|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
10-267 |
5.37e-103 |
|
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: 300.61 E-value: 5.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 10 KFLCELATEKVGPIIKSKSGTQKDYDLKtgSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETviTDDPTF 89
Cdd:cd01639 3 NIAIEAARKAGEILLEAYEKLGLNVEEK--GSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGL--TDEPTW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 90 IIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKDYDYKSKLEsmgsliLNKSVVAL 169
Cdd:cd01639 79 IIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKE------LKDALVAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 170 QPGSAREgKNFQTKMATYEKLLSCdygFVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGA 249
Cdd:cd01639 153 GFPYDRG-DNFDRYLNNFAKLLAK---AVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDF 228
|
250
....*....|....*...
gi 6321836 250 NPGEWsiDVDNRTYLAVR 267
Cdd:cd01639 229 DGGPF--DLMSGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
4-288 |
2.51e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 271.91 E-value: 2.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 4 DLASIEKFLCELATeKVGPIIKSKSGTQKDYDLKTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVI 83
Cdd:pfam00459 1 DLEEVLKVAVELAA-KAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 84 T--DDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyKSKLESmGSLI 161
Cdd:pfam00459 80 LtdDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQ----PLPVSR-APPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 162 LNKSVVALQPGSAREGKNFQTKMATYEKLLSCdygfvHGFRNLGSSAMTMAYIAMGYLDSYWDGG-CYSWDVCAGWCILK 240
Cdd:pfam00459 155 SEALLVTLFGVSSRKDTSEASFLAKLLKLVRA-----PGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6321836 241 EVGGRVVGANPGEwsidvdnRTYLAVRGTINNESDEQTKYITDFWNCV 288
Cdd:pfam00459 230 EAGGVVTDADGGP-------FDLLAGRVIAANPKVLHELLAAALEEII 270
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
7-270 |
1.22e-62 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 198.76 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 7 SIEKFL--CELATEKVGPIIKSKSGTQKDYDLKTgsrSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESY-VKGETVI 83
Cdd:PLN02553 6 DLEQFLevAVDAAKAAGQIIRKGFYQTKHVEHKG---QVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTaASGGTEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 84 TDDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKDYDYKSKLEsmgsliLN 163
Cdd:PLN02553 83 TDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSE------LG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 164 KSVVALQPGSAREGknfQTKMATYEKLLSCDYGfVHGFRNLGSSAMTMAYIAMGYLDSYWD---GGCysWDVCAGWCILK 240
Cdd:PLN02553 157 KALLATEVGTKRDK---ATVDATTNRINALLYK-VRSLRMSGSCALNLCGVACGRLDIFYEigfGGP--WDVAAGAVIVK 230
|
250 260 270
....*....|....*....|....*....|
gi 6321836 241 EVGGRVVGANPGEWsiDVDNRTYLAVRGTI 270
Cdd:PLN02553 231 EAGGLVFDPSGGPF--DIMSRRVAASNGHL 258
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
11-270 |
5.35e-55 |
|
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: 178.89 E-value: 5.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 11 FLCELAtEKVGPIIKSKSGtQKDYDLKTGSRSvDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETviTDDPTFI 90
Cdd:COG0483 6 LALRAA-RAAGALILRRFR-ELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR--DSGYVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 91 IDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyksKLESMGSLILNKSVVALq 170
Cdd:COG0483 81 IDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGR------RLRVSARTDLEDALVAT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 171 pGSAREGKNFQTkMATYEKLLSCdygfVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGAN 250
Cdd:COG0483 154 -GFPYLRDDREY-LAALAALLPR----VRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLD 227
|
250 260
....*....|....*....|
gi 6321836 251 PGEWsiDVDNRTYLAVRGTI 270
Cdd:COG0483 228 GEPL--DLGSGSLVAANPAL 245
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
44-246 |
7.28e-20 |
|
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273949 [Multi-domain] Cd Length: 251 Bit Score: 86.59 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 44 DIVTAIDKQVEKLIWESVKTQYPTFKFIGEEsyvKGETVITDDP-TFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVG 122
Cdd:TIGR02067 34 TPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAErVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 123 VIYNPHINLLVSASKGNGMRVNNKDYdYKSKLESMGS-LILNKSVVALQPGSAREGknFQT-KMATYEKLLSCDYGfvhg 200
Cdd:TIGR02067 111 VIFQPATGERWWAAGGGAAFLGGRRL-RVSSCANLSDaVLFTTSPDLLDDPGNRPA--FERlRRAARLTRYGGDCY---- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321836 201 frnlgssAMTMAyiAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRV 246
Cdd:TIGR02067 184 -------AYLMV--AGGAVDIVVEPGLSPWDIAALIPVIEEAGGCF 220
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
10-267 |
5.37e-103 |
|
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: 300.61 E-value: 5.37e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 10 KFLCELATEKVGPIIKSKSGTQKDYDLKtgSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETviTDDPTF 89
Cdd:cd01639 3 NIAIEAARKAGEILLEAYEKLGLNVEEK--GSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGL--TDEPTW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 90 IIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKDYDYKSKLEsmgsliLNKSVVAL 169
Cdd:cd01639 79 IIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKE------LKDALVAT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 170 QPGSAREgKNFQTKMATYEKLLSCdygFVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGA 249
Cdd:cd01639 153 GFPYDRG-DNFDRYLNNFAKLLAK---AVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDF 228
|
250
....*....|....*...
