|
Name |
Accession |
Description |
Interval |
E-value |
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
7-258 |
2.54e-94 |
|
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: 277.60 E-value: 2.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 7 DIYFLHKLADVADAETLPRFRShiDLEIQTKlkknVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAI-ENGEIR 85
Cdd:cd01641 1 DLAFALELADAAGQITLPYFRT--RLQVETK----ADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEgGDAGYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 86 WILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWSD-GESSFHQYNKVqKKLKIQRNKKISEAILHIN 164
Cdd:cd01641 75 WVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGArGGGTFLNGAGG-RPLRVRACADLAEAVLSTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 165 HPRSSNLYPHINFTELSEQVLMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH-KGG 243
Cdd:cd01641 154 DPHFFTPGDRAAFERLARAVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTgGSG 233
|
250
....*....|....*
gi 690994542 244 TIVAASSQSLHEQAL 258
Cdd:cd01641 234 RVVAAGDAELHEALL 248
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
10-262 |
2.41e-81 |
|
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: 244.52 E-value: 2.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 10 FLHKLADVADAETLPRFRSHiDLEIQTKLKKNvsfdPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIE--NGEIRWI 87
Cdd:TIGR02067 4 FAEDLADAAGETILPFFRAS-LLVVDKKSDKT----PVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEegDAERVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 88 LDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWSDGEssfHQYNKVQKKLKIQRNKKISEAILHINHPR 167
Cdd:TIGR02067 79 LDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGG---GAAFLGGRRLRVSSCANLSDAVLFTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 168 SsnLYP---HINFTELSEQVLMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAHKGGT 244
Cdd:TIGR02067 156 L--LDDpgnRPAFERLRRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGG 233
|
250
....*....|....*...
gi 690994542 245 IVAASSQSLHEQALKILN 262
Cdd:TIGR02067 234 AVAAGNAMLHDEALEILN 251
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-263 |
1.86e-80 |
|
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: 242.44 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 6 PDIYFLHKLADVADAETLPRFRShIDLEIQTKlkknVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIE--NGE 83
Cdd:COG0483 2 PLLELALRAARAAGALILRRFRE-LDLEVETK----GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEgrDSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 84 IRWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFW-SDGESSFHqyNKvqKKLKIQRNKKISEAILH 162
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTaARGGGAFL--NG--RRLRVSARTDLEDALVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 163 INHPRSSNLYPHIN-FTELSEQVL-MTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH 240
Cdd:COG0483 153 TGFPYLRDDREYLAaLAALLPRVRrVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250 260
....*....|....*....|...
gi 690994542 241 KGGTIVAASSQSLHEQALKILNS 263
Cdd:COG0483 233 LGSGSLVAANPALHDELLALLRE 255
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
5-261 |
9.11e-65 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 204.18 E-value: 9.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 5 FPDIY--FLHKLADVADAETLPRFRSHIDLEIqtklKKNVSfdPVTIADKAAEYAMRKMITEYYPDHSIMGEEFG-AIEN 81
Cdd:PLN02911 32 VLDRFvdVAHKLADAAGEVTRKYFRTKFEIID----KEDLS--PVTIADRAAEEAMRSIILENFPSHAIFGEEHGlRCGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 82 G--EIRWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERfW--SDGESSFhqYNKvqKKLKIQRNKKIS 157
Cdd:PLN02911 106 GssDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKER-WvgVAGRATT--LNG--EEISTRSCASLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 158 EAILHINHPR---SSNLYPhinFTELSEQVLMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTL 234
Cdd:PLN02911 181 DAYLYTTSPHmfsGDAEDA---FARVRDKVKVPLYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDW 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 690994542 235 DGSSAH---------KGGTIVAASSQSLHEQALKIL 261
Cdd:PLN02911 258 KGRKLRwepspgslaTSFNVVAAGDARLHKQALDIL 293
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-261 |
9.81e-44 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 149.03 E-value: 9.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 6 PDIYFLHKLADVADAETLPRFrsHIDLEIQTKLKKNVSfDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEIR 85
Cdd:pfam00459 4 EVLKVAVELAAKAGEILREAF--SNKLTIEEKGKSGAN-DLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 86 ------WILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWS-DGESSFhqYNkvQKKLKIQRNKKISE 158
Cdd:pfam00459 81 tddgptWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAaKGKGAF--LN--GQPLPVSRAPPLSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 159 AILHINHPRSSNlyPHINFTELSEQVL-------MTRYGAECYAFAMLAAGYIDICFEFS-LQPYDIAALIPIIENAGGV 230
Cdd:pfam00459 157 ALLVTLFGVSSR--KDTSEASFLAKLLklvrapgVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGV 234
|
250 260 270
....*....|....*....|....*....|..
