|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
67-313 |
2.41e-129 |
|
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: 369.17 E-value: 2.41e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 67 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 145
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 146 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSS 225
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 226 RtPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLM 305
Cdd:cd01639 158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236
|
....*...
gi 221625487 306 SRRVIAAN 313
Cdd:cd01639 237 SGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
64-330 |
5.37e-108 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 316.21 E-value: 5.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 64 WQECMDY-AVTLARQAGEVVCEAIKNEMNVMLKS--SPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSIL 140
Cdd:pfam00459 1 DLEEVLKvAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 141 TDN-PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLV 219
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 220 TELGSSRTPETV-RMVLSNMEKLFCIPvhGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDV 297
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKLVRAP--GVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238
|
250 260 270
....*....|....*....|....*....|...
gi 221625487 298 TGGPFDLMSRRVIAANNRILAERIAKEIQVIPL 330
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
62-313 |
2.23e-95 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 283.89 E-value: 2.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 62 DPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILT 141
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 142 DNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTE 221
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 222 LGSSRTPETVRMVLSNMEKLfcipVHGIRSV---GTAAVNMCLVATGGADAYYEMGI-HCWDVAGAGIIVTEAGGVLMDV 297
Cdd:PLN02553 164 VGTKRDKATVDATTNRINAL----LYKVRSLrmsGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDP 239
|
250
....*....|....*.
gi 221625487 298 TGGPFDLMSRRVIAAN 313
Cdd:PLN02553 240 SGGPFDIMSRRVAASN 255
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
65-319 |
5.77e-82 |
|
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: 249.38 E-value: 5.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 65 QECMDYAVTLARQAGEVVCEAIKN-EMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltDN 143
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 144 PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELG 223
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 224 SSRTPETVRMVLSNMEKlfciPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFD 303
Cdd:COG0483 157 YLRDDREYLAALAALLP----RVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250
....*....|....*.
gi 221625487 304 LMSRRVIAANNRILAE 319
Cdd:COG0483 233 LGSGSLVAANPALHDE 248
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
74-303 |
3.19e-33 |
|
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: 123.33 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 74 LARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPI 151
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAdnSPV---TEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 152 DGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAF--CNGQ--KLQVSQQEDITKSLLVTELGSSRT 227
Cdd:TIGR01331 85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQalKAPIHVRPWPSGPLLVVISRSHAE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221625487 228 PETVRMvLSNMEKLFCIPvhgirsvGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDVTGGPFD 303
Cdd:TIGR01331 165 EKTTEY-LANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
67-313 |
2.41e-129 |
|
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: 369.17 E-value: 2.41e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 67 CMDYAVTLARQAGEVVCEAIKN-EMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksiLTDNPT 145
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKlGLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGG---LTDEPT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 146 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSS 225
Cdd:cd01639 78 WIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 226 RtPETVRMVLSNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLM 305
Cdd:cd01639 158 R-GDNFDRYLNNFAKLLAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLM 236
|
....*...
gi 221625487 306 SRRVIAAN 313
Cdd:cd01639 237 SGNILAGN 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
64-330 |
5.37e-108 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 316.21 E-value: 5.37e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 64 WQECMDY-AVTLARQAGEVVCEAIKNEMNVMLKS--SPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSIL 140
Cdd:pfam00459 1 DLEEVLKvAVELAAKAGEILREAFSNKLTIEEKGksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 141 TDN-PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLV 219
Cdd:pfam00459 81 TDDgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 220 TELGSSRTPETV-RMVLSNMEKLFCIPvhGIRSVGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDV 297
Cdd:pfam00459 161 TLFGVSSRKDTSeASFLAKLLKLVRAP--GVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDA 238
|
250 260 270
....*....|....*....|....*....|...
gi 221625487 298 TGGPFDLMSRRVIAANNRILAERIAKEIQVIPL 330
Cdd:pfam00459 239 DGGPFDLLAGRVIAANPKVLHELLAAALEEIIE 271
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
62-313 |
2.23e-95 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 283.89 E-value: 2.23e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 62 DPWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILT 141
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQ-VDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 142 DNPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTE 221
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATE 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 222 LGSSRTPETVRMVLSNMEKLfcipVHGIRSV---GTAAVNMCLVATGGADAYYEMGI-HCWDVAGAGIIVTEAGGVLMDV 297
Cdd:PLN02553 164 VGTKRDKATVDATTNRINAL----LYKVRSLrmsGSCALNLCGVACGRLDIFYEIGFgGPWDVAAGAVIVKEAGGLVFDP 239
|
250
....*....|....*.
