|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
1-252 |
1.29e-128 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 364.61 E-value: 1.29e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 1 MDWSKIGKRIAIEIEKEVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDIALKYLEPLG--VNIVSEELGAI-DKGSEWT 77
Cdd:PRK12676 4 MEWLEICDDMAKEVEKAIMPLFGTPDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGrcVNIISEELGEIvGNGPEYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 78 VVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKV---KDFNPKDVIISYYPD 154
Cdd:PRK12676 84 VVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVsktSELNESAVSIYGYRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 155 ENVDIKKLREKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICKEAGAIITDENGEELKFELNATDRI 234
Cdd:PRK12676 164 GKERTVKLGRKVRRVRILGAIALELCYVASGRLDAFVDVRNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLPLNVTERT 243
|
250
....*....|....*...
gi 506213410 235 KVLVANSKEMLNIILDII 252
Cdd:PRK12676 244 NLIAANGEELHKKILELL 261
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
3-252 |
3.95e-107 |
|
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: 310.08 E-value: 3.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 3 WSKIGKRIAIEIEKEVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDIALKYLEPLG-VNIVSEELGAIDKG--SEWTVV 79
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGADGTPTKLIDKVAEDAAIEILKKLGsVNIVSEEIGVIDNGdePEYTVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 80 IDPIDGSFNFINGIPFFGFCFGVFKNN--NPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKVKDFNPKD--VIISYYPDE 155
Cdd:cd01515 81 LDPLDGTYNAINGIPFYSVSVAVFKIDksDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKsiSVSYYIYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 156 NVDIK-KLREKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICKEAGAIITDENGEELKFELNATDRI 234
Cdd:cd01515 161 NHDRTfKICRKVRRVRIFGSVALELCYVASGALDAFVDVRENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKLNVTERV 240
|
250
....*....|....*...
gi 506213410 235 KVLVANSkEMLNIILDII 252
Cdd:cd01515 241 NIIAANS-ELHKKLLELL 257
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
8-252 |
1.17e-51 |
|
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: 168.48 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 8 KRIAIEIEKEVLQYFGRKDRSyvIGTSPSGDETEIFDKVSEDIALKYLEPL--GVNIVSEELGAID-KGSEWTVVIDPID 84
Cdd:COG0483 8 LRAARAAGALILRRFRELDLE--VETKGDGDLVTEADRAAEAAIRERLRAAfpDHGILGEESGASEgRDSGYVWVIDPID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 85 GSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKV-KDFNPKDVIISYYPDENVD----- 158
Cdd:COG0483 86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVsARTDLEDALVATGFPYLRDdreyl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 159 --IKKLREKIKRVRIFGAFGLEMCYVANGILDAIFdvRPKVRAVDIASSYIICKEAGAIITDENGEELKFELNAtdrikv 236
Cdd:COG0483 166 aaLAALLPRVRRVRRLGSAALDLAYVAAGRLDAFV--EAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS------ 237
|
250
....*....|....*.
gi 506213410 237 LVANSKEMLNIILDII 252
Cdd:COG0483 238 LVAANPALHDELLALL 253
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
8-245 |
2.88e-34 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 123.99 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 8 KRIAIEIekeVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDI---ALKYLEPlGVNIVSEELGAIDKGSE-----WTVV 79
Cdd:pfam00459 13 AAKAGEI---LREAFSNKLTIEEKGKSGANDLVTAADKAAEELileALAALFP-SHKIIGEEGGAKGDQTEltddgPTWI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 80 IDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKVKDFNPKDVIISYY---PDEN 156
Cdd:pfam00459 89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTlfgVSSR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 157 VDIKKLREKIK--------RVRIFGAFGLEMCYVANGILDA-IFDVRPKVRavDIASSYIICKEAGAIITDENGEELKFE 227
Cdd:pfam00459 169 KDTSEASFLAKllklvrapGVRRVGSAALKLAMVAAGKADAyIEFGRLKPW--DHAAGVAILREAGGVVTDADGGPFDLL 246
|
250
....*....|....*...
gi 506213410 228 LnatdrIKVLVANSKEML 245
Cdd:pfam00459 247 A-----GRVIAANPKVLH 259
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
1-252 |
1.29e-128 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 364.61 E-value: 1.29e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 1 MDWSKIGKRIAIEIEKEVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDIALKYLEPLG--VNIVSEELGAI-DKGSEWT 77
Cdd:PRK12676 4 MEWLEICDDMAKEVEKAIMPLFGTPDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGrcVNIISEELGEIvGNGPEYT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 78 VVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKV---KDFNPKDVIISYYPD 154
Cdd:PRK12676 84 VVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVsktSELNESAVSIYGYRR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 155 ENVDIKKLREKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICKEAGAIITDENGEELKFELNATDRI 234
Cdd:PRK12676 164 GKERTVKLGRKVRRVRILGAIALELCYVASGRLDAFVDVRNYLRVTDIAAGKLICEEAGGIVTDEDGNELKLPLNVTERT 243
|
250
....*....|....*...
