|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
1-269 |
0e+00 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 518.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 1 MADNDSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVT 80
Cdd:PLN02553 1 MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALL 160
Cdd:PLN02553 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 161 VTEAGTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 240
Cdd:PLN02553 161 ATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPS 240
|
250 260
....*....|....*....|....*....
gi 15232993 241 GKDLDITSQRIAASNASLKELFAEALRLT 269
Cdd:PLN02553 241 GGPFDIMSRRVAASNGHLKDAFVEALRQT 269
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
22-255 |
2.68e-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: 336.05 E-value: 2.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYE-TKHVEHKG-QVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteLTDEPTWIVDPLDGTTNF 99
Cdd:cd01639 13 GEILLEAYEKlGLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKaTLDDTTNR 179
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD-NFDRYLNN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232993 180 INSLLTK-VRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 255
Cdd:cd01639 169 FAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
22-267 |
6.49e-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: 279.81 E-value: 6.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKH-VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNFV 100
Cdd:COG0483 15 GALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SGYVWVIDPIDGTTNFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKatlDDTTNRI 180
Cdd:COG0483 92 HGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLRDD---REYLAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 181 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKE 260
Cdd:COG0483 169 AALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHD 247
|
....*..
gi 15232993 261 LFAEALR 267
Cdd:COG0483 248 ELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
7-267 |
3.90e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 270.76 E-value: 3.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 7 LDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQ---VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELT 83
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKsgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 84 DE-PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVT 162
Cdd:pfam00459 82 DDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 163 EAGTKRDKATLDDTTnrINSLLTKVR--SLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 240
Cdd:pfam00459 162 LFGVSSRKDTSEASF--LAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|....*...
gi 15232993 241 GKDLDITSQRIAASNAS-LKELFAEALR 267
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKvLHELLAAALE 267
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
22-245 |
1.32e-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: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:TIGR01331 13 GEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDGTKEFIN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTA----LLVTEAGTKRDkatlDDTT 177
Cdd:TIGR01331 93 RNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVRPWpsgpLLVVISRSHAE----EKTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232993 178 NRINSLltkVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 245
Cdd:TIGR01331 169 EYLANL---GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
1-269 |
0e+00 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 518.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 1 MADNDSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVT 80
Cdd:PLN02553 1 MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALL 160
Cdd:PLN02553 81 ELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 161 VTEAGTKRDKATLDDTTNRINSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 240
Cdd:PLN02553 161 ATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPS 240
|
250 260
....*....|....*....|....*....
gi 15232993 241 GKDLDITSQRIAASNASLKELFAEALRLT 269
Cdd:PLN02553 241 GGPFDIMSRRVAASNGHLKDAFVEALRQT 269
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
22-255 |
2.68e-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: 336.05 E-value: 2.68e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYE-TKHVEHKG-QVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteLTDEPTWIVDPLDGTTNF 99
Cdd:cd01639 13 GEILLEAYEKlGLNVEEKGsPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKaTLDDTTNR 179
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD-NFDRYLNN 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15232993 180 INSLLTK-VRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 255
Cdd:cd01639 169 FAKLLAKaVRGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
22-267 |
6.49e-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: 279.81 E-value: 6.49e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKH-VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNFV 100
Cdd:COG0483 15 GALILRRFRELDLeVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SGYVWVIDPIDGTTNFV 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKatlDDTTNRI 180
Cdd:COG0483 92 HGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLRDD---REYLAAL 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 181 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASNASLKE 260
Cdd:COG0483 169 AALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPALHD 247
|
....*..
gi 15232993 261 LFAEALR 267
Cdd:COG0483 248 ELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
7-267 |
3.90e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 270.76 E-value: 3.90e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 7 LDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQ---VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELT 83
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKsgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 84 DE-PTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVT 162
Cdd:pfam00459 82 DDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 163 EAGTKRDKATLDDTTnrINSLLTKVR--SLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPS 240
Cdd:pfam00459 162 LFGVSSRKDTSEASF--LAKLLKLVRapGVRRVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|....*...