gi 6321836 250 NPGEWsiDVDNRTYLAVR 267
Cdd:cd01639 229 DGGPF--DLMSGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
4-288 |
2.51e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 271.91 E-value: 2.51e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 4 DLASIEKFLCELATeKVGPIIKSKSGTQKDYDLKTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVI 83
Cdd:pfam00459 1 DLEEVLKVAVELAA-KAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 84 T--DDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyKSKLESmGSLI 161
Cdd:pfam00459 80 LtdDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQ----PLPVSR-APPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 162 LNKSVVALQPGSAREGKNFQTKMATYEKLLSCdygfvHGFRNLGSSAMTMAYIAMGYLDSYWDGG-CYSWDVCAGWCILK 240
Cdd:pfam00459 155 SEALLVTLFGVSSRKDTSEASFLAKLLKLVRA-----PGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILR 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 6321836 241 EVGGRVVGANPGEwsidvdnRTYLAVRGTINNESDEQTKYITDFWNCV 288
Cdd:pfam00459 230 EAGGVVTDADGGP-------FDLLAGRVIAANPKVLHELLAAALEEII 270
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
7-270 |
1.22e-62 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 198.76 E-value: 1.22e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 7 SIEKFL--CELATEKVGPIIKSKSGTQKDYDLKTgsrSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESY-VKGETVI 83
Cdd:PLN02553 6 DLEQFLevAVDAAKAAGQIIRKGFYQTKHVEHKG---QVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTaASGGTEL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 84 TDDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKDYDYKSKLEsmgsliLN 163
Cdd:PLN02553 83 TDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSE------LG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 164 KSVVALQPGSAREGknfQTKMATYEKLLSCDYGfVHGFRNLGSSAMTMAYIAMGYLDSYWD---GGCysWDVCAGWCILK 240
Cdd:PLN02553 157 KALLATEVGTKRDK---ATVDATTNRINALLYK-VRSLRMSGSCALNLCGVACGRLDIFYEigfGGP--WDVAAGAVIVK 230
|
250 260 270
....*....|....*....|....*....|
gi 6321836 241 EVGGRVVGANPGEWsiDVDNRTYLAVRGTI 270
Cdd:PLN02553 231 EAGGLVFDPSGGPF--DIMSRRVAASNGHL 258
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
11-270 |
5.35e-55 |
|
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: 178.89 E-value: 5.35e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 11 FLCELAtEKVGPIIKSKSGtQKDYDLKTGSRSvDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETviTDDPTFI 90
Cdd:COG0483 6 LALRAA-RAAGALILRRFR-ELDLEVETKGDG-DLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR--DSGYVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 91 IDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyksKLESMGSLILNKSVVALq 170
Cdd:COG0483 81 IDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGR------RLRVSARTDLEDALVAT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 171 pGSAREGKNFQTkMATYEKLLSCdygfVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGAN 250
Cdd:COG0483 154 -GFPYLRDDREY-LAALAALLPR----VRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLD 227
|
250 260
....*....|....*....|
gi 6321836 251 PGEWsiDVDNRTYLAVRGTI 270
Cdd:COG0483 228 GEPL--DLGSGSLVAANPAL 245
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
11-254 |
4.51e-45 |
|
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: 152.47 E-value: 4.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 11 FLCELAtEKVGPIIKSKSGTQKDYDLKTGSRsvDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGeTVITDDPTFI 90
Cdd:cd01637 3 LALKAV-REAGALILEAFGEELTVETKKGDG--DLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSG-NVSDGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 91 IDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyksKLESMGSLILNKSVVALQ 170
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGK------KLPLSKDTPLNDALLSTN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 171 PGSAREGknfqtKMATYEKLLSCdygfVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGAN 250
Cdd:cd01637 153 ASMLRSN-----RAAVLASLVNR----ALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLD 223
|
....
