|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
11-259 |
1.00e-105 |
|
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: 307.16 E-value: 1.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 11 LYDFIYPLAVRAGEILLEGYQNAGKAVALKdGEFYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNdnvtkELTD 90
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEK-GSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG-----GLTD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 91 APTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEV 170
Cdd:cd01639 75 EPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 171 CLLHAPKIRNK---HIKRIYHVGSNARRLlaYSAVVDsLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGG 247
Cdd:cd01639 155 PYDRGDNFDRYlnnFAKLLAKAVRGVRRL--GSAALD-LAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGG 231
|
250
....*....|..
gi 24664918 248 PFDIMKPDLICA 259
Cdd:cd01639 232 PFDLMSGNILAG 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
9-277 |
1.65e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 272.30 E-value: 1.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 9 EELYDFIYPLAVRAGEILLEGYQNAGKAVALKDGEFYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNDNVTKEl 88
Cdd:pfam00459 3 EEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 89 TDAPTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAY 168
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 169 EVCLLHAPKIRNKHIKRIYHVGSNAR--RLLAYSAVvdSLCMVAAGNLDAFH-IEDMYPWDCAAGYLLIREAGGVVTHPY 245
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRAPgvRRVGSAAL--KLAMVAAGKADAYIeFGRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260 270
....*....|....*....|....*....|..
gi 24664918 246 GGPFDIMKPDLICAGTETLRAEIEHLIRKADQ 277
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
9-274 |
9.74e-79 |
|
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: 238.98 E-value: 9.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 9 EELYDFIYPLAVRAGEILLEGYQNAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHkndnvTKEL 88
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDLEVETKGDG--DLVTEADRAAEAAIRERLRAAFPDHGILGEESGA-----SEGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 89 TDAPTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAY 168
Cdd:COG0483 74 DSGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 169 EVCLLHAPKIRNKHIKRIYHVGSNARRLlaYSAVVDsLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGGP 248
Cdd:COG0483 154 GFPYLRDDREYLAALAALLPRVRRVRRL--GSAALD-LAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEP 230
|
250 260
....*....|....*....|....*.
gi 24664918 249 FDIMKPDLIcAGTETLRAEIEHLIRK 274
Cdd:COG0483 231 LDLGSGSLV-AANPALHDELLALLRE 255
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
19-271 |
5.52e-65 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 204.54 E-value: 5.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 19 AVRAGEILLEGYqNAGKAVALKDGefYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNDnvTKELTDAPTWIIDP 98
Cdd:PLN02553 18 AKAAGQIIRKGF-YQTKHVEHKGQ--VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASG--GTELTDEPTWIVDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 99 IDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVCLLHAPKI 178
Cdd:PLN02553 93 LDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKRDKAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 179 RNKHIKRIYHVGSNARRLLAYSAVVDSLCMVAAGNLDAFHiEDMY--PWDCAAGYLLIREAGGVVTHPYGGPFDIMKPDL 256
Cdd:PLN02553 173 VDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFY-EIGFggPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRV 251
|
250
....*....|....*
gi 24664918 257 ICAGTETLRAEIEHL 271
Cdd:PLN02553 252 AASNGHLKDAFVEAL 266
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
14-268 |
7.59e-38 |
|
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: 133.97 E-value: 7.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 14 FIYPLAVRAGEILLEGYQNAGKAVALKDGEFynVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKndnvtkELTDAP- 92
Cdd:TIGR02067 4 FAEDLADAAGETILPFFRASLLVVDKKSDKT--PVTEADRAAEEAMRELIAAFFPDHGILGEEFGHN------EEGDAEr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 93 TWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVCL 172
Cdd:TIGR02067 76 VWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 173 LHAPKIRNKHIKRIYhvgsNARRLLAYSAVVDSLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGGPFdIM 252
Cdd:TIGR02067 156 LLDDPGNRPAFERLR----RAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PD 230
|
250
....*....|....*.
gi 24664918 253 KPDLICAGTETLRAEI 268
Cdd:TIGR02067 231 GGGAVAAGNAMLHDEA 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
11-259 |
1.00e-105 |
|
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: 307.16 E-value: 1.00e-105
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 11 LYDFIYPLAVRAGEILLEGYQNAGKAVALKdGEFYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNdnvtkELTD 90
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLGLNVEEK-GSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG-----GLTD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 91 APTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEV 170
Cdd:cd01639 75 EPTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 171 CLLHAPKIRNK---HIKRIYHVGSNARRLlaYSAVVDsLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGG 247
Cdd:cd01639 155 PYDRGDNFDRYlnnFAKLLAKAVRGVRRL--GSAALD-LAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGG 231
|
250
....*....|..
