|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-260 |
3.23e-115 |
|
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: 331.04 E-value: 3.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPT 92
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES---GAAGGLTDEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 93 WIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILQLGSI 172
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 173 RSPVMQKsFVDSYKTvMFDKQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDV 252
Cdd:cd01639 158 RGDNFDR-YLNNFAK-LLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDL 235
|
....*...
gi 146350806 253 MSRKVLCA 260
Cdd:cd01639 236 MSGNILAG 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
17-265 |
7.38e-90 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 267.67 E-value: 7.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFdSPESKVDTKS--SNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWT-DAPTW 93
Cdd:pfam00459 9 AVELAAKAGEILREAF-SNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTdDGPTW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 94 IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLIlqlgSIR 173
Cdd:pfam00459 88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV----TLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 174 SPVMQKSFVDSY--KTVMFDKQCHGHRSFGSAAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGSPF 250
Cdd:pfam00459 164 GVSSRKDTSEASflAKLLKLVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGGPF 243
|
250
....*....|....*
gi 146350806 251 DVMSRKVLCAGTAEL 265
Cdd:pfam00459 244 DLLAGRVIAANPKVL 258
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
17-273 |
4.77e-86 |
|
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: 257.47 E-value: 4.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPESKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKiewTDAPTWIID 96
Cdd:COG0483 7 ALRAARAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR---DSGYVWVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILqlgSIRSPV 176
Cdd:COG0483 83 PIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVAT---GFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 177 MQKSFVDSYKTVMfdKQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDVMSRK 256
Cdd:COG0483 160 DDREYLAALAALL--PRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 146350806 257 VLcAGTAELGRDLSACL 273
Cdd:COG0483 238 LV-AANPALHDELLALL 253
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
7-274 |
7.63e-77 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 234.58 E-value: 7.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 7 HEEEQvFVDYAIELVKKAGTLVRTAFDSPEsKVDTKSSnTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIE 86
Cdd:PLN02553 5 DDLEQ-FLEVAVDAAKAAGQIIRKGFYQTK-HVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 87 WTDAPTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLI 166
Cdd:PLN02553 82 LTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 167 LQLGSIRSpvmqKSFVDSyktvMFDK------QCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHA-WDVAAPSIIVTEAG 239
Cdd:PLN02553 162 TEVGTKRD----KATVDA----TTNRinallyKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAG 233
|
250 260 270
....*....|....*....|....*....|....*
gi 146350806 240 GVVTDPTGSPFDVMSRKVLCAGtAELGRDLSACLT 274
Cdd:PLN02553 234 GLVFDPSGGPFDIMSRRVAASN-GHLKDAFVEALR 267
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
17-273 |
1.42e-37 |
|
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: 133.20 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPESKVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPTWIID 96
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKT-PVTEADRAAEEAMRELIAAFFPDHGILGEEF---GHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLilqlgSIRSPV 176
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVL-----FTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 177 MQKSFVDSYKTVMFDKQCHGHRSFGSaAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFdVMSRK 256
Cdd:TIGR02067 156 LLDDPGNRPAFERLRRAARLTRYGGD-CYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGG 233
|
250
....*....|....*..
gi 146350806 257 VLCAGTAELGRDLSACL 273
Cdd:TIGR02067 234 AVAAGNAMLHDEALEIL 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-260 |
3.23e-115 |
|
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: 331.04 E-value: 3.23e-115
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPT 92
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES---GAAGGLTDEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 93 WIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILQLGSI 172
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 173 RSPVMQKsFVDSYKTvMFDKQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDV 252
Cdd:cd01639 158 RGDNFDR-YLNNFAK-LLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDL 235
|
....*...
