|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.39e-123 |
|
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: 351.84 E-value: 1.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRASEHVShIQIDNK-EQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG--NEYTWI 80
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLG-LNVEEKgSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGltDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 81 IDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKAq 160
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 161 qQKYLDAYLEMF-KAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLES 239
Cdd:cd01639 159 -GDNFDRYLNNFaKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
....*..
gi 2544591926 240 GNIITGN 246
Cdd:cd01639 238 GNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
2.71e-121 |
|
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: 346.45 E-value: 2.71e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 2 HPMLTIAIRAARNAGDIILRASEHVShIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG--NEYTW 79
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGrdSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 80 IIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKA 159
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 160 QQqkylDAYLEMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLES 239
Cdd:COG0483 160 DD----REYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGS 235
|
250 260
....*....|....*....|
gi 2544591926 240 GNIITGNPKMHQLMFQLINP 259
Cdd:COG0483 236 GSLVAANPALHDELLALLRE 255
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-266 |
1.33e-108 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 314.82 E-value: 1.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 1 MHPMLTIAIRAARNAGDIILRASEHVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEGNEY--T 78
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQdvQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 79 WIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFK 158
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 159 AQQqkYLDAYLEMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLE 238
Cdd:PRK10757 161 AKQ--HATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYML 238
|
250 260
....*....|....*....|....*...
gi 2544591926 239 SGNIITGNPKMHQLMFQLINPHVTDNLK 266
Cdd:PRK10757 239 TGNIVAGNPRVVKAMLANMRDELSDALK 266
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-251 |
7.64e-84 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 251.88 E-value: 7.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 1 MHPMLTIAIRAARNAGDIILRASEHVSHIQIDNKE-QHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG----- 74
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSgANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDqtelt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 75 -NEYTWIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGT 153
Cdd:pfam00459 82 dDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 154 GFPFKAQQ---QKYLDAYLEMFkavcINTSGIRRTGSAAIDLAFLAMGRLDGFWEVD-LKPWDIAAGIIIVKEAGGVVTD 229
Cdd:pfam00459 162 LFGVSSRKdtsEASFLAKLLKL----VRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTD 237
|
250 260
....*....|....*....|..
gi 2544591926 230 LAFNDQYLESGNIITGNPKMHQ 251
Cdd:pfam00459 238 ADGGPFDLLAGRVIAANPKVLH 259
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-258 |
1.02e-55 |
|
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: 179.42 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIILRASEhVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHE--GNEYTWIID 82
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFR-ASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEegDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 83 PLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKAQQQ 162
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 163 KYLDAYLEMFKAVcintsGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQyLESGNI 242
Cdd:TIGR02067 161 GNRPAFERLRRAA-----RLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGA 234
|
250
....*....|....*..
gi 2544591926 243 I-TGNPKMHQLMFQLIN 258
Cdd:TIGR02067 235 VaAGNAMLHDEALEILN 251
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.39e-123 |
|
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: 351.84 E-value: 1.39e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRASEHVShIQIDNK-EQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG--NEYTWI 80
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLG-LNVEEKgSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGltDEPTWI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 81 IDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKAq 160
Cdd:cd01639 80 IDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDR- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 161 qQKYLDAYLEMF-KAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLES 239
Cdd:cd01639 159 -GDNFDRYLNNFaKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
....*..
gi 2544591926 240 GNIITGN 246
Cdd:cd01639 238 GNILAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-259 |
2.71e-121 |
|
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: 346.45 E-value: 2.71e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 2 HPMLTIAIRAARNAGDIILRASEHVShIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG--NEYTW 79
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGrdSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 80 IIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKA 159
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 160 QQqkylDAYLEMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLES 239
Cdd:COG0483 160 DD----REYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGS 235
|
250 260
....*....|....*....|
gi 2544591926 240 GNIITGNPKMHQLMFQLINP 259
Cdd:COG0483 236 GSLVAANPALHDELLALLRE 255
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-266 |
1.33e-108 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 314.82 E-value: 1.33e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 1 MHPMLTIAIRAARNAGDIILRASEHVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEGNEY--T 78
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQdvQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 79 WIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFK 158
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 159 AQQqkYLDAYLEMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLE 238
Cdd:PRK10757 161 AKQ--HATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYML 238
|
250 260
....*....|....*....|....*...
