|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-267 |
0e+00 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 594.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 1 MHPMLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 WVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 161 AKQHATTYMNILGKLFTECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGHNYMSTG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 556423901 241 NVVAGNPRVVKAMLANMRDELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.46e-135 |
|
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: 381.88 E-value: 1.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVI 83
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 84 DPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFKAKQ 163
Cdd:cd01639 81 DPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 164 HATTYMNILGKLFT-ECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGHNYMSTGNV 242
Cdd:cd01639 161 NFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNI 240
|
....
gi 556423901 243 VAGN 246
Cdd:cd01639 241 LAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-258 |
5.71e-128 |
|
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: 363.40 E-value: 5.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 2 HPMLTIAVRAARKAGNVIAKHYETPDsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 82 VIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 162 KQHAttYMNILGKLFTECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGHNYMSTGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 556423901 242 VVAGNPRVVKAMLANMR 258
Cdd:COG0483 238 LVAANPALHDELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-255 |
1.95e-89 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 266.13 E-value: 1.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 1 MHPMLTIAVRAARKAGNVIAKHYETP-DSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEH----EGT 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKgdqtELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 76 DQDVQWVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 156 GFPFKAKQHATTYMNILGKLF-TECADFRRTGSAALDLAYVATGRVDGYFELS-LKPWDFAAGELIAREAGAIVCDFTGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|..
gi 556423901 234 HNYMSTGNVVAGNPRVVKAMLA 255
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLA 263
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-255 |
1.37e-41 |
|
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: 143.21 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVEtSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 85 PLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFP---FKA 161
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdllDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 162 KQHAttymnilgklftecADFRRTGSAALDLAY--------VATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGG 233
Cdd:TIGR02067 161 GNRP--------------AFERLRRAARLTRYGgdcyaylmVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGK 226
|
250 260
....*....|....*....|..
gi 556423901 234 HNYMSTGNVVAGNPRVVKAMLA 255
Cdd:TIGR02067 227 PAPDGGGAVAAGNAMLHDEALE 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-267 |
0e+00 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 594.86 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 1 MHPMLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQ 80
Cdd:PRK10757 1 MHPMLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 WVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFK 160
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 161 AKQHATTYMNILGKLFTECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGHNYMSTG 240
Cdd:PRK10757 161 AKQHATTYINIVGKLFTECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYMLTG 240
|
250 260
....*....|....*....|....*..
gi 556423901 241 NVVAGNPRVVKAMLANMRDELSDALKR 267
Cdd:PRK10757 241 NIVAGNPRVVKAMLANMRDELSDALKR 267
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
4-246 |
1.46e-135 |
|
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: 381.88 E-value: 1.46e-135
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVI 83
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPTWII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 84 DPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFKAKQ 163
Cdd:cd01639 81 DPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 164 HATTYMNILGKLFT-ECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGHNYMSTGNV 242
Cdd:cd01639 161 NFDRYLNNFAKLLAkAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNI 240
|
....
gi 556423901 243 VAGN 246
Cdd:cd01639 241 LAGN 244
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
2-258 |
5.71e-128 |
|
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: 363.40 E-value: 5.71e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 2 HPMLTIAVRAARKAGNVIAKHYETPDsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQW 81
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELD-LEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 82 VIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFKA 161
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 162 KQHAttYMNILGKLFTECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGHNYMSTGN 241
Cdd:COG0483 160 DDRE--YLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSGS 237
|
250
....*....|....*..
gi 556423901 242 VVAGNPRVVKAMLANMR 258
Cdd:COG0483 238 LVAANPALHDELLALLR 254
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
1-255 |
1.95e-89 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 266.13 E-value: 1.95e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 1 MHPMLTIAVRAARKAGNVIAKHYETP-DSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEH----EGT 75
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKlTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKgdqtELT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 76 DQDVQWVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILAT 155
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 156 GFPFKAKQHATTYMNILGKLF-TECADFRRTGSAALDLAYVATGRVDGYFELS-LKPWDFAAGELIAREAGAIVCDFTGG 233
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGG 241
|
250 260
....*....|....*....|..
