|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
3-266 |
0e+00 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 510.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 3 DNDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDE 82
Cdd:PLN02553 6 DLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 83 PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAG 162
Cdd:PLN02553 86 PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 163 TKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 242
Cdd:PLN02553 166 TKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPFD 245
|
250 260
....*....|....*....|....
gi 186509703 243 ITSQRIAASNASLKELFAEALRLT 266
Cdd:PLN02553 246 IMSRRVAASNGHLKDAFVEALRQT 269
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
19-252 |
3.11e-117 |
|
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: 335.66 E-value: 3.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYE-TKHVEHKG-QVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteLTDEPTWIVDPLDGTTNF 96
Cdd:cd01639 13 GEILLEAYEKlGLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 97 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKaTLDDTTNR 176
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD-NFDRYLNN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186509703 177 INSLLTK-VRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 252
Cdd:cd01639 169 FAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
19-264 |
6.48e-95 |
|
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: 279.42 E-value: 6.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKH-VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNFV 97
Cdd:COG0483 15 GALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SGYVWVIDPIDGTTNFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 98 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKatlDDTTNRI 177
Cdd:COG0483 92 HGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLRDD---REYLAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 178 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKE 257
Cdd:COG0483 169 AALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHD 247
|
....*..
gi 186509703 258 LFAEALR 264
Cdd:COG0483 248 ELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
3-264 |
1.27e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 271.91 E-value: 1.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 3 DNDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQ---VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTEL 79
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKsgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 80 TDE-PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLV 158
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 159 TEAGTKRDKATLDDTTnrINSLLTKVR--SLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDP 236
Cdd:pfam00459 161 TLFGVSSRKDTSEASF--LAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDA 238
|
250 260
....*....|....*....|....*....
gi 186509703 237 SGKDLDITSQRIAASNAS-LKELFAEALR 264
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKvLHELLAAALE 267
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
19-242 |
1.21e-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: 130.26 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVH 98
Cdd:TIGR01331 13 GEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDGTKEFIN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 99 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTA----LLVTEAGTKRDkatlDDTT 174
Cdd:TIGR01331 93 RNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVRPWpsgpLLVVISRSHAE----EKTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186509703 175 NRINSLltkVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 242
Cdd:TIGR01331 169 EYLANL---GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
3-266 |
0e+00 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 510.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 3 DNDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDE 82
Cdd:PLN02553 6 DLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 83 PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAG 162
Cdd:PLN02553 86 PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 163 TKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 242
Cdd:PLN02553 166 TKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPFD 245
|
250 260
....*....|....*....|....
gi 186509703 243 ITSQRIAASNASLKELFAEALRLT 266
Cdd:PLN02553 246 IMSRRVAASNGHLKDAFVEALRQT 269
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
19-252 |
3.11e-117 |
|
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: 335.66 E-value: 3.11e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYE-TKHVEHKG-QVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteLTDEPTWIVDPLDGTTNF 96
Cdd:cd01639 13 GEILLEAYEKlGLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 97 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKaTLDDTTNR 176
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD-NFDRYLNN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 186509703 177 INSLLTK-VRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 252
Cdd:cd01639 169 FAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
19-264 |
6.48e-95 |
|
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: 279.42 E-value: 6.48e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKH-VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNFV 97
Cdd:COG0483 15 GALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SGYVWVIDPIDGTTNFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 98 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKatlDDTTNRI 177
Cdd:COG0483 92 HGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLRDD---REYLAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 178 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKE 257
Cdd:COG0483 169 AALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHD 247
|
....*..
gi 186509703 258 LFAEALR 264
Cdd:COG0483 248 ELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
3-264 |
1.27e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 271.91 E-value: 1.27e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 3 DNDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQ---VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTEL 79
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKsgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 80 TDE-PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLV 158
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 159 TEAGTKRDKATLDDTTnrINSLLTKVR--SLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDP 236
Cdd:pfam00459 161 TLFGVSSRKDTSEASF--LAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDA 238
|
250 260
....*....|....*....|....*....
