|
Name |
Accession |
Description |
Interval |
E-value |
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
22-262 |
4.22e-58 |
|
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: 186.59 E-value: 4.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 22 RLAEIARGAALAVRMPLLEAFRS-EMAVDYKADlHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTG--DGEFQWY 98
Cdd:COG0483 2 PLLELALRAARAAGALILRRFRElDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEgrDSGYVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 99 VDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADL-ESAELNGNALASRAADNEKHATLITGYPVARD 177
Cdd:COG0483 81 IDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARgGGAFLNGRRLRVSARTDLEDALVATGFPYLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 178 frvdgREAALANFGILVETFSTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTLGKVAADG 257
Cdd:COG0483 161 -----DREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGS 235
|
....*
gi 636775990 258 PDFMC 262
Cdd:COG0483 236 GSLVA 240
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
25-268 |
5.20e-56 |
|
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: 180.59 E-value: 5.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 25 EIARGAALAVRMPLLEAFRSEMAVDYKADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGG---QTGDGEFQWYVDP 101
Cdd:cd01637 2 ELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGgsgNVSDGGRVWVIDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 102 IDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLES-AELNGNALASRAADNEKHATLITGYPVARDFRV 180
Cdd:cd01637 82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKgAFLNGKKLPLSKDTPLNDALLSTNASMLRSNRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 181 DGREAalanfgiLVETFSTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTLGKVaadgPDF 260
Cdd:cd01637 162 AVLAS-------LVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPL----DTL 230
|
....*...
gi 636775990 261 MCPGYIAT 268
Cdd:cd01637 231 NRSGIIAA 238
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
23-284 |
4.28e-36 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 130.16 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRMPLLEAFRSEMAVDYK--ADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQ------TGDGE 94
Cdd:pfam00459 5 VLKVAVELAAKAGEILREAFSNKLTIEEKgkSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAkgdqteLTDDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 95 FQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSA-DLESAELNGNALASRAADNEKHATLITGYP 173
Cdd:pfam00459 85 PTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAaKGKGAFLNGQPLPVSRAPPLSEALLVTLFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 174 V-ARDFRVDGREAALANFGILVETFstlRRPGSAALSIAHVAA-GWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTLG 251
Cdd:pfam00459 165 VsSRKDTSEASFLAKLLKLVRAPGV---RRVGSAALKLAMVAAgKADAYIEFGRLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260 270
....*....|....*....|....*....|...
gi 636775990 252 kvaadGPDFMCPGYIATGRGADYPTLERVARSI 284
Cdd:pfam00459 242 -----PFDLLAGRVIAANPKVLHELLAAALEEI 269
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
55-243 |
1.16e-26 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 105.27 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 55 HDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTG--DGEFQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAV 132
Cdd:PRK10757 37 NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEgeDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 133 YDPVADLMFSADL-ESAELNGNALASRAADNEKHATLITGYPvardFRVDGREAALAN-FGILVETFSTLRRPGSAALSI 210
Cdd:PRK10757 117 YDPMRNELFTATRgQGAQLNGYRLRGSTARDLDGTILATGFP----FKAKQHATTYINiVGKLFTECADFRRTGSAALDL 192
|
170 180 190
....*....|....*....|....*....|...
gi 636775990 211 AHVAAGWADAAAGFGVNAWDVAAATLILKNAGG 243
Cdd:PRK10757 193 AYVAAGRVDGFFEIGLKPWDFAAGELLVREAGG 225
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
23-257 |
1.61e-22 |
|
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: 93.52 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRMPLLEAFRSEMAVDYKADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQT--GDGEFQWYVD 100
Cdd:TIGR02067 1 LLAFAEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNeeGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 101 PIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLESAELNGNA-LASRAADNEKHATLITGYPVARDFR 179
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRrLRVSSCANLSDAVLFTTSPDLLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 180 VDG------REAALanfgilvetfstLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTlGKV 253
Cdd:TIGR02067 161 GNRpaferlRRAAR------------LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWD-GKP 227
|
....