gi 690994542 231 ISTLDGSS-AHKGGTIVAASSQSLHEQALKIL 261
Cdd:pfam00459 235 VTDADGGPfDLLAGRVIAANPKVLHELLAAAL 266
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
7-258 |
2.54e-94 |
|
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: 277.60 E-value: 2.54e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 7 DIYFLHKLADVADAETLPRFRShiDLEIQTKlkknVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAI-ENGEIR 85
Cdd:cd01641 1 DLAFALELADAAGQITLPYFRT--RLQVETK----ADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEgGDAGYV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 86 WILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWSD-GESSFHQYNKVqKKLKIQRNKKISEAILHIN 164
Cdd:cd01641 75 WVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGArGGGTFLNGAGG-RPLRVRACADLAEAVLSTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 165 HPRSSNLYPHINFTELSEQVLMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH-KGG 243
Cdd:cd01641 154 DPHFFTPGDRAAFERLARAVRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLTgGSG 233
|
250
....*....|....*
gi 690994542 244 TIVAASSQSLHEQAL 258
Cdd:cd01641 234 RVVAAGDAELHEALL 248
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
10-262 |
2.41e-81 |
|
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: 244.52 E-value: 2.41e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 10 FLHKLADVADAETLPRFRSHiDLEIQTKLKKNvsfdPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIE--NGEIRWI 87
Cdd:TIGR02067 4 FAEDLADAAGETILPFFRAS-LLVVDKKSDKT----PVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEegDAERVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 88 LDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWSDGEssfHQYNKVQKKLKIQRNKKISEAILHINHPR 167
Cdd:TIGR02067 79 LDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGG---GAAFLGGRRLRVSSCANLSDAVLFTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 168 SsnLYP---HINFTELSEQVLMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAHKGGT 244
Cdd:TIGR02067 156 L--LDDpgnRPAFERLRRAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDGGG 233
|
250
....*....|....*...
gi 690994542 245 IVAASSQSLHEQALKILN 262
Cdd:TIGR02067 234 AVAAGNAMLHDEALEILN 251
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-263 |
1.86e-80 |
|
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: 242.44 E-value: 1.86e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 6 PDIYFLHKLADVADAETLPRFRShIDLEIQTKlkknVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIE--NGE 83
Cdd:COG0483 2 PLLELALRAARAAGALILRRFRE-LDLEVETK----GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEgrDSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 84 IRWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFW-SDGESSFHqyNKvqKKLKIQRNKKISEAILH 162
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTaARGGGAFL--NG--RRLRVSARTDLEDALVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 163 INHPRSSNLYPHIN-FTELSEQVL-MTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH 240
Cdd:COG0483 153 TGFPYLRDDREYLAaLAALLPRVRrVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250 260
....*....|....*....|...
gi 690994542 241 KGGTIVAASSQSLHEQALKILNS 263
Cdd:COG0483 233 LGSGSLVAANPALHDELLALLRE 255
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
5-261 |
9.11e-65 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 204.18 E-value: 9.11e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 5 FPDIY--FLHKLADVADAETLPRFRSHIDLEIqtklKKNVSfdPVTIADKAAEYAMRKMITEYYPDHSIMGEEFG-AIEN 81
Cdd:PLN02911 32 VLDRFvdVAHKLADAAGEVTRKYFRTKFEIID----KEDLS--PVTIADRAAEEAMRSIILENFPSHAIFGEEHGlRCGE 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 82 G--EIRWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERfW--SDGESSFhqYNKvqKKLKIQRNKKIS 157
Cdd:PLN02911 106 GssDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKER-WvgVAGRATT--LNG--EEISTRSCASLK 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 158 EAILHINHPR---SSNLYPhinFTELSEQVLMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTL 234
Cdd:PLN02911 181 DAYLYTTSPHmfsGDAEDA---FARVRDKVKVPLYGCDCYAYGLLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDW 257
|
250 260 270
....*....|....*....|....*....|....*.
