAVEASQKGSN-----DFVTNVDRDAERLIVEVIRKSYPQHTIIGEE-------CGE 71
Cdd:cd01640 1 LLRSLLAVAEKAGGIARDVVKKGRLLILLVEGKTkeganDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEdnefenqEDE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 72 L--VGEDPAV-------QWV----------IDPLDGTTNFIK-RLPHFAVSIAVRIKGRTEVAVVYDPMRNElftatrgq 131
Cdd:cd01640 81 SrdVDLDEEIleescpsPSKdlpeedlgvwVDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEK-------- 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504729117 132 gaQLNGYRLRSSTARDLEGtVLATGFPFKLKQ----------HSKSYINAIGALFTHCADFRRTGSAALDLAYVAAGRVD 201
Cdd:cd01640 153 --TAGAGAWLGRTIWGLSG-LGAHSSDFKEREdagkiivstsHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLAD 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504729117 202 G--FFEIGLKPWDFAGGELLVREAGGIVTDFVGghNYLAsgNLVAGNPRVVKSILGTIREELSDALKR 267
Cdd:cd01640 230 AyvHSTGGIKKWDICAPEAILRALGGDMTDLHG--EPLS--YSKAVKPVNKGGLLATIRSNHEAYLDK 293
|
|
| |
