|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
8-218 |
4.58e-106 |
|
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: 306.39 E-value: 4.58e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 8 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE-------------- 152
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKelkdalvatgfpyd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 ---------------------GIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 211
Cdd:cd01639 158 rgdnfdrylnnfakllakavrGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
....*..
gi 149048447 212 RRIIAAS 218
Cdd:cd01639 238 GNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
5-235 |
5.54e-89 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 263.82 E-value: 5.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 5 WQECMDYAVI-LARQAGEMIREALKNKMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVF 81
Cdd:pfam00459 1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 82 TEQ-PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE-------- 152
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPplseallv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 ---------------------------GIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTG 204
Cdd:pfam00459 161 tlfgvssrkdtseasflakllklvrapGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADG 240
|
250 260 270
....*....|....*....|....*....|.
gi 149048447 205 GPFDLMSRRIIAASNIALAERIAKELEIIPL 235
Cdd:pfam00459 241 GPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
3-234 |
1.36e-80 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 242.67 E-value: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 3 DPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFT 82
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 83 EQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQ----------- 151
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQselgkallate 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 152 ---------------------EGIRSV---GTAAVNMCLVATGGADAYYEMGI-HCWDMAGAGIIVIEAGGVLLDVTGGP 206
Cdd:PLN02553 164 vgtkrdkatvdattnrinallYKVRSLrmsGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGP 243
|
250 260
....*....|....*....|....*...
gi 149048447 207 FDLMSRRiIAASNIALAERIAKELEIIP 234
Cdd:PLN02553 244 FDIMSRR-VAASNGHLKDAFVEALRQTE 270
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-230 |
2.75e-72 |
|
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: 220.87 E-value: 2.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 6 QECMDYAVILARQAGEMIREALKN-KMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQ 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 85 PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE------------ 152
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTdledalvatgfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 --------------------GIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSR 212
Cdd:COG0483 157 ylrddreylaalaallprvrRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSG 236
|
250
....*....|....*...
gi 149048447 213 RIIAAsNIALAERIAKEL 230
Cdd:COG0483 237 SLVAA-NPALHDELLALL 253
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-208 |
7.14e-30 |
|
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: 111.77 E-value: 7.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 15 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 92
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAdnSP---VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 93 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAF--CNGQKLRVSQQEG----------------- 153
Cdd:TIGR01331 85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQALKAPIHVRpwpsgpllvvisrshae 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149048447 154 -------------IRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFD 208
Cdd:TIGR01331 165 ektteylanlgydLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
8-218 |
4.58e-106 |
|
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: 306.39 E-value: 4.58e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 8 CMDYAVILARQAGEMIREALKN-KMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPT 86
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT---DEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE-------------- 152
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKelkdalvatgfpyd 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 ---------------------GIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 211
Cdd:cd01639 158 rgdnfdrylnnfakllakavrGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
....*..
gi 149048447 212 RRIIAAS 218
Cdd:cd01639 238 GNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
5-235 |
5.54e-89 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 263.82 E-value: 5.54e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 5 WQECMDYAVI-LARQAGEMIREALKNKMDVMIKS--SPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVF 81
Cdd:pfam00459 1 DLEEVLKVAVeLAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 82 TEQ-PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE-------- 152
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPplseallv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 ---------------------------GIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTG 204
Cdd:pfam00459 161 tlfgvssrkdtseasflakllklvrapGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADG 240
|
250 260 270
....*....|....*....|....*....|.
gi 149048447 205 GPFDLMSRRIIAASNIALAERIAKELEIIPL 235
Cdd:pfam00459 241 GPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
3-234 |
1.36e-80 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 242.67 E-value: 1.36e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 3 DPWQECMDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFT 82
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 83 EQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQ----------- 151
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQselgkallate 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 152 ---------------------EGIRSV---GTAAVNMCLVATGGADAYYEMGI-HCWDMAGAGIIVIEAGGVLLDVTGGP 206
Cdd:PLN02553 164 vgtkrdkatvdattnrinallYKVRSLrmsGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGP 243
|
250 260
....*....|....*....|....*...
gi 149048447 207 FDLMSRRiIAASNIALAERIAKELEIIP 234
Cdd:PLN02553 244 FDIMSRR-VAASNGHLKDAFVEALRQTE 270
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-230 |
2.75e-72 |
|
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: 220.87 E-value: 2.75e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 6 QECMDYAVILARQAGEMIREALKN-KMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQ 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES---GASEGRDSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 85 PTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE------------ 152
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTdledalvatgfp 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 --------------------GIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSR 212
Cdd:COG0483 157 ylrddreylaalaallprvrRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSG 236
|
250
....*....|....*...
