|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
9-254 |
5.18e-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: 350.68 E-value: 5.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQH-DRKVMTKSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEacvLTDSPTW 87
Cdd:cd01639 2 LNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 88 IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSR 167
Cdd:cd01639 79 IIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 168 dPEVVEKIFSSLKNILCIPVHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELDLMS 247
Cdd:cd01639 159 -GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
....*..
gi 1593659322 248 RRIVAAN 254
Cdd:cd01639 238 GNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
11-266 |
1.80e-97 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 287.32 E-value: 1.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 11 HAVALARRAGEVVREALQHDRKVMTKSCS--VDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDS-PTW 87
Cdd:pfam00459 8 VAVELAAKAGEILREAFSNKLTIEEKGKSgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDDgPTW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 88 IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSR 167
Cdd:pfam00459 88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTLFGVSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 168 DPEVVEKIFssLKNILC-IPVHGVRGAGTAAVNMCLVASGCVEAYYEMG-IHVWDVAAGSLIVSEAGGVLMDVDGGELDL 245
Cdd:pfam00459 168 RKDTSEASF--LAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGGPFDL 245
|
250 260
....*....|....*....|.
gi 1593659322 246 MSRRIVAANSRAVAERLVAEI 266
Cdd:pfam00459 246 LAGRVIAANPKVLHELLAAAL 266
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
12-264 |
3.08e-94 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 278.88 E-value: 3.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDRKVMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDSPTWIIDP 91
Cdd:PLN02553 14 AVDAAKAAGQIIRKGFYQTKHVEHKG-QVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDEPTWIVDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 92 IDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSRDPEV 171
Cdd:PLN02553 93 LDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKRDKAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 172 VEKIFSSLKNILcIPVHGVRGAGTAAVNMCLVASGCVEAYYEMGI-HVWDVAAGSLIVSEAGGVLMDVDGGELDLMSRRI 250
Cdd:PLN02553 173 VDATTNRINALL-YKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRV 251
|
250
....*....|....*..
gi 1593659322 251 VAANS---RAVAERLVA 264
Cdd:PLN02553 252 AASNGhlkDAFVEALRQ 268
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-268 |
1.75e-84 |
|
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: 253.61 E-value: 1.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 6 QNAMDHAVALARRAGEVVREALQH-DRKVMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEAcvlTDS 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR---DSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 85 PTWIIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFG 164
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 165 SSRDPEVVEKIFSSLKNilciPVHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELD 244
Cdd:COG0483 157 YLRDDREYLAALAALLP----RVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250 260
....*....|....*....|....
gi 1593659322 245 LMSRRIVAANsRAVAERLVAEIDA 268
Cdd:COG0483 233 LGSGSLVAAN-PALHDELLALLRE 255
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
12-266 |
8.57e-32 |
|
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: 118.18 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDRKVMTKSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEEsvaAGEACVLTDSPTWIIDP 91
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 92 IDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSRDPEV 171
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 172 VEKIFSSLKNILcipvhGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELdLMSRRIV 251
Cdd:TIGR02067 162 NRPAFERLRRAA-----RLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAV 235
|
250
....*....|....*
gi 1593659322 252 AANSRAVAeRLVAEI 266
Cdd:TIGR02067 236 AAGNAMLH-DEALEI 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
9-254 |
5.18e-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: 350.68 E-value: 5.18e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQH-DRKVMTKSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEacvLTDSPTW 87
Cdd:cd01639 2 LNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPTW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 88 IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSR 167
Cdd:cd01639 79 IIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 168 dPEVVEKIFSSLKNILCIPVHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELDLMS 247
Cdd:cd01639 159 -GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
....*..
