|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-260 |
9.63e-105 |
|
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: 304.85 E-value: 9.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 13 YYQVSLELVRKCGPLFLEGFQKPKTDYEVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAktppELTDAP 92
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG----GLTDEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 93 TWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISL 172
Cdd:cd01639 77 TWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 173 IVVSKgRDKNVKRLYKLASSAT-GTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRVYHTSGARFDV 251
Cdd:cd01639 157 DRGDN-FDRYLNNFAKLLAKAVrGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDL 235
|
....*....
gi 320545930 252 MKPDCVCTS 260
Cdd:cd01639 236 MSGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
10-273 |
2.19e-87 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 261.51 E-value: 2.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 10 LEVYYQVSLELVRKCGPLFLEGFQKPKT-DYEVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPEL 88
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTiEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 89 TDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCY 168
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 169 EISLIVVSKGRDKNVKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHV-ENLKPWDLAGGAVILREAGGRVYHTSGA 247
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRAPGVRRVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|....*.
gi 320545930 248 RFDVMKPDCVCTSSEELAKSVIQLIE 273
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLAAALE 267
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
15-274 |
6.58e-83 |
|
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: 249.76 E-value: 6.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 15 QVSLELVRKCGPLFLEGFQKPKTDYEVKSAFyDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPEltdaPTW 94
Cdd:COG0483 5 ELALRAARAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSG----YVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 95 IIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISliv 174
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 175 VSKGRDKNVKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRVYHTSGARFDvMKP 254
Cdd:COG0483 157 YLRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD-LGS 235
|
250 260
....*....|....*....|
gi 320545930 255 DCVCTSSEELAKSVIQLIEG 274
Cdd:COG0483 236 GSLVAANPALHDELLALLRE 255
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
7-262 |
2.27e-71 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 220.72 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 7 EEKLEVYYQVSLELVRKCGPLFLEGFQKPKtDYEVKSAFyDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPp 86
Cdd:PLN02553 4 NDDLEQFLEVAVDAAKAAGQIIRKGFYQTK-HVEHKGQV-DLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 87 ELTDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALV 166
Cdd:PLN02553 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 167 CYEISLivvskGRDKN-----VKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHVENL-KPWDLAGGAVILREAGGR 240
Cdd:PLN02553 161 ATEVGT-----KRDKAtvdatTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGL 235
|
250 260
....*....|....*....|..
gi 320545930 241 VYHTSGARFDVMKPDCVCTSSE 262
Cdd:PLN02553 236 VFDPSGGPFDIMSRRVAASNGH 257
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
49-241 |
1.56e-26 |
|
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: 104.31 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 49 VTVYDKQIEATLTDGLLKTFPESKIIGEEAMANaktpPELTDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGI 128
Cdd:TIGR02067 36 VTEADRAAEEAMRELIAAFFPDHGILGEEFGHN----EEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 129 VYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISLIVVSKGRDKNVKRLYKlassATGTRSFGCAALTLCY 208
Cdd:TIGR02067 112 IFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPGNRPAFERLRR----AARLTRYGGDCYAYLM 187
|
170 180 190
....*....|....*....|....*....|...
gi 320545930 209 IAAGRCDAYHVENLKPWDLAGGAVILREAGGRV 241
Cdd:TIGR02067 188 VAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCF 220
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-260 |
9.63e-105 |
|
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: 304.85 E-value: 9.63e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 13 YYQVSLELVRKCGPLFLEGFQKPKTDYEVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAktppELTDAP 92
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG----GLTDEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 93 TWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISL 172
Cdd:cd01639 77 TWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 173 IVVSKgRDKNVKRLYKLASSAT-GTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRVYHTSGARFDV 251
Cdd:cd01639 157 DRGDN-FDRYLNNFAKLLAKAVrGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDL 235
|
....*....
gi 320545930 252 MKPDCVCTS 260
Cdd:cd01639 236 MSGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
10-273 |
2.19e-87 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 261.51 E-value: 2.19e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 10 LEVYYQVSLELVRKCGPLFLEGFQKPKT-DYEVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPEL 88
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTiEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 89 TDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCY 168
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 169 EISLIVVSKGRDKNVKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHV-ENLKPWDLAGGAVILREAGGRVYHTSGA 247
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRAPGVRRVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|....*.