gi 149048447 213 RIIAAsNIALAERIAKEL 230
Cdd:COG0483 237 SLVAA-NPALHDELLALL 253
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
9-217 |
2.95e-72 |
|
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: 220.26 E-value: 2.95e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 9 MDYAVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaAGEKTVFTEQPTWI 88
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 89 IDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQ----------------- 151
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDtplndallstnasmlrs 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 152 -------------EGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFD-LMSRRIIAA 217
Cdd:cd01637 159 nraavlaslvnraLGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtLNRSGIIAA 238
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
9-202 |
1.78e-50 |
|
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: 162.95 E-value: 1.78e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 9 MDYAVILARQAGEMIREALKNK--MDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPT 86
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRElsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 87 WIIDPIDGTTNFVHRFPFVAVSIGfvvnkemeFGVVYSCVEDKMytgrkgKGAFCNGQKLRVSQQEGIRSVGTAAVNMCL 166
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIA--------VYVILILAEPSH------KRVDEKKAELQLLAVYRIRIVGSAVAKMCL 146
|
170 180 190
....*....|....*....|....*....|....*...
gi 149048447 167 VATGGADAYYEMGI--HCWDMAGAGIIVIEAGGVLLDV 202
Cdd:cd01636 147 VALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTDW 184
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
15-223 |
3.81e-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: 145.94 E-value: 3.81e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 15 LARQAGEMIREALKNKMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaaGEKTVFTEQPTWIIDPIDG 94
Cdd:cd01643 7 IAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVIDPIDG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 95 TTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE---------------------- 152
Cdd:cd01643 82 TTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLqlpdcnvgfnrssrasaravlr 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149048447 153 --------GIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIAASNIALA 223
Cdd:cd01643 162 vilrrfpgKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYLSAGFPTLI 240
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
13-226 |
8.69e-41 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 143.02 E-value: 8.69e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 13 VILARQAG-EMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTvftEQPTWIIDP 91
Cdd:PLN02737 83 AELAAKTGaEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS---SDYLWCIDP 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 92 IDGTTNFVHRFPFVAVSIGFVVNKE------MEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQE------------- 152
Cdd:PLN02737 159 LDGTTNFAHGYPSFAVSVGVLFRGTpaaatvVEFVGGPMCWNTRTFSASAGGGAFCNGQKIHVSQTDkversllvtgfgy 238
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 153 ---------------------GIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMS 211
Cdd:PLN02737 239 ehddawatnielfkeftdvsrGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFD 318
|
250
....*....|....*
gi 149048447 212 RRIIaASNIALAERI 226
Cdd:PLN02737 319 RSVL-VSNGVLHPKL 332
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
12-218 |
3.34e-40 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 139.17 E-value: 3.34e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 12 AVILARQAGEMIREALKNKMDVMI-KSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQPTWIID 90
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEAsQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 91 PIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVS--------------------- 149
Cdd:PRK10757 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGStardldgtilatgfpfkakqh 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 150 -------------QQEGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRIIA 216
Cdd:PRK10757 165 attyinivgklftECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVA 244
|
..
gi 149048447 217 AS 218
Cdd:PRK10757 245 GN 246
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
15-219 |
2.22e-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: 2.22e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 15 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 92
Cdd:COG1218 11 IAREAGEAILEIYRADFEVEEKAddSP---VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 93 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFC-----NGQKLRVSQ---QEGIRSVG------ 158
Cdd:COG1218 88 DGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDrppAEPLRVVAsrshrd 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 159 --TAA----------VNM------CLVATGGADAYYEMGIHC-WDMAGAGIIVIEAGGVLLDVTGGPF------DLMSRR 213
Cdd:COG1218 168 eeTEAllarlgvaelVSVgsslkfCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRVTDLDGKPLrynkkeDLLNPG 247
|
....*.