gi 146350806 253 MSRKVLCA 260
Cdd:cd01639 236 MSGNILAG 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
17-265 |
7.38e-90 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 267.67 E-value: 7.38e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFdSPESKVDTKS--SNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWT-DAPTW 93
Cdd:pfam00459 9 AVELAAKAGEILREAF-SNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTdDGPTW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 94 IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLIlqlgSIR 173
Cdd:pfam00459 88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV----TLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 174 SPVMQKSFVDSY--KTVMFDKQCHGHRSFGSAAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGSPF 250
Cdd:pfam00459 164 GVSSRKDTSEASflAKLLKLVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGGPF 243
|
250
....*....|....*
gi 146350806 251 DVMSRKVLCAGTAEL 265
Cdd:pfam00459 244 DLLAGRVIAANPKVL 258
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
17-273 |
4.77e-86 |
|
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: 257.47 E-value: 4.77e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPESKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKiewTDAPTWIID 96
Cdd:COG0483 7 ALRAARAAGALILRRFRELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR---DSGYVWVID 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILqlgSIRSPV 176
Cdd:COG0483 83 PIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVAT---GFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 177 MQKSFVDSYKTVMfdKQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDVMSRK 256
Cdd:COG0483 160 DDREYLAALAALL--PRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 146350806 257 VLcAGTAELGRDLSACL 273
Cdd:COG0483 238 LV-AANPALHDELLALL 253
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
7-274 |
7.63e-77 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 234.58 E-value: 7.63e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 7 HEEEQvFVDYAIELVKKAGTLVRTAFDSPEsKVDTKSSnTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIE 86
Cdd:PLN02553 5 DDLEQ-FLEVAVDAAKAAGQIIRKGFYQTK-HVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 87 WTDAPTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLI 166
Cdd:PLN02553 82 LTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 167 LQLGSIRSpvmqKSFVDSyktvMFDK------QCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHA-WDVAAPSIIVTEAG 239
Cdd:PLN02553 162 TEVGTKRD----KATVDA----TTNRinallyKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAG 233
|
250 260 270
....*....|....*....|....*....|....*
gi 146350806 240 GVVTDPTGSPFDVMSRKVLCAGtAELGRDLSACLT 274
Cdd:PLN02553 234 GLVFDPSGGPFDIMSRRVAASN-GHLKDAFVEALR 267
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
15-261 |
3.97e-71 |
|
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: 219.11 E-value: 3.97e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 15 DYAIELVKKAGTLVRTAFDSPESkVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvaGGAKIEWTDAPTWI 94
Cdd:cd01637 2 ELALKAVREAGALILEAFGEELT-VETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 95 IDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILQLGSIRS 174
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 175 pvmqksfvDSYKTVMFDKQCHGH-RSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDVM 253
Cdd:cd01637 159 --------NRAAVLASLVNRALGiRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTL 230
|
....*...
gi 146350806 254 SRKVLCAG 261
Cdd:cd01637 231 NRSGIIAA 238
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
15-262 |
4.95e-49 |
|
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: 162.50 E-value: 4.95e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 15 DYAIELVKKAGTLVRTAFDSpESKVDTKSsNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTdaptWI 94
Cdd:cd01643 2 SLAEAIAQEAGDRALADFGN-SLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY----WV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 95 IDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRAS-KNQFIAESVLILQlgSIR 173
Cdd:cd01643 76 IDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHpPLQLPDCNVGFNR--SSR 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 174 SPVMQKSfvdsykTVMFDKQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFDVM 253
Cdd:cd01643 154 ASARAVL------RVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQ 227
|
....*....