gi 556423901 234 HNYMSTGNVVAGNPRVVKAMLA 255
Cdd:pfam00459 242 PFDLLAGRVIAANPKVLHELLA 263
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
5-245 |
1.57e-82 |
|
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: 247.23 E-value: 1.57e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVETSqKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGT-DQDVQWVI 83
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETK-KGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVsDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 84 DPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFKAKQ 163
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSN 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 164 HAttymNILGKLFTECADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGG-HNYMSTGNV 242
Cdd:cd01637 160 RA----AVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEpLDTLNRSGI 235
|
...
gi 556423901 243 VAG 245
Cdd:cd01637 236 IAA 238
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
5-259 |
2.01e-68 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 212.63 E-value: 2.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVEtsQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEES----GEHEGTDqDVQ 80
Cdd:PLN02553 11 LEVAVDAAKAAGQIIRKGFYQTKHVE--HKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaasGGTELTD-EPT 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 WVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFK 160
Cdd:PLN02553 88 WIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTK 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 161 A-KQHATTYMNILGKLFTECADFRRTGSAALDLAYVATGRVDGYFELSL-KPWDFAAGELIAREAGAIVCDFTGGHNYMS 238
Cdd:PLN02553 168 RdKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIM 247
|
250 260
....*....|....*....|.
gi 556423901 239 TGNVVAGNPRVVKAMLANMRD 259
Cdd:PLN02553 248 SRRVAASNGHLKDAFVEALRQ 268
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
5-252 |
3.17e-58 |
|
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: 185.62 E-value: 3.17e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVETsqKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVqWVID 84
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAET--KADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWY-WVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 85 PLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPFKAKQH 164
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 165 ATT--YMNILGklftecADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTG-GHNYMSTGN 241
Cdd:cd01643 158 AVLrvILRRFP------GKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEePAFLQTKDY 231
|
250
....*....|.
gi 556423901 242 VVAGNPRVVKA 252
Cdd:cd01643 232 LSAGFPTLIAA 242
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
4-233 |
1.58e-56 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 185.00 E-value: 1.58e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVetSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVI 83
Cdd:PLN02737 79 LLAVAELAAKTGAEVVMEAVNKPRNI--SYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYLWCI 156
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 84 DPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYD----PM--RNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGF 157
Cdd:PLN02737 157 DPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEfvggPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGF 236
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556423901 158 PFKAKQHATTYMNiLGKLFTE-CADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGG 233
Cdd:PLN02737 237 GYEHDDAWATNIE-LFKEFTDvSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGG 312
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
5-254 |
1.23e-50 |
|
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: 166.28 E-value: 1.23e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVETsqKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEhEGTDQDVQWVID 84
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVET--KADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGN-EGGDAGYVWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 85 PLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLN---GYRLRCSNARDLDGTILATGFPFKA 161
Cdd:cd01641 79 PIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTTDPHFF 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 162 KQHAT-TYMNILGKlftecADFRRTGSAALDLAYVATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGG-HNYMST 239
Cdd:cd01641 159 TPGDRaAFERLARA-----VRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGpLTGGSG 233
|
250
....*....|....*
gi 556423901 240 GNVVAGNPRVVKAML 254
Cdd:cd01641 234 RVVAAGDAELHEALL 248
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-232 |
1.88e-50 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 166.10 E-value: 1.88e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 1 MHPMLTIAVRAARKAGNVIAKHYETPdsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESgEHEGTDQDVQ 80
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRAD--FEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEES-AAIPYEERKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 ----WVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGA-----QLNGYRLRCSNARDLDGT 151
Cdd:COG1218 78 wdrfWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAfketgGGERQPIRVRDRPPAEPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 152 ILATGfpfkaKQHATTYM-NILGKLftECADFRRTGSaALDLAYVATGRVDGYfeLSLKP---WDFAAGELIAREAGAIV 227
Cdd:COG1218 158 RVVAS-----RSHRDEETeALLARL--GVAELVSVGS-SLKFCLVAEGEADLY--PRLGPtmeWDTAAGQAILEAAGGRV 227
|
....*
gi 556423901 228 CDFTG 232
Cdd:COG1218 228 TDLDG 232
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
4-255 |
6.59e-47 |
|
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: 157.15 E-value: 6.59e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKG-SNDFVTNVDKAAEAIIIETIRKSYPQhTIITEESGE-HEGTDQDVQW 81
Cdd:cd01515 1 WLEIARNIAKEIEKAIKPLFGTEDASEVVKIGaDGTPTKLIDKVAEDAAIEILKKLGSV-NIVSEEIGViDNGDEPEYTV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 82 VIDPLDGTTNFVKRLPHFSVSIAV--RIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILAtgfpf 159
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVS----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 160 kakqhATTYMNILGKLFTECADFRRT---GSAALDLAYVATGRVDGYFEL--SLKPWDFAAGELIAREAGAIVCDFTGGH 234
Cdd:cd01515 155 -----YYIYGKNHDRTFKICRKVRRVrifGSVALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKE 229
|
250 260
....*....|....*....|....*.