gi 149048447 214 IIAASN 219
Cdd:COG1218 248 FIASGD 253
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
10-207 |
1.05e-31 |
|
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: 116.17 E-value: 1.05e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 10 DYAVILARQAGEMIREALKNKMDVMIKSsPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEktVFTEQPTWII 89
Cdd:cd01638 3 ELLIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFWLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 90 DPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEGIRSVGTAAV------- 162
Cdd:cd01638 80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVvasrshp 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 163 -----------------NM------CLVATGGADAYYEMGIHC-WDMAgAGIIVI-EAGGVLLDVTGGPF 207
Cdd:cd01638 160 deeleallaalgvaevvSIgsslkfCLVAEGEADIYPRLGPTMeWDTA-AGDAVLrAAGGAVSDLDGSPL 228
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
9-227 |
1.34e-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: 116.20 E-value: 1.34e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 9 MDYAVILARQAGEMIREALKNKMDVMIKSSpADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTeqptWI 88
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV----WV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 89 IDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCN---GQKLRVS---------------- 149
Cdd:cd01641 77 LDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRacadlaeavlsttdph 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 150 -----QQEGIRSV---------GTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSRRII 215
Cdd:cd01641 157 fftpgDRAAFERLaravrltryGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVV 236
|
250
....*....|..
gi 149048447 216 AASNIALAERIA 227
Cdd:cd01641 237 AAGDAELHEALL 248
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-208 |
7.14e-30 |
|
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: 111.77 E-value: 7.14e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 15 LARQAGEMIREALKNKMDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVFTEQPTWIIDPI 92
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAdnSP---VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 93 DGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAF--CNGQKLRVSQQEG----------------- 153
Cdd:TIGR01331 85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQALKAPIHVRpwpsgpllvvisrshae 164
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 149048447 154 -------------IRSVGTAAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFD 208
Cdd:TIGR01331 165 ektteylanlgydLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
12-231 |
1.75e-29 |
|
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: 110.86 E-value: 1.75e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 12 AVILARQAGEMIREALKNKMDVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDP 91
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 92 IDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEG------------------ 153
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANlsdavlfttspdllddpg 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 154 --------IRSV-----GTAAVNMCLVATGGADAYYEMGIHCWDMAGAGIIVIEAGGVLLDVTGGPFdLMSRRIIAASNI 220
Cdd:TIGR02067 162 nrpaferlRRAArltryGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAVAAGNA 240
|
250
....*....|.
gi 149048447 221 ALAERIAKELE 231
Cdd:TIGR02067 241 MLHDEALEILN 251
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
9-218 |
3.28e-27 |
|
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: 105.47 E-value: 3.28e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 9 MDYAVILARQAGEMIREALKNKM--DVMIKSSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAgektvftEQPT 86
Cdd:cd01517 2 LEVAILAVRAAASLTLPVFRNLGagDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGRF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 87 WIIDPIDGTTNFVHRFPFvAVSIGFVVNKEMEFGVVYSCV-------EDKMYTGRKGKGAFCNG------QKLRVSQ--- 150
Cdd:cd01517 75 WVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAWLRPldgsslQPLSVRQltn 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 151 -------------------QEGIRSVG--TAAVNM------CLVATGGADAY--------YEMGIhcWDMAGAGIIVIEA 195
Cdd:cd01517 154 aarasfcesvesahsshrlQAAIKALGgtPQPVRLdsqakyAAVARGAADFYlrlplsmsYREKI--WDHAAGVLIVEEA 231
|
250 260 270
....*....|....*....|....*....|
gi 149048447 196 GGVLLDVTGGPFD-------LMSRRIIAAS 218
Cdd:cd01517 232 GGKVTDADGKPLDfgkgrklLNNGGLIAAP 261
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
47-231 |
6.90e-24 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 96.13 E-value: 6.90e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 47 DQKVEKMLMSSIKEKYPYHSFIGEEsvaAGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCV 126
Cdd:PRK12676 47 DKVAEDIILEVLKPLGRCVNIISEE---LGEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLA 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 127 EDKMYTGRKGKGAFCNGQKLRVSQQ--------------------EGIRSV-------GTAAVNMCLVATGGADAYYEMG 179
Cdd:PRK12676 124 TGDFYEAIPGKGAYLNGKPIKVSKTselnesavsiygyrrgkertVKLGRKvrrvrilGAIALELCYVASGRLDAFVDVR 203
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 149048447 180 --IHCWDMAGAGIIVIEAGGVLLDVTGGPFDL-----MSRRIIAASNIALAERIAKELE 231
Cdd:PRK12676 204 nyLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvtERTNLIAANGEELHKKILELLE 262
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
19-226 |
2.04e-22 |
|
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: 92.06 E-value: 2.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 19 AGEMIREALKNKMDVM--------IKSSP-ADLVTVTDQKVEKMLMSSIKEKYPYhSFIGEESvaaGEKtVFTEQPTW-- 87
Cdd:cd01515 5 ARNIAKEIEKAIKPLFgtedasevVKIGAdGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEI---GVI-DNGDEPEYtv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 88 IIDPIDGTTNFVHRFPFVAVSIGFVVNKE--MEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRVSQQEG------------ 153
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSlksisvsyyiyg 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 154 ---------------IRSVGTAAVNMCLVATGGADAYYEM--GIHCWDMAGAGIIVIEAGGVLLDVTGGP----FDLMSR 212
Cdd:cd01515 160 knhdrtfkicrkvrrVRIFGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKElklkLNVTER 239
|
250
....*....|....