gi 1593659322 248 RRIVAAN 254
Cdd:cd01639 238 GNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
11-266 |
1.80e-97 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 287.32 E-value: 1.80e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 11 HAVALARRAGEVVREALQHDRKVMTKSCS--VDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDS-PTW 87
Cdd:pfam00459 8 VAVELAAKAGEILREAFSNKLTIEEKGKSgaNDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTDDgPTW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 88 IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSR 167
Cdd:pfam00459 88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVTLFGVSS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 168 DPEVVEKIFssLKNILC-IPVHGVRGAGTAAVNMCLVASGCVEAYYEMG-IHVWDVAAGSLIVSEAGGVLMDVDGGELDL 245
Cdd:pfam00459 168 RKDTSEASF--LAKLLKlVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDADGGPFDL 245
|
250 260
....*....|....*....|.
gi 1593659322 246 MSRRIVAANSRAVAERLVAEI 266
Cdd:pfam00459 246 LAGRVIAANPKVLHELLAAAL 266
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
12-264 |
3.08e-94 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 278.88 E-value: 3.08e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDRKVMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDSPTWIIDP 91
Cdd:PLN02553 14 AVDAAKAAGQIIRKGFYQTKHVEHKG-QVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDEPTWIVDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 92 IDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSRDPEV 171
Cdd:PLN02553 93 LDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKRDKAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 172 VEKIFSSLKNILcIPVHGVRGAGTAAVNMCLVASGCVEAYYEMGI-HVWDVAAGSLIVSEAGGVLMDVDGGELDLMSRRI 250
Cdd:PLN02553 173 VDATTNRINALL-YKVRSLRMSGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRV 251
|
250
....*....|....*..
gi 1593659322 251 VAANS---RAVAERLVA 264
Cdd:PLN02553 252 AASNGhlkDAFVEALRQ 268
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-268 |
1.75e-84 |
|
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: 253.61 E-value: 1.75e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 6 QNAMDHAVALARRAGEVVREALQH-DRKVMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEAcvlTDS 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGR---DSG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 85 PTWIIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFG 164
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 165 SSRDPEVVEKIFSSLKNilciPVHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELD 244
Cdd:COG0483 157 YLRDDREYLAALAALLP----RVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250 260
....*....|....*....|....
gi 1593659322 245 LMSRRIVAANsRAVAERLVAEIDA 268
Cdd:COG0483 233 LGSGSLVAAN-PALHDELLALLRE 255
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
9-253 |
3.93e-74 |
|
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: 226.43 E-value: 3.93e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQHDRKVMTKSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEacVLTDSPTWI 88
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGN--VSDGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 89 IDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSRD 168
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 169 PEVveKIFSSlkniLCIPVHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELD-LMS 247
Cdd:cd01637 159 NRA--AVLAS----LVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtLNR 232
|
....*.
gi 1593659322 248 RRIVAA 253
Cdd:cd01637 233 SGIIAA 238
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
12-267 |
2.71e-57 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 187.70 E-value: 2.71e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDRKVMTKSCSvDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEacvlTDSP-TWIID 90
Cdd:PLN02737 83 AELAAKTGAEVVMEAVNKPRNISYKGLT-DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGD----SSSDyLWCID 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 91 PIDGTTNFVHAFPFVAVSIG--FSVNKQMQFGVVYS----CLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFG 164
Cdd:PLN02737 158 PLDGTTNFAHGYPSFAVSVGvlFRGTPAAATVVEFVggpmCWNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFG 237
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 165 SSRDPEVVEKI--FSSLKNIlcipVHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGE 242
Cdd:PLN02737 238 YEHDDAWATNIelFKEFTDV----SRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGK 313
|
250 260
....*....|....*....|....*
gi 1593659322 243 LDLMSRRIVAANSrAVAERLVAEID 267
Cdd:PLN02737 314 FSVFDRSVLVSNG-VLHPKLLDRIG 337
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
12-270 |
2.49e-50 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 166.52 E-value: 2.49e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDRKVMT-KSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESvaaGEACVLTDSPTWIID 90
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEAsQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 91 PIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEF------G 164
Cdd:PRK10757 85 PLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFpfkakqH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 165 SSRDPEVVEKIFSSLKNIlcipvhgvRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELD 244
Cdd:PRK10757 165 ATTYINIVGKLFTECADF--------RRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNY 236
|
250 260
....*....|....*....|....*.