gi 690994542 235 DGSSAH---------KGGTIVAASSQSLHEQALKIL 261
Cdd:PLN02911 258 KGRKLRwepspgslaTSFNVVAAGDARLHKQALDIL 293
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
10-248 |
3.73e-55 |
|
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: 177.51 E-value: 3.73e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 10 FLHKLADVADAETLPRFRSHIDLEIqtklkKNVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGA---IENGEIRW 86
Cdd:cd01637 3 LALKAVREAGALILEAFGEELTVET-----KKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGsgnVSDGGRVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 87 ILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFW-SDGESSFhqYNKvqKKLKIQRNKKISEAILhINH 165
Cdd:cd01637 78 VIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYaGRGKGAF--LNG--KKLPLSKDTPLNDALL-STN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 166 PRSSNLYPHINFTELSEQVLMTR-YGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH--KG 242
Cdd:cd01637 153 ASMLRSNRAAVLASLVNRALGIRiYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtlNR 232
|
....*.
gi 690994542 243 GTIVAA 248
Cdd:cd01637 233 SGIIAA 238
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
20-250 |
5.23e-46 |
|
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: 154.23 E-value: 5.23e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 20 AETLPRFRSHIDLEIQTKLKKNvsfDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIE--NGEIRWILDPIDGTRPY 97
Cdd:cd01639 13 GEILLEAYEKLGLNVEEKGSPV---DLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGglTDEPTWIIDPLDGTTNF 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 98 LLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFW-SDGESSFhqYNkvQKKLKIQRNKKISEAILHINHPRSSNLYPHIN 176
Cdd:cd01639 90 VHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTaVRGQGAF--LN--GRRIRVSGRKELKDALVATGFPYDRGDNFDRY 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 690994542 177 FTELSEQVLMT-----RYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAHKGGTIVAASS 250
Cdd:cd01639 166 LNNFAKLLAKAvrgvrRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMSGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-261 |
9.81e-44 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 149.03 E-value: 9.81e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 6 PDIYFLHKLADVADAETLPRFrsHIDLEIQTKLKKNVSfDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEIR 85
Cdd:pfam00459 4 EVLKVAVELAAKAGEILREAF--SNKLTIEEKGKSGAN-DLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 86 ------WILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWS-DGESSFhqYNkvQKKLKIQRNKKISE 158
Cdd:pfam00459 81 tddgptWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAaKGKGAF--LN--GQPLPVSRAPPLSE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 159 AILHINHPRSSNlyPHINFTELSEQVL-------MTRYGAECYAFAMLAAGYIDICFEFS-LQPYDIAALIPIIENAGGV 230
Cdd:pfam00459 157 ALLVTLFGVSSR--KDTSEASFLAKLLklvrapgVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGV 234
|
250 260 270
....*....|....*....|....*....|..
