|
Name |
Accession |
Description |
Interval |
E-value |
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
7-251 |
2.17e-86 |
|
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: 257.47 E-value: 2.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 7 LKDLVFNAGRKLLE-WREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPID 85
Cdd:COG0483 7 ALRAARAAGALILRrFRELDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDPID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 86 GTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNL----RGHTY 161
Cdd:COG0483 86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPylrdDREYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 162 KFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYI 241
Cdd:COG0483 166 AALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPAL 245
|
250
....*....|
gi 504063338 242 HERLLKIIQG 251
Cdd:COG0483 246 HDELLALLRE 255
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
4-235 |
4.96e-78 |
|
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: 235.29 E-value: 4.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 4 FEYLKDLVFNAGRKLLEWREEEFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY-WVID 82
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRvWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 83 PIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGN--LRGHT 160
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNAsmLRSNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504063338 161 YKFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAI 235
Cdd:cd01637 161 AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGI 235
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
7-253 |
1.29e-56 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 181.77 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 7 LKDLVFNAGRKLLEWREEEFSVNTKS--SKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY----WV 80
Cdd:pfam00459 9 AVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDdgptWI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 81 IDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKK---VIPHWNKDIESSMISLGNLR 157
Cdd:pfam00459 89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPlpvSRAPPLSEALLVTLFGVSSR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 158 GHTYK--FFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNK 232
Cdd:pfam00459 169 KDTSEasFLAKLLklVRAPGVRRVGSAALKLAMVAAGKADAYIEFgRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAG 248
|
250 260
....*....|....*....|..
gi 504063338 233 KAIYSNPY-IHERLLKIIQGVQ 253
Cdd:pfam00459 249 RVIAANPKvLHELLAAALEEII 270
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
80-251 |
1.09e-41 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 143.12 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 80 VIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISlgnLRGH 159
Cdd:PRK12676 85 VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVS---IYGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 160 TYKFFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISVKGN--SWDVAAGYIIVKEAGGIITDYSGNKATI-FNKKA 234
Cdd:PRK12676 162 RRGKERTVKlgRKVRRVRILGAIALELCYVASGRLDAFVDVRNYlrVTDIAAGKLICEEAGGIVTDEDGNELKLpLNVTE 241
|
170 180
....*....|....*....|..
gi 504063338 235 ----IYSNP-YIHERLLKIIQG 251
Cdd:PRK12676 242 rtnlIAANGeELHKKILELLEG 263
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
13-239 |
6.11e-39 |
|
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: 135.66 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 13 NAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED---GFDKKPSTKGYWVIDPIDGTVN 89
Cdd:TIGR01331 11 AAGEEILPVYQKELAVAQKADN-SPVTEADRAAHRFILEGLRALTPDIPVLSEEDasiPLTPRQTWQRFWLVDPLDGTKE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 90 FAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYE-----NGKKVIPHWNKDIESSMISLGnlRGH-TYKF 163
Cdd:TIGR01331 90 FINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegdgqALKAPIHVRPWPSGPLLVVIS--RSHaEEKT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338 164 FRALENNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATiFNKKAIYSNP 239
Cdd:TIGR01331 168 TEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLgPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL-YGKRESFRNP 243
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
7-251 |
2.17e-86 |
|
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: 257.47 E-value: 2.17e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 7 LKDLVFNAGRKLLE-WREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPID 85
Cdd:COG0483 7 ALRAARAAGALILRrFRELDLEVETKGD-GDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVWVIDPID 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 86 GTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNL----RGHTY 161
Cdd:COG0483 86 GTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPylrdDREYL 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 162 KFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYI 241
Cdd:COG0483 166 AALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGSLVAANPAL 245
|
250
....*....|
gi 504063338 242 HERLLKIIQG 251
Cdd:COG0483 246 HDELLALLRE 255
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
4-235 |
4.96e-78 |
|
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: 235.29 E-value: 4.96e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 4 FEYLKDLVFNAGRKLLEWREEEFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY-WVID 82