gi 146350806 254 SRKVLCAGT 262
Cdd:cd01643 228 TKDYLSAGF 236
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
17-247 |
2.87e-48 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 161.51 E-value: 2.87e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPTWIID 96
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILQLgsirsPV 176
Cdd:PRK10757 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGF-----PF 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 146350806 177 MQKSFVDSYKTV---MFDkQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTG 247
Cdd:PRK10757 160 KAKQHATTYINIvgkLFT-ECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTG 232
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
13-265 |
6.53e-45 |
|
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: 152.02 E-value: 6.53e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 13 FVDYAIELVKKAGTLVRTAFDSPeSKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEEsvaGGAkiEWTDAP- 91
Cdd:cd01641 1 DLAFALELADAAGQITLPYFRTR-LQVETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEE---FGN--EGGDAGy 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 92 TWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGF---PIRASKNQFIAESVLILQ 168
Cdd:cd01641 74 VWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAggrPLRVRACADLAEAVLSTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 169 LGSIRSPVMQKSFVDSYKTVmfdkqchGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGS 248
Cdd:cd01641 154 DPHFFTPGDRAAFERLARAV-------RLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGG 226
|
250
....*....|....*..
gi 146350806 249 PFDVMSRKVLCAGTAEL 265
Cdd:cd01641 227 PLTGGSGRVVAAGDAEL 243
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
14-250 |
2.05e-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: 2.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 14 VDYAIELVKKAGTLVRTAFDSPESkVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDapTW 93
Cdd:cd01638 2 LELLIRIAREAGDAILEVYRGGFT-VERKEDGS-PVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDR--FW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 94 IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILQLGSIR 173
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 146350806 174 SPvmqKSFVDSYKTVMFDKQChghRSFGSAAiNMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGSPF 250
Cdd:cd01638 158 HP---DEELEALLAALGVAEV---VSIGSSL-KFCLVAEGEADIYPRLGpTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
18-263 |
2.18e-40 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 143.40 E-value: 2.18e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 18 IELVKKAGT-LVRTAFDSPESkVDTKSSnTDLVTETDQAVEKLLIEGLSERFKGHRFIGEES-VAGGAKIEWTdaptWII 95
Cdd:PLN02737 83 AELAAKTGAeVVMEAVNKPRN-ISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGgVIGDSSSDYL----WCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 96 DPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYN----PI--TNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILQL 169
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 170 GS------IRSPVMQKSFVDsyktvmfdkQCHGHRSFGSAAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVT 243
Cdd:PLN02737 237 GYehddawATNIELFKEFTD---------VSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVT 307
|
250 260
....*....|....*....|
gi 146350806 244 DPTGSPFDVMSRKVLCAGTA 263
Cdd:PLN02737 308 RMDGGKFSVFDRSVLVSNGV 327
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
17-251 |
6.59e-38 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 134.13 E-value: 6.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPeSKVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTWIID 96
Cdd:COG1218 8 AIEIAREAGEAILEIYRAD-FEVEEKADDS-PVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGF-----PIRASKNQfiAESVLILqLGS 171
Cdd:COG1218 86 PLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGggerqPIRVRDRP--PAEPLRV-VAS 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 172 iRS--PVMQKSFVDSYKTvmfdkqcHGHRSFGSaAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGS 248
Cdd:COG1218 163 -RShrDEETEALLARLGV-------AELVSVGS-SLKFCLVAEGEADLYPRLGpTMEWDTAAGQAILEAAGGRVTDLDGK 233
|
...
gi 146350806 249 PFD 251
Cdd:COG1218 234 PLR 236
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
17-273 |
1.42e-37 |
|
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: 133.20 E-value: 1.42e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPESKVDTKSSNTdLVTETDQAVEKLLIEGLSERFKGHRFIGEESvagGAKIEWTDAPTWIID 96
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKT-PVTEADRAAEEAMRELIAAFFPDHGILGEEF---GHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 97 PIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLilqlgSIRSPV 176
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVL-----FTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 177 MQKSFVDSYKTVMFDKQCHGHRSFGSaAINMVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAGGVVTDPTGSPFdVMSRK 256
Cdd:TIGR02067 156 LLDDPGNRPAFERLRRAARLTRYGGD-CYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGG 233
|
250
....*....|....*..
