|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
1-267 |
0e+00 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 511.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 1 MADNDSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVT 80
Cdd:PLN02553 1 MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKA--QSELLTALL 158
Cdd:PLN02553 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKAssQSELGKALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 159 VTEAGTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 238
Cdd:PLN02553 161 ATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPS 240
|
250 260
....*....|....*....|....*....
gi 79312679 239 GKDLDITSQRIAASNASLKELFAEALRLT 267
Cdd:PLN02553 241 GGPFDIMSRRVAASNGHLKDAFVEALRQT 269
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
22-253 |
1.61e-113 |
|
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: 326.42 E-value: 1.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYE-TKHVEHKG-QVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteLTDEPTWIVDPLDGTTNF 99
Cdd:cd01639 13 GEILLEAYEKlGLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRI--KAQSELLTALLVTEAGTKRDKaTLDDTTNR 177
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIrvSGRKELKDALVATGFPYDRGD-NFDRYLNN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79312679 178 INSLLTK-VRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 253
Cdd:cd01639 169 FAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
22-265 |
3.58e-91 |
|
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: 270.18 E-value: 3.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKH-VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNFV 100
Cdd:COG0483 15 GALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SGYVWVIDPIDGTTNFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIK--AQSELLTALLVTEAGTKRDKatlDDTTNRI 178
Cdd:COG0483 92 HGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRvsARTDLEDALVATGFPYLRDD---REYLAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 179 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKE 258
Cdd:COG0483 169 AALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHD 247
|
....*..
gi 79312679 259 LFAEALR 265
Cdd:COG0483 248 ELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
7-265 |
4.20e-88 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 263.05 E-value: 4.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 7 LDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQ---VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELT 83
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKsgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 84 DE-PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKA--QSELLTALLVT 160
Cdd:pfam00459 82 DDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVsrAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 161 EAGTKRDKATLDDTTnrINSLLTKVR--SLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 238
Cdd:pfam00459 162 LFGVSSRKDTSEASF--LAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|....*...
gi 79312679 239 GKDLDITSQRIAASNAS-LKELFAEALR 265
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKvLHELLAAALE 267
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
22-243 |
4.51e-36 |
|
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: 128.72 E-value: 4.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:TIGR01331 13 GEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDGTKEFIN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKAQSEL------LTALLVTEAGTKRDkatlDDTT 175
Cdd:TIGR01331 93 RNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIhvrpwpSGPLLVVISRSHAE----EKTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79312679 176 NRINSLltkVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 243
Cdd:TIGR01331 169 EYLANL---GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
1-267 |
0e+00 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 511.16 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 1 MADNDSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVT 80
Cdd:PLN02553 1 MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKA--QSELLTALL 158
Cdd:PLN02553 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKAssQSELGKALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 159 VTEAGTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 238
Cdd:PLN02553 161 ATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPS 240
|
250 260
....*....|....*....|....*....
gi 79312679 239 GKDLDITSQRIAASNASLKELFAEALRLT 267
Cdd:PLN02553 241 GGPFDIMSRRVAASNGHLKDAFVEALRQT 269
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
22-253 |
1.61e-113 |
|
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: 326.42 E-value: 1.61e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYE-TKHVEHKG-QVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteLTDEPTWIVDPLDGTTNF 99
Cdd:cd01639 13 GEILLEAYEKlGLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRI--KAQSELLTALLVTEAGTKRDKaTLDDTTNR 177
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIrvSGRKELKDALVATGFPYDRGD-NFDRYLNN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 79312679 178 INSLLTK-VRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 253
Cdd:cd01639 169 FAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
22-265 |
3.58e-91 |
|
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: 270.18 E-value: 3.58e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKH-VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNFV 100
Cdd:COG0483 15 GALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SGYVWVIDPIDGTTNFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIK--AQSELLTALLVTEAGTKRDKatlDDTTNRI 178
Cdd:COG0483 92 HGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRvsARTDLEDALVATGFPYLRDD---REYLAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 179 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKE 258
Cdd:COG0483 169 AALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHD 247
|
....*..
gi 79312679 259 LFAEALR 265
Cdd:COG0483 248 ELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
7-265 |
4.20e-88 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 263.05 E-value: 4.20e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 7 LDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQ---VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELT 83
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKsgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 84 DE-PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKA--QSELLTALLVT 160
Cdd:pfam00459 82 DDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVsrAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 161 EAGTKRDKATLDDTTnrINSLLTKVR--SLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 238
Cdd:pfam00459 162 LFGVSSRKDTSEASF--LAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|....*...