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRvWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 83 PIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGN--LRGHT 160
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNAsmLRSNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 504063338 161 YKFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAI 235
Cdd:cd01637 161 AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGI 235
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-232 |
3.58e-71 |
|
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: 218.18 E-value: 3.58e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 4 FEYLKDLVFNAGRKLLE-WREEEFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVID 82
Cdd:cd01639 2 LNIAIEAARKAGEILLEaYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 83 PIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMIS--LGNLRGHT 160
Cdd:cd01639 82 PLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVAtgFPYDRGDN 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338 161 YK-----FFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNK 232
Cdd:cd01639 162 FDrylnnFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSG 238
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
7-253 |
1.29e-56 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 181.77 E-value: 1.29e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 7 LKDLVFNAGRKLLEWREEEFSVNTKS--SKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGY----WV 80
Cdd:pfam00459 9 AVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDdgptWI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 81 IDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKK---VIPHWNKDIESSMISLGNLR 157
Cdd:pfam00459 89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPlpvSRAPPLSEALLVTLFGVSSR 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 158 GHTYK--FFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNK 232
Cdd:pfam00459 169 KDTSEasFLAKLLklVRAPGVRRVGSAALKLAMVAAGKADAYIEFgRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAG 248
|
250 260
....*....|....*....|..
gi 504063338 233 KAIYSNPY-IHERLLKIIQGVQ 253
Cdd:pfam00459 249 RVIAANPKvLHELLAAALEEII 270
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
4-220 |
1.33e-52 |
|
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: 170.59 E-value: 1.33e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 4 FEYLKDLVFNAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKkPSTKGYWVIDP 83
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAETKADG-SLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIF-PSSGWYWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 84 IDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSmiSLGNLRGHTYKF 163
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDC--NVGFNRSSRASA 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504063338 164 FRALENNVMR----VRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIIT 220
Cdd:cd01643 157 RAVLRVILRRfpgkIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWT 217
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
5-224 |
7.32e-45 |
|
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: 150.84 E-value: 7.32e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 5 EYLKDLVFNAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKG-YWVIDP 83
Cdd:cd01638 3 ELLIRIAREAGDAILEVYRGGFTVERKEDG-SPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDrFWLVDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 84 IDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHW---NKDIESSMISLGnlRGHT 160
Cdd:cd01638 82 LDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLqarPPPLQPLRVVAS--RSHP 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338 161 YKFFRALeNNVMRVRLLGTAA--LQIAYVGTGNLDAFISVKG-NSWDVAAGYIIVKEAGGIITDYSG 224
Cdd:cd01638 160 DEELEAL-LAALGVAEVVSIGssLKFCLVAEGEADIYPRLGPtMEWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
52-249 |
1.73e-42 |
|
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: 145.21 E-value: 1.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 52 ELTKKFPEIGFLAEEDGFDKKPSTKGYWVI-DPIDGTVNFAKGIPNFCISAA--YVEDDEPLYGVIYAPVMNQLIYAEKG 128
Cdd:cd01515 51 EILKKLGSVNIVSEEIGVIDNGDEPEYTVVlDPLDGTYNAINGIPFYSVSVAvfKIDKSDPYYGYVYNLATGDLYYAIKG 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 129 KGVYENGKKVIPHWNKDIESSMISL-GNLRGHTYKFfrALENNVMRVRLLGTAALQIAYVGTGNLDAFISVKGNS--WDV 205
Cdd:cd01515 131 KGAYLNGKRIKVSDFSSLKSISVSYyIYGKNHDRTF--KICRKVRRVRIFGSVALELCYVASGALDAFVDVRENLrlVDI 208
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504063338 206 AAGYIIVKEAGGIITDYSGNKATI-FNKKA----IYSNPYIHERLLKII 249
Cdd:cd01515 209 AAGYLIAEEAGGIVTDENGKELKLkLNVTErvniIAANSELHKKLLELL 257
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
80-251 |
1.09e-41 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 143.12 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 80 VIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISlgnLRGH 159
Cdd:PRK12676 85 VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVS---IYGY 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 160 TYKFFRALE--NNVMRVRLLGTAALQIAYVGTGNLDAFISVKGN--SWDVAAGYIIVKEAGGIITDYSGNKATI-FNKKA 234
Cdd:PRK12676 162 RRGKERTVKlgRKVRRVRILGAIALELCYVASGRLDAFVDVRNYlrVTDIAAGKLICEEAGGIVTDEDGNELKLpLNVTE 241
|
170 180
....*....|....*....|..