gi 146350806 257 VLCAGTAELGRDLSACL 273
Cdd:TIGR02067 234 AVAAGNAMLHDEALEIL 250
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
15-244 |
1.22e-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: 125.97 E-value: 1.22e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 15 DYAIELVKKAGTLVRTAFDSPES-KVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTW 93
Cdd:cd01636 2 EELCRVAKEAGLAILKAFGRELSgKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 94 IIDPIDGTTNFVHRIPMIAICVGLAikkqiragivynpITNELYlaqlgkgafknGFPIRASKNQFIAESVLilqlgsir 173
Cdd:cd01636 82 VIDPIDGTKNFINGLPFVAVVIAVY-------------VILILA-----------EPSHKRVDEKKAELQLL-------- 129
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 146350806 174 spvmqksfvdsyktvmfdkQCHGHRSFGSAAINMVMVAQGSCDGYVEYGI--HAWDVAAPSIIVTEAGGVVTD 244
Cdd:cd01636 130 -------------------AVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTD 183
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
15-251 |
2.53e-35 |
|
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: 127.81 E-value: 2.53e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 15 DYAIELVKKAGTLVRTAFDS-PESKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAggakiewTDAPTW 93
Cdd:cd01517 3 EVAILAVRAAASLTLPVFRNlGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA-------ALGRFW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 94 IIDPIDGTTNFVhRIPMIAICVGLAIKKQIRAGIVYNPITNE-------LYLAQLGKGAFkngfpIRASKNQFiAESVLI 166
Cdd:cd01517 76 VLDPIDGTKGFL-RGDQFAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAW-----LRPLDGSS-LQPLSV 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 167 LQLGSIRSPVMQKSFVDSYKTVMFDKQCHgHRSFGSAAINM------VMVAQGSCDGY------VEYGIHAWDVAAPSII 234
Cdd:cd01517 149 RQLTNAARASFCESVESAHSSHRLQAAIK-ALGGTPQPVRLdsqakyAAVARGAADFYlrlplsMSYREKIWDHAAGVLI 227
|
250
....*....|....*..
gi 146350806 235 VTEAGGVVTDPTGSPFD 251
Cdd:cd01517 228 VEEAGGKVTDADGKPLD 244
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
9-252 |
2.03e-33 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 122.71 E-value: 2.03e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 9 EEQVFVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNTDLVTE-TDQAVEKLLIEGLSERFKGHRFIGEES-VAGGAKIE 86
Cdd:PRK12676 2 SIMEWLEICDDMAKEVEKAIMPLFGTPDAGETVGMGADGTPTKlIDKVAEDIILEVLKPLGRCVNIISEELgEIVGNGPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 87 WTdaptWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKN-QFIAESVL 165
Cdd:PRK12676 82 YT----VVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTsELNESAVS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 166 ILQLGSIRSPVMQKsfVDSYKTVmfdkqchghRSFGSAAINMVMVAQGSCDGYVEYG--IHAWDVAAPSIIVTEAGGVVT 243
Cdd:PRK12676 158 IYGYRRGKERTVKL--GRKVRRV---------RILGAIALELCYVASGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVT 226
|
....*....
gi 146350806 244 DPTGSPFDV 252
Cdd:PRK12676 227 DEDGNELKL 235
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
18-251 |
7.43e-33 |
|
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: 120.63 E-value: 7.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 18 IELVKKAGTLVRTAFDSpESKVDTKSSNTDlVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAPTWIIDP 97
Cdd:TIGR01331 6 IKIARAAGEEILPVYQK-ELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 98 IDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNG--------FPIRASKNqfiaESVLILQL 169
Cdd:TIGR01331 84 LDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkapIHVRPWPS----GPLLVVIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 170 GSIRSPVMqKSFVDSYKtvmFDKqchghRSFGSAAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGVVTDPTGS 248
Cdd:TIGR01331 160 RSHAEEKT-TEYLANLG---YDL-----RTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGS 230
|
...