gi 221625487 298 TGGPFDLMSRRVIAAN 313
Cdd:PLN02553 240 SGGPFDIMSRRVAASN 255
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
68-312 |
7.35e-83 |
|
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: 251.08 E-value: 7.35e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 68 MDYAVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaAGEKSILTDNPTWI 147
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEG--GGSGNVSDGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 148 IDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRT 227
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 228 PEtvrmvLSNMEKLfCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFD-LMS 306
Cdd:cd01637 159 NR-----AAVLASL-VNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDtLNR 232
|
....*.
gi 221625487 307 RRVIAA 312
Cdd:cd01637 233 SGIIAA 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
65-319 |
5.77e-82 |
|
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: 249.38 E-value: 5.77e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 65 QECMDYAVTLARQAGEVVCEAIKN-EMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltDN 143
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKG-DGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD---SG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 144 PTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELG 223
Cdd:COG0483 77 YVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 224 SSRTPETVRMVLSNMEKlfciPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFD 303
Cdd:COG0483 157 YLRDDREYLAALAALLP----RVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLD 232
|
250
....*....|....*.
gi 221625487 304 LMSRRVIAANNRILAE 319
Cdd:COG0483 233 LGSGSLVAANPALHDE 248
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
68-297 |
2.55e-60 |
|
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: 191.45 E-value: 2.55e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 68 MDYAVTLARQAGEVVCEAIKNEMNVML--KSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPT 145
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVkiTKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 146 WIIDPIDGTTNFVHRFPFVAVSIGFAvnkkiefgvvyscvegkmytarkgkgafcngqklqvsqqeditKSLLVTELGSS 225
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY-------------------------------------------VILILAEPSHK 117
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 221625487 226 RTPEtvrmvlsNMEKLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGI--HCWDVAGAGIIVTEAGGVLMDV 297
Cdd:cd01636 118 RVDE-------KKAELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
63-322 |
1.90e-52 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 176.91 E-value: 1.90e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 63 PWQECMDYAVTLARQAGEVVCEAIKNEMNVMLKSSpVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSiltD 142
Cdd:PLN02737 75 PAEELLAVAELAAKTGAEVVMEAVNKPRNISYKGL-TDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSS---S 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 143 NPTWIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKM------YTARKGKGAFCNGQKLQVSQQEDITKS 216
Cdd:PLN02737 151 DYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPMcwntrtFSASAGGGAFCNGQKIHVSQTDKVERS 230
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 217 LLVTELGSsrtpETVRMVLSNME--KLFCIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVL 294
Cdd:PLN02737 231 LLVTGFGY----EHDDAWATNIElfKEFTDVSRGVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTV 306
|
250 260 270
....*....|....*....|....*....|.
gi 221625487 295 MDVTGGPFDLMSRRVIAANNRI---LAERIA 322
Cdd:PLN02737 307 TRMDGGKFSVFDRSVLVSNGVLhpkLLDRIG 337
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
71-317 |
1.56e-48 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 163.82 E-value: 1.56e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 71 AVTLARQAGEVVCEAIKNEMNVML--KSSPvDLVTATDQKVEKMLISSIKEKYPSHSFIGEESvaaGEKSILTDNPTWII 148
Cdd:PRK10757 8 AVRAARKAGNLIAKNYETPDAVEAsqKGSN-DFVTNVDKAAEAVIIDTIRKSYPQHTIITEES---GELEGEDQDVQWVI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 149 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTEL---GSS 225
Cdd:PRK10757 84 DPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGFpfkAKQ 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 226 RTPETVRMVlsnmEKLFcIPVHGIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLM 305
Cdd:PRK10757 164 HATTYINIV----GKLF-TECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGHNYML 238
|
250
....*....|..