gi 2544591926 239 SGNIITGNPKMHQLMFQLINPHVTDNLK 266
Cdd:PRK10757 239 TGNIVAGNPRVVKAMLANMRDELSDALK 266
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-251 |
7.64e-84 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 251.88 E-value: 7.64e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 1 MHPMLTIAIRAARNAGDIILRASEHVSHIQIDNKE-QHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG----- 74
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSgANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDqtelt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 75 -NEYTWIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGT 153
Cdd:pfam00459 82 dDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 154 GFPFKAQQ---QKYLDAYLEMFkavcINTSGIRRTGSAAIDLAFLAMGRLDGFWEVD-LKPWDIAAGIIIVKEAGGVVTD 229
Cdd:pfam00459 162 LFGVSSRKdtsEASFLAKLLKL----VRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTD 237
|
250 260
....*....|....*....|..
gi 2544591926 230 LAFNDQYLESGNIITGNPKMHQ 251
Cdd:pfam00459 238 ADGGPFDLLAGRVIAANPKVLH 259
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-230 |
8.19e-77 |
|
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: 232.98 E-value: 8.19e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIILRASEHVSHIQIDnKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESG---QHEGNEYTWII 81
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGgsgNVSDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 82 DPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKAQQ 161
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2544591926 162 QKYLDAYLEmfkavcINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDL 230
Cdd:cd01637 160 RAAVLASLV------NRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDL 222
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-247 |
1.05e-70 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 218.41 E-value: 1.05e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIIlRASEHvSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEES-----GQHEGNEYTW 79
Cdd:PLN02553 11 LEVAVDAAKAAGQII-RKGFY-QTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaasgGTELTDEPTW 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 80 IIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKa 159
Cdd:PLN02553 89 IVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTK- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 160 QQQKYLDAYLEMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDL-KPWDIAAGIIIVKEAGGVVTDLAFNDQYLE 238
Cdd:PLN02553 168 RDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIM 247
|
....*....
gi 2544591926 239 SGNIITGNP 247
Cdd:PLN02553 248 SRRVAASNG 256
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-247 |
1.53e-64 |
|
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: 201.79 E-value: 1.53e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIILRASEhvSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG-NEYTWIIDP 83
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFG--NSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPsSGWYWVIDP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 84 LDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKAQQQK 163
Cdd:cd01643 79 IDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASARA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 164 YLDAYLEMFKAVcintsgIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQYLESGNII 243
Cdd:cd01643 159 VLRVILRRFPGK------IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYL 232
|
....*
gi 2544591926 244 T-GNP 247
Cdd:cd01643 233 SaGFP 237
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-253 |
1.25e-61 |
|
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: 194.39 E-value: 1.25e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIIL---RASehvshIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESG-QHEGNEYTWI 80
Cdd:cd01641 2 LAFALELADAAGQITLpyfRTR-----LQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGnEGGDAGYVWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 81 IDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLN---NRRIRVTKQATLTGALIGTGFP- 156
Cdd:cd01641 77 LDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTTDPh 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 157 -FKAQQQKyldAYLEMFKAVcintsGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQ 235
Cdd:cd01641 157 fFTPGDRA---AFERLARAV-----RLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPL 228
|
250
....*....|....*....
gi 2544591926 236 YLESGNII-TGNPKMHQLM 253
Cdd:cd01641 229 TGGSGRVVaAGDAELHEAL 247
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-266 |
2.56e-56 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 184.62 E-value: 2.56e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRASEHVSHIQIdnKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESG--QHEGNEYTWII 81
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNISY--KGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGviGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 82 DPLDGTTNFLHGFPHYAVSIA-LKHKNRLEVGVIYL---PL--TNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGF 155
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGvLFRGTPAAATVVEFvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 156 PFKaqqqkYLDAY---LEMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAF 232
Cdd:PLN02737 237 GYE-----HDDAWatnIELFKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDG 311
|
250 260 270
....*....|....*....|....*....|....
