|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
4-242 |
9.86e-91 |
|
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: 268.41 E-value: 9.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 4 YDYAKSLVLEAGNNVRKWMVEDLAIEEKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEGVVWVID 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 84 PIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWLTKPI 163
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1689986244 164 LsSILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPNSILMG 242
Cdd:cd01637 161 A-AVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
1-252 |
1.36e-82 |
|
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: 248.22 E-value: 1.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 1 MHLYDYAKSLVLEAGNNVRKWMVE-DLAIEEKSnPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhGHDIESTEGVV 79
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES-GASEGRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 80 WVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWL 159
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 160 TKPI-LSSILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPNs 238
Cdd:COG0483 159 RDDReYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS- 237
|
250
....*....|....
gi 1689986244 239 ILMGNAQVHEEIRR 252
Cdd:COG0483 238 LVAANPALHDELLA 251
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
3-253 |
4.15e-64 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 201.80 E-value: 4.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 3 LYDYAKSLVLEAGNNVRKWMVEDLAIEEKS--NPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhGHDIESTE---- 76
Cdd:pfam00459 5 VLKVAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEG-GAKGDQTEltdd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 77 GVVWVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIG--- 153
Cdd:pfam00459 84 GPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVtlf 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 154 ---MNPNWLTKPILSSILqPIISDsRSARAYGSAALEIVYVATGQLAAYLT-PRLQPWDYAGGMIILNEVGGVATNFAGE 229
Cdd:pfam00459 164 gvsSRKDTSEASFLAKLL-KLVRA-PGVRRVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|....
gi 1689986244 230 PLSITAPNSILMGNAQVHEEIRRD 253
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLAAA 265
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
13-246 |
1.72e-43 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 148.80 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 13 EAGNNVRKWMVEDLAIE-EKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEgVVWVIDPIDGTLNF 91
Cdd:PRK10757 14 KAGNLIAKNYETPDAVEaSQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQD-VQWVIDPLDGTTNF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 92 IHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAyinqnaipQLEGTQVResiiGMNPNWLTKPILSS----- 166
Cdd:PRK10757 93 IKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGA--------QLNGYRLR----GSTARDLDGTILATgfpfk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 167 ----------ILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAP 236
Cdd:PRK10757 161 akqhattyinIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250
....*....|
gi 1689986244 237 NsILMGNAQV 246
Cdd:PRK10757 241 N-IVAGNPRV 249
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
10-243 |
2.64e-28 |
|
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: 108.69 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 10 LVLEAGNNVRKWMVEDLAIEEKSNpNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTE--GVVWVIDPIDG 87
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAD-NSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQtwQRFWLVDPLDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 88 TLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVResiigmnpNWLTKPILSSI 167
Cdd:TIGR01331 87 TKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVR--------PWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 168 lqpiisdSRSARA----------------YGSAALEIVYVATGQLAAYltPRLQP---WDYAGGMIILNEVGGVATNFAG 228
Cdd:TIGR01331 159 -------SRSHAEektteylanlgydlrtSGGSSLKFCLVAEGSADIY--PRLGPtgeWDTAAGHAVLAAAGGAIFDLDG 229
|
250
....*....|....*
gi 1689986244 229 EPLSITAPNSILMGN 243
Cdd:TIGR01331 230 SPLLYGKRESFRNPN 244
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
4-242 |
9.86e-91 |
|
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: 268.41 E-value: 9.86e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 4 YDYAKSLVLEAGNNVRKWMVEDLAIEEKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEGVVWVID 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 84 PIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWLTKPI 163
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSNR 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1689986244 164 LsSILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPNSILMG 242
Cdd:cd01637 161 A-AVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
1-252 |
1.36e-82 |
|
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: 248.22 E-value: 1.36e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 1 MHLYDYAKSLVLEAGNNVRKWMVE-DLAIEEKSnPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhGHDIESTEGVV 79
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEES-GASEGRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 80 WVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWL 159
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 160 TKPI-LSSILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPNs 238
Cdd:COG0483 159 RDDReYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS- 237
|
250
....*....|....