gi 1593659322 245 LMSRRIVAANSRAVAERLVAEIDAFS 270
Cdd:PRK10757 237 MLTGNIVAGNPRVVKAMLANMRDELS 262
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
12-259 |
4.92e-45 |
|
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: 152.10 E-value: 4.92e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEvvrEALQHDRK---VMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEEsvaaGEACVLTDSPTWI 88
Cdd:cd01643 4 AEAIAQEAGD---RALADFGNslsAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 89 IDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGS-SR 167
Cdd:cd01643 76 IDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSrAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 168 DPEVVEKIFSSLknilciPVHgVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELDLMS 247
Cdd:cd01643 156 ARAVLRVILRRF------PGK-IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQT 228
|
250
....*....|..
gi 1593659322 248 RRIVAANSRAVA 259
Cdd:cd01643 229 KDYLSAGFPTLI 240
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
9-238 |
1.26e-44 |
|
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: 149.47 E-value: 1.26e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQHDRKVMT--KSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDSPT 86
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVkiTKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 87 WIIDPIDGTTNFVHAFPFVAVSIGfsvnkqmqfgvVYSCLedkmytarrgngafcngeplqvsqqqdvkqsmIATEFGSS 166
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIA-----------VYVIL--------------------------------ILAEPSHK 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593659322 167 RDPEVVEKIFsslknilCIPVHGVRGAGTAAVNMCLVASGCVEAYYEMGI--HVWDVAAGSLIVSEAGGVLMDV 238
Cdd:cd01636 118 RVDEKKAELQ-------LLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTDW 184
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
9-263 |
1.56e-38 |
|
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: 135.46 E-value: 1.56e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQHDRKVMTKSCSvDLVTQTDQKVETLIIQSVKEKFPTHRFIGEEsvaAGEACvlTDSP-TW 87
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKADF-SPVTEADRAAEAAMRELIAAAFPDHGILGEE---FGNEG--GDAGyVW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 88 IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCN---GEPLQVSQQQDVKQSMIAT--- 161
Cdd:cd01641 76 VLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTtdp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 162 EFGSSRDPEVVEKIFSSlknilcipvHGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGG 241
Cdd:cd01641 156 HFFTPGDRAAFERLARA---------VRLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGG 226
|
250 260
....*....|....*....|..
gi 1593659322 242 ELDLMSRRIVAANSRAVAERLV 263
Cdd:cd01641 227 PLTGGSGRVVAAGDAELHEALL 248
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
47-258 |
2.73e-37 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 132.72 E-value: 2.73e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 47 DQKVETLIIQSVKEKFPTHRFIGEEsvaAGEacVLTDSPTW--IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYS 124
Cdd:PRK12676 47 DKVAEDIILEVLKPLGRCVNIISEE---LGE--IVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 125 CLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATeFGSSRDPEVVEKIFSSLKNilcipvhgVRGAGTAAVNMCLVA 204
Cdd:PRK12676 122 LATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSI-YGYRRGKERTVKLGRKVRR--------VRILGAIALELCYVA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1593659322 205 SGCVEAYYEMG--IHVWDVAAGSLIVSEAGGVLMDVDGGELDL-----MSRRIVAANSRAV 258
Cdd:PRK12676 193 SGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvtERTNLIAANGEEL 253
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
10-243 |
1.80e-36 |
|