gi 636775990 254 AADG 257
Cdd:TIGR02067 228 APDG 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
22-262 |
4.22e-58 |
|
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: 186.59 E-value: 4.22e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 22 RLAEIARGAALAVRMPLLEAFRS-EMAVDYKADlHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTG--DGEFQWY 98
Cdd:COG0483 2 PLLELALRAARAAGALILRRFRElDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEgrDSGYVWV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 99 VDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADL-ESAELNGNALASRAADNEKHATLITGYPVARD 177
Cdd:COG0483 81 IDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARgGGAFLNGRRLRVSARTDLEDALVATGFPYLRD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 178 frvdgREAALANFGILVETFSTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTLGKVAADG 257
Cdd:COG0483 161 -----DREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGS 235
|
....*
gi 636775990 258 PDFMC 262
Cdd:COG0483 236 GSLVA 240
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
25-268 |
5.20e-56 |
|
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: 180.59 E-value: 5.20e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 25 EIARGAALAVRMPLLEAFRSEMAVDYKADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGG---QTGDGEFQWYVDP 101
Cdd:cd01637 2 ELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGgsgNVSDGGRVWVIDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 102 IDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLES-AELNGNALASRAADNEKHATLITGYPVARDFRV 180
Cdd:cd01637 82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKgAFLNGKKLPLSKDTPLNDALLSTNASMLRSNRA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 181 DGREAalanfgiLVETFSTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTLGKVaadgPDF 260
Cdd:cd01637 162 AVLAS-------LVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPL----DTL 230
|
....*...
gi 636775990 261 MCPGYIAT 268
Cdd:cd01637 231 NRSGIIAA 238
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
23-244 |
3.01e-49 |
|
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: 163.48 E-value: 3.01e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRMPLLEAF-RSEMAVDYKADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTGDG--EFQWYV 99
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYeKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLtdEPTWII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 100 DPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADL-ESAELNGNALASRAADNEKHATLITGYPVARDF 178
Cdd:cd01639 81 DPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRgQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD 160
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 636775990 179 RVDgreAALANFGILVETFST-LRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGR 244
Cdd:cd01639 161 NFD---RYLNNFAKLLAKAVRgVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGL 224
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
38-249 |
7.11e-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: 136.70 E-value: 7.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 38 LLEAFRSEMAVDYKADLhDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQT-GDGEFQWYVDPIDGTANFARGIAFWC 116
Cdd:cd01643 15 ALADFGNSLSAETKADG-SLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIfPSSGWYWVIDPIDGTTNFARGIPIWA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 117 VSVAVVREGAVLAGAVYDPVADLMFSA-DLESAELNGNALASRAADNEKHATLITGypvaRDFRVDGREA---ALANFGI 192
Cdd:cd01643 94 ISIALLYRGEPVFGVIALPALNQTFVAfKGGGAFLNGKPLALHPPLQLPDCNVGFN----RSSRASARAVlrvILRRFPG 169
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 636775990 193 lvetfsTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLT 249
Cdd:cd01643 170 ------KIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILD 220
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
23-284 |
4.28e-36 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 130.16 E-value: 4.28e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRMPLLEAFRSEMAVDYK--ADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQ------TGDGE 94
Cdd:pfam00459 5 VLKVAVELAAKAGEILREAFSNKLTIEEKgkSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAkgdqteLTDDG 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 95 FQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSA-DLESAELNGNALASRAADNEKHATLITGYP 173
Cdd:pfam00459 85 PTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAaKGKGAFLNGQPLPVSRAPPLSEALLVTLFG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 174 V-ARDFRVDGREAALANFGILVETFstlRRPGSAALSIAHVAA-GWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTLG 251
Cdd:pfam00459 165 VsSRKDTSEASFLAKLLKLVRAPGV---RRVGSAALKLAMVAAgKADAYIEFGRLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260 270
....*....|....*....|....*....|...