gi 1689986244 239 ILMGNAQVHEEIRR 252
Cdd:COG0483 238 LVAANPALHDELLA 251
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
3-243 |
9.45e-68 |
|
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: 210.09 E-value: 9.45e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 3 LYDYAKSLVLEAGNNVRK-WMVEDLAIEEKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhGHDIESTEGVVWV 81
Cdd:cd01639 1 LLNIAIEAARKAGEILLEaYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES-GAAGGLTDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 82 IDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWLTK 161
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 162 PI----LSSILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPN 237
Cdd:cd01639 160 DNfdryLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGN 239
|
....*.
gi 1689986244 238 sILMGN 243
Cdd:cd01639 240 -ILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
3-253 |
4.15e-64 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 201.80 E-value: 4.15e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 3 LYDYAKSLVLEAGNNVRKWMVEDLAIEEKS--NPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhGHDIESTE---- 76
Cdd:pfam00459 5 VLKVAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEG-GAKGDQTEltdd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 77 GVVWVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIG--- 153
Cdd:pfam00459 84 GPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVtlf 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 154 ---MNPNWLTKPILSSILqPIISDsRSARAYGSAALEIVYVATGQLAAYLT-PRLQPWDYAGGMIILNEVGGVATNFAGE 229
Cdd:pfam00459 164 gvsSRKDTSEASFLAKLL-KLVRA-PGVRRVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|....
gi 1689986244 230 PLSITAPNSILMGNAQVHEEIRRD 253
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLAAA 265
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-243 |
6.31e-49 |
|
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: 161.73 E-value: 6.31e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 5 DYAKSLVLEAGNNVRKWMVEDLAIEEKSnPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGhdIESTEGVVWVIDP 84
Cdd:cd01643 2 SLAEAIAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGG--IFPSSGWYWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 85 IDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWltkPIL 164
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSS---RAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 165 SSILQPIISDSR--SARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPNSILMG 242
Cdd:cd01643 156 ARAVLRVILRRFpgKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYLSAG 235
|
.
gi 1689986244 243 N 243
Cdd:cd01643 236 F 236
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
13-246 |
1.72e-43 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 148.80 E-value: 1.72e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 13 EAGNNVRKWMVEDLAIE-EKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEgVVWVIDPIDGTLNF 91
Cdd:PRK10757 14 KAGNLIAKNYETPDAVEaSQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQD-VQWVIDPLDGTTNF 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 92 IHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAyinqnaipQLEGTQVResiiGMNPNWLTKPILSS----- 166
Cdd:PRK10757 93 IKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGA--------QLNGYRLR----GSTARDLDGTILATgfpfk 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 167 ----------ILQPIISDSRSARAYGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAP 236
Cdd:PRK10757 161 akqhattyinIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250
....*....|
gi 1689986244 237 NsILMGNAQV 246
Cdd:PRK10757 241 N-IVAGNPRV 249
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
2-232 |
2.45e-36 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 129.90 E-value: 2.45e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 2 HLYDYAKSLVLEAGNNVRKWMVEDLAIEEKSnPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGH--GHDIESTEGVV 79
Cdd:COG1218 3 ALLEAAIEIAREAGEAILEIYRADFEVEEKA-DDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAaiPYEERKSWDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 80 WVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYinqnaipQLEGTQVRESI---IGMNP 156
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAF-------KETGGGERQPIrvrDRPPA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 157 NWLTkpILSS------ILQPIISDSRSA--RAYGSaALEIVYVATGQLAAYltPRLQP---WDYAGGMIILNEVGGVATN 225
Cdd:COG1218 155 EPLR--VVASrshrdeETEALLARLGVAelVSVGS-SLKFCLVAEGEADLY--PRLGPtmeWDTAAGQAILEAAGGRVTD 229
|
....*..