gi 320545930 248 RFDVMKPDCVCTSSEELAKSVIQLIE 273
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLAAALE 267
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
15-274 |
6.58e-83 |
|
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: 249.76 E-value: 6.58e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 15 QVSLELVRKCGPLFLEGFQKPKTDYEVKSAFyDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPEltdaPTW 94
Cdd:COG0483 5 ELALRAARAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSG----YVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 95 IIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISliv 174
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP--- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 175 VSKGRDKNVKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRVYHTSGARFDvMKP 254
Cdd:COG0483 157 YLRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD-LGS 235
|
250 260
....*....|....*....|
gi 320545930 255 DCVCTSSEELAKSVIQLIEG 274
Cdd:COG0483 236 GSLVAANPALHDELLALLRE 255
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
7-262 |
2.27e-71 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 220.72 E-value: 2.27e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 7 EEKLEVYYQVSLELVRKCGPLFLEGFQKPKtDYEVKSAFyDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPp 86
Cdd:PLN02553 4 NDDLEQFLEVAVDAAKAAGQIIRKGFYQTK-HVEHKGQV-DLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 87 ELTDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALV 166
Cdd:PLN02553 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 167 CYEISLivvskGRDKN-----VKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHVENL-KPWDLAGGAVILREAGGR 240
Cdd:PLN02553 161 ATEVGT-----KRDKAtvdatTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGL 235
|
250 260
....*....|....*....|..
gi 320545930 241 VYHTSGARFDVMKPDCVCTSSE 262
Cdd:PLN02553 236 VFDPSGGPFDIMSRRVAASNGH 257
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
14-241 |
7.15e-65 |
|
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: 202.93 E-value: 7.15e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 14 YQVSLELVRKCGPLFLEGFQKPKTDyEVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPeltDAPT 93
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTV-ETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSD---GGRV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 94 WIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISli 173
Cdd:cd01637 77 WVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNAS-- 154
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320545930 174 VVSKGRDKNVKrlyKLASSATGTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRV 241
Cdd:cd01637 155 MLRSNRAAVLA---SLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIV 219
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
19-241 |
9.52e-43 |
|
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: 146.33 E-value: 9.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 19 ELVRKCGPLFLEGFQKpKTDYEVKsAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAmanAKTPPELTDapTWIIDP 98
Cdd:cd01643 6 AIAQEAGDRALADFGN-SLSAETK-ADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG---GGIFPSSGW--YWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 99 IDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISLIVVSKG 178
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASARA 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 320545930 179 RDKNVKRLYklassATGTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRV 241
Cdd:cd01643 159 VLRVILRRF-----PGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSW 216
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
16-247 |
2.25e-42 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 146.11 E-value: 2.25e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 16 VSLELVRKCGPLFLEGFQKPKTDYEVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPELTdaptWI 95
Cdd:PRK10757 7 IAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ----WV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 96 IDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISLiVV 175
Cdd:PRK10757 83 IDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPF-KA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 320545930 176 SKGRDKNVKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRVYHTSGA 247
Cdd:PRK10757 162 KQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGG 233
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
15-249 |
1.10e-36 |
|
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: 130.42 E-value: 1.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 15 QVSLELVRKCGPLFLEGFQKPKT--DYEVKSafydLVTVYDKQIEATLTDGLLKTFPESKIIGEEAmanAKTPPELTDAP 92
Cdd:cd01638 3 ELLIRIAREAGDAILEVYRGGFTveRKEDGS----PVTAADLAANAFIVEGLAALRPDIPVLSEES---ADDPLRLGWDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 93 TWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQAlvcyEISL 172
Cdd:cd01638 76 FWLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPL----QPLR 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 320545930 173 IVVSKGR-DKNVKRLYKLASSATgTRSFGcAALTLCYIAAGRCDAY-HVENLKPWDLAGGAVILREAGGRVYHTSGARF 249
Cdd:cd01638 152 VVASRSHpDEELEALLAALGVAE-VVSIG-SSLKFCLVAEGEADIYpRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
93-274 |
6.09e-36 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 129.26 E-value: 6.09e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 93 TWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQalvcyeiSL 172
Cdd:PRK12676 83 TVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNE-------SA 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 173 IVVSkGRDKNVKRLYKLASSATGTRSFGCAALTLCYIAAGRCDAYhV---ENLKPWDLAGGAVILREAGGRVYHTSGARF 249