gi 6321836 251 PGEW 254
Cdd:cd01637 224 GEPL 227
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
12-246 |
1.54e-39 |
|
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: 138.24 E-value: 1.54e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 12 LCELATEKVGPIIKSKSGTQKDYDLKtgsRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESyvkGETVITDDPTFII 91
Cdd:cd01643 3 LAEAIAQEAGDRALADFGNSLSAETK---ADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG---GGIFPSSGWYWVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 92 DPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyKSKLEsmgslilnksvVALQP 171
Cdd:cd01643 77 DPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGK----PLALH-----------PPLQL 141
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 6321836 172 GSAREGKNFQTKMATYEKLLSCDYGFVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRV 246
Cdd:cd01643 142 PDCNVGFNRSSRASARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSW 216
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
42-246 |
9.16e-31 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 116.06 E-value: 9.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 42 SVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESyvkGETVITD-DPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPV 120
Cdd:PRK10757 36 SNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDqDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 121 VGVIYNPHINLLVSASKGNGMRVNnkDYdyksKLESMGSLILNKSVVAlqpgsarEGKNFQTKM--ATYEKLLSCDYGFV 198
Cdd:PRK10757 113 VAVVYDPMRNELFTATRGQGAQLN--GY----RLRGSTARDLDGTILA-------TGFPFKAKQhaTTYINIVGKLFTEC 179
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 6321836 199 HGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRV 246
Cdd:PRK10757 180 ADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIV 227
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
11-249 |
7.09e-29 |
|
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: 108.63 E-value: 7.09e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 11 FLCELAtEKVGPIIKSKSGTQKDYDLKTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVI-TDDPTF 89
Cdd:cd01636 3 ELCRVA-KEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGrRDEYTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 90 IIDPIDGTTNFVHDFPFSCTSLGLtvnkepvvgviynphINLLVSAskgngmrvnnkdYDYKSKLESmgslilnksvval 169
Cdd:cd01636 82 VIDPIDGTKNFINGLPFVAVVIAV---------------YVILILA------------EPSHKRVDE------------- 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 170 qpgsaregknfqtkmATYEKLLSCdygfVHGFRNLGSSAMTMAYIAMGYLDSYWD--GGCYSWDVCAGWCILKEVGGRVV 247
Cdd:cd01636 122 ---------------KKAELQLLA----VYRIRIVGSAVAKMCLVALGLADIYYEpgGKRRAWDVAASAAIVREAGGIMT 182
|
..
gi 6321836 248 GA 249
Cdd:cd01636 183 DW 184
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
44-270 |
1.05e-22 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 96.41 E-value: 1.05e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 44 DIVTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETviTDDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGV 123
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDS--SSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAAT 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 124 IYN----PH--INLLVSASKGNGMRVNNKDYdYKSKLESmgsliLNKSVVALQPGSAREgKNFQTKMATYEkllscDYGF 197
Cdd:PLN02737 189 VVEfvggPMcwNTRTFSASAGGGAFCNGQKI-HVSQTDK-----VERSLLVTGFGYEHD-DAWATNIELFK-----EFTD 256
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 6321836 198 V-HGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRVVGANPGEWSidVDNRTYLAVRGTI 270
Cdd:PLN02737 257 VsRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFS--VFDRSVLVSNGVL 328
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
1-266 |
6.28e-22 |
|
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family (FBPase class IV). These are Mg++ dependent phosphatases. Members in this family may have both fructose-1,6-bisphosphatase and inositol-monophosphatase activity. In hyperthermophilic archaea, inositol monophosphatase is thought to play a role in the biosynthesis of di-myo-inositol-1,1'-phosphate, an osmolyte unique to hyperthermophiles.