gi 2544591926 233 NDQYLESGNIITGNPKMHQLMFQLINPhVTDNLK 266
Cdd:PLN02737 312 GKFSVFDRSVLVSNGVLHPKLLDRIGP-ATEKLK 344
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-258 |
1.02e-55 |
|
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: 179.42 E-value: 1.02e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIILRASEhVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHE--GNEYTWIID 82
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFR-ASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEegDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 83 PLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFPFKAQQQ 162
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 163 KYLDAYLEMFKAVcintsGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTDLAFNDQyLESGNI 242
Cdd:TIGR02067 161 GNRPAFERLRRAA-----RLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGA 234
|
250
....*....|....*..
gi 2544591926 243 I-TGNPKMHQLMFQLIN 258
Cdd:TIGR02067 235 VaAGNAMLHDEALEILN 251
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-233 |
3.80e-47 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 157.63 E-value: 3.80e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 1 MHPMLTIAIRAARNAGDIILRASEhvSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEES-----GQHEGN 75
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYR--ADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESaaipyEERKSW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 76 EYTWIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNN-----RRIRVTKQATLTGAL 150
Cdd:COG1218 79 DRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerQPIRVRDRPPAEPLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 151 IGTGfpfKAQQQKYLDAYLEMFKAVcintsGIRRTGSaAIDLAFLAMGrldgfwEVDLKP-------WDIAAGIIIVKEA 223
Cdd:COG1218 159 VVAS---RSHRDEETEALLARLGVA-----ELVSVGS-SLKFCLVAEG------EADLYPrlgptmeWDTAAGQAILEAA 223
|
250
....*....|
gi 2544591926 224 GGVVTDLAFN 233
Cdd:COG1218 224 GGRVTDLDGK 233
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-243 |
5.27e-47 |
|
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: 156.62 E-value: 5.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRasEHVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQH---EGNEYTWI 80
Cdd:cd01638 1 LLELLIRIAREAGDAILE--VYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDplrLGWDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 81 IDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQA---TLTGALIGTGfpf 157
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQArppPLQPLRVVAS--- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 158 KAQQQKYLDAYLEMFKAVcintsGIRRTGSAAiDLAFLAMGRLDGFWEvdLKP---WDIAAGIIIVKEAGGVVTD----- 229
Cdd:cd01638 156 RSHPDEELEALLAALGVA-----EVVSIGSSL-KFCLVAEGEADIYPR--LGPtmeWDTAAGDAVLRAAGGAVSDldgsp 227
|
250
....*....|....
gi 2544591926 230 LAFNDQYLESGNII 243
Cdd:cd01638 228 LTYNREDFLNPDFI 241
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
5-258 |
2.89e-45 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 152.75 E-value: 2.89e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIIL------RASEHVShIQIDNKEqhdfvTE-IDRQAEAEIIKNIKTAYPEHAILAEESG--QHEGN 75
Cdd:PRK12676 7 LEICDDMAKEVEKAIMplfgtpDAGETVG-MGADGTP-----TKlIDKVAEDIILEVLKPLGRCVNIISEELGeiVGNGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 76 EYTWIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGT-G 154
Cdd:PRK12676 81 EYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSIyG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 155 FPFKaqqqkyldayLEMFKAVCINtsgIRRT---GSAAIDLAFLAMGRLDGFWEV--DLKPWDIAAGIIIVKEAGGVVTD 229
Cdd:PRK12676 161 YRRG----------KERTVKLGRK---VRRVrilGAIALELCYVASGRLDAFVDVrnYLRVTDIAAGKLICEEAGGIVTD 227
|
250 260 270
....*....|....*....|....*....|....*
gi 2544591926 230 -----LAFNDQYLESGNII-TGNPKMHQLMFQLIN 258
Cdd:PRK12676 228 edgneLKLPLNVTERTNLIaANGEELHKKILELLE 262
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-257 |
4.40e-45 |
|
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: 152.15 E-value: 4.40e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIIL------RASEHVShIQIDNKEqhdfVTEIDRQAEAEIIKNIKTAYPEHaILAEESGQ-HEGN- 75
Cdd:cd01515 1 WLEIARNIAKEIEKAIKplfgteDASEVVK-IGADGTP----TKLIDKVAEDAAIEILKKLGSVN-IVSEEIGViDNGDe 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 76 -EYTWIIDPLDGTTNFLHGFPHYAVSIAL--KHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIG 152
Cdd:cd01515 75 pEYTVVLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 153 TGFPFKAQQQKYLdaylemfkaVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEV--DLKPWDIAAGIIIVKEAGGVVTD- 229
Cdd:cd01515 155 YYIYGKNHDRTFK---------ICRKVRRVRIFGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDe 225
|
250 260 270
....*....|....*....|....*....|..