gi 636775990 252 kvaadGPDFMCPGYIATGRGADYPTLERVARSI 284
Cdd:pfam00459 242 -----PFDLLAGRVIAANPKVLHELLAAALEEI 269
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
55-243 |
1.16e-26 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 105.27 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 55 HDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTG--DGEFQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAV 132
Cdd:PRK10757 37 NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEgeDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 133 YDPVADLMFSADL-ESAELNGNALASRAADNEKHATLITGYPvardFRVDGREAALAN-FGILVETFSTLRRPGSAALSI 210
Cdd:PRK10757 117 YDPMRNELFTATRgQGAQLNGYRLRGSTARDLDGTILATGFP----FKAKQHATTYINiVGKLFTECADFRRTGSAALDL 192
|
170 180 190
....*....|....*....|....*....|...
gi 636775990 211 AHVAAGWADAAAGFGVNAWDVAAATLILKNAGG 243
Cdd:PRK10757 193 AYVAAGRVDGFFEIGLKPWDFAAGELLVREAGG 225
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
17-259 |
2.43e-26 |
|
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: 103.87 E-value: 2.43e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 17 AALSGRLAEIARGAalavrmpLLEAFRSEMAVDYKADLhDIVTVHDRRAEAIIRAYILEHEPNSAIMGEE-GGQTGDGEF 95
Cdd:cd01641 2 LAFALELADAAGQI-------TLPYFRTRLQVETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEEfGNEGGDAGY 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 96 QWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLESAEL----NGNALASRAADNEKHATLITG 171
Cdd:cd01641 74 VWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFlngaGGRPLRVRACADLAEAVLSTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 172 YPvarDFRVDGREAAlanFGILVETfSTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRY-----E 246
Cdd:cd01641 154 DP---HFFTPGDRAA---FERLARA-VRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVItdwdgG 226
|
250
....*....|....*.
gi 636775990 247 PLTLGK---VAADGPD 259
Cdd:cd01641 227 PLTGGSgrvVAAGDAE 242
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
25-259 |
4.72e-26 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 103.62 E-value: 4.72e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 25 EIARGAALAVRMPLLEAFRSEMAVDYKADLhDIVTVHDRRAEAIIRAYILEHEPNSAIMGEE-----GGQTGDGEFQWYV 99
Cdd:PLN02553 12 EVAVDAAKAAGQIIRKGFYQTKHVEHKGQV-DLVTETDKACEDLIFNHLKQAFPSHKFIGEEttaasGGTELTDEPTWIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 100 DPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSA-DLESAELNGNALASRAADNEKHATLITGYPVARDf 178
Cdd:PLN02553 91 DPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAvKGKGAFLNGKPIKASSQSELGKALLATEVGTKRD- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 179 rvdgREAALANFGI---LVETFSTLRRPGSAALSIAHVAAGWADAAAGFGVNA-WDVAAATLILKNAGGR-YEP------ 247
Cdd:PLN02553 170 ----KATVDATTNRinaLLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAGGLvFDPsggpfd 245
|
250
....*....|..
gi 636775990 248 LTLGKVAADGPD 259
Cdd:PLN02553 246 IMSRRVAASNGH 257
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
5-244 |
5.27e-26 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 105.27 E-value: 5.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 5 PSSGSHIADPDSAAlsgRLAEIARGAALAVRMPLLEAFRSEMAVDYKAdLHDIVTVHDRRAEAIIRAYILEHEPNSAIMG 84
Cdd:PLN02737 64 PRVGAASTGPIPAE---ELLAVAELAAKTGAEVVMEAVNKPRNISYKG-LTDLVTDTDKASEAAILEVVRKNFPDHLILG 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 85 EEGGQTGD--GEFQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLM------FSADL-ESAELNGNAL 155
Cdd:PLN02737 140 EEGGVIGDssSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPMcwntrtFSASAgGGAFCNGQKI 219
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 156 ASRAADNEKHATLITGYPVARDfrvDGREAALANFGILVETFSTLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAAT 235
Cdd:PLN02737 220 HVSQTDKVERSLLVTGFGYEHD---DAWATNIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGV 296
|
....*....
