|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
8-254 |
6.55e-130 |
|
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.
Pssm-ID: 238817 [Multi-domain] Cd Length: 244 Bit Score: 368.02 E-value: 6.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 8 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 86
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSS 166
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 167 RtPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLM 246
Cdd:cd01639 158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236
|
....*...
1IMD_B 247 SRRVIAAN 254
Cdd:cd01639 237 SGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
5-271 |
1.09e-108 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 315.44 E-value: 1.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 5 WQECMDY-AVTLARQAGEVVCEAIKNEMNVMLKS--SPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSIL 81
Cdd:pfam00459 1 DLEEVLKvAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 82 TDN-PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLV 160
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 161 TELGSSRTPETV-RMVLSNMEKLFCIPvhGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDV 238
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKLVRAP--GVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238
|
250 260 270
....*....|....*....|....*....|...
1IMD_B 239 TGGPFDLMSRRVIAANNRILAERIAKEIQVIPL 271
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
3-254 |
4.50e-96 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 283.50 E-value: 4.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 3 DPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILT 82
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 83 DNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTE 162
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 163 LGSSRTPETVRMVLSNMEKLfcipVHGIRSV---GTAAVNMCLVATGGADAYYEMGI-HCWDVAGAGIIVTEAGGVLMDV 238
Cdd:PLN02553 164 VGTKRDKATVDATTNRINAL----LYKVRSLrmsGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDP 239
|
250
....*....|....*.
1IMD_B 239 TGGPFDLMSRRVIAAN 254
Cdd:PLN02553 240 SGGPFDIMSRRVAASN 255
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-260 |
5.91e-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: 249.38 E-value: 5.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 6 QECMDYAVTLARQAGEVVCEAIKN-EMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltDN 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 85 PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELG 164
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 165 SSRTPETVRMVLSNMEKlfciPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFD 244
Cdd:COG0483 157 YLRDDREYLAALAALLP----RVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250
....*....|....*.
1IMD_B 245 LMSRRVIAANNRILAE 260
Cdd:COG0483 233 LGSGSLVAANPALHDE 248
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-244 |
7.71e-34 |
|
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 130398 [Multi-domain] Cd Length: 249 Bit Score: 123.33 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 15 LARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPI 92
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAdnSPV---TEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 93 DGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAF--CNGQ--KLQVSQQEDITKSLLVTELGSSRT 168
Cdd:TIGR01331 85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQalKAPIHVRPWPSGPLLVVISRSHAE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1IMD_B 169 PETVRMvLSNMEKLFCIPvhgirsvGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDVTGGPFD 244
Cdd:TIGR01331 165 EKTTEY-LANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
8-254 |
6.55e-130 |
|
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, inhibited by lithium, many of which may act on inositol monophosphate substrate. They dephosphorylate inositol phosphate to generate inositol, which may be recycled into inositol lipids; in eukaryotes IMPase plays a vital role in intracellular signaling. IMPase is one of the proposed targets of Li+ therapy in manic-depressive illness. This family contains some bacterial members of the inositol monophosphatase family classified as SuhB-like. E. coli SuhB has been suggested to participate in posstranscriptional control of gene expression, and its inositol monophosphatase activity doesn't appear to be sufficient for its cellular function. It has been proposed, that SuhB plays a role in the biosynthesis of phosphatidylinositol in mycobacteria.
Pssm-ID: 238817 [Multi-domain] Cd Length: 244 Bit Score: 368.02 E-value: 6.55e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 8 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 86
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSS 166
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 167 RtPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLM 246
Cdd:cd01639 158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236
|
....*...
1IMD_B 247 SRRVIAAN 254
Cdd:cd01639 237 SGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
5-271 |
1.09e-108 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 315.44 E-value: 1.09e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 5 WQECMDY-AVTLARQAGEVVCEAIKNEMNVMLKS--SPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSIL 81
Cdd:pfam00459 1 DLEEVLKvAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 82 TDN-PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLV 160
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 161 TELGSSRTPETV-RMVLSNMEKLFCIPvhGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDV 238
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKLVRAP--GVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238
|
250 260 270
....*....|....*....|....*....|...