gi 186509703 237 SGKDLDITSQRIAASNAS-LKELFAEALR 264
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKvLHELLAAALE 267
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
19-251 |
1.23e-70 |
|
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: 217.18 E-value: 1.23e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVEHK-GQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAfgVTELTDEPTWIVDPLDGTTNFV 97
Cdd:cd01637 12 GALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGS--GNVSDGGRVWVIDPIDGTTNFV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 98 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRdkatlDDTTNRI 177
Cdd:cd01637 90 AGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLR-----SNRAAVL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186509703 178 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDI-TSQRIAAS 251
Cdd:cd01637 165 ASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSG-LNPWDYAAGALIVEEAGGIVTDLDGEPLDTlNRSGIIAA 238
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
19-263 |
5.53e-55 |
|
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: 177.45 E-value: 5.53e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaaFGVTELTDEPTWIVDPLDGTTNFVH 98
Cdd:cd01641 13 GQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEE----FGNEGGDAGYVWVLDPIDGTKSFIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 99 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLN---GKRIKVSAQSELLTALLVT---EAGTKRDKATLDD 172
Cdd:cd01641 89 GLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTtdpHFFTPGDRAAFER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 173 ttnrinsLLTKVRSLRMSGSCaLDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 252
Cdd:cd01641 169 -------LARAVRLTRYGGDC-YAYALVASGRVDLVVEAGL-KPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVVAAG 239
|
250
....*....|.
gi 186509703 253 ASlkELFAEAL 263
Cdd:cd01641 240 DA--ELHEALL 248
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
19-264 |
9.91e-51 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 167.29 E-value: 9.91e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVE--HKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNF 96
Cdd:PRK10757 16 GNLIAKNYETPDAVEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGED---QDVQWVIDPLDGTTNF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 97 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRdKATLDDTTNR 176
Cdd:PRK10757 93 IKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKA-KQHATTYINI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 177 INSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN---- 252
Cdd:PRK10757 172 VGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGL-KPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNprvv 250
|
250
....*....|....*.
gi 186509703 253 ----ASLKELFAEALR 264
Cdd:PRK10757 251 kamlANMRDELSDALK 266
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
20-257 |
3.04e-49 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 166.13 E-value: 3.04e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 20 QIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaafGVTELTD-EPTWIVDPLDGTTNFVH 98
Cdd:PLN02737 92 EVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG----GVIGDSSsDYLWCIDPLDGTTNFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 99 GFPFVCVSIGLTIGKVPVVGVVYN----PI--MEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKATldd 172
Cdd:PLN02737 168 GYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHDDAW--- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 173 TTN-RINSLLTKV-RSLRMSGSCALDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAA 250
Cdd:PLN02737 245 ATNiELFKEFTDVsRGVRRLGAAAVDMCHVALGIVEAYWEYRL-KPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLV 323
|
....*..
gi 186509703 251 SNASLKE 257
Cdd:PLN02737 324 SNGVLHP 330
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
19-242 |
7.38e-47 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 156.86 E-value: 7.38e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKgFYETK-HVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFV 97
Cdd:COG1218 16 GEAILE-IYRADfEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPLDGTKEFI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 98 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFL-----NGKRIKVSAQSElLTALLVTEAGTKRDKAtldd 172
Cdd:COG1218 95 KRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPP-AEPLRVVASRSHRDEE---- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 173 TTNRINSLltKVRSLRMSGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 242
Cdd:COG1218 170 TEALLARL--GVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLR 236
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
42-264 |
8.06e-47 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 156.99 E-value: 8.06e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 42 TET---DKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteltDEPTW--IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPV 116
Cdd:PRK12676 41 TPTkliDKVAEDIILEVLKPLGRCVNIISEELGEIVG-----NGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 117 VGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSElLTALLVTEAGTKRDKatlddttNRINSLLTKVRSLRMSGSCALD 196
Cdd:PRK12676 116 YGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSE-LNESAVSIYGYRRGK-------ERTVKLGRKVRRVRILGAIALE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186509703 197 LCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDI----TSQR--IAASNASLKELFAEALR 264
Cdd:PRK12676 188 LCYVASGRLDAFVDVrNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvTERTnlIAANGEELHKKILELLE 262
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
32-251 |