gi 506213410 235 KVLVANSKEMLNIILDII 252
Cdd:PRK12676 244 NLIAANGEELHKKILELL 261
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
3-252 |
3.95e-107 |
|
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: 310.08 E-value: 3.95e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 3 WSKIGKRIAIEIEKEVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDIALKYLEPLG-VNIVSEELGAIDKG--SEWTVV 79
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGADGTPTKLIDKVAEDAAIEILKKLGsVNIVSEEIGVIDNGdePEYTVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 80 IDPIDGSFNFINGIPFFGFCFGVFKNN--NPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKVKDFNPKD--VIISYYPDE 155
Cdd:cd01515 81 LDPLDGTYNAINGIPFYSVSVAVFKIDksDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKsiSVSYYIYGK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 156 NVDIK-KLREKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICKEAGAIITDENGEELKFELNATDRI 234
Cdd:cd01515 161 NHDRTfKICRKVRRVRIFGSVALELCYVASGALDAFVDVRENLRLVDIAAGYLIAEEAGGIVTDENGKELKLKLNVTERV 240
|
250
....*....|....*...
gi 506213410 235 KVLVANSkEMLNIILDII 252
Cdd:cd01515 241 NIIAANS-ELHKKLLELL 257
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
6-226 |
6.64e-52 |
|
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: 168.65 E-value: 6.64e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 6 IGKRIAIEIEKEVLQYFGRKDrsYVIGTSPSGDETEIFDKVSEDIALKYLEPL--GVNIVSEELGA--IDKGSEWTVVID 81
Cdd:cd01637 3 LALKAVREAGALILEAFGEEL--TVETKKGDGDLVTEADLAAEELIVDVLKALfpDDGILGEEGGGsgNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 82 PIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRI-KVKDFNPKDVIISYYP-----DE 155
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLpLSKDTPLNDALLSTNAsmlrsNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 506213410 156 NVDIKKLREKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVraVDIASSYIICKEAGAIITDENGEELKF 226
Cdd:cd01637 161 AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNP--WDYAAGALIVEEAGGIVTDLDGEPLDT 229
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
8-252 |
1.17e-51 |
|
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: 168.48 E-value: 1.17e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 8 KRIAIEIEKEVLQYFGRKDRSyvIGTSPSGDETEIFDKVSEDIALKYLEPL--GVNIVSEELGAID-KGSEWTVVIDPID 84
Cdd:COG0483 8 LRAARAAGALILRRFRELDLE--VETKGDGDLVTEADRAAEAAIRERLRAAfpDHGILGEESGASEgRDSGYVWVIDPID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 85 GSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKV-KDFNPKDVIISYYPDENVD----- 158
Cdd:COG0483 86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVsARTDLEDALVATGFPYLRDdreyl 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 159 --IKKLREKIKRVRIFGAFGLEMCYVANGILDAIFdvRPKVRAVDIASSYIICKEAGAIITDENGEELKFELNAtdrikv 236
Cdd:COG0483 166 aaLAALLPRVRRVRRLGSAALDLAYVAAGRLDAFV--EAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS------ 237
|
250
....*....|....*.