gi 146350806 249 PFD 251
Cdd:TIGR01331 231 PLL 233
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
22-269 |
1.33e-29 |
|
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: 112.47 E-value: 1.33e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 22 KKAGTLVRTAFDSPESKVdtkssnTDLVTEtDQAVEKLlieglsERFKGHRFIGEES--VAGGAKIEWTdaptWIIDPID 99
Cdd:cd01515 23 EDASEVVKIGADGTPTKL------IDKVAE-DAAIEIL------KKLGSVNIVSEEIgvIDNGDEPEYT----VVLDPLD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 100 GTTNFVHRIPMIAICVGLAIKKQIRA--GIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLILqLGSIRSPVM 177
Cdd:cd01515 86 GTYNAINGIPFYSVSVAVFKIDKSDPyyGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSY-YIYGKNHDR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 178 QKSFVDSYKTVmfdkqchghRSFGSAAINMVMVAQGSCDGYV---EYgIHAWDVAAPSIIVTEAGGVVTDPTGSP----F 250
Cdd:cd01515 165 TFKICRKVRRV---------RIFGSVALELCYVASGALDAFVdvrEN-LRLVDIAAGYLIAEEAGGIVTDENGKElklkL 234
|
250
....*....|....*....
gi 146350806 251 DVMSRKVLCAGTAELGRDL 269
Cdd:cd01515 235 NVTERVNIIAANSELHKKL 253
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
13-265 |
3.01e-19 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 85.16 E-value: 3.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 13 FVDYAIELVKKAGTLVRTAFDSP---ESKVDTKSsntdlVTETDQAVEKLLIEGLSERFKGHRFIGEES--VAGGAKIEW 87
Cdd:PLN02911 36 FVDVAHKLADAAGEVTRKYFRTKfeiIDKEDLSP-----VTIADRAAEEAMRSIILENFPSHAIFGEEHglRCGEGSSDY 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 88 TdaptWIIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKGAFKNGFPIRASKNQFIAESVLIL 167
Cdd:PLN02911 111 V----WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 168 QlgsirSPVM-----QKSFV---DSYKTVMFDKQCHGHrsfgsaainmVMVAQGSCDGYVEYGIHAWDVAAPSIIVTEAG 239
Cdd:PLN02911 187 T-----SPHMfsgdaEDAFArvrDKVKVPLYGCDCYAY----------GLLASGHVDLVVESGLKPYDYLALVPVVEGAG 251
|
250 260 270
....*....|....*....|....*....|....
gi 146350806 240 GVVTDPTGSPF------DVMSRK--VLCAGTAEL 265
Cdd:PLN02911 252 GVITDWKGRKLrwepspGSLATSfnVVAAGDARL 285
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
23-269 |
5.71e-18 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 83.62 E-value: 5.71e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 23 KAGTLVRTAFDSpeskvdTKSSNTDLVTEtDQAVEKLlieglsERFKGHRFIGEESvagGAKIEWTDAPTWI--IDPIDG 100
Cdd:PRK14076 28 KAGEVVKIGADG------TPTKRIDLIAE-NIAINSL------EKFCSGILISEEI---GFKKIGKNKPEYIfvLDPIDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 101 TTNFVHRIPMIAICVGLA-IKKQ----------------IRAGIVYNPITNELYLAQLGKGAF----KNGFPIRASKNQF 159
Cdd:PRK14076 92 TYNALKDIPIYSASIAIAkIDGFdkkikefigknltindLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISN 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 160 IAESVLILQLGSIRSPVMQksFVDSYKTVMFdkqchghRSFGSAAINMVMVAQGSCDGY--VEYGIHAWDVAAPSIIVTE 237
Cdd:PRK14076 172 LKDASIGLFAYGLSLDTLK--FIKDRKVRRI-------RLFGSIALEMCYVASGALDAFinVNETTRLCDIAAGYVICKE 242
|
250 260 270
....*....|....*....|....*....|....*.