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: 130.04 E-value: 1.80e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 10 DHAVALARRAGEVVREALQHDRKVMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEacVLTDSPTWII 89
Cdd:cd01638 3 ELLIRIAREAGDAILEVYRGGFTVERKE-DGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFWLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 90 DPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGS-SRD 168
Cdd:cd01638 80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASrSHP 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1593659322 169 PEVVEKIFSSLKNILCIPVhgvrgaGTAAvNMCLVASGCVEAYYEMG-IHVWDVAAGSLIVSEAGGVLMDVDGGEL 243
Cdd:cd01638 160 DEELEALLAALGVAEVVSI------GSSL-KFCLVAEGEADIYPRLGpTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
9-257 |
3.03e-35 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 127.20 E-value: 3.03e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQHDRKVMTKS-CSVdlVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDSPTW 87
Cdd:COG1218 5 LEAAIEIAREAGEAILEIYRADFEVEEKAdDSP--VTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 88 IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFC-----NGEPLQVSQQQDVKQSMIATe 162
Cdd:COG1218 83 LVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPLRVVA- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 163 fgsSR---DPEvVEKIFSSLknilciPVHGVRGAGtAAVNMCLVASGCVEAYYEMG-IHVWDVAAGSLIVSEAGGVLMDV 238
Cdd:COG1218 162 ---SRshrDEE-TEALLARL------GVAELVSVG-SSLKFCLVAEGEADLYPRLGpTMEWDTAAGQAILEAAGGRVTDL 230
|
250 260
....*....|....*....|....*
gi 1593659322 239 DGGEL------DLMSRRIVAANSRA 257
Cdd:COG1218 231 DGKPLrynkkeDLLNPGFIASGDHA 255
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
12-266 |
8.57e-32 |
|
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: 118.18 E-value: 8.57e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDRKVMTKSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEEsvaAGEACVLTDSPTWIIDP 91
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 92 IDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATEFGSSRDPEV 171
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 172 VEKIFSSLKNILcipvhGVRGAGTAAVNMCLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLMDVDGGELdLMSRRIV 251
Cdd:TIGR02067 162 NRPAFERLRRAA-----RLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGGGAV 235
|
250
....*....|....*
gi 1593659322 252 AANSRAVAeRLVAEI 266
Cdd:TIGR02067 236 AAGNAMLH-DEALEI 249
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
9-245 |
9.42e-31 |
|
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: 115.87 E-value: 9.42e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEV----VREALQHDRKVMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAgeacvltDS 84
Cdd:cd01517 1 ELEVAILAVRAAASltlpVFRNLGAGDVVWKKS-DKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 85 PTWIIDPIDGTTNFVHAFPFvAVSIGFSVNKQMQFGVVYSCL-------EDKMYTARRGNGAFCN---GEPLQVSQQQDV 154
Cdd:cd01517 73 RFWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAWLRpldGSSLQPLSVRQL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 155 KQSMIATEFGSSRDPEVVEKIFSSLKNilcipvhgvRGAGTAAVNM------CLVASGCVEAY----YEMG--IHVWDVA 222
Cdd:cd01517 152 TNAARASFCESVESAHSSHRLQAAIKA---------LGGTPQPVRLdsqakyAAVARGAADFYlrlpLSMSyrEKIWDHA 222
|
250 260
....*....|....*....|...
gi 1593659322 223 AGSLIVSEAGGVLMDVDGGELDL 245
Cdd:cd01517 223 AGVLIVEEAGGKVTDADGKPLDF 245
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
47-257 |
4.17e-30 |
|
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: 113.63 E-value: 4.17e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 47 DQKVETLIIqSVKEKFPTHRFIGEESvaaGEAcVLTDSPTW--IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQ--FGVV 122