gi 1689986244 226 FAGEPLS 232
Cdd:COG1218 230 LDGKPLR 236
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
36-250 |
1.10e-35 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 130.69 E-value: 1.10e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 36 DLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhGHDIESTEGVVWVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFV 115
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEG-GVIGDSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATV 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 116 YDVM------ADLLYHAKVGHGAYINQNAIPQLEGTQVRESII------GMNPNWLTkpilSSILQPIISD-SRSARAYG 182
Cdd:PLN02737 190 VEFVggpmcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLvtgfgyEHDDAWAT----NIELFKEFTDvSRGVRRLG 265
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1689986244 183 SAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITaPNSILMGNAQVHEEI 250
Cdd:PLN02737 266 AAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVF-DRSVLVSNGVLHPKL 332
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
41-250 |
1.49e-34 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 125.40 E-value: 1.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 41 VDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEGVVwVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMA 120
Cdd:PRK12676 46 IDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTV-VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLAT 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 121 DLLYHAKVGHGAYINQNAIPQLEGTQVRE---SIIGMNPNwltkpilSSILQPIISDSRSARAYGSAALEIVYVATGQLA 197
Cdd:PRK12676 125 GDFYEAIPGKGAYLNGKPIKVSKTSELNEsavSIYGYRRG-------KERTVKLGRKVRRVRILGAIALELCYVASGRLD 197
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 198 AYLTPR--LQPWDYAGGMIILNEVGGVATNFAGE----PLSITAPNSILMGNAQ-VHEEI 250
Cdd:PRK12676 198 AFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNelklPLNVTERTNLIAANGEeLHKKI 257
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
3-237 |
2.85e-34 |
|
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: 123.88 E-value: 2.85e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 3 LYDYAKSLVLEAGNNVRKWMVEDLAIEEKSnPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEGVVWVI 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDRFWLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 83 DPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINqNAIPQLEGTQVRESIIGMN------- 155
Cdd:cd01638 80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKN-GRPGAVSLQARPPPLQPLRvvasrsh 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 156 PNWLTKPILSSILQPiisDSRSArayGSaALEIVYVATGQLAAYltPRLQP---WDYAGGMIILNEVGGVATNFAGEPLS 232
Cdd:cd01638 159 PDEELEALLAALGVA---EVVSI---GS-SLKFCLVAEGEADIY--PRLGPtmeWDTAAGDAVLRAAGGAVSDLDGSPLT 229
|
....*
gi 1689986244 233 ITAPN 237
Cdd:cd01638 230 YNRED 234
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-244 |
2.41e-33 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 122.49 E-value: 2.41e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 5 DYAKSlvleAGNNVRKWMVEDLAIEEKsNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHD--IESTEGVVWVI 82
Cdd:PLN02553 16 DAAKA----AGQIIRKGFYQTKHVEHK-GQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASggTELTDEPTWIV 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 83 DPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESI----IGMNPNW 158
Cdd:PLN02553 91 DPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALlateVGTKRDK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 159 LTKPILSSILQPIISDSRSARAYGSAALEIVYVATGQLAA-YLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITApN 237
Cdd:PLN02553 171 ATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIfYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMS-R 249
|
....*..