gi 636775990 236 LILKNAGGR 244
Cdd:PLN02737 297 LIVEEAGGT 305
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
23-274 |
8.48e-26 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 102.55 E-value: 8.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAvrmpLLEAFRSEMAVDYKADlHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTGDGEFQ-----W 97
Cdd:COG1218 8 AIEIAREAGEA----ILEIYRADFEVEEKAD-DSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKswdrfW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 98 YVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSAD------LESAELNGNALASRAADNEKHATLItg 171
Cdd:COG1218 83 LVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAkgqgafKETGGGERQPIRVRDRPPAEPLRVV-- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 172 ypVARDFRVDGREAALANFGILvetfsTLRRPGSaALSIAHVaagwadaaagfgvnA---------------WDVAAATL 236
Cdd:COG1218 161 --ASRSHRDEETEALLARLGVA-----ELVSVGS-SLKFCLV--------------AegeadlyprlgptmeWDTAAGQA 218
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 636775990 237 ILKNAGGR-----YEPLTLGKvaadGPDFMCPGYIATGRGADY 274
Cdd:COG1218 219 ILEAAGGRvtdldGKPLRYNK----KEDLLNPGFIASGDHAAI 257
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
23-267 |
1.79e-23 |
|
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: 96.14 E-value: 1.79e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAvrmpLLEAFRSEMAVDYKADlHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTGD---GEFQWYV 99
Cdd:cd01638 5 LIRIAREAGDA----ILEVYRGGFTVERKED-GSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLrlgWDRFWLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 100 DPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLES-AELNGNALA-SRAADNEKHATLItgYPVARD 177
Cdd:cd01638 80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGgAYKNGRPGAvSLQARPPPLQPLR--VVASRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 178 FRVDGREAALANFGilvetFSTLRRPGSaALSIAHVAA-GWADAAAGFGVNAWDVAAATLILKNAGGR-----YEPLTLG 251
Cdd:cd01638 158 HPDEELEALLAALG-----VAEVVSIGS-SLKFCLVAEgEADIYPRLGPTMEWDTAAGDAVLRAAGGAvsdldGSPLTYN 231
|
250
....*....|....*.
gi 636775990 252 KvaadgPDFMCPGYIA 267
Cdd:cd01638 232 R-----EDFLNPDFIA 242
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
23-257 |
1.61e-22 |
|
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: 93.52 E-value: 1.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRMPLLEAFRSEMAVDYKADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQT--GDGEFQWYVD 100
Cdd:TIGR02067 1 LLAFAEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNeeGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 101 PIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLESAELNGNA-LASRAADNEKHATLITGYPVARDFR 179
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRrLRVSSCANLSDAVLFTTSPDLLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 180 VDG------REAALanfgilvetfstLRRPGSAALSIAHVAAGWADAAAGFGVNAWDVAAATLILKNAGGRYEPLTlGKV 253
Cdd:TIGR02067 161 GNRpaferlRRAAR------------LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWD-GKP 227
|
....