gi 15232993 241 GKDLDITSQRIAASNAS-LKELFAEALR 267
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKvLHELLAAALE 267
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
22-254 |
1.38e-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: 1.38e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKHVEHK-GQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAfgVTELTDEPTWIVDPLDGTTNFV 100
Cdd:cd01637 12 GALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGS--GNVSDGGRVWVIDPIDGTTNFV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRdkatlDDTTNRI 180
Cdd:cd01637 90 AGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLR-----SNRAAVL 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232993 181 NSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGfGGPWDIAAGIVIVKEAGGLIFDPSGKDLDI-TSQRIAAS 254
Cdd:cd01637 165 ASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSG-LNPWDYAAGALIVEEAGGIVTDLDGEPLDTlNRSGIIAA 238
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
22-266 |
5.35e-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: 177.83 E-value: 5.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaaFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:cd01641 13 GQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEE----FGNEGGDAGYVWVLDPIDGTKSFIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLN---GKRIKVSAQSELLTALLVT---EAGTKRDKATLDD 175
Cdd:cd01641 89 GLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTtdpHFFTPGDRAAFER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 176 ttnrinsLLTKVRSLRMSGSCaLDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN 255
Cdd:cd01641 169 -------LARAVRLTRYGGDC-YAYALVASGRVDLVVEAGL-KPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVVAAG 239
|
250
....*....|.
gi 15232993 256 ASlkELFAEAL 266
Cdd:cd01641 240 DA--ELHEALL 248
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
22-267 |
1.04e-50 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 167.29 E-value: 1.04e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKHVE--HKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTeltDEPTWIVDPLDGTTNF 99
Cdd:PRK10757 16 GNLIAKNYETPDAVEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGED---QDVQWVIDPLDGTTNF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRdKATLDDTTNR 179
Cdd:PRK10757 93 IKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFKA-KQHATTYINI 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 180 INSLLTKVRSLRMSGSCALDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAASN---- 255
Cdd:PRK10757 172 VGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGL-KPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNprvv 250
|
250
....*....|....*.
gi 15232993 256 ----ASLKELFAEALR 267
Cdd:PRK10757 251 kamlANMRDELSDALK 266
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
23-260 |
2.94e-49 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 166.51 E-value: 2.94e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 23 QIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaafGVTELTD-EPTWIVDPLDGTTNFVH 101
Cdd:PLN02737 92 EVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG----GVIGDSSsDYLWCIDPLDGTTNFAH 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 102 GFPFVCVSIGLTIGKVPVVGVVYN----PI--MEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKATldd 175
Cdd:PLN02737 168 GYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHDDAW--- 244
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 176 TTN-RINSLLTKV-RSLRMSGSCALDLCGVACGRVDIFYELGFgGPWDIAAGIVIVKEAGGLIFDPSGKDLDITSQRIAA 253
Cdd:PLN02737 245 ATNiELFKEFTDVsRGVRRLGAAAVDMCHVALGIVEAYWEYRL-KPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLV 323
|
....*..
gi 15232993 254 SNASLKE 260
Cdd:PLN02737 324 SNGVLHP 330
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
22-245 |
7.67e-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: 7.67e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKgFYETK-HVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFV 100
Cdd:COG1218 16 GEAILE-IYRADfEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDPLDGTKEFI 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 101 HGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFL-----NGKRIKVSAQSElLTALLVTEAGTKRDKAtldd 175
Cdd:COG1218 95 KRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPP-AEPLRVVASRSHRDEE---- 169
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 176 TTNRINSLltKVRSLRMSGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 245
Cdd:COG1218 170 TEALLARL--GVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLR 236
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-267 |
9.02e-47 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 156.99 E-value: 9.02e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 45 TET---DKGCEELVFNHLKQLFPNHKFIGEETTAAFGvteltDEPTW--IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPV 119
Cdd:PRK12676 41 TPTkliDKVAEDIILEVLKPLGRCVNIISEELGEIVG-----NGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 120 VGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSElLTALLVTEAGTKRDKatlddttNRINSLLTKVRSLRMSGSCALD 199
Cdd:PRK12676 116 YGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSE-LNESAVSIYGYRRGK-------ERTVKLGRKVRRVRILGAIALE 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232993 200 LCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDI----TSQR--IAASNASLKELFAEALR 267
Cdd:PRK12676 188 LCYVASGRLDAFVDVrNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvTERTnlIAANGEELHKKILELLE 262
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
35-254 |
7.91e-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: 7.91e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 35 VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaafGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTI 114