1IMD_B 239 TGGPFDLMSRRVIAANNRILAERIAKEIQVIPL 271
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
3-254 |
4.50e-96 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 283.50 E-value: 4.50e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 3 DPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILT 82
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 83 DNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTE 162
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 163 LGSSRTPETVRMVLSNMEKLfcipVHGIRSV---GTAAVNMCLVATGGADAYYEMGI-HCWDVAGAGIIVTEAGGVLMDV 238
Cdd:PLN02553 164 VGTKRDKATVDATTNRINAL----LYKVRSLrmsGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDP 239
|
250
....*....|....*.
1IMD_B 239 TGGPFDLMSRRVIAAN 254
Cdd:PLN02553 240 SGGPFDIMSRRVAASN 255
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
9-253 |
1.96e-83 |
|
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: 249.92 E-value: 1.96e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 9 MDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaAGEKSILTDNPTWI 88
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 89 IDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRT 168
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 169 PEtvrmvLSNMEKLfCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFD-LMS 247
Cdd:cd01637 159 NR-----AAVLASL-VNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtLNR 232
|
....*.
1IMD_B 248 RRVIAA 253
Cdd:cd01637 233 SGIIAA 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-260 |
5.91e-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: 249.38 E-value: 5.91e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 6 QECMDYAVTLARQAGEVVCEAIKN-EMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltDN 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 85 PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELG 164
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 165 SSRTPETVRMVLSNMEKlfciPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFD 244
Cdd:COG0483 157 YLRDDREYLAALAALLP----RVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250
....*....|....*.
1IMD_B 245 LMSRRVIAANNRILAE 260
Cdd:COG0483 233 LGSGSLVAANPALHDE 248
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
9-238 |
1.75e-60 |
|
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: 189.91 E-value: 1.75e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 9 MDYAVTLARQAGEVVCEAIKNEMNVML--KSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPT 86
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVkiTKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 87 WIIDPIDGTTNFVHRFPFVAVSIGFAvnkkiefgvvyscvegkmytarkgkgafcngqklqvsqqeditKSLLVTELGSS 166
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY-------------------------------------------VILILAEPSHK 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
1IMD_B 167 RTPEtvrmvlsNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGI--HCWDVAGAGIIVTEAGGVLMDV 238
Cdd:cd01636 118 RVDE-------KKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-263 |
1.22e-53 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 178.07 E-value: 1.22e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 4 PWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltD 83
Cdd:PLN02737 75 PAEELLAVAELAAKTGAEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS---S 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 84 NPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKM------YTARKGKGAFCNGQKLQVSQQEDITKS 157
Cdd:PLN02737 151 DYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPMcwntrtFSASAGGGAFCNGQKIHVSQTDKVERS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 158 LLVTELGSsrtpETVRMVLSNME--KLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVL 235
Cdd:PLN02737 231 LLVTGFGY----EHDDAWATNIElfKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTV 306
|
250 260 270
....*....|....*....|....*....|.
1IMD_B 236 MDVTGGPFDLMSRRVIAANNRI---LAERIA 263
Cdd:PLN02737 307 TRMDGGKFSVFDRSVLVSNGVLhpkLLDRIG 337
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
12-258 |
2.79e-49 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 163.82 E-value: 2.79e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 12 AVTLARQAGEVVCEAIKNEMNVML--KSSPvDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaaGEKSILTDNPTWII 89
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEAsqKGSN-DFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 90 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTEL---GSS 166
Cdd:PRK10757 84 DPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFpfkAKQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 167 RTPETVRMVlsnmEKLFcIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLM 246
Cdd:PRK10757 164 HATTYINIV----GKLF-TECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYML 238
|
250
....*....|..