gi 24664918 248 PFDIMKPDLICA 259
Cdd:cd01639 232 PFDLMSGNILAG 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
9-277 |
1.65e-91 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 272.30 E-value: 1.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 9 EELYDFIYPLAVRAGEILLEGYQNAGKAVALKDGEFYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNDNVTKEl 88
Cdd:pfam00459 3 EEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELT- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 89 TDAPTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAY 168
Cdd:pfam00459 82 DDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLVT 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 169 EVCLLHAPKIRNKHIKRIYHVGSNAR--RLLAYSAVvdSLCMVAAGNLDAFH-IEDMYPWDCAAGYLLIREAGGVVTHPY 245
Cdd:pfam00459 162 LFGVSSRKDTSEASFLAKLLKLVRAPgvRRVGSAAL--KLAMVAAGKADAYIeFGRLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260 270
....*....|....*....|....*....|..
gi 24664918 246 GGPFDIMKPDLICAGTETLRAEIEHLIRKADQ 277
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
9-274 |
9.74e-79 |
|
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: 238.98 E-value: 9.74e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 9 EELYDFIYPLAVRAGEILLEGYQNAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHkndnvTKEL 88
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDLEVETKGDG--DLVTEADRAAEAAIRERLRAAFPDHGILGEESGA-----SEGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 89 TDAPTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAY 168
Cdd:COG0483 74 DSGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVAT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 169 EVCLLHAPKIRNKHIKRIYHVGSNARRLlaYSAVVDsLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGGP 248
Cdd:COG0483 154 GFPYLRDDREYLAALAALLPRVRRVRRL--GSAALD-LAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEP 230
|
250 260
....*....|....*....|....*.
gi 24664918 249 FDIMKPDLIcAGTETLRAEIEHLIRK 274
Cdd:COG0483 231 LDLGSGSLV-AANPALHDELLALLRE 255
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
19-271 |
5.52e-65 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 204.54 E-value: 5.52e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 19 AVRAGEILLEGYqNAGKAVALKDGefYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNDnvTKELTDAPTWIIDP 98
Cdd:PLN02553 18 AKAAGQIIRKGF-YQTKHVEHKGQ--VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASG--GTELTDEPTWIVDP 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 99 IDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVCLLHAPKI 178
Cdd:PLN02553 93 LDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKRDKAT 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 179 RNKHIKRIYHVGSNARRLLAYSAVVDSLCMVAAGNLDAFHiEDMY--PWDCAAGYLLIREAGGVVTHPYGGPFDIMKPDL 256
Cdd:PLN02553 173 VDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFY-EIGFggPWDVAAGAVIVKEAGGLVFDPSGGPFDIMSRRV 251
|
250
....*....|....*
gi 24664918 257 ICAGTETLRAEIEHL 271
Cdd:PLN02553 252 AASNGHLKDAFVEAL 266
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
12-242 |
3.21e-59 |
|
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: 188.68 E-value: 3.21e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 12 YDFIYPLAVRAGEILLEGYQNAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNdnvtKELTDA 91
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDG--DLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSG----NVSDGG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 92 PTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVc 171
Cdd:cd01637 75 RVWVIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNA- 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24664918 172 llhAPKIRNKHIKRIyHVGSNARRLLAYSAVVDSLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVT 242
Cdd:cd01637 154 ---SMLRSNRAAVLA-SLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVT 220
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
13-266 |
1.41e-42 |
|
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: 145.94 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 13 DFIYPLAVRAGEILLEGYQNAGKAVALKDGEFynvVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHkndnvTKELTDAp 92
Cdd:cd01643 2 SLAEAIAQEAGDRALADFGNSLSAETKADGSL---VTAADRWVEQLIRARLAAQFPDDGVLGEEGGG-----IFPSSGW- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 93 TWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVC- 171
Cdd:cd01643 73 YWVIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSs 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 172 -LLHAPKIRNKHIKRIYHVgsnarRLLAYSAVvdSLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGGPFD 250
Cdd:cd01643 153 rASARAVLRVILRRFPGKI-----RMLGSASL--NLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAF 225
|
250
....*....|....*.