gi 504063338 235 ----IYSNP-YIHERLLKIIQG 251
Cdd:PRK12676 242 rtnlIAANGeELHKKILELLEG 263
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
36-252 |
1.26e-39 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 138.28 E-value: 1.26e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEED--GFDKKPST-KGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYG 112
Cdd:PLN02553 42 DLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaASGGTELTdEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 113 VIYAPVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMIS--LGNLRGH-----TYKFFRALENNVMRVRLLGTAALQIA 185
Cdd:PLN02553 122 VVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLAteVGTKRDKatvdaTTNRINALLYKVRSLRMSGSCALNLC 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 504063338 186 YVGTGNLDAFISVK-GNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYIHERLLKIIQGV 252
Cdd:PLN02553 202 GVACGRLDIFYEIGfGGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRVAASNGHLKDAFVEALRQT 269
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
2-247 |
2.10e-39 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 137.21 E-value: 2.10e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 2 KEFEYLKDLVFNAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED---GFDKKPSTKGY 78
Cdd:COG1218 3 ALLEAAIEIAREAGEAILEIYRADFEVEEKADD-SPVTEADLAAHAIILAGLAALTPDIPVLSEESaaiPYEERKSWDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 79 WVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGK-------KVIPHWNKD----IE 147
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGggerqpiRVRDRPPAEplrvVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 148 SsmislgnlRGHTYKFFRALENNvmrvrlLGTA-------ALQIAYVGTGNLDAFISVKGNS-WDVAAGYIIVKEAGGII 219
Cdd:COG1218 162 S--------RSHRDEETEALLAR------LGVAelvsvgsSLKFCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRV 227
|
250 260 270
....*....|....*....|....*....|...
gi 504063338 220 TDYSGNKATiFNKKAIYSNPYI-----HERLLK 247
Cdd:COG1218 228 TDLDGKPLR-YNKKEDLLNPGFiasgdHAAILA 259
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
13-239 |
6.11e-39 |
|
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: 135.66 E-value: 6.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 13 NAGRKLLEWREEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED---GFDKKPSTKGYWVIDPIDGTVN 89
Cdd:TIGR01331 11 AAGEEILPVYQKELAVAQKADN-SPVTEADRAAHRFILEGLRALTPDIPVLSEEDasiPLTPRQTWQRFWLVDPLDGTKE 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 90 FAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYE-----NGKKVIPHWNKDIESSMISLGnlRGH-TYKF 163
Cdd:TIGR01331 90 FINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKRegdgqALKAPIHVRPWPSGPLLVVIS--RSHaEEKT 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 504063338 164 FRALENNVMRVRLLGTAALQIAYVGTGNLDAFISV-KGNSWDVAAGYIIVKEAGGIITDYSGNKATiFNKKAIYSNP 239
Cdd:TIGR01331 168 TEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLgPTGEWDTAAGHAVLAAAGGAIFDLDGSPLL-YGKRESFRNP 243
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
25-250 |
3.49e-35 |
|
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: 126.66 E-value: 3.49e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 25 EFSVNTKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGfdkkpSTKG-YWVIDPIDGTVNFAKGIPnFCISAAY 103
Cdd:cd01517 25 AGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS-----AALGrFWVLDPIDGTKGFLRGDQ-FAVALAL 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 104 VEDDEPLYGVIYAPVMNQ-------LIYAEKGKGVYENG--------KKVIPHWNKDIESSMISLGnlRGHTYKFFRALE 168
Cdd:cd01517 99 IEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWLRPldgsslqpLSVRQLTNAARASFCESVE--SAHSSHRLQAAI 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 169 NNVMRVRLLGTAALQIAY--VGTGNLDAFI------SVKGNSWDVAAGYIIVKEAGGIITDYSGN------KATIFNKKA 234
Cdd:cd01517 177 KALGGTPQPVRLDSQAKYaaVARGAADFYLrlplsmSYREKIWDHAAGVLIVEEAGGKVTDADGKpldfgkGRKLLNNGG 256
|
250
....*....|....*..