Cdd:cd01515 42 DKVAEDAAI-EILKKLGSVNIVSEEI---GVI-DNGDEPEYtvVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDpyYGYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 123 YSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIATeFGSSRDPEVVEKIfsslknilCIPVHGVRGAGTAAVNMCL 202
Cdd:cd01515 117 YNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSY-YIYGKNHDRTFKI--------CRKVRRVRIFGSVALELCY 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1593659322 203 VASGCVEAYYEM--GIHVWDVAAGSLIVSEAGGVLMDVDGGELDL----MSR-RIVAANSRA 257
Cdd:cd01515 188 VASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKELKLklnvTERvNIIAANSEL 249
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-244 |
1.39e-26 |
|
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: 104.07 E-value: 1.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 15 LARRAGEVVREALQHDRKVMTKSCSVDlVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDSPTWIIDPIDG 94
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKADNSP-VTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPLDG 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 95 TTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQ---SMIATEFGSSRDPEV 171
Cdd:TIGR01331 87 TKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKAPIHVRPwpsGPLLVVISRSHAEEK 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1593659322 172 VEKIFSSLKNILCIPvhgvrgaGTAAVNMCLVASGCVEAYYEMG-IHVWDVAAGSLIVSEAGGVLMDVDGGELD 244
Cdd:TIGR01331 167 TTEYLANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
51-264 |
1.20e-19 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 88.25 E-value: 1.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 51 ETLIIQSVkEKFPTHRFIGEEsvaAGEACVLTDSPTWI--IDPIDGTTNFVHAFPFVAVSI------GFSVNKQ------ 116
Cdd:PRK14076 50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIaiakidGFDKKIKefigkn 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 117 -----MQFGVVYSCLEDKMYTARRGNGAF----CNGEPLQVSQQQDVKQSMIAT-EFGSSRDpevvekifsSLKNILCIP 186
Cdd:PRK14076 126 ltindLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDASIGLfAYGLSLD---------TLKFIKDRK 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 187 VHGVRGAGTAAVNMCLVASGCVEAYYEM--GIHVWDVAAGSLIVSEAGGVLMDVDGGE----LDLMSRRIVAANSRAVAE 260
Cdd:PRK14076 197 VRRIRLFGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHK 276
|
....
gi 1593659322 261 RLVA 264
Cdd:PRK14076 277 KLVG 280
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
9-268 |
1.27e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 72.44 E-value: 1.27e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARR----AGEVVREALQHDRKVMTKScsvDL--VTQTDQKVETLIIQSVKEKFPTHRFIGEESvaaGEACVLT 82
Cdd:PLN02911 33 LDRFVDVAHKladaAGEVTRKYFRTKFEIIDKE---DLspVTIADRAAEEAMRSIILENFPSHAIFGEEH---GLRCGEG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 83 DSP-TWIIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLQVSQQQDVKQSMIAT 161
Cdd:PLN02911 107 SSDyVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYT 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 162 E----F-GSSRDPevvekiFSSLKNILCIPVHGVRGAGTAavnmcLVASGCVEAYYEMGIHVWDVAAGSLIVSEAGGVLM 236
Cdd:PLN02911 187 TsphmFsGDAEDA------FARVRDKVKVPLYGCDCYAYG-----LLASGHVDLVVESGLKPYDYLALVPVVEGAGGVIT 255
|
250 260 270
....*....|....*....|....*....|..
gi 1593659322 237 DVDGGELdlmsRRIVAANSRAVAERLVAEIDA 268
Cdd:PLN02911 256 DWKGRKL----RWEPSPGSLATSFNVVAAGDA 283
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
9-264 |
1.12e-13 |
|
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.
Pssm-ID: 273558 [Multi-domain] Cd Length: 353 Bit Score: 70.28 E-value: 1.12e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAG----EVVREALQHDRK-VMTKScSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEES----------- 72