gi 24664918 251 IMKPDLICAGTETLRA 266
Cdd:cd01643 226 LQTKDYLSAGFPTLIA 241
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
11-257 |
8.64e-42 |
|
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: 143.91 E-value: 8.64e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 11 LYDFIYPLAVRAGEILLEgYQNAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHkndnvTKELTD 90
Cdd:cd01638 1 LLELLIRIAREAGDAILE-VYRGGFTVERKEDG--SPVTAADLAANAFIVEGLAALRPDIPVLSEESAD-----DPLRLG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 91 APT-WIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSscehLNDANVAYE 169
Cdd:cd01638 73 WDRfWLVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVS----LQARPPPLQ 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 170 VCLL-----HAPKIR------NKHIKRIyHVGSNARrllaysavvdsLCMVAAGNLDA-FHIEDMYPWDCAAGYLLIREA 237
Cdd:cd01638 149 PLRVvasrsHPDEELeallaaLGVAEVV-SIGSSLK-----------FCLVAEGEADIyPRLGPTMEWDTAAGDAVLRAA 216
|
250 260
....*....|....*....|
gi 24664918 238 GGVVTHPYGGPFDIMKPDLI 257
Cdd:cd01638 217 GGAVSDLDGSPLTYNREDFL 236
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
14-268 |
7.59e-38 |
|
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: 133.97 E-value: 7.59e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 14 FIYPLAVRAGEILLEGYQNAGKAVALKDGEFynVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKndnvtkELTDAP- 92
Cdd:TIGR02067 4 FAEDLADAAGETILPFFRASLLVVDKKSDKT--PVTEADRAAEEAMRELIAAFFPDHGILGEEFGHN------EEGDAEr 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 93 TWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVCL 172
Cdd:TIGR02067 76 VWVLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 173 LHAPKIRNKHIKRIYhvgsNARRLLAYSAVVDSLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGGPFdIM 252
Cdd:TIGR02067 156 LLDDPGNRPAFERLR----RAARLTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PD 230
|
250
....*....|....*.
gi 24664918 253 KPDLICAGTETLRAEI 268
Cdd:TIGR02067 231 GGGAVAAGNAMLHDEA 246
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
13-268 |
3.23e-37 |
|
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: 131.99 E-value: 3.23e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 13 DFIYPLAVRAGEILLEGYQnAGKAVALKDGefYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEdtHKNDNvtkelTDAP 92
Cdd:cd01641 3 AFALELADAAGQITLPYFR-TRLQVETKAD--FSPVTEADRAAEAAMRELIAAAFPDHGILGEE--FGNEG-----GDAG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 93 -TWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCN---GKPIQVSSCEHLNDANVAY 168
Cdd:cd01641 73 yVWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLST 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 169 EvcllhAPKIRNKHIKRIYHVGSNARRLLAYsaVVD--SLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYG 246
Cdd:cd01641 153 T-----DPHFFTPGDRAAFERLARAVRLTRY--GGDcyAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDG 225
|
250 260
....*....|....*....|..
gi 24664918 247 GPFDIMKPDLICAGTETLRAEI 268
Cdd:cd01641 226 GPLTGGSGRVVAAGDAELHEAL 247
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
19-247 |
3.98e-37 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 132.62 E-value: 3.98e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 19 AVRAGEILLEGYQNAGKAVALKDGEfYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEdthKNDNVTKEltDAPTWIIDP 98
Cdd:PRK10757 12 ARKAGNLIAKNYETPDAVEASQKGS-NDFVTNVDKAAEAVIIDTIRKSYPQHTIITEE---SGELEGED--QDVQWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 99 IDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVCL---LHA 175
Cdd:PRK10757 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFPFkakQHA 165
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24664918 176 PKIRNKhIKRIYHVGSNARRllAYSAVVDsLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGG 247
Cdd:PRK10757 166 TTYINI-VGKLFTECADFRR--TGSAALD-LAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGG 233
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
9-260 |
9.80e-37 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 131.05 E-value: 9.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 9 EELYDFIYPLAVRAGEILLEgYQNAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNDnvTKEL 88
Cdd:COG1218 2 EALLEAAIEIAREAGEAILE-IYRADFEVEEKADD--SPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPY--EERK 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 89 TDAPTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFC-----NGKPIQVSSCE---- 159
Cdd:COG1218 77 SWDRFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPpaep 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 160 --------HLNDANVAYevcllhapkIRNKHIKRIYHVGSnarrllaysavvdSL--CMVAAGnlDAfhieDMYP----- 224
Cdd:COG1218 157 lrvvasrsHRDEETEAL---------LARLGVAELVSVGS-------------SLkfCLVAEG--EA----DLYPrlgpt 208
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 24664918 225 --WDCAAGYLLIREAGGVVTHPYGGPF------DIMKPDLICAG 260
Cdd:COG1218 209 meWDTAAGQAILEAAGGRVTDLDGKPLrynkkeDLLNPGFIASG 252
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
93-274 |
1.23e-35 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 128.49 E-value: 1.23e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 93 TWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVA-Yevc 171
Cdd:PRK12676 83 TVVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSiY--- 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 172 llhapkIRNKHIKRIYHVGSNARRLLAYSAVVDSLCMVAAGNLDAFHieDMYPW----DCAAGYLLIREAGGVVTHPYGG 247
Cdd:PRK12676 160 ------GYRRGKERTVKLGRKVRRVRILGAIALELCYVASGRLDAFV--DVRNYlrvtDIAAGKLICEEAGGIVTDEDGN 231
|
170 180 190
....*....|....*....|....*....|..