gi 221625487 306 SRRVIAANNRIL 317
Cdd:PRK10757 239 TGNIVAGNPRVV 250
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
69-318 |
1.06e-43 |
|
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: 150.56 E-value: 1.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 69 DYAVTLARQAGEVVCEAIKNEMNVMLKSsPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEEsvaaGEKSILTDNPTWII 148
Cdd:cd01643 2 SLAEAIAQEAGDRALADFGNSLSAETKA-DGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE----GGGIFPSSGWYWVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 149 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTP 228
Cdd:cd01643 77 DPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFNRSSRASA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 229 ETVRMVLSNMEklfciPVHgIRSVGTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDLMSRR 308
Cdd:cd01643 157 RAVLRVILRRF-----PGK-IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQTKD 230
|
250
....*....|
gi 221625487 309 VIAANNRILA 318
Cdd:cd01643 231 YLSAGFPTLI 240
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
71-319 |
8.41e-40 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 140.68 E-value: 8.41e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 71 AVTLARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWII 148
Cdd:COG1218 8 AIEIAREAGEAILEIYRADFEVEEKAddSPV---TEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 149 DPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFC-----NGQKLQVSQQEDITKSLLVTelg 223
Cdd:COG1218 85 DPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVRDRPPAEPLRVVA--- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 224 sSR---TPETVRMvlsnMEKLfciPVHGIRSVGtAAVNMCLVATGGADAYYEMGIHC-WDVAGAGIIVTEAGGVLMDVTG 299
Cdd:COG1218 162 -SRshrDEETEAL----LARL---GVAELVSVG-SSLKFCLVAEGEADLYPRLGPTMeWDTAAGQAILEAAGGRVTDLDG 232
|
250 260
....*....|....*....|....*...
gi 221625487 300 GPF------DLMSRRVIAANN--RILAE 319
Cdd:COG1218 233 KPLrynkkeDLLNPGFIASGDhaAILAA 260
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
69-302 |
3.01e-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: 130.81 E-value: 3.01e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 69 DYAVTLARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEksILTDNPTW 146
Cdd:cd01638 3 ELLIRIAREAGDAILEVYRGGFTVERKEdgSPV---TAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 147 IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSR 226
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRS 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221625487 227 TPETVRMVLSNMeklfcIPVHGIRSVGTAAvNMCLVATGGADAYYEMGIHC-WDVAGAGIIVTEAGGVLMDVTGGPF 302
Cdd:cd01638 158 HPDEELEALLAA-----LGVAEVVSIGSSL-KFCLVAEGEADIYPRLGPTMeWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
68-318 |
1.50e-34 |
|
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: 127.43 E-value: 1.50e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 68 MDYAVTLARQAGEVVCEAIKNEMN---VMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAgeksiltDNP 144
Cdd:cd01517 1 ELEVAILAVRAAASLTLPVFRNLGagdVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA-------LGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 145 TWIIDPIDGTTNFVHRFPFvAVSIGFAVNKKIEFGVVYSCV-------EGKMYTARKGKGAFC---NGQKLQVSQQEDIT 214
Cdd:cd01517 74 FWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNlplddggGGDLFSAVRGQGAWLrplDGSSLQPLSVRQLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 215 KSLLVTELGSSRTPETVRMVLSNMEKLfcipvhGIRSVGTAAVNMC---LVATGGADAY--------YEMGIhcWDVAGA 283
Cdd:cd01517 153 NAARASFCESVESAHSSHRLQAAIKAL------GGTPQPVRLDSQAkyaAVARGAADFYlrlplsmsYREKI--WDHAAG 224
|
250 260 270
....*....|....*....|....*....|....*
gi 221625487 284 GIIVTEAGGVLMDVTGGPFDLMSRRVIAANNRILA 318
Cdd:cd01517 225 VLIVEEAGGKVTDADGKPLDFGKGRKLLNNGGLIA 259
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
68-322 |
8.68e-34 |
|
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: 124.67 E-value: 8.68e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 68 MDYAVTLARQAGEVVCEAIKNEMNVMLK--SSPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTdnpt 145
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKadFSPV---TEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYV---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 146 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCN---GQKLQVSQQEDITKSLLVTEl 222
Cdd:cd01641 75 WVLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLSTT- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 223 gssrTPETVRMVLSN-MEKLfcipvhgIRSV-----GTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMD 296
Cdd:cd01641 154 ----DPHFFTPGDRAaFERL-------ARAVrltryGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITD 222
|
250 260
....*....|....*....|....*.