Cdd:cd01643 25 AETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG----GGIFPSSGWYWVIDPIDGTTNFARGIPIWAISIALLY 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 115 GKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSelltallvteagTKRDKATLDDTTNRINSLLTKVRSL---- 190
Cdd:cd01643 101 RGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPL------------QLPDCNVGFNRSSRASARAVLRVILrrfp 168
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15232993 191 ---RMSGSCALDLCGVACGRVDIFYElGFGGPWDIAAGIVIVKEAGGLI--------FDPSGKDLDITSQRIAAS 254
Cdd:cd01643 169 gkiRMLGSASLNLASVAAGQTLGYVE-ATPKIWDIAAAWVILREAGGSWtildeepaFLQTKDYLSAGFPTLIAA 242
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
45-261 |
4.88e-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: 4.88e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 45 TET---DKGCEELVFNHLKQLFPNhKFIGEEttaaFGVTELTDEPTWIV--DPLDGTTNFVHGFPF--VCVSIGLTIGKV 117
Cdd:cd01515 36 TPTkliDKVAEDAAIEILKKLGSV-NIVSEE----IGVIDNGDEPEYTVvlDPLDGTYNAINGIPFysVSVAVFKIDKSD 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 118 PVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKatlddttnRINSLLTKVRSLRMSGSCA 197
Cdd:cd01515 111 PYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYIYGKNHD--------RTFKICRKVRRVRIFGSVA 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 15232993 198 LDLCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDIT---SQR---IAASNASLKEL 261
Cdd:cd01515 183 LELCYVASGALDAFVDVrENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKlnvTERvniIAANSELHKKL 253
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
22-244 |
7.22e-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: 7.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETtaAFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:cd01638 13 GDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEES--ADDPLRLGWDRFWLVDPLDGTREFIK 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEAGTKRDKAtlDDTTNRIN 181
Cdd:cd01638 91 GNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRSHPD--EELEALLA 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232993 182 SLltKVRSLRMSGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDL 244
Cdd:cd01638 169 AL--GVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
31-267 |
3.67e-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: 3.67e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 31 ETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAfgvteltDEPTWIVDPLDGTTNFVHGFPFvCVSI 110
Cdd:cd01517 25 AGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGRFWVLDPIDGTKGFLRGDQF-AVAL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 111 GLTIGKVPVVGVVYNPIMEE-------LFTGVQGKGAFL----NGKRIKVSAQSELLTALLVTEAGtkRDKATLD-DTTN 178
Cdd:cd01517 97 ALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLrpldGSSLQPLSVRQLTNAARASFCES--VESAHSShRLQA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 179 RINSLLTKVRSLRMSGSC--ALdlcgVACGRVDIFYELGFGG-----PWDIAAGIVIVKEAGGLIFDPSGKDLDITSQR- 250
Cdd:cd01517 175 AIKALGGTPQPVRLDSQAkyAA----VARGAADFYLRLPLSMsyrekIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRk 250
|
250 260
....*....|....*....|...
gi 15232993 251 ------IAASNASLKELFAEALR 267
Cdd:cd01517 251 llnnggLIAAPGEIHEQVLEALR 273
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
22-245 |
1.32e-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: 1.32e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 22 GQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVH 101
Cdd:TIGR01331 13 GEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDGTKEFIN 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 102 GFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTA----LLVTEAGTKRDkatlDDTT 177
Cdd:TIGR01331 93 RNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVRPWpsgpLLVVISRSHAE----EKTT 168
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15232993 178 NRINSLltkVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLD 245
Cdd:TIGR01331 169 EYLANL---GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
41-238 |
3.67e-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: 3.67e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 41 VDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGltigkvpvv 120
Cdd:cd01636 34 NDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTWVIDPIDGTKNFINGLPFVAVVIA--------- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 121 gvvynpimeelftgvqgkgaflngkrikvsaqseLLTALLVTEAGTKRdkatldDTTNRINSLLTKVRSLRMSGSCALDL 200
Cdd:cd01636 105 ----------------------------------VYVILILAEPSHKR------VDEKKAELQLLAVYRIRIVGSAVAKM 144
|
170 180 190
....*....|....*....|....*....|....*....
gi 15232993 201 CGVACGRVDIFYELG-FGGPWDIAAGIVIVKEAGGLIFD 238
Cdd:cd01636 145 CLVALGLADIYYEPGgKRRAWDVAASAAIVREAGGIMTD 183
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
5-258 |
1.39e-25 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 102.49 E-value: 1.39e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 5 DSLDQFLAAAIDAAKKAGQIIRKGFYETKHVEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaaFGVT--EL 82
Cdd:PLN02911 31 AVLDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEE----HGLRcgEG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 83 TDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVT 162
Cdd:PLN02911 107 SSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 163 eagtkrdkatlddTTNRINSLLTKVRSLRMSGSCALDLCG--------VACGRVDIFYELGFgGPWDIAAGIVIVKEAGG 234
Cdd:PLN02911 187 -------------TSPHMFSGDAEDAFARVRDKVKVPLYGcdcyayglLASGHVDLVVESGL-KPYDYLALVPVVEGAGG 252
|
250 260 270
....*....|....*....|....*....|...