gi 24664918 248 PFDI-----MKPDLICAGTETLRAEIEHLIRK 274
Cdd:PRK12676 232 ELKLplnvtERTNLIAANGEELHKKILELLEG 263
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
93-262 |
2.02e-31 |
|
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: 117.09 E-value: 2.02e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 93 TWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVL--GVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEV 170
Cdd:cd01515 78 TVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPyyGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSYYI 157
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 171 cllhaPKIRNKHIKRIYhvgSNARRLLAYSAVVDSLCMVAAGNLDAFH--IEDMYPWDCAAGYLLIREAGGVVTHPYGGP 248
Cdd:cd01515 158 -----YGKNHDRTFKIC---RKVRRVRIFGSVALELCYVASGALDAFVdvRENLRLVDIAAGYLIAEEAGGIVTDENGKE 229
|
170
....*....|....*....
gi 24664918 249 FDIM-----KPDLICAGTE 262
Cdd:cd01515 230 LKLKlnvteRVNIIAANSE 248
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
46-249 |
2.50e-28 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 111.43 E-value: 2.50e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 46 NVVTAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNDNVTKELtdaptWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIV 125
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDYL-----WCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPA 185
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 126 LGVV----NNPA--QNKLYTAKLGQGAFCNGKPIQVSSCEHLNDANVAYEVCLLH--APKIRNKHIKRIYHVGSNARRLL 197
Cdd:PLN02737 186 AATVvefvGGPMcwNTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHddAWATNIELFKEFTDVSRGVRRLG 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 24664918 198 AysAVVDsLCMVAAGNLDAFHIEDMYPWDCAAGYLLIREAGGVVTHPYGGPF 249
Cdd:PLN02737 266 A--AAVD-MCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKF 314
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
48-250 |
1.45e-27 |
|
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: 107.40 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 48 VTAYDNQIEEFLVEKILARYPDHKFIGEEDTHkndnvtkelTDAPTWIIDPIDGTSNFIKQIPHVsVSIGLSIKKQIVLG 127
Cdd:cd01517 38 VTVADYGAQALITAALARLFPSDPIVGEEDSA---------ALGRFWVLDPIDGTKGFLRGDQFA-VALALIEDGEVVLG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 128 VVNNPAQN-------KLYTAKLGQGAFCNgkPIQVSSCEHLNDANVAYEVCLLHAPKIRNKHIKRIYHVGSNARRLLAYS 200
Cdd:cd01517 108 VIGCPNLPlddggggDLFSAVRGQGAWLR--PLDGSSLQPLSVRQLTNAARASFCESVESAHSSHRLQAAIKALGGTPQP 185
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 24664918 201 AVVDSLC---MVAAGNLDAF------HIEDMYPWDCAAGYLLIREAGGVVTHPYGGPFD 250
Cdd:cd01517 186 VRLDSQAkyaAVARGAADFYlrlplsMSYREKIWDHAAGVLIVEEAGGKVTDADGKPLD 244
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
18-260 |
4.45e-25 |
|
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: 100.22 E-value: 4.45e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 18 LAVRAGEILLEGYQnAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDthKNDNVTKELTDAPTWIID 97
Cdd:TIGR01331 8 IARAAGEEILPVYQ-KELAVAQKADN--SPVTEADRAAHRFILEGLRALTPDIPVLSEED--ASIPLTPRQTWQRFWLVD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 98 PIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNG------KPIQVSSCEHLNDANVAyevc 171
Cdd:TIGR01331 83 PLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkAPIHVRPWPSGPLLVVI---- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 172 llhAPKIRNKHIKRIYHVGSNARRLLAYSAVvdSLCMVAAGNLdafhieDMYP-------WDCAAGYLLIREAGGVVTHP 244
Cdd:TIGR01331 159 ---SRSHAEEKTTEYLANLGYDLRTSGGSSL--KFCLVAEGSA------DIYPrlgptgeWDTAAGHAVLAAAGGAIFDL 227
|
250 260
....*....|....*....|..