Cdd:TIGR01330 6 LDVATQAVRLASlltkKVQSELISHKDStVITKD-DKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDssglseadftl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 73 -------------------------VAAGEACVLTDSPT---------WIIDPIDGTTNFVHAFPFvAVSIGFSVNKQMQ 118
Cdd:TIGR01330 85 grvnelvnetlvyaknykkddqfplKSLEDVLQIIDFGNyeggrkgrhWVLDPIDGTKGFLRGDQY-AVCLALIENGKVV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 119 FGVV--------YSCLEDK--------MYTARRGNGAFCNG------EPLQVsQQQDVKQSMIATEFgssrdpEVVEKIF 176
Cdd:TIGR01330 164 LGVIgcpnlplsSYGAQNLkgseskgcIFRAVRGSGAFMYSlssdaeSPTKV-HVSSVKDTKDAIFC------EGVEKGH 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 177 S------SLKNILcipvhGVRGAGT---AAVNMCLVASGCVEAYYEMGI------HVWDVAAGSLIVSEAGGVLMDVDGG 241
Cdd:TIGR01330 237 SshdeqtAIANKL-----GISKSPLrldSQAKYAALARGDADVYLRLPIklsyqeKIWDHAAGNVIVEEAGGIVTDAMGK 311
|
330 340 350
....*....|....*....|....*....|
gi 1593659322 242 ELDL-------MSRRIVAANSRAVAERLVA 264
Cdd:TIGR01330 312 PLDFgkgrtlaLDKGVIAASGPRVLHDLVV 341
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
12-245 |
9.19e-11 |
|
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: 61.18 E-value: 9.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 12 AVALARRAGEVVREALQHDR------KVMTKSCSVDLVTQTDQKVETLIIQSVKEKFPTHRFIGEESVAAGEACVLTDSP 85
Cdd:cd01640 5 LLAVAEKAGGIARDVVKKGRllillvEGKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 86 ------------------------TWiIDPIDGTTNFVHAFPF-VAVSIGFSVNKQMQFGVV----YSCLEDKMYTARR- 135
Cdd:cd01640 85 dldeeileescpspskdlpeedlgVW-VDPLDATQEYTEGLLEyVTVLIGVAVKGKPIAGVIhqpfYEKTAGAGAWLGRt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 136 -----GNGAFCNgeplQVSQQQDVKQSMIATEfGSSRDPEVVEKIFSSLKNILcipvhGVRGAGTAAVnmcLVASGCVEA 210
Cdd:cd01640 164 iwglsGLGAHSS----DFKEREDAGKIIVSTS-HSHSVKEVQLITAGNKDEVL-----RAGGAGYKVL---QVLEGLADA 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 1593659322 211 YY--EMGIHVWDVAAGSLIVSEAGGVLMDVDGGELDL 245
Cdd:cd01640 231 YVhsTGGIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
9-248 |
1.89e-10 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 59.71 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 9 MDHAVALARRAGEVVREALQHDR--KVMTKSCSVDlVTQTDQKVETLIIQSVKEKFPTHRFIGEEsvaageacvltDSPT 86
Cdd:PRK10931 2 LEQICQLARNAGDAIMQVYDGTKplDVASKADDSP-VTAADIAAHTVIKDGLRTLTPDIPVLSEE-----------DPPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 87 W----------IIDPIDGTTNFVHAFPFVAVSIGFSVNKQMQFGVVYSCLEDKMYTARRGNgAF--CNGEPLQVsQQQDV 154
Cdd:PRK10931 70 WevrqhwqrywLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI-QVRDA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 155 KQSMIATEfGSSRDPEVVE-----------KIFSSLKnilcipvhgvrgagtaavnMCLVASGCVEAYYEMG-IHVWDVA 222
Cdd:PRK10931 148 RPPLVVIS-RSHADAELKEylqqlgehqttSIGSSLK-------------------FCLVAEGQAQLYPRFGpTNIWDTA 207
|
250 260
....*....|....*....|....*.
gi 1593659322 223 AGSLIVSEAGGVLMDVDGGELDLMSR 248
Cdd:PRK10931 208 AGHAVAIAAGAHVHDWQGKTLDYTPR 233
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
41-232 |
5.42e-10 |
|
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: 58.23 E-value: 5.42e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 41 DLVTQTDQKVETLIIQSVKEKFPTHRFIGEESvaaGEACVLTDSPTWIIDPIDGTTNFVHAFPFVAVSIGF--------- 111
Cdd:cd01642 34 DVTRVADLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALadprskvka 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1593659322 112 ----SVNKQMQFGVVYSCLEDKMYTARRGNGAFCNGEPLqvsqqqdvkqSMIATEFGSSRDPevvEKIFSSLKNILcipv 187
Cdd:cd01642 111 atldNFVSGEGGLKVYSPPTRFSYISVPKLGPPLVPEVP----------SKIGIYEGSSRNP---EKFLLLSRNGL---- 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1593659322 188 hGVRGAGTAAVNMCLVASGCVEAYYEM--GIHVWDVAAGSLIVSEAG 232
Cdd:cd01642 174 -KFRSLGSAALELAYTCEGSFVLFLDLrgKLRNFDVAAALGACKRLG 219
|
|
| |