Cdd:PRK12676 156 VSIY-GYRRGKERTVKLGRKVRRVRILGAIALELCYVASGRLDAF-VdvrNYLRVTDIAAGKLICEEAGGIVTDEDGNEL 233
|
170 180 190
....*....|....*....|....*....|
gi 320545930 250 DV-----MKPDCVCTSSEELAKSVIQLIEG 274
Cdd:PRK12676 234 KLplnvtERTNLIAANGEELHKKILELLEG 263
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
49-250 |
1.17e-34 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 125.66 E-value: 1.17e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 49 VTVYDKQIEATLTDGLLKTFPESKIIGEEAmANAKTPPELTDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGI 128
Cdd:COG1218 38 VTEADLAAHAIILAGLAALTPDIPVLSEES-AAIPYEERKSWDRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 129 VYNPSANELYSAWQGHGAYL-----NGQPIEVSNAKKINQALVcyeisliVVSKG-RDKNVKRLYKlASSATGTRSFGcA 202
Cdd:COG1218 117 VYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPLRV-------VASRShRDEETEALLA-RLGVAELVSVG-S 187
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 320545930 203 ALTLCYIAAGRCDAYhvenlkP-------WDLAGGAVILREAGGRVYHTSGARFD 250
Cdd:COG1218 188 SLKFCLVAEGEADLY------PrlgptmeWDTAAGQAILEAAGGRVTDLDGKPLR 236
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
93-272 |
3.15e-33 |
|
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: 122.10 E-value: 3.15e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 93 TWIIDPIDGTNNYVRKIPHCCISVGLAINKELVL--GIVYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEI 170
Cdd:cd01515 78 TVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPyyGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 171 SLIVVSKGRD--KNVKRlyklassatgTRSFGCAALTLCYIAAGRCDAY-HV-ENLKPWDLAGGAVILREAGGRVYHTSG 246
Cdd:cd01515 158 YGKNHDRTFKicRKVRR----------VRIFGSVALELCYVASGALDAFvDVrENLRLVDIAAGYLIAEEAGGIVTDENG 227
|
170 180 190
....*....|....*....|....*....|
gi 320545930 247 A----RFDVMKPDCVCTSSEELAKSVIQLI 272
Cdd:cd01515 228 KelklKLNVTERVNIIAANSELHKKLLELL 257
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
47-251 |
1.54e-32 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 122.60 E-value: 1.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 47 DLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPELTdaptWIIDPIDGTNNYVRKIPHCCISVGLAINKELVL 126
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYL----WCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAA 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 127 GIVYN----PSA--NELYSAWQGHGAYLNGQPIEVSNAKKINQalvcyeiSLIVVSKGRD------KNVKRLYKLASSAT 194
Cdd:PLN02737 187 ATVVEfvggPMCwnTRTFSASAGGGAFCNGQKIHVSQTDKVER-------SLLVTGFGYEhddawaTNIELFKEFTDVSR 259
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 320545930 195 GTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRVYHTSGARFDV 251
Cdd:PLN02737 260 GVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSV 316
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
41-250 |
1.98e-31 |
|
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase family, and catalyses the hydrolysis of 3'-phosphoadenosine-5'-phosphate (PAP) to AMP. In Saccharomyces cerevisiae, HAL2 (MET22) is involved in methionine biosynthesis and provides increased salt tolerance when over-expressed. Bacterial members of this domain family may differ in their substrate specificity and dephosphorylate different targets, as the substrate binding site does not appear to be conserved in that sub-set.
Pssm-ID: 238775 [Multi-domain] Cd Length: 274 Bit Score: 117.80 E-value: 1.98e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 41 VKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMAnaktppelTDAPTWIIDPIDGTNNYVRKIPHCcISVGLAI 120
Cdd:cd01517 30 WKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA--------ALGRFWVLDPIDGTKGFLRGDQFA-VALALIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 121 NKELVLGIVYNPSANE-------LYSAWQGHGAYLNgqPIEVSNAKKInQALVCYEISLIVVSKGRDKNvkrlYKLASSA 193
Cdd:cd01517 101 DGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLR--PLDGSSLQPL-SVRQLTNAARASFCESVESA----HSSHRLQ 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320545930 194 TGTRSFGCAALTLCY--------IAAGRCDAY------HVENLKPWDLAGGAVILREAGGRVYHTSGARFD 250
Cdd:cd01517 174 AAIKALGGTPQPVRLdsqakyaaVARGAADFYlrlplsMSYREKIWDHAAGVLIVEEAGGKVTDADGKPLD 244
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
18-241 |
2.01e-31 |
|
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: 116.97 E-value: 2.01e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 18 LELVRKCGPLFLEGFQKPkTDYEVKSAFyDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMAnaktppELTDAP-TWII 96
Cdd:cd01641 6 LELADAAGQITLPYFRTR-LQVETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEEFGN------EGGDAGyVWVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 97 DPIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLN---GQPIEVSNAKKINQAlVCYEISLI 173
Cdd:cd01641 78 DPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEA-VLSTTDPH 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 320545930 174 VVSKGRDKNVKRLYKlassATGTRSFGCAALTLCYIAAGRCDAYHVENLKPWDLAGGAVILREAGGRV 241
Cdd:cd01641 157 FFTPGDRAAFERLAR----AVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVI 220
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
49-241 |
1.56e-26 |
|
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: 104.31 E-value: 1.56e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 49 VTVYDKQIEATLTDGLLKTFPESKIIGEEAMANaktpPELTDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGI 128
Cdd:TIGR02067 36 VTEADRAAEEAMRELIAAFFPDHGILGEEFGHN----EEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 129 VYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVCYEISLIVVSKGRDKNVKRLYKlassATGTRSFGCAALTLCY 208
Cdd:TIGR02067 112 IFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPGNRPAFERLRR----AARLTRYGGDCYAYLM 187
|
170 180 190
....*....|....*....|....*....|...