7.79e-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: 7.79e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 32 VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaafGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTI 111
Cdd:cd01643 25 AETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG----GGIFPSSGWYWVIDPIDGTTNFARGIPIWAISIALLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 112 GKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSelltallvteagTKRDKATLDDTTNRINSLLTKVRSL---- 187
Cdd:cd01643 101 RGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPL------------QLPDCNVGFNRSSRASARAVLRVILrrfp 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 186509703 188 ---RMSGSCALDLCGVACGRVDIFYElGFGGPWDIAAGIVIVKEAGGLI--------FDPSGKDLDITSQRIAAS 251
Cdd:cd01643 169 gkiRMLGSASLNLASVAAGQTLGYVE-ATPKIWDIAAAWVILREAGGSWtildeepaFLQTKDYLSAGFPTLIAA 242
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
42-258 |
3.77e-40 |
|
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: 139.43 E-value: 3.77e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 42 TET---DKGCEELVFNHLKQLFPNhKFIGEEttaaFGVTELTDEPTWIV--DPLDGTTNFVHGFPF--VCVSIGLTIGKV 114
Cdd:cd01515 36 TPTkliDKVAEDAAIEILKKLGSV-NIVSEE----IGVIDNGDEPEYTVvlDPLDGTYNAINGIPFysVSVAVFKIDKSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 115 PVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKatlddttnRINSLLTKVRSLRMSGSCA 194
Cdd:cd01515 111 PYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYIYGKNHD--------RTFKICRKVRRVRIFGSVA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 186509703 195 LDLCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDIT---SQR---IAASNASLKEL 258
Cdd:cd01515 183 LELCYVASGALDAFVDVrENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKlnvTERvniIAANSELHKKL 253
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
19-241 |
6.15e-39 |
|
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: 135.82 E-value: 6.15e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaAFGVTELTDEPTWIVDPLDGTTNFVH 98
Cdd:cd01638 13 GDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEES--ADDPLRLGWDRFWLVDPLDGTREFIK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 99 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKAtlDDTTNRIN 178
Cdd:cd01638 91 GNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRSHPD--EELEALLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186509703 179 SLltKVRSLRMSGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDL 241
Cdd:cd01638 169 AL--GVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
28-264 |
3.30e-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: 3.30e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 28 ETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAfgvteltDEPTWIVDPLDGTTNFVHGFPFvCVSI 107
Cdd:cd01517 25 AGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGRFWVLDPIDGTKGFLRGDQF-AVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 108 GLTIGKVPVVGVVYNPIMEE-------LFTGVQGKGAFL----NGKRIKVSAQSELLTALLVTEAGtkRDKATLD-DTTN 175
Cdd:cd01517 97 ALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLrpldGSSLQPLSVRQLTNAARASFCES--VESAHSShRLQA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 176 RINSLLTKVRSLRMSGSC--ALdlcgVACGRVDIFYELGFGG-----PWDIAAGIVIVKEAGGLIFDPSGKDLDITSQR- 247
Cdd:cd01517 175 AIKALGGTPQPVRLDSQAkyAA----VARGAADFYLRLPLSMsyrekIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRk 250
|
250 260
....*....|....*....|...
gi 186509703 248 ------IAASNASLKELFAEALR 264
Cdd:cd01517 251 llnnggLIAAPGEIHEQVLEALR 273
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
19-242 |
1.21e-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: 130.26 E-value: 1.21e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVH 98
Cdd:TIGR01331 13 GEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDGTKEFIN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 99 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTA----LLVTEAGTKRDkatlDDTT 174
Cdd:TIGR01331 93 RNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVRPWpsgpLLVVISRSHAE----EKTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 186509703 175 NRINSLltkVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 242
Cdd:TIGR01331 169 EYLANL---GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
38-235 |
3.39e-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: 124.43 E-value: 3.39e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 38 VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGltigkvpvv 117
Cdd:cd01636 34 NDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTWVIDPIDGTKNFINGLPFVAVVIA--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 118 gvvynpimeelftgvqgkgaflngkrikvsaqseLLTALLVTEAGTKRdkatldDTTNRINSLLTKVRSLRMSGSCALDL 197
Cdd:cd01636 105 ----------------------------------VYVILILAEPSHKR------VDEKKAELQLLAVYRIRIVGSAVAKM 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 186509703 198 CGVACGRVDIFYELG-FGGPWDIAAGIVIVKEAGGLIFD 235
Cdd:cd01636 145 CLVALGLADIYYEPGgKRRAWDVAASAAIVREAGGIMTD 183
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
19-255 |
5.42e-25 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 100.56 E-value: 5.42e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 19 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaaFGVT--ELTDEPTWIVDPLDGTTNF 96
Cdd:PLN02911 48 GEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEE----HGLRcgEGSSDYVWVLDPIDGTKSF 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 97 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTeagtkrdkatlddTTNR 176
Cdd:PLN02911 124 ITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYT-------------TSPH 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 177 INSLLTKVRSLRMSGSCALDLCG--------VACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDL------- 241
Cdd:PLN02911 191 MFSGDAEDAFARVRDKVKVPLYGcdcyayglLASGHVDLVVESGL-KPYDYLALVPVVEGAGGVITDWKGRKLrwepspg 269
|
250
....*....|....*.