gi 79312679 239 GKDLDITSQRIAASNAS-LKELFAEALR 265
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKvLHELLAAALE 267
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
22-252 |
3.83e-68 |
|
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: 211.02 E-value: 3.83e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKHVEHK-GQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAfgVTELTDEPTWIVDPLDGTTNFV 100
Cdd:cd01637 12 GALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGS--GNVSDGGRVWVIDPIDGTTNFV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIK--AQSELLTALLVTEAGTKRdkatlDDTTNRI 178
Cdd:cd01637 90 AGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPlsKDTPLNDALLSTNASMLR-----SNRAAVL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 79312679 179 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDI-TSQRIAAS 252
Cdd:cd01637 165 ASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSG-LNPWDYAAGALIVEEAGGIVTDLDGEPLDTlNRSGIIAA 238
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
22-264 |
1.06e-51 |
|
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: 168.97 E-value: 1.06e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaaFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:cd01641 13 GQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEE----FGNEGGDAGYVWVLDPIDGTKSFIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGK-----RIKAQSELLTALLVT---EAGTKRDKATLDD 173
Cdd:cd01641 89 GLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAggrplRVRACADLAEAVLSTtdpHFFTPGDRAAFER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 174 ttnrinsLLTKVRSLRMSGSCaLDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 253
Cdd:cd01641 169 -------LARAVRLTRYGGDC-YAYALVASGRVDLVVEAGL-KPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVVAAG 239
|
250
....*....|.
gi 79312679 254 ASlkELFAEAL 264
Cdd:cd01641 240 DA--ELHEALL 248
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
22-265 |
3.27e-49 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 163.44 E-value: 3.27e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKHVE--HKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNF 99
Cdd:PRK10757 16 GNLIAKNYETPDAVEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGED---QDVQWVIDPLDGTTNF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKAQS--ELLTALLVTEAGTKRdKATLDDTTNR 177
Cdd:PRK10757 93 IKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTarDLDGTILATGFPFKA-KQHATTYINI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 178 INSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN---- 253
Cdd:PRK10757 172 VGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGL-KPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNprvv 250
|
250
....*....|....*.
gi 79312679 254 ----ASLKELFAEALR 265
Cdd:PRK10757 251 kamlANMRDELSDALK 266
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
23-258 |
2.13e-46 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 158.81 E-value: 2.13e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 23 QIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaafGVTELTD-EPTWIVDPLDGTTNFVH 101
Cdd:PLN02737 92 EVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG----GVIGDSSsDYLWCIDPLDGTTNFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 102 GFPFVCVSIGLTIGKVPVVGVVYN----PI--MEELFTGVQGKGAFLNGKRIKAQ--SELLTALLVTEAGTKRDKATldd 173
Cdd:PLN02737 168 GYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSqtDKVERSLLVTGFGYEHDDAW--- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 174 TTN-RINSLLTKV-RSLRMSGSCALDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAA 251
Cdd:PLN02737 245 ATNiELFKEFTDVsRGVRRLGAAAVDMCHVALGIVEAYWEYRL-KPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLV 323
|
....*..
gi 79312679 252 SNASLKE 258
Cdd:PLN02737 324 SNGVLHP 330
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
22-243 |
4.80e-45 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 152.24 E-value: 4.80e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKgFYETK-HVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFV 100
Cdd:COG1218 16 GEAILE-IYRADfEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPLDGTKEFI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFL-----NGKRIKAQSEL-LTALLVTEAGTKRDKAtlddT 174
Cdd:COG1218 95 KRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPpAEPLRVVASRSHRDEE----T 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 79312679 175 TNRINSLltKVRSLRMSGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 243
Cdd:COG1218 171 EALLARL--GVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLR 236
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
35-252 |
5.88e-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: 151.72 E-value: 5.88e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 35 VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaafGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTI 114
Cdd:cd01643 25 AETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG----GGIFPSSGWYWVIDPIDGTTNFARGIPIWAISIALLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 115 GKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKAQSELltallvteagTKRDKATLDDTTNRINSLLTKVRSL------ 188