gi 504063338 235 -IYSNPYIHERLLKIIQ 250
Cdd:cd01517 257 lIAAPGEIHEQVLEALR 273
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
36-250 |
4.54e-33 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 121.07 E-value: 4.54e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIY 115
Cdd:PRK10757 38 DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVY 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APVMNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLG---NLRGHTYKFFRALENNVMRV---RLLGTAALQIAYVGT 189
Cdd:PRK10757 118 DPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGfpfKAKQHATTYINIVGKLFTECadfRRTGSAALDLAYVAA 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 504063338 190 GNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYIHERLLKIIQ 250
Cdd:PRK10757 198 GRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTGNIVAGNPRVVKAMLANMR 258
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
36-249 |
1.33e-31 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 119.13 E-value: 1.33e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIY 115
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVV 190
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APV------MNQLIYAEKGKGVYENGKKVIPHWNKDIESSMISLGNLRGH------TYKFFRALENNVMRVRLLGTAALQ 183
Cdd:PLN02737 191 EFVggpmcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHddawatNIELFKEFTDVSRGVRRLGAAAVD 270
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 504063338 184 IAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSNPYIHERLLKII 249
Cdd:PLN02737 271 MCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLVSNGVLHPKLLDRI 336
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-221 |
3.11e-30 |
|
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: 111.33 E-value: 3.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 5 EYLKDLVFNAGRKLLEWREEEFSVNTKSSKF--DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKG---YW 79
Cdd:cd01636 2 EELCRVAKEAGLAILKAFGRELSGKVKITKSdnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRdeyTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 80 VIDPIDGTVNFAKGIPNFCISAAyveddeplygviyapVMNQLIYAEKGKgvyengkkviphwnkdiessmislgnlRGH 159
Cdd:cd01636 82 VIDPIDGTKNFINGLPFVAVVIA---------------VYVILILAEPSH---------------------------KRV 119
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 504063338 160 TYKFFRALENNVMRVRLLGTAALQIAYVGTGNLDAFISV--KGNSWDVAAGYIIVKEAGGIITD 221
Cdd:cd01636 120 DEKKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPggKRRAWDVAASAAIVREAGGIMTD 183
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
52-249 |
1.78e-28 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 112.90 E-value: 1.78e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 52 ELTKKFPEIGFLAEEDGFDK--KPSTKGYWVIDPIDGTVNFAKGIPNFCISAAY----VEDDEPLYGVIYAPVMNQL--- 122
Cdd:PRK14076 55 NSLEKFCSGILISEEIGFKKigKNKPEYIFVLDPIDGTYNALKDIPIYSASIAIakidGFDKKIKEFIGKNLTINDLevg 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 123 ----------IYAEKGKGVYE--NGKKVIPHWNKDIESSMISLG----NLRGHTYKFFRalENNVMRVRLLGTAALQIAY 186
Cdd:PRK14076 135 vvkniatgdtYYAEKGEGAYLlkKGEKKKIEISNISNLKDASIGlfayGLSLDTLKFIK--DRKVRRIRLFGSIALEMCY 212
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 187 VGTGNLDAFISVKGNS--WDVAAGYIIVKEAGGIITDYSG----NKATIFNKKA-IYSNPYIHERLLKII 249
Cdd:PRK14076 213 VASGALDAFINVNETTrlCDIAAGYVICKEAGGIITNKNGkplnMKLDINEKTSvICSNEILHKKLVGIF 282
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
55-250 |
2.14e-27 |
|