gi 320545930 209 IAAGRCDAYHVENLKPWDLAGGAVILREAGGRV 241
Cdd:TIGR02067 188 VAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCF 220
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
19-250 |
9.98e-26 |
|
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: 102.14 E-value: 9.98e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 19 ELVRKCGPLFLEGFQKPktdYEVKS-AFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAmANAKTPPELTDAPTWIID 97
Cdd:TIGR01331 7 KIARAAGEEILPVYQKE---LAVAQkADNSPVTEADRAAHRFILEGLRALTPDIPVLSEED-ASIPLTPRQTWQRFWLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 98 PIDGTNNYVRKIPHCCISVGLAINKELVLGIVYNPSANELYSAWQGHGAYLNG------QPIEVSNAKkiNQALvcyeis 171
Cdd:TIGR01331 83 PLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkAPIHVRPWP--SGPL------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 172 LIVVSKGRDKNVKRLYkLASSATGTRSFGCAALTLCYIAAGRCDAYhvENLKP---WDLAGGAVILREAGGRVYHTSGAR 248
Cdd:TIGR01331 155 LVVISRSHAEEKTTEY-LANLGYDLRTSGGSSLKFCLVAEGSADIY--PRLGPtgeWDTAAGHAVLAAAGGAIFDLDGSP 231
|
..
gi 320545930 249 FD 250
Cdd:TIGR01331 232 LL 233
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
64-272 |
8.03e-24 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 100.57 E-value: 8.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 64 LLKTFPESKIIGEEA--MANAKTPPELTdaptWIIDPIDGTNNYVRKIPHCCISVGLA-INKE----------------L 124
Cdd:PRK14076 56 SLEKFCSGILISEEIgfKKIGKNKPEYI----FVLDPIDGTYNALKDIPIYSASIAIAkIDGFdkkikefigknltindL 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 125 VLGIVYNPSANELYSAWQGHGAYL----NGQPIEVSNAKKINQA---LVCYEISLIVVSKGRDKNVKRLyklassatgtR 197
Cdd:PRK14076 132 EVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDAsigLFAYGLSLDTLKFIKDRKVRRI----------R 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 198 SFGCAALTLCYIAAGRCDAY-HV-ENLKPWDLAGGAVILREAGGRVYHTSGA----RFDVMKPDCVCTSSEELAKSVIQL 271
Cdd:PRK14076 202 LFGSIALEMCYVASGALDAFiNVnETTRLCDIAAGYVICKEAGGIITNKNGKplnmKLDINEKTSVICSNEILHKKLVGI 281
|
.