gi 1689986244 238 SILMGNA 244
Cdd:PLN02553 250 RVAASNG 256
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
30-250 |
1.45e-32 |
|
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: 120.49 E-value: 1.45e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 30 EKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGhghdiESTEGVVWVIDPIDGTLNFIhQGENFAISVGIFKDGK 109
Cdd:cd01517 30 WKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEED-----SAALGRFWVLDPIDGTKGFL-RGDQFAVALALIEDGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 110 PYAGFVYDVMADL-------LYHAKVGHGAYINQNAIPQLEGTQVREsiigmnpnwLTKPILSSILQPIISDS------- 175
Cdd:cd01517 104 VVLGVIGCPNLPLddggggdLFSAVRGQGAWLRPLDGSSLQPLSVRQ---------LTNAARASFCESVESAHsshrlqa 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 176 --------RSARAYGSAAlEIVYVATGQLAAYL------TPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITAPNS--- 238
Cdd:cd01517 175 aikalggtPQPVRLDSQA-KYAAVARGAADFYLrlplsmSYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKlln 253
|
250
....*....|....*
gi 1689986244 239 ---ILMGNAQVHEEI 250
Cdd:cd01517 254 nggLIAAPGEIHEQV 268
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-251 |
1.65e-32 |
|
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: 119.67 E-value: 1.65e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 5 DYAKSLVLEAGNNVRKWMVEDLAIEEKSNpNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHdiESTEGVVWVIDP 84
Cdd:cd01641 3 AFALELADAAGQITLPYFRTRLQVETKAD-FSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNE--GGDAGYVWVLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 85 IDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQ--------NAIPQLEgtqvRESIIGMNP 156
Cdd:cd01641 80 IDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGaggrplrvRACADLA----EAVLSTTDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 157 NWLTkPILSSILQPIISDSRSARAYGSA---ALeivyVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSI 233
Cdd:cd01641 156 HFFT-PGDRAAFERLARAVRLTRYGGDCyayAL----VASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTG 230
|
250
....*....|....*...
gi 1689986244 234 TAPNSILMGNAQVHEEIR 251
Cdd:cd01641 231 GSGRVVAAGDAELHEALL 248
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
41-250 |
1.66e-32 |
|
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: 119.79 E-value: 1.66e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 41 VDKAIEQFIVQQIQESYPHhRIIGEEGHGHDIESTEGVVWVIDPIDGTLNFIHQGENFAISVGIFKDGK--PYAGFVYDV 118
Cdd:cd01515 41 IDKVAEDAAIEILKKLGSV-NIVSEEIGVIDNGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNL 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 119 MADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIGMNPNWLTKPILSSILQPIisdsRSARAYGSAALEIVYVATGQLAA 198
Cdd:cd01515 120 ATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYIYGKNHDRTFKICRKV----RRVRIFGSVALELCYVASGALDA 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 1689986244 199 YLTPR--LQPWDYAGGMIILNEVGGVATNFAGEPL----SITAPNSILMGNAQVHEEI 250
Cdd:cd01515 196 FVDVRenLRLVDIAAGYLIAEEAGGIVTDENGKELklklNVTERVNIIAANSELHKKL 253
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
10-243 |
2.64e-28 |
|
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: 108.69 E-value: 2.64e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 10 LVLEAGNNVRKWMVEDLAIEEKSNpNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTE--GVVWVIDPIDG 87
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAD-NSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQtwQRFWLVDPLDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 88 TLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVResiigmnpNWLTKPILSSI 167
Cdd:TIGR01331 87 TKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVR--------PWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 168 lqpiisdSRSARA----------------YGSAALEIVYVATGQLAAYltPRLQP---WDYAGGMIILNEVGGVATNFAG 228
Cdd:TIGR01331 159 -------SRSHAEektteylanlgydlrtSGGSSLKFCLVAEGSADIY--PRLGPtgeWDTAAGHAVLAAAGGAIFDLDG 229
|
250
....*....|....*
gi 1689986244 229 EPLSITAPNSILMGN 243
Cdd:TIGR01331 230 SPLLYGKRESFRNPN 244
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-226 |
2.79e-28 |
|
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: 106.71 E-value: 2.79e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 5 DYAKSLVLEAGNNVRKWM--VEDLAIEEKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEgHGHDIESTE---GVV 79