gi 149048447 213 RIIAASNIALAERI 226
Cdd:cd01515 240 VNIIAANSELHKKL 253
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
51-226 |
4.93e-18 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 82.47 E-value: 4.93e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 51 EKMLMSSIkEKYPYHSFIGEEsvaAGEKTVFTEQPTWI--IDPIDGTTNFVHRFPFVAVSIG-------------FVVN- 114
Cdd:PRK14076 50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIAiakidgfdkkikeFIGKn 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 115 ---KEMEFGVVYSCVEDKMYTGRKGKGAF----CNGQKLRVSQQEG----------------------------IRSVGT 159
Cdd:PRK14076 126 ltiNDLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNlkdasiglfayglsldtlkfikdrkvrrIRLFGS 205
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149048447 160 AAVNMCLVATGGADAYYEM--GIHCWDMAGAGIIVIEAGGVLLDVTGGP----FDLMSRRIIAASNIALAERI 226
Cdd:PRK14076 206 IALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKKL 278
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
10-148 |
8.81e-15 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 72.06 E-value: 8.81e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 10 DYAVILARQAGEMIREALKNKMDVMIK--SSPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEE-SVAAGEKtvFTEQpT 86
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSP---VTIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEG--SSDY-V 111
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149048447 87 WIIDPIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKGAFCNGQKLRV 148
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEIST 173
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
15-212 |
2.30e-14 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 70.11 E-value: 2.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 15 LARQAGEMIREALKNK--MDVMIKS--SPadlVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEKTVfTEQPTWIID 90
Cdd:PRK10931 8 LARNAGDAIMQVYDGTkpLDVASKAddSP---VTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 91 PIDGTTNFVHRFPFVAVSIGFVVNKEMEFGVVYSCVEDKMYTGRKGKgAF--CNGQKLRVS------------------- 149
Cdd:PRK10931 84 PLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQIQvrdarpplvvisrshadae 162
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 149048447 150 -----QQEG---IRSVGTaAVNMCLVATGGADAYYEMG-IHCWDMAGAGIIVIEAGGVLLDVTGGPFDLMSR 212
Cdd:PRK10931 163 lkeylQQLGehqTTSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPR 233
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
41-175 |
6.72e-08 |
|
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: 51.68 E-value: 6.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 41 DLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESvaaGEKTVFTEQPTWIIDPIDGTTNFVHRFPFVAVSIGF-----VVNK 115
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALadprsKVKA 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 116 EMEFGVVYSCVEDKMYT-------------------GRKGK-----GAFCNGQKLRVSQQEG--IRSVGTAAVNMCLVAT 169
Cdd:cd01642 111 ATLDNFVSGEGGLKVYSpptrfsyisvpklgpplvpEVPSKigiyeGSSRNPEKFLLLSRNGlkFRSLGSAALELAYTCE 190
|
....*.
gi 149048447 170 GGADAY 175
Cdd:cd01642 191 GSFVLF 196
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| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
12-123 |
7.52e-05 |
|
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: 43.08 E-value: 7.52e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 149048447 12 AVILARQAGEMIREALKN----KMDVMIK--SSPADLVTVTDQKVEKMLMSSIKEKYPYHSFIGEESVAAGEK------- 78
Cdd:cd01640 5 LLAVAEKAGGIARDVVKKgrllILLVEGKtkEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQedesrdv 84
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90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 149048447 79 ---TVFTEQPT--------------WIiDPIDGTTNFVH-RFPFVAVSIGFVVNKEMEFGVVY 123
Cdd:cd01640 85 dldEEILEESCpspskdlpeedlgvWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIH 146
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