Cdd:cd01643 101 RGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPL----------QLPDCNVGFNRSSRASARAVLRVILrrfpgk 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79312679 189 -RMSGSCALDLCGVACGRVDIFYElGFGGPWDIAAGIVIVKEAGGLI--------FDPSGKDLDITSQRIAAS 252
Cdd:cd01643 171 iRMLGSASLNLASVAAGQTLGYVE-ATPKIWDIAAAWVILREAGGSWtildeepaFLQTKDYLSAGFPTLIAA 242
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-265 |
1.22e-43 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 148.90 E-value: 1.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 45 TET---DKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteltDEPTW--IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPV 119
Cdd:PRK12676 41 TPTkliDKVAEDIILEVLKPLGRCVNIISEELGEIVG-----NGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 120 VGVVYNPIMEELFTGVQGKGAFLNGKRIKAQSE-LLTALLVTEAGTKRDKatlddttNRINSLLTKVRSLRMSGSCALDL 198
Cdd:PRK12676 116 YGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTsELNESAVSIYGYRRGK-------ERTVKLGRKVRRVRILGAIALEL 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 79312679 199 CGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDI----TSQR--IAASNASLKELFAEALR 265
Cdd:PRK12676 189 CYVASGRLDAFVDVrNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvTERTnlIAANGEELHKKILELLE 262
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
31-265 |
2.80e-38 |
|
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: 135.13 E-value: 2.80e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 31 ETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAfgvteltDEPTWIVDPLDGTTNFVHGFPFvCVSI 110
Cdd:cd01517 25 AGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGRFWVLDPIDGTKGFLRGDQF-AVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 111 GLTIGKVPVVGVVYNPIMEE-------LFTGVQGKGAFLNGKRIkaqSELLTALLVTEAGTKRDKAT--------LDDTT 175
Cdd:cd01517 97 ALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLRPLDG---SSLQPLSVRQLTNAARASFCesvesahsSHRLQ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 176 NRINSLLTKVRSLRMSGSC--ALdlcgVACGRVDIFYELGFGG-----PWDIAAGIVIVKEAGGLIFDPSGKDLDITSQR 248
Cdd:cd01517 174 AAIKALGGTPQPVRLDSQAkyAA----VARGAADFYLRLPLSMsyrekIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGR 249
|
250 260
....*....|....*....|....
gi 79312679 249 -------IAASNASLKELFAEALR 265
Cdd:cd01517 250 kllnnggLIAAPGEIHEQVLEALR 273
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
22-242 |
1.19e-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: 132.73 E-value: 1.19e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaAFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:cd01638 13 GDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEES--ADDPLRLGWDRFWLVDPLDGTREFIK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKAQsellTALLVTEAGTKRDKATLDDTTNRINSL 181
Cdd:cd01638 91 GNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVS----LQARPPPLQPLRVVASRSHPDEELEAL 166
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 79312679 182 LTKVRSLRM-SGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDL 242
Cdd:cd01638 167 LAALGVAEVvSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
45-259 |
5.76e-37 |
|
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: 131.35 E-value: 5.76e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 45 TET---DKGCEELVFNHLKQLFPNhKFIGEEttaaFGVTELTDEPTWIV--DPLDGTTNFVHGFPF--VCVSIGLTIGKV 117
Cdd:cd01515 36 TPTkliDKVAEDAAIEILKKLGSV-NIVSEE----IGVIDNGDEPEYTVvlDPLDGTYNAINGIPFysVSVAVFKIDKSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 118 PVVGVVYNPIMEELFTGVQGKGAFLNGKRIKA--QSELLTALLVTEAGTKRDKatlddttnRINSLLTKVRSLRMSGSCA 195
Cdd:cd01515 111 PYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVsdFSSLKSISVSYYIYGKNHD--------RTFKICRKVRRVRIFGSVA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 79312679 196 LDLCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDIT---SQR---IAASNASLKEL 259
Cdd:cd01515 183 LELCYVASGALDAFVDVrENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKlnvTERvniIAANSELHKKL 253
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
22-243 |
4.51e-36 |
|
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: 128.72 E-value: 4.51e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:TIGR01331 13 GEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDGTKEFIN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKAQSEL------LTALLVTEAGTKRDkatlDDTT 175
Cdd:TIGR01331 93 RNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIhvrpwpSGPLLVVISRSHAE----EKTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 79312679 176 NRINSLltkVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 243
Cdd:TIGR01331 169 EYLANL---GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
41-236 |
1.56e-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: 125.58 E-value: 1.56e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 41 VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGltigkvpvv 120
Cdd:cd01636 34 NDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTWVIDPIDGTKNFINGLPFVAVVIA--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 121 gvvynpimeelftgvqgkgaflngkrikaqseLLTALLVTEAGTKRdkatldDTTNRINSLLTKVRSLRMSGSCALDLCG 200
Cdd:cd01636 105 --------------------------------VYVILILAEPSHKR------VDEKKAELQLLAVYRIRIVGSAVAKMCL 146
|
170 180 190
....*....|....*....|....*....|....*..