1IMD_B 247 SRRVIAANNRIL 258
Cdd:PRK10757 239 TGNIVAGNPRVV 250
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
10-259 |
8.87e-45 |
|
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: 151.33 E-value: 8.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 10 DYAVTLARQAGEVVCEAIKNEMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEEsvaaGEKSILTDNPTWII 89
Cdd:cd01643 2 SLAEAIAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 90 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTP 169
Cdd:cd01643 77 DPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 170 ETVRMVLSNMEklfciPVHgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLMSRR 249
Cdd:cd01643 157 RAVLRVILRRF-----PGK-IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKD 230
|
250
....*....|
1IMD_B 250 VIAANNRILA 259
Cdd:cd01643 231 YLSAGFPTLI 240
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
12-260 |
1.78e-40 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 140.68 E-value: 1.78e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 12 AVTLARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWII 89
Cdd:COG1218 8 AIEIAREAGEAILEIYRADFEVEEKAddSPV---TEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 90 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFC-----NGQKLQVSQQEDITKSLLVTelg 164
Cdd:COG1218 85 DPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPLRVVA--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 165 sSR---TPETVRMvlsnMEKLfciPVHGIRSVGtAAVNMCLVATGGADAYYEMGIHC-WDVAGAGIIVTEAGGVLMDVTG 240
Cdd:COG1218 162 -SRshrDEETEAL----LARL---GVAELVSVG-SSLKFCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRVTDLDG 232
|
250 260
....*....|....*....|....*...
1IMD_B 241 GPF------DLMSRRVIAANN--RILAE 260
Cdd:COG1218 233 KPLrynkkeDLLNPGFIASGDhaAILAA 260
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
10-243 |
4.91e-37 |
|
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: 131.19 E-value: 4.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 10 DYAVTLARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksILTDNPTW 87
Cdd:cd01638 3 ELLIRIAREAGDAILEVYRGGFTVERKEdgSPV---TAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 88 IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSR 167
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1IMD_B 168 TPETVRMVLSNMeklfcIPVHGIRSVGTAAvNMCLVATGGADAYYEMGIHC-WDVAGAGIIVTEAGGVLMDVTGGPF 243
Cdd:cd01638 158 HPDEELEALLAA-----LGVAEVVSIGSSL-KFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
9-259 |
2.43e-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: 2.43e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 9 MDYAVTLARQAGEVVCEAIKNEMN---VMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAgeksiltDNP 85
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGagdVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 86 TWIIDPIDGTTNFVHRFPFvAVSIGFAVNKKIEFGVVYSCV-------EGKMYTARKGKGAFC---NGQKLQVSQQEDIT 155
Cdd:cd01517 74 FWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAWLrplDGSSLQPLSVRQLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 156 KSLLVTELGSSRTPETVRMVLSNMEKLfcipvhGIRSVGTAAVNMC---LVATGGADAY--------YEMGIhcWDVAGA 224
Cdd:cd01517 153 NAARASFCESVESAHSSHRLQAAIKAL------GGTPQPVRLDSQAkyaAVARGAADFYlrlplsmsYREKI--WDHAAG 224
|
250 260 270
....*....|....*....|....*....|....*
1IMD_B 225 GIIVTEAGGVLMDVTGGPFDLMSRRVIAANNRILA 259
Cdd:cd01517 225 VLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIA 259
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
9-263 |
1.67e-34 |
|
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: 125.06 E-value: 1.67e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 9 MDYAVTLARQAGEVVCEAIKNEMNVMLK--SSPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTdnpt 86
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKadFSPV---TEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCN---GQKLQVSQQEDITKSLLVTEl 163
Cdd:cd01641 75 WVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 164 gssrTPETVRMVLSN-MEKLfcipvhgIRSV-----GTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMD 237
Cdd:cd01641 154 ----DPHFFTPGDRAaFERL-------ARAVrltryGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITD 222
|
250 260
....*....|....*....|....*.