gi 186509703 242 --DITSQRIAASNASL 255
Cdd:PLN02911 270 slATSFNVVAAGDARL 285
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
49-242 |
4.38e-21 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 92.10 E-value: 4.38e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 49 EELVFNHLKQlFPNHKFIGEEttaaFGVTELTDE-PTWIV--DPLDGTTNFVHGFPFVCVSIGltIGKVPV--------- 116
Cdd:PRK14076 50 ENIAINSLEK-FCSGILISEE----IGFKKIGKNkPEYIFvlDPIDGTYNALKDIPIYSASIA--IAKIDGfdkkikefi 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 117 ----------VGVVYNPIMEELFTGVQGKGAFL----NGKRIKVSAQSELLTAL--LVTEAGTKrdkATLDDTTNRinsl 180
Cdd:PRK14076 123 gknltindleVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDASigLFAYGLSL---DTLKFIKDR---- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 186509703 181 ltKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPW-DIAAGIVIVKEAGGLIFDPSGKDLD 242
Cdd:PRK14076 196 --KVRRIRLFGSIALEMCYVASGALDAFINVNETTRLcDIAAGYVICKEAGGIITNKNGKPLN 256
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
32-244 |
6.95e-15 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 72.03 E-value: 6.95e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 32 VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTElTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTI 111
Cdd:PRK10931 28 VASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVDPLDGTKEFIKRNGEFTVNIALIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 112 GKVPVVGVVYNPIMEELFTGVQGKgAFL--NGKRIKVSAQSELLTalLVTEAGTKRDkATLDDTTNRINSLLTKvrslrM 189
Cdd:PRK10931 107 QGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGVRKQIQVRDARPP--LVVISRSHAD-AELKEYLQQLGEHQTT-----S 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 186509703 190 SGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDIT 244
Cdd:PRK10931 178 IGS-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
39-237 |
9.82e-15 |
|
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: 71.71 E-value: 9.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 39 DLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPV-- 116
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVka 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 117 ---VGVVYNpIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEaGTKRDKATLDDTTNriNSLltKVRSLrmsGSC 193
Cdd:cd01642 111 atlDNFVSG-EGGLKVYSPPTRFSYISVPKLGPPLVPEVPSKIGIYE-GSSRNPEKFLLLSR--NGL--KFRSL---GSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 186509703 194 ALDLCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIfDPS 237
Cdd:cd01642 182 ALELAYTCEGSFVLFLDLrGKLRNFDVAAALGACKRLGLHG-DPS 225
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
33-242 |
1.51e-12 |
|
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: 66.19 E-value: 1.51e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 33 EHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEP------------------------TWIvD 88
Cdd:cd01640 34 TKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVdldeeileescpspskdlpeedlgVWV-D 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 89 PLDGTTNFVHGFPF-VCVSIGLTIGKVPVVGVVYNPIME----------ELFTGVQGKGAFLNGKRIKVSAQSELLtall 157
Cdd:cd01640 113 PLDATQEYTEGLLEyVTVLIGVAVKGKPIAGVIHQPFYEktagagawlgRTIWGLSGLGAHSSDFKEREDAGKIIV---- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 158 vteagTKRDKATLDDTTNRINSLLTKVrsLRMSGSCALDLCgVACGRVDIF-YELGFGGPWDIAAGIVIVKEAGGLIFDP 236
Cdd:cd01640 189 -----STSHSHSVKEVQLITAGNKDEV--LRAGGAGYKVLQ-VLEGLADAYvHSTGGIKKWDICAPEAILRALGGDMTDL 260
|
....*.
gi 186509703 237 SGKDLD 242
Cdd:cd01640 261 HGEPLS 266
|
|
| PRK13558 |
PRK13558 |
bacterio-opsin activator; Provisional |
153-268 |
3.43e-03 |
|
bacterio-opsin activator; Provisional
Pssm-ID: 237426 [Multi-domain] Cd Length: 665 Bit Score: 38.67 E-value: 3.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 186509703 153 LTALLVTEAGTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIfyELGFGGPW----DIAAGIVIVKE 228
Cdd:PRK13558 262 VTERKEAELALQRERRKLQRLLERVEGLVNDVTSALVRATDREEIEAAVCDRVGA--GGEYDGAWigeyDPTSGTITVAE 339
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 186509703 229 AGGLIFDPSGKDLDITSQRIAAsnASLKELFAEALRLTGA 268
Cdd:PRK13558 340 AAGGCDGADGDVLDLAAAGPAA--AALQSVVAETEAVEST 377
|
|
| |