Cdd:cd01636 2 EELCRVAKEAGLAILKAFgrELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEE-SGVAEEVMGrrdEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 80 WVIDPIDGTLNFIHQGENFAISVGIFKdgkpyagfvydvmadLLYHAKVGHGAYINQNAIPQLEGTQVresiigmnpnwl 159
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVYV---------------ILILAEPSHKRVDEKKAELQLLAVYR------------ 133
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1689986244 160 tkpilssilqpiisdsrsARAYGSAALEIVYVATGQLAAYLTPRLQ--PWDYAGGMIILNEVGGVATNF 226
Cdd:cd01636 134 ------------------IRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTDW 184
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
25-250 |
1.30e-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: 106.62 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 25 DLAIEEKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEgHGHDIESTEGVVWVIDPIDGTLNFIHQGENFAISVGI 104
Cdd:TIGR02067 23 SLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE-FGHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIAL 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 105 FKDGKPYAGFVYDVMADLLYHAKVGHGAYinQNAIPQlegtQVRE-------SIIGMNPNWLTKPILSSILQPIISDSRS 177
Cdd:TIGR02067 102 VEGGMPVLGVIFQPATGERWWAAGGGAAF--LGGRRL----RVSScanlsdaVLFTTSPDLLDDPGNRPAFERLRRAARL 175
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1689986244 178 ARAYGSAaleIVY--VATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLsITAPNSILMGNAQVHEEI 250
Cdd:TIGR02067 176 TRYGGDC---YAYlmVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAVAAGNAMLHDEA 246
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
45-250 |
1.01e-16 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 79.39 E-value: 1.01e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 45 IEQFIVQQIQESYPHHRIIGEE-GHGHDIESTEGVVWVIDPIDGTLNFIHQGENFAISVGIFK-DGKP------------ 110
Cdd:PRK14076 48 IAENIAINSLEKFCSGILISEEiGFKKIGKNKPEYIFVLDPIDGTYNALKDIPIYSASIAIAKiDGFDkkikefigknlt 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 111 ----YAGFVYDVMADLLYHAKVGHGAYI----NQNAIPQLEGTQVRESIIGMNPNWLTKPILSSILQPIIsdsRSARAYG 182
Cdd:PRK14076 128 indlEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDASIGLFAYGLSLDTLKFIKDRKV---RRIRLFG 204
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1689986244 183 SAALEIVYVATGQLAAYL----TPRLqpWDYAGGMIILNEVGGVATNFAGEP----LSITAPNSILMGNAQVHEEI 250
Cdd:PRK14076 205 SIALEMCYVASGALDAFInvneTTRL--CDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKKL 278
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
77-231 |
2.36e-14 |
|
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: 71.82 E-value: 2.36e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 77 GVVWVIDPIDGTLNFIhQGENFAISVGIFKDGKPYAG------FVYDVMAD----------LLYHAKVGHGAYINQNAIP 140
Cdd:TIGR01330 130 GRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGvigcpnLPLSSYGAqnlkgseskgCIFRAVRGSGAFMYSLSSD 208
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 141 QLEGTQVR-------------ESIIGMNPNWLTKPILSSIL----QPIISDSRSARAYGSAALEIVYVatgQLAAYLTPR 203
Cdd:TIGR01330 209 AESPTKVHvssvkdtkdaifcEGVEKGHSSHDEQTAIANKLgiskSPLRLDSQAKYAALARGDADVYL---RLPIKLSYQ 285
|
170 180
....*....|....*....|....*...
gi 1689986244 204 LQPWDYAGGMIILNEVGGVATNFAGEPL 231
Cdd:TIGR01330 286 EKIWDHAAGNVIVEEAGGIVTDAMGKPL 313
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
5-249 |
1.20e-13 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 69.36 E-value: 1.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 5 DYAKSLVLEAGNNVRKWMVEDLAIEEKSnpnDL--VTNVDKAIEQFIVQQIQESYPHHRIIGEEghgHDIESTEGV---V 79
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTKFEIIDKE---DLspVTIADRAAEEAMRSIILENFPSHAIFGEE---HGLRCGEGSsdyV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 80 WVIDPIDGTLNFIHQGENFAISVGIFKDGKPYAGFVYDVMADLLYHAKVGHGAYINQNAIPQLEGTQVRESIIgmnpnWL 159
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYL-----YT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 160 TKPILSS--ILQPIISDSRSARA--YGSAALEIVYVATGQLAAYLTPRLQPWDYAGGMIILNEVGGVATNFAGEPLSITA 235
Cdd:PLN02911 187 TSPHMFSgdAEDAFARVRDKVKVplYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKLRWEP 266
|
250 260
....*....|....*....|..