gi 556423901 235 -----NYMSTGNVVAGNPRVVKAMLA 255
Cdd:cd01515 230 lklklNVTERVNIIAANSELHKKLLE 255
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
4-232 |
1.07e-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: 153.54 E-value: 1.07e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVEtsQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEES-GEHEGTDQDVQWV 82
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVE--RKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESaDDPLRLGWDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 83 IDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNG----YRLRCSNARDLDGTILAtgfp 158
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGrpgaVSLQARPPPLQPLRVVA---- 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556423901 159 fkAKQHATTYMNILGKLFTECaDFRRTGSaALDLAYVATGRVDGYFELSLKP-WDFAAGELIAREAGAIVCDFTG 232
Cdd:cd01638 155 --SRSHPDEELEALLAALGVA-EVVSIGS-SLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
5-233 |
1.06e-43 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 148.90 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVETSQKG-SNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVI 83
Cdd:PRK12676 7 LEICDDMAKEVEKAIMPLFGTPDAGETVGMGaDGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 84 DPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLD-GTILATGFPFKak 162
Cdd:PRK12676 87 DPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNeSAVSIYGYRRG-- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556423901 163 qhattYMNILGKlfteCADFRRT---GSAALDLAYVATGRVDGYFEL--SLKPWDFAAGELIAREAGAIVCDFTGG 233
Cdd:PRK12676 165 -----KERTVKL----GRKVRRVrilGAIALELCYVASGRLDAFVDVrnYLRVTDIAAGKLICEEAGGIVTDEDGN 231
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
5-255 |
1.37e-41 |
|
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: 143.21 E-value: 1.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVEtSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVID 84
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVV-DKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERVWVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 85 PLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFP---FKA 161
Cdd:TIGR02067 81 PIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPdllDDP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 162 KQHAttymnilgklftecADFRRTGSAALDLAY--------VATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGG 233
Cdd:TIGR02067 161 GNRP--------------AFERLRRAARLTRYGgdcyaylmVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGK 226
|
250 260
....*....|....*....|..
gi 556423901 234 HNYMSTGNVVAGNPRVVKAMLA 255
Cdd:TIGR02067 227 PAPDGGGAVAAGNAMLHDEALE 248
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
4-233 |
6.02e-37 |
|
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: 131.03 E-value: 6.02e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVEtsQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQ--- 80
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVA--QKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWqrf 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 WVIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNG--------YRLRCSNARDLDGTI 152
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkapIHVRPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 153 LATgfpfKAKQHATTYMNILGKLFTECadfrrtGSAALDLAYVATGRVDGYfeLSLKP---WDFAAGELIAREAGAIVCD 229
Cdd:TIGR01331 159 SRS----HAEEKTTEYLANLGYDLRTS------GGSSLKFCLVAEGSADIY--PRLGPtgeWDTAAGHAVLAAAGGAIFD 226
|
....