gi 690994542 231 ISTLDGSS-AHKGGTIVAASSQSLHEQALKIL 261
Cdd:pfam00459 235 VTDADGGPfDLLAGRVIAANPKVLHELLAAAL 266
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
10-240 |
1.27e-31 |
|
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: 116.67 E-value: 1.27e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 10 FLHKLADVADAETLPRFRSHIDleIQTKLKKnvsfDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEIR-WIL 88
Cdd:cd01643 3 LAEAIAQEAGDRALADFGNSLS--AETKADG----SLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWyWVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 89 DPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWS-DGESSFhqYNKvqKKLKIQRNKKISEAILHINhpR 167
Cdd:cd01643 77 DPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAfKGGGAF--LNG--KPLALHPPLQLPDCNVGFN--R 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 690994542 168 SSNLYPHINFTELSEQV--LMTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH 240
Cdd:cd01643 151 SSRASARAVLRVILRRFpgKIRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAF 225
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
40-234 |
1.59e-31 |
|
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: 114.80 E-value: 1.59e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 40 KNVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEIR-----WILDPIDGTRPYLLGIPVWGTLIGLehnd 114
Cdd:cd01636 30 TKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRrdeytWVIDPIDGTKNFINGLPFVAVVIAV---- 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 115 kmclgmlsqpFTNERFWSDGESSFHQYNKVQKKLKIQRnkkiseailhinhprssnlyphinftelseqvlMTRYGAECY 194
Cdd:cd01636 106 ----------YVILILAEPSHKRVDEKKAELQLLAVYR---------------------------------IRIVGSAVA 142
|
170 180 190 200
....*....|....*....|....*....|....*....|..
gi 690994542 195 AFAMLAAGYIDICFEF--SLQPYDIAALIPIIENAGGVISTL 234
Cdd:cd01636 143 KMCLVALGLADIYYEPggKRRAWDVAASAAIVREAGGIMTDW 184
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
13-261 |
1.73e-21 |
|
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: 90.45 E-value: 1.73e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 13 KLADVADAETLPRFRSHIDLEIQTKlkKNvSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEfGAIENGEIrWILDPID 92
Cdd:cd01517 7 LAVRAAASLTLPVFRNLGAGDVVWK--KS-DKSPVTVADYGAQALITAALARLFPSDPIVGEE-DSAALGRF-WVLDPID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 93 GTRPYLLGIPvWGTLIGLEHNDKMCLGMLSQPFTNERFWSDG-------------ESSFHqyNKVQKKLKIQRNKKISEA 159
Cdd:cd01517 82 GTKGFLRGDQ-FAVALALIEDGEVVLGVIGCPNLPLDDGGGGdlfsavrgqgawlRPLDG--SSLQPLSVRQLTNAARAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 160 ILhiNHPRSSNLypHINFTELSEQVLMTRYGAECYA---FAMLAAG----YIDICFEFSLQ--PYDIAALIPIIENAGGV 230
Cdd:cd01517 159 FC--ESVESAHS--SHRLQAAIKALGGTPQPVRLDSqakYAAVARGaadfYLRLPLSMSYRekIWDHAAGVLIVEEAGGK 234
|
250 260 270
....*....|....*....|....*....|....*...
gi 690994542 231 ISTLDGSS--AHKGGTI-----VAASSQSLHEQALKIL 261
Cdd:cd01517 235 VTDADGKPldFGKGRKLlnnggLIAAPGEIHEQVLEAL 272
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
11-237 |
1.71e-19 |
|
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: 84.58 E-value: 1.71e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 11 LHKLADVADAETLPRFRSHIDLEIqtklKKNVSfdPVTIADKAAEYAMRKMITEYYPDHSIMGEEfgAIENGEIR----- 85
Cdd:cd01638 5 LIRIAREAGDAILEVYRGGFTVER----KEDGS--PVTAADLAANAFIVEGLAALRPDIPVLSEE--SADDPLRLgwdrf 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 86 WILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGMLSQPFTNERFWSDGESSFHQYNKVQKKLKIQRNKKISEAILHI-- 163
Cdd:cd01638 77 WLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVAsr 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 164 NHPrssnlyphinfTELSEQVLMTRYGAEC------YAFAMLAAGYIDICFEFSLQP-YDIAALIPIIENAGGVISTLDG 236
Cdd:cd01638 157 SHP-----------DEELEALLAALGVAEVvsigssLKFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDG 225
|
.