gi 506213410 237 LVANSKEMLNIILDII 252
Cdd:COG0483 238 LVAANPALHDELLALL 253
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
6-219 |
6.92e-45 |
|
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: 149.08 E-value: 6.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 6 IGKRIAIEIEKEVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDIALKYLEPL--GVNIVSEELGAID----KGSEWTVV 79
Cdd:cd01636 3 ELCRVAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSfpDVKIVGEESGVAEevmgRRDEYTWV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 80 IDPIDGSFNFINGIPFFGFCFGVFKNNnpyfgLTYEFLTKRFYEAKigegaflngkrikvkdfnpkdviisyypdenvdI 159
Cdd:cd01636 83 IDPIDGTKNFINGLPFVAVVIAVYVIL-----ILAEPSHKRVDEKK---------------------------------A 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 160 KKLREKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICKEAGAIITDE 219
Cdd:cd01636 125 ELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGKRRAWDVAASAAIVREAGGIMTDW 184
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
1-240 |
7.32e-41 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 147.57 E-value: 7.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 1 MDWSKIGKRIAIEIEKEVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDIALKYLEPLGVNI-VSEELGAIDKGS---EW 76
Cdd:PRK14076 3 MDMLKIALKVAKEIEKKIKPLIGWEKAGEVVKIGADGTPTKRIDLIAENIAINSLEKFCSGIlISEEIGFKKIGKnkpEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 77 TVVIDPIDGSFNFINGIPFFGFCFGV-----------------FKNNNPYFGLTYEFLTKRFYEAKIGEGAFL----NGK 135
Cdd:PRK14076 83 IFVLDPIDGTYNALKDIPIYSASIAIakidgfdkkikefigknLTINDLEVGVVKNIATGDTYYAEKGEGAYLlkkgEKK 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 136 RIKVKDF-NPKDVIISYY----PDENVDIKKLReKIKRVRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICK 210
Cdd:PRK14076 163 KIEISNIsNLKDASIGLFayglSLDTLKFIKDR-KVRRIRLFGSIALEMCYVASGALDAFINVNETTRLCDIAAGYVICK 241
|
250 260 270
....*....|....*....|....*....|
gi 506213410 211 EAGAIITDENGEELKFELNATDRIKVLVAN 240
Cdd:PRK14076 242 EAGGIITNKNGKPLNMKLDINEKTSVICSN 271
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
8-245 |
2.88e-34 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 123.99 E-value: 2.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 8 KRIAIEIekeVLQYFGRKDRSYVIGTSPSGDETEIFDKVSEDI---ALKYLEPlGVNIVSEELGAIDKGSE-----WTVV 79
Cdd:pfam00459 13 AAKAGEI---LREAFSNKLTIEEKGKSGANDLVTAADKAAEELileALAALFP-SHKIIGEEGGAKGDQTEltddgPTWI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 80 IDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKVKDFNPKDVIISYY---PDEN 156
Cdd:pfam00459 89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTlfgVSSR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 157 VDIKKLREKIK--------RVRIFGAFGLEMCYVANGILDA-IFDVRPKVRavDIASSYIICKEAGAIITDENGEELKFE 227
Cdd:pfam00459 169 KDTSEASFLAKllklvrapGVRRVGSAALKLAMVAAGKADAyIEFGRLKPW--DHAAGVAILREAGGVVTDADGGPFDLL 246
|
250
....*....|....*...
gi 506213410 228 LnatdrIKVLVANSKEML 245
Cdd:pfam00459 247 A-----GRVIAANPKVLH 259
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
10-224 |
1.37e-33 |
|
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: 121.49 E-value: 1.37e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 10 IAIEIEKE----VLQYFGRKDRSYVIGTSPSGDETEIfDKVSEDI---ALKYLEPlGVNIVSEELGAIDKG-SEWTVVID 81
Cdd:cd01639 4 IAIEAARKageiLLEAYEKLGLNVEEKGSPVDLVTEV-DKAVEKLiieILKKAYP-DHGFLGEESGAAGGLtDEPTWIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 82 PIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKVKDFNP-KDVII----SYYPDEN 156
Cdd:cd01639 82 PLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKElKDALVatgfPYDRGDN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 506213410 157 VD------IKKLREKIKRVRIFGAFGLEMCYVANGILDAIFDVrpKVRAVDIASSYIICKEAGAIITDENGEEL 224
Cdd:cd01639 162 FDrylnnfAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWER--GLKPWDVAAGALIVREAGGLVTDFDGGPF 233
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
10-239 |
9.24e-29 |
|
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: 108.96 E-value: 9.24e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 10 IAIEIEKEV----LQYFGRkdrSYVIGTSPSGD---------ETEIFDKVSEDIalkylePlGVNIVSEELGAIDKGSEW 76
Cdd:cd01643 3 LAEAIAQEAgdraLADFGN---SLSAETKADGSlvtaadrwvEQLIRARLAAQF------P-DDGVLGEEGGGIFPSSGW 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 77 TVVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKVK-DFNPKDVI------I 149
Cdd:cd01643 73 YWVIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHpPLQLPDCNvgfnrsS 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 150 SYYPDENVDIKKLREKIKrVRIFGAFGLEMCYVANGILDAIfdVRPKVRAVDIASSYIICKEAGAIIT--DENGEELKFE 227
Cdd:cd01643 153 RASARAVLRVILRRFPGK-IRMLGSASLNLASVAAGQTLGY--VEATPKIWDIAAAWVILREAGGSWTilDEEPAFLQTK 229
|
250
....*....|..