gi 556423901 230 FTGG 233
Cdd:TIGR01331 227 LDGS 230
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
5-230 |
7.04e-37 |
|
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: 129.05 E-value: 7.04e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVETSQKGS-NDFVTNVDKAAEAIIIETIRKSYPQHTIITEESG---EHEGTDQDVQ 80
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKITKSdNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGvaeEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 WVIDPLDGTTNFVKRLPHFSVSIAVrikgrtevavvydpmrnelftatrgqgaqlngYRLRCSNARDLDGTILATGFPFK 160
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAV--------------------------------YVILILAEPSHKRVDEKKAELQL 128
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556423901 161 AKQHAttymnilgklftecadFRRTGSAALDLAYVATGRVDGYFEL--SLKPWDFAAGELIAREAGAIVCDF 230
Cdd:cd01636 129 LAVYR----------------IRIVGSAVAKMCLVALGLADIYYEPggKRRAWDVAASAAIVREAGGIMTDW 184
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
4-232 |
1.24e-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: 123.19 E-value: 1.24e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAK-HYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTdqdvQWV 82
Cdd:cd01517 1 ELEVAILAVRAAASLTLPvFRNLGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAALGR----FWV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 83 IDPLDGTTNFVKRLPhFSVSIAVRIKGRTEVAVVYDPMRNE-------LFTATRGQGA---QLNGYRLRCSNARDLDGTI 152
Cdd:cd01517 77 LDPIDGTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLddggggdLFSAVRGQGAwlrPLDGSSLQPLSVRQLTNAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 153 LATGFPFKAKQHATTYMNILGKLFTECADFRRTGSAAlDLAYVATGRVDGYFELS------LKPWDFAAGELIAREAGAI 226
Cdd:cd01517 156 RASFCESVESAHSSHRLQAAIKALGGTPQPVRLDSQA-KYAAVARGAADFYLRLPlsmsyrEKIWDHAAGVLIVEEAGGK 234
|
....*.
gi 556423901 227 VCDFTG 232
Cdd:cd01517 235 VTDADG 240
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
6-257 |
4.23e-24 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 98.25 E-value: 4.23e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 6 TIAVRAARKAGNVIAKHYETPdsVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESG-EHEGTDQDVQWVID 84
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTK--FEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGlRCGEGSSDYVWVLD 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 85 PLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRCSNARDLDGTILATGFPfkakqH 164
Cdd:PLN02911 116 PIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTTSP-----H 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 165 ATTYMNIlgKLFTECADFRRTGSAALD-LAY--VATGRVDGYFELSLKPWDFAAGELIAREAGAIVCDFTGGH------- 234
Cdd:PLN02911 191 MFSGDAE--DAFARVRDKVKVPLYGCDcYAYglLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWKGRKlrwepsp 268
|
250 260
....*....|....*....|....*
gi 556423901 235 NYMSTG-NVVA-GNPRVVKAMLANM 257
Cdd:PLN02911 269 GSLATSfNVVAaGDARLHKQALDIL 293
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
37-225 |
2.78e-23 |
|
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. These are Mg++ dependent phosphatases. Members in this family may have fructose-1,6-bisphosphatase and/or inositol-monophosphatase activity. Fructose-1,6-bisphosphatase catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway.