Pssm-ID: 238773 [Multi-domain] Cd Length: 257 Bit Score: 92.06 E-value: 6.28e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 1 MTIDLA-SIEKFLCEL-ATEKVGPIIK-SKSGTQkdydlktgsrsvdiVTAIDKQVEKLIWESVKTQYPTfKFIGEESyv 77
Cdd:cd01515 4 IARNIAkEIEKAIKPLfGTEDASEVVKiGADGTP--------------TKLIDKVAEDAAIEILKKLGSV-NIVSEEI-- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 78 kGETVITDDP--TFIIDPIDGTTNFVHDFPFSCTSLGLTVNKE--PVVGVIYNPHINLLVSASKGNGMRVNNKdydyksK 153
Cdd:cd01515 67 -GVIDNGDEPeyTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGK------R 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 154 LESMGSLILNKSVVALQPGsareGKNFQTKMATYEKllscdygfVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYS--WD 231
Cdd:cd01515 140 IKVSDFSSLKSISVSYYIY----GKNHDRTFKICRK--------VRRVRIFGSVALELCYVASGALDAFVDVRENLrlVD 207
|
250 260 270
....*....|....*....|....*....|....*..
gi 6321836 232 VCAGWCILKEVGGRVVGANPGEWSI--DVDNRTYLAV 266
Cdd:cd01515 208 IAAGYLIAEEAGGIVTDENGKELKLklNVTERVNIIA 244
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
46-250 |
2.75e-21 |
|
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: 89.98 E-value: 2.75e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 46 VTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGEtVITDDPTFIIDPIDGTTNFVH---DFpfsCTSLGLTVNKEPVVG 122
Cdd:cd01638 35 VTAADLAANAFIVEGLAALRPDIPVLSEESADDPL-RLGWDRFWLVDPLDGTREFIKgngEF---AVNIALVEDGRPVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 123 VIYNPHINLLVSASKGNGMRVNNKDYDykSKLESMGSLILNKSVVAlqpgSAREGKNFQTKMATyekllscDYGfVHGFR 202
Cdd:cd01638 111 VVYAPALGELYYALRGGGAYKNGRPGA--VSLQARPPPLQPLRVVA----SRSHPDEELEALLA-------ALG-VAEVV 176
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 6321836 203 NLGSSAMTMAyIAMGYLDSYWD-GGCYSWDVCAGWCILKEVGGRVVGAN 250
Cdd:cd01638 177 SIGSSLKFCL-VAEGEADIYPRlGPTMEWDTAAGDAVLRAAGGAVSDLD 224
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
10-264 |
2.85e-20 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 87.66 E-value: 2.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 10 KFLCELATEKVGPIIKSKSGTQK-DYDLKTGSrSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEESyvkGEtVITDDP- 87
Cdd:PRK12676 7 LEICDDMAKEVEKAIMPLFGTPDaGETVGMGA-DGTPTKLIDKVAEDIILEVLKPLGRCVNIISEEL---GE-IVGNGPe 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 88 -TFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNKdydyksKLESMGSLILNKSV 166
Cdd:PRK12676 82 yTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGK------PIKVSKTSELNESA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 167 VALqpgSAReGKNFQTKMATYEKllscdygfVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCY--SWDVCAGWCILKEVGG 244
Cdd:PRK12676 156 VSI---YGY-RRGKERTVKLGRK--------VRRVRILGAIALELCYVASGRLDAFVDVRNYlrVTDIAAGKLICEEAGG 223
|
250 260
....*....|....*....|..
gi 6321836 245 RVVGANPGEWSI--DVDNRTYL 264
Cdd:PRK12676 224 IVTDEDGNELKLplNVTERTNL 245
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
14-246 |
4.62e-20 |
|
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: 86.92 E-value: 4.62e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 14 ELATEkVGPIIKSKSGTQKDYDLKTGSrsvDIVTAIDKQVEKLIWESVKTQYPTFKFIGEEsyvKGETVITDDPTFIIDP 93
Cdd:cd01641 7 ELADA-AGQITLPYFRTRLQVETKADF---SPVTEADRAAEAAMRELIAAAFPDHGILGEE---FGNEGGDAGYVWVLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 94 IDGTTNFVHDFPFSCTSLGLTVNKEPVVGVIYNPHINLLVSASKGNGMRVNNkdydykskleSMGSLILNKSVVALQ--- 170
Cdd:cd01641 80 IDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNG----------AGGRPLRVRACADLAeav 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 171 -----PGSAREGKNfqtkmATYEKLLScdygfVHGFRNLGSSAMTMAYIAMGYLDSYWDGGCYSWDVCAGWCILKEVGGR 245
Cdd:cd01641 150 lsttdPHFFTPGDR-----AAFERLAR-----AVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGV 219
|
.