gi 506213410 228 LNATDRIKVLVA 239
Cdd:cd01643 230 DYLSAGFPTLIA 241
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
9-214 |
2.47e-23 |
|
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: 94.82 E-value: 2.47e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 9 RIAIEIEKEVLQYF-GRKDRSYV-IGTSPSGDETEIFDKVSEDIALKYL--EPLGVNIVSEELGAIDKGS-EWTVVIDPI 83
Cdd:cd01642 3 EVLEKITKEIILLLnEKNRQGLVkLIRGAGGDVTRVADLKAEEIILKLLreEGVFGQIISEESGEIRKGSgEYIAVLDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 84 DGSFNFINGIPFFGFCFGVF-KNNNPYFGLTYEFLTKRFY---EAKIGEGAFLNGKRIKVKDF-NPKDVIISYYPDENVD 158
Cdd:cd01642 83 DGSTNYLSGIPFYSVSVALAdPRSKVKAATLDNFVSGEGGlkvYSPPTRFSYISVPKLGPPLVpEVPSKIGIYEGSSRNP 162
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506213410 159 IKKLREKIKR--VRIFGAFGLEMCYVANGILDAIFDVRPKVRAVDIASSYIICKEAGA 214
Cdd:cd01642 163 EKFLLLSRNGlkFRSLGSAALELAYTCEGSFVLFLDLRGKLRNFDVAAALGACKRLGL 220
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
44-240 |
2.50e-20 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 88.70 E-value: 2.50e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 44 DKVSEDIALKYLEPLGVN--IVSEELGAI-DKGSEWTVVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFL--- 117
Cdd:PLN02737 117 DKASEAAILEVVRKNFPDhlILGEEGGVIgDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVggp 196
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 118 ---TKRFYEAKIGEGAFLNGKRIKVKdfNPKDVIIS-------YYPDE----NVDIKKLREKIKR-VRIFGAFGLEMCYV 182
Cdd:PLN02737 197 mcwNTRTFSASAGGGAFCNGQKIHVS--QTDKVERSllvtgfgYEHDDawatNIELFKEFTDVSRgVRRLGAAAVDMCHV 274
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506213410 183 ANGILDAIFDVRPKvrAVDIASSYIICKEAGAIITDENGeeLKFELnaTDRiKVLVAN 240
Cdd:PLN02737 275 ALGIVEAYWEYRLK--PWDMAAGVLIVEEAGGTVTRMDG--GKFSV--FDR-SVLVSN 325
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
44-241 |
2.20e-19 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 84.36 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 44 DKVSEDIALKYLEPLGVN--IVSEE----LGAIDKGSEWTVVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFL 117
Cdd:PLN02553 48 DKACEDLIFNHLKQAFPShkFIGEEttaaSGGTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPI 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 118 TKRFYEAKIGEGAFLNGKRIKV--KDFNPKDVI---ISYYPDE-NVD-----IKKLREKIKRVRIFGAFGLEMCYVANGI 186
Cdd:PLN02553 128 LDELFTAVKGKGAFLNGKPIKAssQSELGKALLateVGTKRDKaTVDattnrINALLYKVRSLRMSGSCALNLCGVACGR 207
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 506213410 187 LDAIFDVR---PkvraVDIASSYIICKEAGAIITDENGEElkFELNATdriKVLVANS 241
Cdd:PLN02553 208 LDIFYEIGfggP----WDVAAGAVIVKEAGGLVFDPSGGP--FDIMSR---RVAASNG 256
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
9-249 |
7.26e-16 |
|
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: 74.60 E-value: 7.26e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 9 RIAIEIEKEVLQYFGRkdrSYVIGTSPSGDETEIFDKVSED-----IALKYlePlGVNIVSEELGAIDKGSEWTVVIDPI 83
Cdd:cd01641 7 ELADAAGQITLPYFRT---RLQVETKADFSPVTEADRAAEAamrelIAAAF--P-DHGILGEEFGNEGGDAGYVWVLDPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 84 DGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLN---GKRIKV-KDFNPKDVIIS-----YYPD 154
Cdd:cd01641 81 DGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVrACADLAEAVLSttdphFFTP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 155 ENVDI-KKLREKIKRVRIFGAfglemCY----VANGILDAIFDvrPKVRAVDIASSYIICKEAGAIITDENGEELkfELN 229
Cdd:cd01641 161 GDRAAfERLARAVRLTRYGGD-----CYayalVASGRVDLVVE--AGLKPYDVAALIPIIEGAGGVITDWDGGPL--TGG 231
|
250 260
....*....|....*....|
gi 506213410 230 ATDrikVLVANSKEMLNIIL 249
Cdd:cd01641 232 SGR---VVAAGDAELHEALL 248
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
62-221 |
1.10e-13 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 68.68 E-value: 1.10e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 62 IVSEELGAI---DKGSEWtvVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIK 138
Cdd:PRK10757 64 IITEESGELegeDQDVQW--VIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLR 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 139 ---VKD-----------FNPKDVIISYYpdeNVdIKKLREKIKRVRIFGAFGLEMCYVANGILDAIFDVrpKVRAVDIAS 204
Cdd:PRK10757 142 gstARDldgtilatgfpFKAKQHATTYI---NI-VGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEI--GLKPWDFAA 215
|
170
....*....|....*..