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: 105.46 E-value: 2.14e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 55 KKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYEN 134
Cdd:TIGR02067 53 AFFPDHGILGEEFGHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLG 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 135 GKKVIPHWNKDIESSMISLGNLR----GHTYKFFRALENNVmRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYI 210
Cdd:TIGR02067 133 GRRLRVSSCANLSDAVLFTTSPDllddPGNRPAFERLRRAA-RLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIP 211
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 504063338 211 IVKEAGGIITDYSGnKATIFNKKAIYS-NPYIHERLLKIIQ 250
Cdd:TIGR02067 212 VIEEAGGCFTDWDG-KPAPDGGGAVAAgNAMLHDEALEILN 251
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
14-246 |
2.94e-27 |
|
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: 105.03 E-value: 2.94e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 14 AGRKLLEWREEEFSVNTKSSkFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDkkPSTKGY-WVIDPIDGTVNFAK 92
Cdd:cd01641 12 AGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNE--GGDAGYvWVLDPIDGTKSFIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 93 GIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGVYENGKKVIPHWNK---DIESSMISLGN---LRGHTYKFFRA 166
Cdd:cd01641 89 GLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVRacaDLAEAVLSTTDphfFTPGDRAAFER 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 167 LENNVMRVRlLGTAALQIAYVGTGNLDAFISVKGNSWDVAAGYIIVKEAGGIITDYSGNKATIFNKKAIYSN-PYIHERL 245
Cdd:cd01641 169 LARAVRLTR-YGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTGGSGRVVAAGdAELHEAL 247
|
.
gi 504063338 246 L 246
Cdd:cd01641 248 L 248
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
38-224 |
5.09e-16 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 75.11 E-value: 5.09e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 38 VTSLDFRVQDFLYNELTKKFPEIGFLAEED--GFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIY 115
Cdd:PRK10931 37 VTAADIAAHTVIKDGLRTLTPDIPVLSEEDppAWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVY 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APVMNQLIYAEKGKG-VYENGKK-------------VI--PHWNKDIESSMISLGNLR----GHTYKFFRALEnnvmrvr 175
Cdd:PRK10931 117 APVMNVMYSAAEGKAwKEECGVRkqiqvrdarpplvVIsrSHADAELKEYLQQLGEHQttsiGSSLKFCLVAE------- 189
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 504063338 176 llGTAALQIAYVGTgnldafisvkgNSWDVAAGYIIVKEAGGIITDYSG 224
Cdd:PRK10931 190 --GQAQLYPRFGPT-----------NIWDTAAGHAVAIAAGAHVHDWQG 225
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
53-252 |
3.28e-15 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 73.60 E-value: 3.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 53 LTKKFPEIGFLAEEDGFDKKPSTKGY-WVIDPIDGTVNFAKGIPNFCISAAYVEDDEPLYGVIYAPVMNQLIYAEKGKGV 131
Cdd:PLN02911 85 ILENFPSHAIFGEEHGLRCGEGSSDYvWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRAT 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 132 YENGKKVIPHWNKDIESSMI---SLGNLRGHTYKFFRALENNVmRVRLLGTAALQIAYVGTGNLDAFISVKGNSWDVAAG 208
Cdd:PLN02911 165 TLNGEEISTRSCASLKDAYLyttSPHMFSGDAEDAFARVRDKV-KVPLYGCDCYAYGLLASGHVDLVVESGLKPYDYLAL 243
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 504063338 209 YIIVKEAGGIITDYSGNK----------ATIFNKKAIySNPYIHERLLKIIQGV 252
Cdd:PLN02911 244 VPVVEGAGGVITDWKGRKlrwepspgslATSFNVVAA-GDARLHKQALDILEWQ 296
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
30-226 |
1.02e-12 |
|
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.