gi 6321836 246 V 246
Cdd:cd01641 220 I 220
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
44-246 |
7.28e-20 |
|
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273949 [Multi-domain] Cd Length: 251 Bit Score: 86.59 E-value: 7.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 44 DIVTAIDKQVEKLIWESVKTQYPTFKFIGEEsyvKGETVITDDP-TFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVG 122
Cdd:TIGR02067 34 TPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAErVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 123 VIYNPHINLLVSASKGNGMRVNNKDYdYKSKLESMGS-LILNKSVVALQPGSAREGknFQT-KMATYEKLLSCDYGfvhg 200
Cdd:TIGR02067 111 VIFQPATGERWWAAGGGAAFLGGRRL-RVSSCANLSDaVLFTTSPDLLDDPGNRPA--FERlRRAARLTRYGGDCY---- 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 6321836 201 frnlgssAMTMAyiAMGYLDSYWDGGCYSWDVCAGWCILKEVGGRV 246
Cdd:TIGR02067 184 -------AYLMV--AGGAVDIVVEPGLSPWDIAALIPVIEEAGGCF 220
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
44-246 |
4.19e-19 |
|
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: 84.67 E-value: 4.19e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 44 DIVTAIDKQVEKLIWESVKTQYPTFKFIGEEsyvkgeTVITDDPTFIIDPIDGTTNFVHDFPFsCTSLGLTVNKEPVVGV 123
Cdd:cd01517 36 SPVTVADYGAQALITAALARLFPSDPIVGEE------DSAALGRFWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGV 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 124 IYNP-------HINLLVSASKGNGMRVNNKDyDYKSKLESMGSLilnKSVVALQPGSAREGKNF-QTKMATYEKLLSCDy 195
Cdd:cd01517 109 IGCPnlplddgGGGDLFSAVRGQGAWLRPLD-GSSLQPLSVRQL---TNAARASFCESVESAHSsHRLQAAIKALGGTP- 183
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 6321836 196 gfvhGFRNLGSSA--MTMA------YIAMGYLDSYWDggcYSWDVCAGWCILKEVGGRV 246
Cdd:cd01517 184 ----QPVRLDSQAkyAAVArgaadfYLRLPLSMSYRE---KIWDHAAGVLIVEEAGGKV 235
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
46-246 |
6.00e-18 |
|
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: 81.34 E-value: 6.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 46 VTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVITDDPTF-IIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVI 124
Cdd:TIGR01331 35 VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFwLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 125 YNPHINLLVSASKGNGMRVNNKDYDYKSKLesmgslilnkSVVALQPGSAREGKNFQTKMATYEKLLScDYGFVhgFRNL 204
Cdd:TIGR01331 115 YAPATGVTYFATAGKAAKREGDGQALKAPI----------HVRPWPSGPLLVVISRSHAEEKTTEYLA-NLGYD--LRTS 181
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 6321836 205 GSSAMTMAYIAMGYLDSYWDGGCYS-WDVCAGWCILKEVGGRV 246
Cdd:TIGR01331 182 GGSSLKFCLVAEGSADIYPRLGPTGeWDTAAGHAVLAAAGGAI 224
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
46-250 |
6.76e-18 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 80.97 E-value: 6.76e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 46 VTAIDKQVEKLIWESVKTQYPTFKFIGEESYVKGETVITDDPTF-IIDPIDGTTNFVH---DFpfsCTSLGLTVNKEPVV 121
Cdd:COG1218 38 VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFwLVDPLDGTKEFIKrngEF---TVNIALIEDGRPVL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 122 GVIYNPHINLLVSASKGNGMRVNNKDYDYK----SKLESMGSLIlnksVVALQPGSAREGKNFQTKMATYEkllscdygf 197
Cdd:COG1218 115 GVVYAPALGRLYYAAKGQGAFKETGGGERQpirvRDRPPAEPLR----VVASRSHRDEETEALLARLGVAE--------- 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 6321836 198 vhgFRNLGSS---AMtmayIAMGYLDSYWD-GGCYSWDVCAGWCILKEVGGRVVGAN 250
Cdd:COG1218 182 ---LVSVGSSlkfCL----VAEGEADLYPRlGPTMEWDTAAGQAILEAAGGRVTDLD 231
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
12-243 |
6.12e-13 |
|