gi 636775990 254 AADG 257
Cdd:TIGR02067 228 APDG 231
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
23-269 |
2.82e-19 |
|
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: 84.81 E-value: 2.82e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVrmplLEAFRSEMAVDYKADlHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTGDGEFQ-----W 97
Cdd:TIGR01331 5 VIKIARAAGEEI----LPVYQKELAVAQKAD-NSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQtwqrfW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 98 YVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADLMFSADLESA---ELNGNALAS----RAADNEKHATLIT 170
Cdd:TIGR01331 80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAakrEGDGQALKApihvRPWPSGPLLVVIS 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 171 gypvaRDFRVDGREAALANFGILvetfstLRRPGSAALSIAHVAAGWADA-AAGFGVNAWDVAAATLILKNAGGR----- 244
Cdd:TIGR01331 160 -----RSHAEEKTTEYLANLGYD------LRTSGGSSLKFCLVAEGSADIyPRLGPTGEWDTAAGHAVLAAAGGAifdld 228
|
250 260
....*....|....*....|....*
gi 636775990 245 YEPLTLGKvaadGPDFMCPGYIATG 269
Cdd:TIGR01331 229 GSPLLYGK----RESFRNPNFVALG 249
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
23-244 |
8.66e-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: 83.90 E-value: 8.66e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRMPLLEAfRSEMAVDYKADLHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTgDGEFqWYVDPI 102
Cdd:cd01517 4 VAILAVRAAASLTLPVFRN-LGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-LGRF-WVLDPI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 103 DGTANFARGIAFwCVSVAVVREGAVLAGAVYDPVADLMFSA--DLESAELNGNA------------LASRAADNEKHATL 168
Cdd:cd01517 81 DGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNLPLDDGGggDLFSAVRGQGAwlrpldgsslqpLSVRQLTNAARASF 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 636775990 169 ITgyPVARDFRVDGREAALANFGILVET--FSTLRRPGSAALSIAHVAAGWADAAAGFGvNAWDVAAATLILKNAGGR 244
Cdd:cd01517 160 CE--SVESAHSSHRLQAAIKALGGTPQPvrLDSQAKYAAVARGAADFYLRLPLSMSYRE-KIWDHAAGVLIVEEAGGK 234
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
1-173 |
2.69e-18 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 82.85 E-value: 2.69e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 1 MQPKPSSGSHIADPDSAALSGRLAEIARGAALAVRMPLLEAFRSEMAVDYKADLHDiVTVHDRRAEAIIRAYILEHEPNS 80
Cdd:PLN02911 14 NSSRANVSMDAASALSDAVLDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKEDLSP-VTIADRAAEEAMRSIILENFPSH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 81 AIMGEEGGQT---GDGEFQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPV-ADLMFSADLESAELNGNALA 156
Cdd:PLN02911 93 AIFGEEHGLRcgeGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVlKERWVGVAGRATTLNGEEIS 172
|
170
....*....|....*..
gi 636775990 157 SRAADNEKHATLITGYP 173
Cdd:PLN02911 173 TRSCASLKDAYLYTTSP 189
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
23-244 |
3.60e-16 |
|
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: 74.74 E-value: 3.60e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 23 LAEIARGAALAVRmpllEAFRSEMAVDYKADLH--DIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGG-----QTGDGEF 95
Cdd:cd01636 4 LCRVAKEAGLAIL----KAFGRELSGKVKITKSdnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeevMGRRDEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 96 QWYVDPIDGTANFARGIAFWCVSVAVVRegavlagavydpvadlmfsadlesaelngnalasraadnekhaTLITGYPVA 175
Cdd:cd01636 80 TWVIDPIDGTKNFINGLPFVAVVIAVYV-------------------------------------------ILILAEPSH 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 636775990 176 RdfRVDGREAALANFGIlvetfSTLRRPGSAALSIAHVAAGWADA--AAGFGVNAWDVAAATLILKNAGGR 244
Cdd:cd01636 117 K--RVDEKKAELQLLAV-----YRIRIVGSAVAKMCLVALGLADIyyEPGGKRRAWDVAASAAIVREAGGI 180
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
62-244 |
1.78e-15 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 74.56 E-value: 1.78e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 62 DRRAEAIIRAYILEHEPNSAIMGEEGG--QTGDGEFQWYVDPIDGTANFARGIAFWCVSVAVVREGAVLAGAVYDPVADL 139
Cdd:PRK12676 47 DKVAEDIILEVLKPLGRCVNIISEELGeiVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGD 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 140 MFSADL-ESAELNGNAL-ASRAADNEKHATLITGYPvardfrvdgreaalANFGILVETFSTLRRP---GSAALSIAHVA 214
Cdd:PRK12676 127 FYEAIPgKGAYLNGKPIkVSKTSELNESAVSIYGYR--------------RGKERTVKLGRKVRRVrilGAIALELCYVA 192
|
170 180 190
....*....|....*....|....*....|..