gi 2544591926 230 ----LAFNDQYLESGNIITGNPKMHQLMFQLI 257
Cdd:cd01515 226 ngkeLKLKLNVTERVNIIAANSELHKKLLELL 257
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
4.22e-39 |
|
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: 134.44 E-value: 4.22e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIILRA-SEHVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESG-----QHEGNEYT 78
Cdd:cd01636 1 LEELCRVAKEAGLAILKAfGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeevMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 79 WIIDPLDGTTNFLHGFPHYAVSIAlkhknrleVGVIYlpltnelftaargegamlnnrrirvtkqatltgalIGTGFPFK 158
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIA--------VYVIL-----------------------------------ILAEPSHK 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2544591926 159 AQQQKyldayleMFKAVCINTSGIRRTGSAAIDLAFLAMGRLDGFWEVDLK--PWDIAAGIIIVKEAGGVVTDL 230
Cdd:cd01636 118 RVDEK-------KAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-251 |
2.16e-33 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 122.91 E-value: 2.16e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 6 TIAIRAARNAGDIIL---RASehvshIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESG---QHEGNEYTW 79
Cdd:PLN02911 38 DVAHKLADAAGEVTRkyfRTK-----FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGlrcGEGSSDYVW 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 80 IIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLNNRRIRVTKQATLTGALIGTGFP--F 157
Cdd:PLN02911 113 VLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSPhmF 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 158 KAQQqkyLDAYLEMFKAVcintsGIRRTGSAAIDLAFLAMGRLDGFWEVDLKPWDIAAGIIIVKEAGGVVTD-------- 229
Cdd:PLN02911 193 SGDA---EDAFARVRDKV-----KVPLYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDwkgrklrw 264
|
250 260
....*....|....*....|...
gi 2544591926 230 LAFNDQYLESGNII-TGNPKMHQ 251
Cdd:PLN02911 265 EPSPGSLATSFNVVaAGDARLHK 287
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-251 |
2.66e-33 |
|
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: 122.04 E-value: 2.66e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRASEHV-SHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGqhEGNEYTWIID 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLgAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDS--AALGRFWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 83 PLDGTTNFLHGFPhYAVSIALKHKNRLEVGVIYLPLTNE-------LFTAARGEGAMLnnRRIRVTKQATLTGALIGTGF 155
Cdd:cd01517 79 PIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAWL--RPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 156 ---PFKAQQQKYLDAYLEMFKAVCINTSGIRRTGS----AAIDL----AFLAMGRLDGFWEvdlKPWDIAAGIIIVKEAG 224
Cdd:cd01517 156 rasFCESVESAHSSHRLQAAIKALGGTPQPVRLDSqakyAAVARgaadFYLRLPLSMSYRE---KIWDHAAGVLIVEEAG 232
|
250 260 270
....*....|....*....|....*....|....
gi 2544591926 225 GVVTDLAFND-------QYLESGNIITGNPKMHQ 251
Cdd:cd01517 233 GKVTDADGKPldfgkgrKLLNNGGLIAAPGEIHE 266
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-230 |
4.76e-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: 107.54 E-value: 4.76e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRASEhvSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEEsGQHEGNEYT----- 78
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQ--KELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEE-DASIPLTPRqtwqr 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 79 -WIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGEGAMLN------NRRIRVTKQATLTGALI 151
Cdd:TIGR01331 78 fWLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREgdgqalKAPIHVRPWPSGPLLVV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 152 GTGFPFKAQQQKYLDAYLEMFkavcintsgiRRTGSAAIDLAFLAMGrldgfwEVDLKP-------WDIAAGIIIVKEAG 224
Cdd:TIGR01331 158 ISRSHAEEKTTEYLANLGYDL----------RTSGGSSLKFCLVAEG------SADIYPrlgptgeWDTAAGHAVLAAAG 221
|
....*.