Pssm-ID: 238818 [Multi-domain] Cd Length: 293 Bit Score: 66.19 E-value: 1.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 30 TKSSKFDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED-------------GFDK--------------KPSTKGYWvID 82
Cdd:cd01640 34 TKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDnefenqedesrdvDLDEeileescpspskdlPEEDLGVW-VD 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 83 PIDGTVNFAKGIPNFC-ISAAYVEDDEPLYGVIYAP----------VMNQLIYAEKGKGVY-------ENGKKVIPHWnk 144
Cdd:cd01640 113 PLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQPfyektagagaWLGRTIWGLSGLGAHssdfkerEDAGKIIVST-- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 145 dIESSMISLgnlrgHTYKFFRaLENNVMRVRLLGTAALQIAyvgTGNLDAFISVKGNS--WDVAAGYIIVKEAGGIITDY 222
Cdd:cd01640 191 -SHSHSVKE-----VQLITAG-NKDEVLRAGGAGYKVLQVL---EGLADAYVHSTGGIkkWDICAPEAILRALGGDMTDL 260
|
....
gi 504063338 223 SGNK 226
Cdd:cd01640 261 HGEP 264
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
36-216 |
1.66e-11 |
|
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: 62.47 E-value: 1.66e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 36 DLVTSLDFRVQDFLYNELTKKFPEIGFLAEEDGFDKKPSTKGYWVIDPIDGTVNFAKGIPNFCISAAYVEDDEPlygvIY 115
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSK----VK 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 116 APVMNQLIYAEKGKGVY-ENGKKVIPHWNKDIESSMISLGNLRGHTYK------FFRALENNVMRVRLLGTAALQIAYVG 188
Cdd:cd01642 110 AATLDNFVSGEGGLKVYsPPTRFSYISVPKLGPPLVPEVPSKIGIYEGssrnpeKFLLLSRNGLKFRSLGSAALELAYTC 189
|
170 180 190
....*....|....*....|....*....|
gi 504063338 189 TGNLDAFISVKGN--SWDVAAGYIIVKEAG 216
Cdd:cd01642 190 EGSFVLFLDLRGKlrNFDVAAALGACKRLG 219
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
23-224 |
1.09e-10 |
|
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: 60.65 E-value: 1.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 23 EEEFSVNTKSSKfDLVTSLDFRVQDFLYNELTKKFPEIGFLAEED----------------------------GFDKKPS 74
Cdd:TIGR01330 30 HKDSTVITKDDK-SPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDssglseadftlgrvnelvnetlvyaknyKKDDQFP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 75 TKG--------------------YWVIDPIDGTVNFAKGiPNFCISAAYVEDDEPLYGVIYAPVM--------------- 119
Cdd:TIGR01330 109 LKSledvlqiidfgnyeggrkgrHWVLDPIDGTKGFLRG-DQYAVCLALIENGKVVLGVIGCPNLplssygaqnlkgses 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 504063338 120 -NQLIYAEKGKGVY--------ENGKKVIPHWNKDIESSMISLGNLRGHTYKFFRALENNVMRVRLLGT---AALQIAYV 187
Cdd:TIGR01330 188 kGCIFRAVRGSGAFmyslssdaESPTKVHVSSVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLrldSQAKYAAL 267
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 504063338 188 GTGNLDAFI------SVKGNSWDVAAGYIIVKEAGGIITDYSG 224
Cdd:TIGR01330 268 ARGDADVYLrlpiklSYQEKIWDHAAGNVIVEEAGGIVTDAMG 310
|
|
|