gi 690994542 237 S 237
Cdd:cd01638 226 S 226
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
40-258 |
6.88e-19 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 84.85 E-value: 6.88e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 40 KNVSF----DPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIEN--GEIRWILDPIDGTRPYLLGIPVWGTLIGLEHN 113
Cdd:PLN02737 102 RNISYkgltDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDssSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFR 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 114 DKMCLG----MLSQPFT-NERFWS--DGESSFHQYNK--VQKKLKIQRNKKISEAILHINHPRSSNLYPHINFTELSEQV 184
Cdd:PLN02737 182 GTPAAAtvveFVGGPMCwNTRTFSasAGGGAFCNGQKihVSQTDKVERSLLVTGFGYEHDDAWATNIELFKEFTDVSRGV 261
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 690994542 185 lmTRYGAECYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAHKGGTIVAASSQSLHEQAL 258
Cdd:PLN02737 262 --RRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLVSNGVLHPKLL 333
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
38-262 |
2.61e-18 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 81.88 E-value: 2.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 38 LKKNVSFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEIRW--ILDPIDGTRPYLLGIPVWGTLIGLEHNDK 115
Cdd:PRK12676 34 VGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGK 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 116 MCLGMLSQPFTNERFWSD-GESSFHQynkvQKKLKIQRNKKISE--AILHINHPRSSNLyphinfTELSEQVLMTR-YGA 191
Cdd:PRK12676 114 PVYGYVYNLATGDFYEAIpGKGAYLN----GKPIKVSKTSELNEsaVSIYGYRRGKERT------VKLGRKVRRVRiLGA 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 690994542 192 ECYAFAMLAAGYIDICFEF--SLQPYDIAALIPIIENAGGVISTLDGS------SAHKGGTIVAASSQSLHEQALKILN 262
Cdd:PRK12676 184 IALELCYVASGRLDAFVDVrnYLRVTDIAAGKLICEEAGGIVTDEDGNelklplNVTERTNLIAANGEELHKKILELLE 262
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
43-249 |
3.73e-18 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 81.39 E-value: 3.73e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 43 SFDPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAI--ENGEIRWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLGM 120
Cdd:PRK10757 36 SNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELegEDQDVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 121 LSQPFTNERFWSD-GESSfhQYNKVqkKLKIQRNKKISEAILHINHPRSSNLY--PHIN-----FTELSEqvlMTRYGAE 192
Cdd:PRK10757 116 VYDPMRNELFTATrGQGA--QLNGY--RLRGSTARDLDGTILATGFPFKAKQHatTYINivgklFTECAD---FRRTGSA 188
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 690994542 193 CYAFAMLAAGYIDICFEFSLQPYDIAALIPIIENAGGVISTLDGSSAH-KGGTIVAAS 249
Cdd:PRK10757 189 ALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYmLTGNIVAGN 246
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
45-261 |
3.59e-17 |
|
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: 78.57 E-value: 3.59e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 45 DPVTIADKAAEYAMRKMITEYYPdHSIMGEEFGAIENG---EIRWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCL--G 119
Cdd:cd01515 36 TPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIDNGdepEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPyyG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 120 MLSQPFTNERFWSD-GESSFhqynkvqkklkiqRN-KKISEAILHINHPRSSNLYP----HINFTELSEQVLMTR-YGAE 192
Cdd:cd01515 115 YVYNLATGDLYYAIkGKGAY-------------LNgKRIKVSDFSSLKSISVSYYIygknHDRTFKICRKVRRVRiFGSV 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 690994542 193 CYAFAMLAAGYIDICFEF--SLQPYDIAALIPIIENAGGVISTLDGS------SAHKGGTIVAASSQsLHEQALKIL 261
Cdd:cd01515 182 ALELCYVASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKelklklNVTERVNIIAANSE-LHKKLLELL 257