gi 636775990 215 AGWADAAA--GFGVNAWDVAAATLILKNAGGR 244
Cdd:PRK12676 193 SGRLDAFVdvRNYLRVTDIAAGKLICEEAGGI 224
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
62-243 |
3.58e-12 |
|
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: 65.09 E-value: 3.58e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 62 DRRAEAIIRAyILEHEPNSAIMGEEGGQTGDG---EFQWYVDPIDGTANFARGIAFWCVSVAVVR--EGAVLAGAVYDP- 135
Cdd:cd01515 42 DKVAEDAAIE-ILKKLGSVNIVSEEIGVIDNGdepEYTVVLDPLDGTYNAINGIPFYSVSVAVFKidKSDPYYGYVYNLa 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 136 VADLMFSADLESAELNGNALASRAADNEKHATLITGYPVARDFRVDgreaalanfgILVETFSTLRRPGSAALSIAHVAA 215
Cdd:cd01515 121 TGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYIYGKNHDRTF----------KICRKVRRVRIFGSVALELCYVAS 190
|
170 180 190
....*....|....*....|....*....|
gi 636775990 216 GW--ADAAAGFGVNAWDVAAATLILKNAGG 243
Cdd:cd01515 191 GAldAFVDVRENLRLVDIAAGYLIAEEAGG 220
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
56-251 |
4.35e-10 |
|
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: 58.61 E-value: 4.35e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 56 DIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGG--QTGDGEFQWYVDPIDGTANFARGIAFWCVSVAVVREG-----AVL 128
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEESGeiRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRskvkaATL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 129 AGAVYDPVADLMFSADLESAELNGNALASRAADNEKHATLItgypvardfrVDGREAALANFGILVETFSTLRRPGSAAL 208
Cdd:cd01642 114 DNFVSGEGGLKVYSPPTRFSYISVPKLGPPLVPEVPSKIGI----------YEGSSRNPEKFLLLSRNGLKFRSLGSAAL 183
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 636775990 209 SIAHVAAGWAD--AAAGFGVNAWDVAAATLILKNAGGRYEPLTLG 251
Cdd:cd01642 184 ELAYTCEGSFVlfLDLRGKLRNFDVAAALGACKRLGLHGDPSNLL 228
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
46-144 |
5.62e-09 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 55.47 E-value: 5.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 636775990 46 MAVDYKADlHDIVTVHDRRAEAIIRAYILEHEPNSAIMGEEGGQTGDgEFQ-----WYVDPIDGTANFARGIAFWCVSVA 120
Cdd:PRK10931 26 LDVASKAD-DSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWE-VRQhwqryWLVDPLDGTKEFIKRNGEFTVNIA 103
|
90 100
....*....|....*....|....
gi 636775990 121 VVREGAVLAGAVYDPVADLMFSAD 144
Cdd:PRK10931 104 LIEQGKPVLGVVYAPVMNVMYSAA 127
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
86-135 |
1.47e-03 |
|
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; 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 plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.
Pssm-ID: 273558 [Multi-domain] Cd Length: 353 Bit Score: 39.85 E-value: 1.47e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 636775990 86 EGGQTGDgefQWYVDPIDGTANFARGIAFwCVSVAVVREGAVLAGAVYDP 135
Cdd:TIGR01330 125 EGGRKGR---HWVLDPIDGTKGFLRGDQY-AVCLALIENGKVVLGVIGCP 170
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
73-123 |
4.70e-03 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 38.56 E-value: 4.70e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 636775990 73 ILEHEPNSAIMGEEGG--QTGDG--EFQWYVDPIDGTANFARGIAFWCVSVAVVR 123
Cdd:PRK14076 56 SLEKFCSGILISEEIGfkKIGKNkpEYIFVLDPIDGTYNALKDIPIYSASIAIAK 110
|
|
| |