Pssm-ID: 238820 [Multi-domain] Cd Length: 244 Bit Score: 94.82 E-value: 2.78e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 37 NDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQWVIDPLDGTTNFVKRLPHFSVSIAV-RIKGRTEVAV 115
Cdd:cd01642 33 GDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALaDPRSKVKAAT 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 116 VYDPMRNELFtatrgqgAQLNGYRLRCSNARDL-DGTILATGFPFKAKQHATTYMNILGKLFTECAD--FRRTGSAALDL 192
Cdd:cd01642 113 LDNFVSGEGG-------LKVYSPPTRFSYISVPkLGPPLVPEVPSKIGIYEGSSRNPEKFLLLSRNGlkFRSLGSAALEL 185
|
170 180 190
....*....|....*....|....*....|....*
gi 556423901 193 AYVATGRVDGYFEL--SLKPWDFAAGELIAREAGA 225
Cdd:cd01642 186 AYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLGL 220
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
4-232 |
8.91e-21 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 91.33 E-value: 8.91e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTN-VDKAAEAIIIETIRKsYPQHTIITEESGEHEGTDQDVQW- 81
Cdd:PRK14076 5 MLKIALKVAKEIEKKIKPLIGWEKAGEVVKIGADGTPTKrIDLIAENIAINSLEK-FCSGILISEEIGFKKIGKNKPEYi 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 82 -VIDPLDGTTNFVKRLPHFSVSIAV-RIKGRT----------------EVAVVYDPMRNELFTATRGQGAQL----NGYR 139
Cdd:PRK14076 84 fVLDPIDGTYNALKDIPIYSASIAIaKIDGFDkkikefigknltindlEVGVVKNIATGDTYYAEKGEGAYLlkkgEKKK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 140 LRCSNARDL-DGTIlatGFPFKAKQHATTYmnilgklFTECADFRRT---GSAALDLAYVATGRVDGYFEL--SLKPWDF 213
Cdd:PRK14076 164 IEISNISNLkDASI---GLFAYGLSLDTLK-------FIKDRKVRRIrlfGSIALEMCYVASGALDAFINVneTTRLCDI 233
|
250
....*....|....*....
gi 556423901 214 AAGELIAREAGAIVCDFTG 232
Cdd:PRK14076 234 AAGYVICKEAGGIITNKNG 252
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
4-232 |
1.08e-19 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 85.13 E-value: 1.08e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 4 MLTIAVRAARKAGNVIAKHYETPDSVETSQKGSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQ--W 81
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQryW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 82 VIDPLDGTTNFVKRLPHFSVSIAVRIKGRTEVAVVYDPMRNELFTATRGQG-AQLNGYR--LRCSNARDLDGTIlatgfp 158
Cdd:PRK10931 81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAwKEECGVRkqIQVRDARPPLVVI------ 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 159 fkAKQHATT----YMNILGKLFTECadfrrTGSaALDLAYVATGRVDGYfelslkP-------WDFAAGELIAREAGAIV 227
Cdd:PRK10931 155 --SRSHADAelkeYLQQLGEHQTTS-----IGS-SLKFCLVAEGQAQLY------PrfgptniWDTAAGHAVAIAAGAHV 220
|
....*
gi 556423901 228 CDFTG 232
Cdd:PRK10931 221 HDWQG 225
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
5-267 |
8.45e-14 |
|
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: 69.66 E-value: 8.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 5 LTIAVRAARKAGNVIAKHYETPDSVETSQK-GSNDFVTNVDKAAEAIIIETIRKSYPQHTIITEESGEHEGTDQDVQ--- 80
Cdd:cd01640 6 LAVAEKAGGIARDVVKKGRLLILLVEGKTKeGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRdvd 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 81 ------------------------WvIDPLDGTTNFVK-RLPHFSVSIAVRIKGRTEVAVVYDPMRNElftaTRGQGAQL 135
Cdd:cd01640 86 ldeeileescpspskdlpeedlgvW-VDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEK----TAGAGAWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556423901 136 NgyrlrcsnaRDLDG--TILATGFPFKAKQ----------HATTYMNILGKLFTECADFRRTGSAALDLAYVATGRVDGY 203
Cdd:cd01640 161 G---------RTIWGlsGLGAHSSDFKEREdagkiivstsHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAY 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556423901 204 F--ELSLKPWDFAAGELIAREAGAIVCDFTgGHNYMSTGNVVAGNPrvvKAMLANMRDELSDALKR 267
Cdd:cd01640 232 VhsTGGIKKWDICAPEAILRALGGDMTDLH-GEPLSYSKAVKPVNK---GGLLATIRSNHEAYLDK 293
|
|
| |