gi 320545930 272 I 272
Cdd:PRK14076 282 F 282
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
15-241 |
1.30e-22 |
|
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: 92.07 E-value: 1.30e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 15 QVSLELVRKCGPLFLEGFQKPKTDY-EVKSAFYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAmANAKTPPELTDAPT 93
Cdd:cd01636 2 EELCRVAKEAGLAILKAFGRELSGKvKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEES-GVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 94 WIIDPIDGTNNYVRKIPHCCISVGLAinkelvlgivynpsanelysawqghgaylngqpievsnakkinqalvcyeISLI 173
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY--------------------------------------------------VILI 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 320545930 174 VVSKGRDKNVKRLYKLASSA-TGTRSFGCAALTLCYIAAGRCDAY-HVEN-LKPWDLAGGAVILREAGGRV 241
Cdd:cd01636 111 LAEPSHKRVDEKKAELQLLAvYRIRIVGSAVAKMCLVALGLADIYyEPGGkRRAWDVAASAAIVREAGGIM 181
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
49-239 |
1.89e-16 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 77.45 E-value: 1.89e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 49 VTVYDKQIEATLTDGLLKTFPESKIIGEEamaNAKTPPELTDAPTWIIDPIDGTNNYVRKIPHCCISVGLAINKELVLGI 128
Cdd:PLN02911 70 VTIADRAAEEAMRSIILENFPSHAIFGEE---HGLRCGEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 129 VYNPSANELYSAWQGHGAYLNGQPIEVSNAKKINQALVcYEISLIVVSKGRDKNVKRLyklaSSATGTRSFGCAaltlCY 208
Cdd:PLN02911 147 IDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYL-YTTSPHMFSGDAEDAFARV----RDKVKVPLYGCD----CY 217
|
170 180 190
....*....|....*....|....*....|....*
gi 320545930 209 ----IAAGRCDAYHVENLKPWDLAGGAVILREAGG 239
Cdd:PLN02911 218 ayglLASGHVDLVVESGLKPYDYLALVPVVEGAGG 252
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
9-242 |
3.58e-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: 71.20 E-value: 3.58e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 9 KLEVYYQVSLE------LVRKCGPLFlEGFQKPKTDyevKSAfYDLVTVYDKQIEATLTDGLLKTFPESKIIGEEAmANA 82
Cdd:cd01640 1 LLRSLLAVAEKaggiarDVVKKGRLL-ILLVEGKTK---EGA-NDFKTLADRLSQRVIKHSLQKQFPKLKIIGEED-NEF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 83 KTPPELTDAP------------------------TWIiDPIDGTNNYVRKIPHCC-ISVGLAINKELVLGIVYNPSANel 137
Cdd:cd01640 75 ENQEDESRDVdldeeileescpspskdlpeedlgVWV-DPLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQPFYE-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 138 YSAWqgHGAYLNGQPIEVSNAKKINQALVCYEISLIVV----SKGRDKNVKRlyKLASSATGTRSFGCAAL-TLCYIAaG 212
Cdd:cd01640 152 KTAG--AGAWLGRTIWGLSGLGAHSSDFKEREDAGKIIvstsHSHSVKEVQL--ITAGNKDEVLRAGGAGYkVLQVLE-G 226
|
250 260 270
....*....|....*....|....*....|..
gi 320545930 213 RCDAY-HVEN-LKPWDLAGGAVILREAGGRVY 242
Cdd:cd01640 227 LADAYvHSTGgIKKWDICAPEAILRALGGDMT 258
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
47-238 |
2.90e-12 |
|
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: 64.78 E-value: 2.90e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 47 DLVTVYDKQIEATLTDGLLKTFPESKIIGEEAMANAKTPPEltdaPTWIIDPIDGTNNYVRKIPHCCISVGLA-----IN 121
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGE----YIAVLDPLDGSTNYLSGIPFYSVSVALAdprskVK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 122 KELVLGIVYNPSANELYSaWQGHGAYLNGQPIEvsnakkinQALVCYEISLIVVSKGRDKNVKRLYKLASSATGTRSFGC 201
Cdd:cd01642 110 AATLDNFVSGEGGLKVYS-PPTRFSYISVPKLG--------PPLVPEVPSKIGIYEGSSRNPEKFLLLSRNGLKFRSLGS 180
|
170 180 190
....*....|....*....|....*....|....*....
gi 320545930 202 AALTLCYIAAGRCDAY--HVENLKPWDLAGGAVILREAG 238
Cdd:cd01642 181 AALELAYTCEGSFVLFldLRGKLRNFDVAAALGACKRLG 219
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
49-250 |
6.79e-10 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 58.17 E-value: 6.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 49 VTVYDKQIEATLTDGLLKTFPESKIIGEEAmanaktPPELTDAPTW----IIDPIDGTNNYVRKIPHCCISVGLAINKEL 124
Cdd:PRK10931 37 VTAADIAAHTVIKDGLRTLTPDIPVLSEED------PPAWEVRQHWqrywLVDPLDGTKEFIKRNGEFTVNIALIEQGKP 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 320545930 125 VLGIVYNPSANELYSAwQGHGAYL--NGQ--PIEVSNAKKinqalvcyeiSLIVVSKG-RDKNVKR-LYKLASSAtgTRS 198
Cdd:PRK10931 111 VLGVVYAPVMNVMYSA-AEGKAWKeeCGVrkQIQVRDARP----------PLVVISRShADAELKEyLQQLGEHQ--TTS 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 320545930 199 FGcAALTLCYIAAGRCDAY------HVenlkpWDLAGGAVILREAGGRVYHTSGARFD 250
Cdd:PRK10931 178 IG-SSLKFCLVAEGQAQLYprfgptNI-----WDTAAGHAVAIAAGAHVHDWQGKTLD 229
|
|
| |