1IMD_B 238 VTGGPFDLMSRRVIAANNRILAERIA 263
Cdd:cd01641 223 WDGGPLTGGSGRVVAAGDAELHEALL 248
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-244 |
7.71e-34 |
|
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in bacteria of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. [Central intermediary metabolism, Sulfur metabolism]
Pssm-ID: 130398 [Multi-domain] Cd Length: 249 Bit Score: 123.33 E-value: 7.71e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 15 LARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPI 92
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAdnSPV---TEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 93 DGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAF--CNGQ--KLQVSQQEDITKSLLVTELGSSRT 168
Cdd:TIGR01331 85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQalKAPIHVRPWPSGPLLVVISRSHAE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
1IMD_B 169 PETVRMvLSNMEKLFCIPvhgirsvGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDVTGGPFD 244
Cdd:TIGR01331 165 EKTTEY-LANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
12-264 |
1.90e-33 |
|
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: 122.03 E-value: 1.90e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 12 AVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaagEKSILTDNP-TWIID 90
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEF----GHNEEGDAErVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 91 PIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPE 170
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 171 TVRMVlsnMEKLfcipvhgIRSV-----GTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFdL 245
Cdd:TIGR02067 161 GNRPA---FERL-------RRAArltryGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-P 229
|
250
....*....|....*....
1IMD_B 246 MSRRVIAANNRILAERIAK 264
Cdd:TIGR02067 230 DGGGAVAAGNAMLHDEALE 248
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
47-266 |
6.03e-32 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 118.47 E-value: 6.03e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 47 DQKVEKMLISSIKEKYPSHSFIGEEsvaAGEksILTDNPTW--IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYS 124
Cdd:PRK12676 47 DKVAEDIILEVLKPLGRCVNIISEE---LGE--IVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 125 CVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTelgSSRTPETVRMVlsnmeKLfCIPVHGIRSVGTAAVNMCLVA 204
Cdd:PRK12676 122 LATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSI---YGYRRGKERTV-----KL-GRKVRRVRILGAIALELCYVA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
1IMD_B 205 TGGADAYYEMG--IHCWDVAGAGIIVTEAGGVLMDVTGGPFDL-----MSRRVIAANNRILAERIAKEI 266
Cdd:PRK12676 193 SGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvtERTNLIAANGEELHKKILELL 261
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
47-258 |
6.20e-30 |
|
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: 113.24 E-value: 6.20e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 47 DQKVEKMLISSIKeKYPSHSFIGEESvaaGEKSIlTDNPTW--IIDPIDGTTNFVHRFPFVAVSIGFAVNKK--IEFGVV 122
Cdd:cd01515 42 DKVAEDAAIEILK-KLGSVNIVSEEI---GVIDN-GDEPEYtvVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 123 YSCVEGKMYTARKGKGAFCNGQKLQVSQQEDItKSLLVTELGSSRTPETVRmvlsnmekLFCIPVHGIRSVGTAAVNMCL 202
Cdd:cd01515 117 YNLATGDLYYAIKGKGAYLNGKRIKVSDFSSL-KSISVSYYIYGKNHDRTF--------KICRKVRRVRIFGSVALELCY 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
1IMD_B 203 VATGGADAYYEM--GIHCWDVAGAGIIVTEAGGVLMDVTGGP----FDLMSR-RVIAANNRIL 258
Cdd:cd01515 188 VASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKElklkLNVTERvNIIAANSELH 250
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
51-262 |
3.34e-24 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 101.73 E-value: 3.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 51 EKMLISSIkEKYPSHSFIGEEsvaAGEKSILTDNPTWI--IDPIDGTTNFVHRFPFVAVSI------GFAVNKK------ 116
Cdd:PRK14076 50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIaiakidGFDKKIKefigkn 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 117 -----IEFGVVYSCVEGKMYTARKGKGAF----CNGQKLQVSQQEDITKSlLVTELGSSRTPETVRMVLSNmeklfciPV 187
Cdd:PRK14076 126 ltindLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDA-SIGLFAYGLSLDTLKFIKDR-------KV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 188 HGIRSVGTAAVNMCLVATGGADAYYEM--GIHCWDVAGAGIIVTEAGGVLMDVTGGP----FDLMSRRVIAANNRILAER 261
Cdd:PRK14076 198 RRIRLFGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKK 277
|
.