gi 15232993 235 LIFDPSGKDL---------DITSQRIAASNASL 258
Cdd:PLN02911 253 VITDWKGRKLrwepspgslATSFNVVAAGDARL 285
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
52-245 |
4.68e-21 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 92.10 E-value: 4.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 52 EELVFNHLKQlFPNHKFIGEEttaaFGVTELTDE-PTWIV--DPLDGTTNFVHGFPFVCVSIGltIGKVPV--------- 119
Cdd:PRK14076 50 ENIAINSLEK-FCSGILISEE----IGFKKIGKNkPEYIFvlDPIDGTYNALKDIPIYSASIA--IAKIDGfdkkikefi 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 120 ----------VGVVYNPIMEELFTGVQGKGAFL----NGKRIKVSAQSELLTAL--LVTEAGTKrdkATLDDTTNRinsl 183
Cdd:PRK14076 123 gknltindleVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDASigLFAYGLSL---DTLKFIKDR---- 195
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15232993 184 ltKVRSLRMSGSCALDLCGVACGRVDIFYELGFGGPW-DIAAGIVIVKEAGGLIFDPSGKDLD 245
Cdd:PRK14076 196 --KVRRIRLFGSIALEMCYVASGALDAFINVNETTRLcDIAAGYVICKEAGGIITNKNGKPLN 256
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
35-247 |
7.28e-15 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 72.03 E-value: 7.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 35 VEHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTElTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTI 114
Cdd:PRK10931 28 VASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQ-HWQRYWLVDPLDGTKEFIKRNGEFTVNIALIE 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 115 GKVPVVGVVYNPIMEELFTGVQGKgAFL--NGKRIKVSAQSELLTalLVTEAGTKRDkATLDDTTNRINSLLTKvrslrM 192
Cdd:PRK10931 107 QGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGVRKQIQVRDARPP--LVVISRSHAD-AELKEYLQQLGEHQTT-----S 177
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 15232993 193 SGScALDLCGVACGRVDIFYELGFGGPWDIAAGIVIVKEAGGLIFDPSGKDLDIT 247
Cdd:PRK10931 178 IGS-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
42-240 |
1.27e-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: 71.33 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 42 DLVTETDKGCEELVFNHLKQLFPNHKFIGEEttaAFGVTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPV-- 119
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEE---SGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVka 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 120 ---VGVVYNpIMEELFTGVQGKGAFLNGKRIKVSAQSELLTALLVTEaGTKRDKATLDDTTNriNSLltKVRSLrmsGSC 196
Cdd:cd01642 111 atlDNFVSG-EGGLKVYSPPTRFSYISVPKLGPPLVPEVPSKIGIYE-GSSRNPEKFLLLSR--NGL--KFRSL---GSA 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 15232993 197 ALDLCGVACGRVDIFYEL-GFGGPWDIAAGIVIVKEAGGLIfDPS 240
Cdd:cd01642 182 ALELAYTCEGSFVLFLDLrGKLRNFDVAAALGACKRLGLHG-DPS 225
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
36-245 |
1.53e-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: 1.53e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 36 EHKGQVDLVTETDKGCEELVFNHLKQLFPNHKFIGEETTAAFGVTELTDEP------------------------TWIvD 91
Cdd:cd01640 34 TKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVdldeeileescpspskdlpeedlgVWV-D 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 92 PLDGTTNFVHGFPF-VCVSIGLTIGKVPVVGVVYNPIME----------ELFTGVQGKGAFLNGKRIKVSAQSELLtall 160
Cdd:cd01640 113 PLDATQEYTEGLLEyVTVLIGVAVKGKPIAGVIHQPFYEktagagawlgRTIWGLSGLGAHSSDFKEREDAGKIIV---- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15232993 161 vteagTKRDKATLDDTTNRINSLLTKVrsLRMSGSCALDLCgVACGRVDIF-YELGFGGPWDIAAGIVIVKEAGGLIFDP 239
Cdd:cd01640 189 -----STSHSHSVKEVQLITAGNKDEV--LRAGGAGYKVLQ-VLEGLADAYvHSTGGIKKWDICAPEAILRALGGDMTDL 260
|
....*.
gi 15232993 240 SGKDLD 245
Cdd:cd01640 261 HGEPLS 266
|
|
| |