gi 24664918 245 YGGPF------DIMKPDLICAG 260
Cdd:TIGR01331 228 DGSPLlygkreSFRNPNFVALG 249
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
18-242 |
9.16e-25 |
|
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: 97.85 E-value: 9.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 18 LAVRAGEILLEGYQNAGKAVALKDGEFYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEdtHKNDNVTKELTDAPTWIID 97
Cdd:cd01636 7 VAKEAGLAILKAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEE--SGVAEEVMGRRDEYTWVID 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 98 PIDGTSNFIKQIPHVSVSIGLsikkqIVLGVVNNPAQNKLYTAKlgqgafcngkpiqvsscehlndanvayevcllhAPK 177
Cdd:cd01636 85 PIDGTKNFINGLPFVAVVIAV-----YVILILAEPSHKRVDEKK---------------------------------AEL 126
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24664918 178 IRNKHiKRIYHVGsnarrllaySAVVDSlCMVAAGNLDA-FHIED-MYPWDCAAGYLLIREAGGVVT 242
Cdd:cd01636 127 QLLAV-YRIRIVG---------SAVAKM-CLVALGLADIyYEPGGkRRAWDVAASAAIVREAGGIMT 182
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
49-259 |
1.31e-22 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 97.11 E-value: 1.31e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 49 TAYDNQIEEFLVEKILARYPDHKFIGEEDTHKNdnVTKELTDApTWIIDPIDGTSNFIKQIPHVSVSIGLS-IKKQ---- 123
Cdd:PRK14076 42 TKRIDLIAENIAINSLEKFCSGILISEEIGFKK--IGKNKPEY-IFVLDPIDGTYNALKDIPIYSASIAIAkIDGFdkki 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 124 ------------IVLGVVNNPAQNKLYTAKLGQGAF----CNGKPIQVSSCEHLNDANV---AYEVCLLHAPKIRNKHIK 184
Cdd:PRK14076 119 kefigknltindLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDASIglfAYGLSLDTLKFIKDRKVR 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 185 RIYHVGSnarrllaysaVVDSLCMVAAGNLDAFhI---EDMYPWDCAAGYLLIREAGGVVTHPYGGP----FDIM-KPDL 256
Cdd:PRK14076 199 RIRLFGS----------IALEMCYVASGALDAF-InvnETTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINeKTSV 267
|
...
gi 24664918 257 ICA 259
Cdd:PRK14076 268 ICS 270
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
1-280 |
6.27e-20 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 87.08 E-value: 6.27e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 1 MAASKSQIEELYDFIYPLAVRAGEILLEGYQnagKAVALKDGEFYNVVTAYDNQIEEFLVEKILARYPDHKFIGEEdthk 80
Cdd:PLN02911 26 SALSDAVLDRFVDVAHKLADAAGEVTRKYFR---TKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEE---- 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 81 NDNVTKELTDAPTWIIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQGAFCNGKPIQVSSCEH 160
Cdd:PLN02911 99 HGLRCGEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCAS 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 161 LNDANV--------------AYEvcllhapKIRNKhiKRIYHVGSNArrlLAYSavvdslcMVAAGNLDAFHIEDMYPWD 226
Cdd:PLN02911 179 LKDAYLyttsphmfsgdaedAFA-------RVRDK--VKVPLYGCDC---YAYG-------LLASGHVDLVVESGLKPYD 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 24664918 227 CAAGYLLIREAGGVVTHPYGGPfdimkpdLICAGTETLRAEIEHLIRKADQEKH 280
Cdd:PLN02911 240 YLALVPVVEGAGGVITDWKGRK-------LRWEPSPGSLATSFNVVAAGDARLH 286
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
15-250 |
1.17e-10 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 60.48 E-value: 1.17e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 15 IYPLAVRAGEILLEGYQ-NAGKAVALKDGEfyNVVTAYDNQIEEFLVEKILARYPDHKFIGEEDthkndnvtkeltdAPT 93
Cdd:PRK10931 5 ICQLARNAGDAIMQVYDgTKPLDVASKADD--SPVTAADIAAHTVIKDGLRTLTPDIPVLSEED-------------PPA 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 94 W----------IIDPIDGTSNFIKQIPHVSVSIGLSIKKQIVLGVVNNPAQNKLYTAKLGQgAF--CNG--KPIQVSsce 159
Cdd:PRK10931 70 WevrqhwqrywLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGvrKQIQVR--- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 160 hlnDANVAYEVcllhapkirnkhIKRiYHVGSNARRLLAY------SAVVDSL--CMVAAGnldafhIEDMYP------- 224
Cdd:PRK10931 146 ---DARPPLVV------------ISR-SHADAELKEYLQQlgehqtTSIGSSLkfCLVAEG------QAQLYPrfgptni 203
|
250 260
....*....|....*....|....*.