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
45-261 |
5.40e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 69.72 E-value: 5.40e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 45 DPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEI-----RWILDPIDGTRPYLLGIPVWGTLIGLEHNDKMCLG 119
Cdd:PLN02553 42 DLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTEltdepTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVG 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 120 MLSQPFTNERFWS-DGESSFhqYNKvqKKLKIQRNKKISEAIL--HINHPRSS----NLYPHINftELSEQVLMTRYGAE 192
Cdd:PLN02553 122 VVYNPILDELFTAvKGKGAF--LNG--KPIKASSQSELGKALLatEVGTKRDKatvdATTNRIN--ALLYKVRSLRMSGS 195
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 690994542 193 CyAFAM--LAAGYIDICFEFSL-QPYDIAALIPIIENAGGVISTLDGSSAHKGGTIVAASSQSLHEQALKIL 261
Cdd:PLN02553 196 C-ALNLcgVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRVAASNGHLKDAFVEAL 266
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
29-237 |
1.49e-11 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 62.87 E-value: 1.49e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 29 HIDLEIQTKLKKnvsfDPVTIADKAAEYAMRKMITEYYPDHSIMGEEfGAIENGEIR------WILDPIDGTRPYLLGIP 102
Cdd:COG1218 24 RADFEVEEKADD----SPVTEADLAAHAIILAGLAALTPDIPVLSEE-SAAIPYEERkswdrfWLVDPLDGTKEFIKRNG 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 103 ---VwgtLIGLEHNDKMCLGMLSQPFTNERFW-SDGESSFHQYNKVQ-KKLKIQRNKKISEAILHINhpRSsnlypHINf 177
Cdd:COG1218 99 eftV---NIALIEDGRPVLGVVYAPALGRLYYaAKGQGAFKETGGGErQPIRVRDRPPAEPLRVVAS--RS-----HRD- 167
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 690994542 178 tELSEQVLMTRYGAECYA------FAMLAAGYIDICFEFSlqP---YDIAALIPIIENAGGVISTLDGS 237
Cdd:COG1218 168 -EETEALLARLGVAELVSvgsslkFCLVAEGEADLYPRLG--PtmeWDTAAGQAILEAAGGRVTDLDGK 233
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
27-251 |
1.79e-08 |
|
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: 54.25 E-value: 1.79e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 27 RSHIDLEIQTKLKKNVSF--DPVTIADKAAEYAMRKMITEYYPDHSIMGEEFGAIENGEIRWI----------------- 87
Cdd:cd01640 20 VKKGRLLILLVEGKTKEGanDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRdvdldeeileescpsps 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 88 -----------LDPIDGTRPYLLGIP--VwGTLIGLEHNDKMCLGMLSQPFTNERFWSDGESSFHQYNKVQKKLKIQRNK 154
Cdd:cd01640 100 kdlpeedlgvwVDPLDATQEYTEGLLeyV-TVLIGVAVKGKPIAGVIHQPFYEKTAGAGAWLGRTIWGLSGLGAHSSDFK 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 155 KISEAILHINHPRSSNLYPHINFTELSEQV-LMTRYGAECYAF---AMLAAGYIDIcfEFSLQPYDIAALIPIIENAGGV 230
Cdd:cd01640 179 EREDAGKIIVSTSHSHSVKEVQLITAGNKDeVLRAGGAGYKVLqvlEGLADAYVHS--TGGIKKWDICAPEAILRALGGD 256
|
250 260 270
....*....|....*....|....*....|
gi 690994542 231 ISTL---------DGSSAHKGGTIVAASSQ 251
Cdd:cd01640 257 MTDLhgeplsyskAVKPVNKGGLLATIRSN 286
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
45-219 |
2.06e-06 |
|
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: 47.44 E-value: 2.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 45 DPVTIADKAAEyamrkmitEYYPDHSIMGEEFGAI---ENGEIRW-------ILDPIDGTRPYLLGIPVWGTLIGL-EHN 113
Cdd:cd01642 34 DVTRVADLKAE--------EIILKLLREEGVFGQIiseESGEIRKgsgeyiaVLDPLDGSTNYLSGIPFYSVSVALaDPR 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 690994542 114 DKMCLGMLSQpftnerFWSdGESSFHQYNKVQKKLKIQRNKKisEAILHINHP------RSSNLYPHInFTELSEQVLMT 187
Cdd:cd01642 106 SKVKAATLDN------FVS-GEGGLKVYSPPTRFSYISVPKL--GPPLVPEVPskigiyEGSSRNPEK-FLLLSRNGLKF 175
|
170 180 190
....*....|....*....|....*....|....*
gi 690994542 188 R-YGAECYAFAMLAAGYIDICFE--FSLQPYDIAA 219
Cdd:cd01642 176 RsLGSAALELAYTCEGSFVLFLDlrGKLRNFDVAA 210
|
|
| |