gi 2544591926 225 GVVTDL 230
Cdd:TIGR01331 222 GAIFDL 227
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
43-258 |
1.88e-23 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 99.03 E-value: 1.88e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 43 IDRQAEAEIIKNIKTaYPEHAILAEESGQ----HEGNEYTWIIDPLDGTTNFLHGFPHYAVSIAL--------KHK---- 106
Cdd:PRK14076 45 IDLIAENIAINSLEK-FCSGILISEEIGFkkigKNKPEYIFVLDPIDGTYNALKDIPIYSASIAIakidgfdkKIKefig 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 107 -----NRLEVGVIYLPLTNELFTAARGEGAML----NNRRIRVTKQATLTGALIGtGFPFkaqqQKYLDAyLEMFKAVCI 177
Cdd:PRK14076 124 knltiNDLEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKKIEISNISNLKDASIG-LFAY----GLSLDT-LKFIKDRKV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 178 ntSGIRRTGSAAIDLAFLAMGRLDGFWEVDL--KPWDIAAGIIIVKEAGGVVTDLafNDQYL-------ESGNIITGNPK 248
Cdd:PRK14076 198 --RRIRLFGSIALEMCYVASGALDAFINVNEttRLCDIAAGYVICKEAGGIITNK--NGKPLnmkldinEKTSVICSNEI 273
|
250
....*....|
gi 2544591926 249 MHQLMFQLIN 258
Cdd:PRK14076 274 LHKKLVGIFG 283
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
38-224 |
2.61e-15 |
|
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: 73.25 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 38 DFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEG--NEYTWIIDPLDGTTNFLHGFPHYAVSIALKHKNRLE----- 110
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKgsGEYIAVLDPLDGSTNYLSGIPFYSVSVALADPRSKVkaatl 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 111 --------VGVIYLPLTNELFTAARGEGAMLnnrrirVTKQATLTGALIGTG-FPFKAqqqkyLDAYLEMFKavcintsg 181
Cdd:cd01642 114 dnfvsgegGLKVYSPPTRFSYISVPKLGPPL------VPEVPSKIGIYEGSSrNPEKF-----LLLSRNGLK-------- 174
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 2544591926 182 IRRTGSAAIDLAFLAMGRLDGFWEV--DLKPWDIAAGIIIVKEAG 224
Cdd:cd01642 175 FRSLGSAALELAYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLG 219
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-129 |
2.80e-15 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 73.19 E-value: 2.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 4 MLTIAIRAARNAGDIILRASEHVSHIQIDNKEQHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESG------QHEgnEY 77
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPpawevrQHW--QR 78
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 2544591926 78 TWIIDPLDGTTNFLHGFPHYAVSIALKHKNRLEVGVIYLPLTNELFTAARGE 129
Cdd:PRK10931 79 YWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK 130
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
5-234 |
2.74e-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: 68.12 E-value: 2.74e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 5 LTIAIRAARNAGDIILRASEHVSHIQIDNKE-QHDFVTEIDRQAEAEIIKNIKTAYPEHAILAEESGQHEGNEYTWI--- 80
Cdd:cd01640 6 LAVAEKAGGIARDVVKKGRLLILLVEGKTKEgANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 81 -------------------------IDPLDGTTNFLHGFPHYA-VSIALKHKNRLEVGVIYLPLTNELFTAARGEGAM-- 132
Cdd:cd01640 86 ldeeileescpspskdlpeedlgvwVDPLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWLGRTiw 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2544591926 133 -LNNRRIRVTKQATLTGALIGTGFPfkAQQQKYLDAYLemfKAVCINTSGIRRTGSAAIDLAFLAmGRLDG--FWEVDLK 209
Cdd:cd01640 166 gLSGLGAHSSDFKEREDAGKIIVST--SHSHSVKEVQL---ITAGNKDEVLRAGGAGYKVLQVLE-GLADAyvHSTGGIK 239
|
250 260
....*....|....*....|....*
gi 2544591926 210 PWDIAAGIIIVKEAGGVVTDLAFND 234
Cdd:cd01640 240 KWDICAPEAILRALGGDMTDLHGEP 264
|
|
| |