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: 67.09 E-value: 6.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 12 LCELAT-EKVGPIIKSKsgtQKDYDLKTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEES--YVKGetviTDDPT 88
Cdd:cd01642 4 VLEKITkEIILLLNEKN---RQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESgeIRKG----SGEYI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 89 FIIDPIDGTTNFVHDFPFSCTSLGLTvnkEPVVGVIYNPHINLlvsASKGNGMRVNNKD--YDYKSKLESMGSLILN-KS 165
Cdd:cd01642 77 AVLDPLDGSTNYLSGIPFYSVSVALA---DPRSKVKAATLDNF---VSGEGGLKVYSPPtrFSYISVPKLGPPLVPEvPS 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 166 VVALQPGSAREGKnfqtkmatyEKLLSCDYGFvhGFRNLGSSAMTMAYIAMGYLDSYWD--GGCYSWDVCAGWCILKEVG 243
Cdd:cd01642 151 KIGIYEGSSRNPE---------KFLLLSRNGL--KFRSLGSAALELAYTCEGSFVLFLDlrGKLRNFDVAAALGACKRLG 219
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
37-247 |
5.50e-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: 65.04 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 37 KTGSRSVDIVTAIDKQVEKLIWESVKTQYPTFKFIGEES-----------------YVKGETVIT-------DDPTFIID 92
Cdd:cd01640 33 KTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDnefenqedesrdvdldeEILEESCPSpskdlpeEDLGVWVD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 93 PIDGTTNFVHDFPFSCTSL-GLTVNKEPVVGVIYNPHINLLVSASK--------GNGMRVNNKDYdykSKLESMGSLILN 163
Cdd:cd01640 113 PLDATQEYTEGLLEYVTVLiGVAVKGKPIAGVIHQPFYEKTAGAGAwlgrtiwgLSGLGAHSSDF---KEREDAGKIIVS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 164 KS----VVALQPGSAREGKNFQTKMATYEKLLScdygFVHGfrnlgssamtmayIAMGYLdsYWDGGCYSWDVCAGWCIL 239
Cdd:cd01640 190 TShshsVKEVQLITAGNKDEVLRAGGAGYKVLQ----VLEG-------------LADAYV--HSTGGIKKWDICAPEAIL 250
|
....*...
gi 6321836 240 KEVGGRVV 247
Cdd:cd01640 251 RALGGDMT 258
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
89-280 |
5.14e-07 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 50.88 E-value: 5.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 89 FIIDPIDGTTNFVHDFPFSCTSLGLT-VNKEPV----------------VGVIYNPHINLLVSASKGNGMRVNNKDYdyK 151
Cdd:PRK14076 84 FVLDPIDGTYNALKDIPIYSASIAIAkIDGFDKkikefigknltindleVGVVKNIATGDTYYAEKGEGAYLLKKGE--K 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 152 SKLESMGSLILNKSVVALQpgsaregknfqTKMATYEKLLSCDYGFVHGFRNLGSSAMTMAYIAMGYLDSYWD--GGCYS 229
Cdd:PRK14076 162 KKIEISNISNLKDASIGLF-----------AYGLSLDTLKFIKDRKVRRIRLFGSIALEMCYVASGALDAFINvnETTRL 230
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 6321836 230 WDVCAGWCILKEVGGRVVGAN--PGEWSIDVDNRTYLAVRGTI----------NNESDEQTKY 280
Cdd:PRK14076 231 CDIAAGYVICKEAGGIITNKNgkPLNMKLDINEKTSVICSNEIlhkklvgifgNKWRIKPTKF 293
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
46-127 |
8.52e-07 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 49.33 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 46 VTAIDKQVEKLIWESVKTQYPTFKFIGEESYVK-GETviTDDPTFIIDPIDGTTNFVHDFPFSCTSLGLTVNKEPVVGVI 124
Cdd:PLN02911 70 VTIADRAAEEAMRSIILENFPSHAIFGEEHGLRcGEG--SSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGII 147
|
...
gi 6321836 125 YNP 127
Cdd:PLN02911 148 DQP 150
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
12-139 |
5.98e-04 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 40.45 E-value: 5.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 6321836 12 LCELATEKVGPIIKSKSGTQKdydLKTGSRSVDI-VTAIDKQVEKLIWESVKTQYPTFKFIGEEsyvkgetvitDDPTF- 89
Cdd:PRK10931 5 ICQLARNAGDAIMQVYDGTKP---LDVASKADDSpVTAADIAAHTVIKDGLRTLTPDIPVLSEE----------DPPAWe 71
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 6321836 90 ---------IIDPIDGTTNFVH---DFpfsCTSLGLTVNKEPVVGVIYNPHINLLVSASKGN 139
Cdd:PRK10931 72 vrqhwqrywLVDPLDGTKEFIKrngEF---TVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK 130
|
|
| |