1IMD_B 262 I 262
Cdd:PRK14076 278 L 278
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
15-248 |
8.36e-15 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 72.03 E-value: 8.36e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 15 LARQAGEVVCEAIKNE--MNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEEsvaageksiltDNPTW--- 87
Cdd:PRK10931 8 LARNAGDAIMQVYDGTkpLDVASKAddSPV---TAADIAAHTVIKDGLRTLTPDIPVLSEE-----------DPPAWevr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 88 -------IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKgAF--CNGQKLQVsQQEDITKSL 158
Cdd:PRK10931 74 qhwqrywLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI-QVRDARPPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 159 LVTelgsSRTPETVRMvlsnMEKLFCIPVHGIRSVGTaAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMD 237
Cdd:PRK10931 152 VVI----SRSHADAEL----KEYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHD 222
|
250
....*....|.
1IMD_B 238 VTGGPFDLMSR 248
Cdd:PRK10931 223 WQGKTLDYTPR 233
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
10-258 |
4.80e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 70.52 E-value: 4.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 10 DYAVTLARQAGEVVCEAIKNEMNVMLK--SSPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEE-SVAAGEKSiltDNPT 86
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSPV---TIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEGS---SDYV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 87 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTElgss 166
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTT---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 167 rTPEtvrMVLSNMEKLFC-------IPVHGIRSVGTAavnmcLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVT 239
Cdd:PLN02911 188 -SPH---MFSGDAEDAFArvrdkvkVPLYGCDCYAYG-----LLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWK 258
|
250 260
....*....|....*....|....*..
1IMD_B 240 GGPFDL--------MSRRVIAANNRIL 258
Cdd:PLN02911 259 GRKLRWepspgslaTSFNVVAAGDARL 285
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
47-224 |
4.51e-10 |
|
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: 58.61 E-value: 4.51e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 47 DQKVEKMLISSIKEKYPSHSFIGEESvaaGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFA-------------V 113
Cdd:cd01642 40 DLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALAdprskvkaatldnF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 114 NKKIEFGVVYSCVEGKMYTARKGKGAFCNGQklqvsqqediTKSLLVTELGSSRTPETVRMVLSNMEKlfcipvhgIRSV 193
Cdd:cd01642 117 VSGEGGLKVYSPPTRFSYISVPKLGPPLVPE----------VPSKIGIYEGSSRNPEKFLLLSRNGLK--------FRSL 178
|
170 180 190
....*....|....*....|....*....|...
1IMD_B 194 GTAAVNMCLVATGGADAYYEM--GIHCWDVAGA 224
Cdd:cd01642 179 GSAALELAYTCEGSFVLFLDLrgKLRNFDVAAA 211
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
12-245 |
1.22e-07 |
|
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: 51.94 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 12 AVTLARQAGEVVCEAIKNEMNVML------KSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGE-------- 77
Cdd:cd01640 5 LLAVAEKAGGIARDVVKKGRLLILlvegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENqedesrdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 78 -----------KSILTDNP-----TWIiDPIDGTTNFVH-RFPFVAVSIGFAVNKKIEFGVVY----------SCVEGKM 130
Cdd:cd01640 85 dldeeileescPSPSKDLPeedlgVWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHqpfyektagaGAWLGRT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
1IMD_B 131 YTARKGKGAFCNgqklQVSQQEDiTKSLLVTELGSSRTPETVRMVLSNMEKLFcipvhgirSVGTAAVNMCLVATGGADA 210
Cdd:cd01640 164 IWGLSGLGAHSS----DFKERED-AGKIIVSTSHSHSVKEVQLITAGNKDEVL--------RAGGAGYKVLQVLEGLADA 230
|
250 260 270
....*....|....*....|....*....|....*..
1IMD_B 211 YY--EMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDL 245
Cdd:cd01640 231 YVhsTGGIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
|
|
| |