gi 506213410 205 SYIICKEAGAIITDENG 221
Cdd:PRK10757 216 GELLVREAGGIVSDFTG 232
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
62-227 |
3.17e-13 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 67.82 E-value: 3.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 62 IVSEELGAI--DKGSEWTVVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKV 139
Cdd:PLN02911 94 IFGEEHGLRcgEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEIST 173
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 140 KDFNpkDVIISY-YP--------DENVDIKKLREKIKrVRIFG----AFGLemcyVANGILDAIfdVRPKVRAVDIASSY 206
Cdd:PLN02911 174 RSCA--SLKDAYlYTtsphmfsgDAEDAFARVRDKVK-VPLYGcdcyAYGL----LASGHVDLV--VESGLKPYDYLALV 244
|
170 180
....*....|....*....|.
gi 506213410 207 IICKEAGAIITDENGEELKFE 227
Cdd:PLN02911 245 PVVEGAGGVITDWKGRKLRWE 265
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
9-226 |
6.31e-12 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 63.64 E-value: 6.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 9 RIAIEIEKEVLQYFGR-------KDRSYVigtspsgdeTEiFDKVSEDIALKYLEPL--GVNIVSEE----LGAIDKGSE 75
Cdd:COG1218 10 EIAREAGEAILEIYRAdfeveekADDSPV---------TE-ADLAAHAIILAGLAALtpDIPVLSEEsaaiPYEERKSWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 76 WTVVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFL-----NGKRIKVKDFNPKD---V 147
Cdd:COG1218 80 RFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEplrV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 148 IIS-YYPDENVD--IKKLREKiKRVRIfGAfGLEMCYVANGilDAifDVRPKVRAV---DIASSYIICKEAGAIITDENG 221
Cdd:COG1218 160 VASrSHRDEETEalLARLGVA-ELVSV-GS-SLKFCLVAEG--EA--DLYPRLGPTmewDTAAGQAILEAAGGRVTDLDG 232
|
....*
gi 506213410 222 EELKF 226
Cdd:COG1218 233 KPLRY 237
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
62-226 |
3.12e-11 |
|
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: 61.47 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 62 IVSEELGAI--DKGSEWTVVIDPIDGSFNFINGIPFFGFCFGVFKNNNPYFGLTYEFLTKRFYEAKIGEGAFLNGKRIKV 139
Cdd:cd01638 59 VLSEESADDplRLGWDRFWLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAV 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 140 KDFNPKD------VIIS--YYPDENVDIKKLREKIKRVRIfgAFGLEMCYVANGILDAIFDVRPKVRAvDIASSYIICKE 211
Cdd:cd01638 139 SLQARPPplqplrVVASrsHPDEELEALLAALGVAEVVSI--GSSLKFCLVAEGEADIYPRLGPTMEW-DTAAGDAVLRA 215
|
170
....*....|....*
gi 506213410 212 AGAIITDENGEELKF 226
Cdd:cd01638 216 AGGAVSDLDGSPLTY 230
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
62-252 |
1.19e-06 |
|
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: 48.46 E-value: 1.19e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 62 IVSEELGAIDkGSEWtvVIDPIDGSFNFINGIPfFGFCFGVFKNNNPYFGLTY-------EFLTKRFYEAKIGEGAFL-- 132
Cdd:cd01517 62 IVGEEDSAAL-GRFW--VLDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGcpnlpldDGGGGDLFSAVRGQGAWLrp 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 506213410 133 --NGKRIKVKDFNPKDVIISYY----------PDENVDIKKLREKIKRVRIfgAFGLEMCYVANGILDAI----FDVRPK 196
Cdd:cd01517 138 ldGSSLQPLSVRQLTNAARASFcesvesahssHRLQAAIKALGGTPQPVRL--DSQAKYAAVARGAADFYlrlpLSMSYR 215
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 506213410 197 VRAVDIASSYIICKEAGAIITDENGEELKFEL-NATDRIKVLVANSKEMLNIILDII 252
Cdd:cd01517 216 EKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKgRKLLNNGGLIAAPGEIHEQVLEAL 272
|
|
| |