gi 24664918 225 WDCAAGYLLIREAGGVVTHPYGGPFD 250
Cdd:PRK10931 204 WDTAAGHAVAIAAGAHVHDWQGKTLD 229
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
94-253 |
5.22e-10 |
|
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: 59.11 E-value: 5.22e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 94 WIIDPIDGTSNFIKQiPHVSVSIGLSIKKQIVLGVVNNP--------AQNK--------LYTAKLGQGAFC----NGKP- 152
Cdd:TIGR01330 133 WVLDPIDGTKGFLRG-DQYAVCLALIENGKVVLGVIGCPnlplssygAQNLkgseskgcIFRAVRGSGAFMyslsSDAEs 211
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 153 ---IQVSSCEHLNDANVAYEVCLLHAPKIRNKHIKRIYHVGSNARRLlaYSAVvdSLCMVAAGNLDA---FHIEDMYP-- 224
Cdd:TIGR01330 212 ptkVHVSSVKDTKDAIFCEGVEKGHSSHDEQTAIANKLGISKSPLRL--DSQA--KYAALARGDADVylrLPIKLSYQek 287
|
170 180 190
....*....|....*....|....*....|
gi 24664918 225 -WDCAAGYLLIREAGGVVTHPYGGPFDIMK 253
Cdd:TIGR01330 288 iWDHAAGNVIVEEAGGIVTDAMGKPLDFGK 317
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
18-255 |
2.83e-07 |
|
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: 50.78 E-value: 2.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 18 LAVRAGEILLEGYQNAGKAVALKDG---EF-YNVVTAYDNQIEEFLVEKILARYPDHKFIGEED-----------THKND 82
Cdd:cd01640 8 VAEKAGGIARDVVKKGRLLILLVEGktkEGaNDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDnefenqedesrDVDLD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 83 NVTKELTDAPTWI----------IDPIDGTSNFIK-QIPHVSVSIGLSIKKQIVLGVVNNPAQNKlytaKLGQGAFCN-- 149
Cdd:cd01640 88 EEILEESCPSPSKdlpeedlgvwVDPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHQPFYEK----TAGAGAWLGrt 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 150 ---GKPIQVSSCEHLNDANvayevcllhAPKI--------RNKHIKRIYHvGSNARRLLAYSAVVDSLCmVAAGNLDAF- 217
Cdd:cd01640 164 iwgLSGLGAHSSDFKERED---------AGKIivstshshSVKEVQLITA-GNKDEVLRAGGAGYKVLQ-VLEGLADAYv 232
|
250 260 270
....*....|....*....|....*....|....*....
gi 24664918 218 HIED-MYPWDCAAGYLLIREAGGVVTHPYGGPFDIMKPD 255
Cdd:cd01640 233 HSTGgIKKWDICAPEAILRALGGDMTDLHGEPLSYSKAV 271
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
90-146 |
1.59e-03 |
|
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: 38.97 E-value: 1.59e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24664918 90 DAPTWIIDPIDGTSNFIKQIPHVSVSIGL-------------SIKKQIVLGVVNNPAQNKLYTAKLGQGA 146
Cdd:cd01642 73 GEYIAVLDPLDGSTNYLSGIPFYSVSVALadprskvkaatldNFVSGEGGLKVYSPPTRFSYISVPKLGP 142
|
|
| |