gi 1689986244 236 --------PNSILMGNAQVHEE 249
Cdd:PLN02911 267 spgslatsFNVVAAGDARLHKQ 288
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
13-240 |
7.70e-13 |
|
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: 66.96 E-value: 7.70e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 13 EAGNNVRKWMV-EDLAIE-----EKSNPNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGH---------------- 70
Cdd:cd01640 11 KAGGIARDVVKkGRLLILlvegkTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFenqedesrdvdldeei 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 71 ----------DIESTEGVVWvIDPIDGTLNFIHqG--ENFAISVGIFKDGKPYAGfvydVMADLLYHAKVGHGAYINQnA 138
Cdd:cd01640 91 leescpspskDLPEEDLGVW-VDPLDATQEYTE-GllEYVTVLIGVAVKGKPIAG----VIHQPFYEKTAGAGAWLGR-T 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 139 IPQLEGTQVRESIIGMNPNWLtKPILSSI---------LQPIISDSRSARAYGsAALEIVYVATGQLAAYL--TPRLQPW 207
Cdd:cd01640 164 IWGLSGLGAHSSDFKEREDAG-KIIVSTShshsvkevqLITAGNKDEVLRAGG-AGYKVLQVLEGLADAYVhsTGGIKKW 241
|
250 260 270
....*....|....*....|....*....|...
gi 1689986244 208 DYAGGMIILNEVGGVATNFAGEPLSITAPNSIL 240
Cdd:cd01640 242 DICAPEAILRALGGDMTDLHGEPLSYSKAVKPV 274
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
26-240 |
6.31e-11 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 60.86 E-value: 6.31e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 26 LAIEEKSNpNDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEG-HGHDIESTEGVVWVIDPIDGTLNFIHQGENFAISVGI 104
Cdd:PRK10931 26 LDVASKAD-DSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDpPAWEVRQHWQRYWLVDPLDGTKEFIKRNGEFTVNIAL 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 105 FKDGKPYAGFVYDVMADLLYHAKvGHGAYINQNAipQLEGTQVRESiigmnpnwltKPilssilqPIISDSRSAR----- 179
Cdd:PRK10931 105 IEQGKPVLGVVYAPVMNVMYSAA-EGKAWKEECG--VRKQIQVRDA----------RP-------PLVVISRSHAdaelk 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1689986244 180 ------------AYGSaALEIVYVATGQlaAYLTPRLQP---WDYAGGMIILNEVGGVATNFAGEPLSITAPNSIL 240
Cdd:PRK10931 165 eylqqlgehqttSIGS-SLKFCLVAEGQ--AQLYPRFGPtniWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFL 237
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
35-212 |
8.05e-09 |
|
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: 54.76 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 35 NDLVTNVDKAIEQFIVQQIQESYPHHRIIGEEGHGHDIESTEgVVWVIDPIDGTLNFIHQGENFAISVGIF-KDGKPYAG 113
Cdd:cd01642 33 GDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGE-YIAVLDPLDGSTNYLSGIPFYSVSVALAdPRSKVKAA 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1689986244 114 FVYDVmADLLYHAKVGH----GAYINQNAIPQlEGTQVRESIIGM------NPNWLTKPILSSIlqpiisdsrSARAYGS 183
Cdd:cd01642 112 TLDNF-VSGEGGLKVYSpptrFSYISVPKLGP-PLVPEVPSKIGIyegssrNPEKFLLLSRNGL---------KFRSLGS 180
|
170 180 190
....*....|....*....|....*....|.
gi 1689986244 184 AALEIVYVATGQLAAYL--TPRLQPWDYAGG 212
Cdd:cd01642 181 AALELAYTCEGSFVLFLdlRGKLRNFDVAAA 211
|
|
| |