gi 79312679 201 VACGRVDIFYELG-FGGPWDIAAGIVIVKEAGGLIFD 236
Cdd:cd01636 147 VALGLADIYYEPGgKRRAWDVAASAAIVREAGGIMTD 183
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
5-256 |
1.48e-25 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 102.11 E-value: 1.48e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 5 DSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaaFGVT--EL 82
Cdd:PLN02911 31 AVLDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEE----HGLRcgEG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 83 TDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKaqselltallvTEA 162
Cdd:PLN02911 107 SSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEIS-----------TRS 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 163 GTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCG--------VACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLI 234
Cdd:PLN02911 176 CASLKDAYLYTTSPHMFSGDAEDAFARVRDKVKVPLYGcdcyayglLASGHVDLVVESGL-KPYDYLALVPVVEGAGGVI 254
|
250 260 270
....*....|....*....|....*....|.
gi 79312679 235 FDPSGKDL---------DITSQRIAASNASL 256
Cdd:PLN02911 255 TDWKGRKLrwepspgslATSFNVVAAGDARL 285
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
52-243 |
7.30e-19 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 85.94 E-value: 7.30e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 52 EELVFNHLKQlFPNHKFIGEEttaaFGVTELTDE-PTWIV--DPLDGTTNFVHGFPFVCVSIGltIGKVPV--------- 119
Cdd:PRK14076 50 ENIAINSLEK-FCSGILISEE----IGFKKIGKNkPEYIFvlDPIDGTYNALKDIPIYSASIA--IAKIDGfdkkikefi 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 120 ----------VGVVYNPIMEELFTGVQGKGAFL--NGKRIKAQSELLTAL------LVTEAGTKrdkATLDDTTNRinsl 181
Cdd:PRK14076 123 gknltindleVGVVKNIATGDTYYAEKGEGAYLlkKGEKKKIEISNISNLkdasigLFAYGLSL---DTLKFIKDR---- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 79312679 182 ltKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPW-DIAAGIVIVKEAGGLIFDPSGKDLD 243
Cdd:PRK14076 196 --KVRRIRLFGSIALEMCYVASGALDAFINVNETTRLcDIAAGYVICKEAGGIITNKNGKPLN 256
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
35-245 |
2.80e-15 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 73.19 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 35 VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTElTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTI 114
Cdd:PRK10931 28 VASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVDPLDGTKEFIKRNGEFTVNIALIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 115 GKVPVVGVVYNPIMEELFTGVQGKgAFL--NGKRIKAQSELLTALLVTEAGTKRDkATLDDTTNRINSLLTKvrslrMSG 192
Cdd:PRK10931 107 QGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGVRKQIQVRDARPPLVVISRSHAD-AELKEYLQQLGEHQTT-----SIG 179
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 79312679 193 ScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDIT 245
Cdd:PRK10931 180 S-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
42-238 |
3.62e-14 |
|
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: 70.17 E-value: 3.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 42 DLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPV-- 119
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVka 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 120 -----------VGVVYNPIMEELFTGVQGKGAFLngkrikaQSELLTALLVTEaGTKRDKATLDDTTNriNSLltKVRSL 188
Cdd:cd01642 111 atldnfvsgegGLKVYSPPTRFSYISVPKLGPPL-------VPEVPSKIGIYE-GSSRNPEKFLLLSR--NGL--KFRSL 178
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 79312679 189 rmsGSCALDLCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIfDPS 238
Cdd:cd01642 179 ---GSAALELAYTCEGSFVLFLDLrGKLRNFDVAAALGACKRLGLHG-DPS 225
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
36-243 |
5.07e-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: 67.35 E-value: 5.07e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 36 EHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEP------------------------TWIvD 91
Cdd:cd01640 34 TKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVdldeeileescpspskdlpeedlgVWV-D 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 92 PLDGTTNFVHGFPF-VCVSIGLTIGKVPVVGVVYNPIME----------ELFTGVQGKGAFlnGKRIKAQSELLTALLvt 160
Cdd:cd01640 113 PLDATQEYTEGLLEyVTVLIGVAVKGKPIAGVIHQPFYEktagagawlgRTIWGLSGLGAH--SSDFKEREDAGKIIV-- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 79312679 161 eagTKRDKATLDDTTNRINSLLTKVrsLRMSGSCALDLCgVACGRVDIF-YELGFGGPWDIAAGIVIVKEAGGLIFDPSG 239
Cdd:cd01640 189 ---STSHSHSVKEVQLITAGNKDEV--LRAGGAGYKVLQ-VLEGLADAYvHSTGGIKKWDICAPEAILRALGGDMTDLHG 262
|
....
gi 79312679 240 KDLD 243
Cdd:cd01640 263 EPLS 266
|
|
| |