gi 146350806 238 AGGVVTDPTGSP----FDVMSRKVLCAGTAELGRDL 269
Cdd:PRK14076 243 AGGIITNKNGKPlnmkLDINEKTSVICSNEILHKKL 278
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
17-251 |
3.89e-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: 68.12 E-value: 3.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 17 AIELVKKAGTLVRTAFDSPE-----SKVDTKSSNTDLVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGGAKIEWTDAP 91
Cdd:cd01640 5 LLAVAEKAGGIARDVVKKGRllillVEGKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 92 ------------------------TWIiDPIDGTTNFVH-RIPMIAICVGLAIKKQIRAGIVYNPITNElylaQLGKGAF 146
Cdd:cd01640 85 dldeeileescpspskdlpeedlgVWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEK----TAGAGAW 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 147 KNgfpiRA--SKNQFIAESVLILQLGSIRSPVMQKSFVDSYKTVMFDKQCHGHR--SFGSAAINMVMVAQGSCDGYV--E 220
Cdd:cd01640 160 LG----RTiwGLSGLGAHSSDFKEREDAGKIIVSTSHSHSVKEVQLITAGNKDEvlRAGGAGYKVLQVLEGLADAYVhsT 235
|
250 260 270
....*....|....*....|....*....|.
gi 146350806 221 YGIHAWDVAAPSIIVTEAGGVVTDPTGSPFD 251
Cdd:cd01640 236 GGIKKWDICAPEAILRALGGDMTDLHGEPLS 266
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
13-230 |
9.71e-13 |
|
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: 66.32 E-value: 9.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 13 FVDYAIELVKKAGTLVRTAFDSPESKVDTKSSNtDLVTETDQAVEKLLIEGLSERFKGHRFIGEES--VAGGAkiewtDA 90
Cdd:cd01642 1 MLEVLEKITKEIILLLNEKNRQGLVKLIRGAGG-DVTRVADLKAEEIILKLLREEGVFGQIISEESgeIRKGS-----GE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 91 PTWIIDPIDGTTNFVHRIPMIAICVGLAIKKQ-------------IRAGIVYNPITNELYLAQLGKGAfkNGFPIRASKN 157
Cdd:cd01642 75 YIAVLDPLDGSTNYLSGIPFYSVSVALADPRSkvkaatldnfvsgEGGLKVYSPPTRFSYISVPKLGP--PLVPEVPSKI 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 146350806 158 QFIAesvlilqlGSIRSPvmqksfvdSYKTVMFDKQCHGhRSFGSAAINMVMVAQGSCDGY--VEYGIHAWDVAA 230
Cdd:cd01642 153 GIYE--------GSSRNP--------EKFLLLSRNGLKF-RSLGSAALELAYTCEGSFVLFldLRGKLRNFDVAA 210
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
18-256 |
4.51e-10 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 58.55 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 18 IELVKKAGTLVRTAFDSPES-KVDTKSSNTDlVTETDQAVEKLLIEGLSERFKGHRFIGEESVAGgakieWTDAPTW--- 93
Cdd:PRK10931 6 CQLARNAGDAIMQVYDGTKPlDVASKADDSP-VTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPA-----WEVRQHWqry 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 94 -IIDPIDGTTNFVHRIPMIAICVGLAIKKQIRAGIVYNPITNELYLAQLGKgAFK--NG--FPIrasknqfiaesvlilQ 168
Cdd:PRK10931 80 wLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGvrKQI---------------Q 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 146350806 169 LGSIRSP--VMQKSFVDSYktvMFD--KQCHGHR--SFGSaAINMVMVAQGSCDGYVEYG-IHAWDVAAPSIIVTEAGGV 241
Cdd:PRK10931 144 VRDARPPlvVISRSHADAE---LKEylQQLGEHQttSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAH 219
|
250
....*....|....*
gi 146350806 242 VTDPTGSPFDVMSRK 256
Cdd:PRK10931 220 VHDWQGKTLDYTPRE 234
|
|
| |