gi 221625487 297 VTGGPFDLMSRRVIAANNRILAERIA 322
Cdd:cd01641 223 WDGGPLTGGSGRVVAAGDAELHEALL 248
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
74-303 |
3.19e-33 |
|
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: 123.33 E-value: 3.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 74 LARQAGEVVCEAIKNEMNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGEKSILTDNPTWIIDPI 151
Cdd:TIGR01331 8 IARAAGEEILPVYQKELAVAQKAdnSPV---TEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWLVDPL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 152 DGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAF--CNGQ--KLQVSQQEDITKSLLVTELGSSRT 227
Cdd:TIGR01331 85 DGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKreGDGQalKAPIHVRPWPSGPLLVVISRSHAE 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 221625487 228 PETVRMvLSNMEKLFCIPvhgirsvGTAAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMDVTGGPFD 303
Cdd:TIGR01331 165 EKTTEY-LANLGYDLRTS-------GGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGSPLL 233
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
71-323 |
1.15e-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: 121.64 E-value: 1.15e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 71 AVTLARQAGEVVCEAIKNEMNVMLKSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEEsvaAGEKSILTDNPTWIIDP 150
Cdd:TIGR02067 5 AEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE---FGHNEEGDAERVWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 151 IDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTELGSSRTPET 230
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTTSPDLLDDPG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 231 VRMVlsnMEKLfcipvhgIRSV-----GTAAVNMCLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFdLM 305
Cdd:TIGR02067 162 NRPA---FERL-------RRAArltryGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PD 230
|
250
....*....|....*...
gi 221625487 306 SRRVIAANNRILAERIAK 323
Cdd:TIGR02067 231 GGGAVAAGNAMLHDEALE 248
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
106-325 |
1.08e-31 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 119.63 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 106 DQKVEKMLISSIKEKYPSHSFIGEEsvaAGEksILTDNPTW--IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYS 183
Cdd:PRK12676 47 DKVAEDIILEVLKPLGRCVNIISEE---LGE--IVGNGPEYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYN 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 184 CVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTelgSSRTPETVRMVlsnmeKLfCIPVHGIRSVGTAAVNMCLVA 263
Cdd:PRK12676 122 LATGDFYEAIPGKGAYLNGKPIKVSKTSELNESAVSI---YGYRRGKERTV-----KL-GRKVRRVRILGAIALELCYVA 192
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 221625487 264 TGGADAYYEMG--IHCWDVAGAGIIVTEAGGVLMDVTGGPFDL-----MSRRVIAANNRILAERIAKEI 325
Cdd:PRK12676 193 SGRLDAFVDVRnyLRVTDIAAGKLICEEAGGIVTDEDGNELKLplnvtERTNLIAANGEELHKKILELL 261
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
106-317 |
7.09e-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: 114.40 E-value: 7.09e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 106 DQKVEKMLISSIKeKYPSHSFIGEESvaaGEKSIlTDNPTW--IIDPIDGTTNFVHRFPFVAVSIGFAVNKK--IEFGVV 181
Cdd:cd01515 42 DKVAEDAAIEILK-KLGSVNIVSEEI---GVIDN-GDEPEYtvVLDPLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYV 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 182 YSCVEGKMYTARKGKGAFCNGQKLQVSQQEDItKSLLVTELGSSRTPETVRMVlsnmeklfCIPVHGIRSVGTAAVNMCL 261
Cdd:cd01515 117 YNLATGDLYYAIKGKGAYLNGKRIKVSDFSSL-KSISVSYYIYGKNHDRTFKI--------CRKVRRVRIFGSVALELCY 187
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 221625487 262 VATGGADAYYEM--GIHCWDVAGAGIIVTEAGGVLMDVTGGP----FDLMSR-RVIAANNRIL 317
Cdd:cd01515 188 VASGALDAFVDVreNLRLVDIAAGYLIAEEAGGIVTDENGKElklkLNVTERvNIIAANSELH 250
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
110-321 |
3.48e-24 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 102.88 E-value: 3.48e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 110 EKMLISSIkEKYPSHSFIGEEsvaAGEKSILTDNPTWI--IDPIDGTTNFVHRFPFVAVSI------GFAVNKK------ 175
Cdd:PRK14076 50 ENIAINSL-EKFCSGILISEE---IGFKKIGKNKPEYIfvLDPIDGTYNALKDIPIYSASIaiakidGFDKKIKefigkn 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 176 -----IEFGVVYSCVEGKMYTARKGKGAF----CNGQKLQVSQQEDITKSlLVTELGSSRTPETVRMVLSNmeklfciPV 246
Cdd:PRK14076 126 ltindLEVGVVKNIATGDTYYAEKGEGAYllkkGEKKKIEISNISNLKDA-SIGLFAYGLSLDTLKFIKDR-------KV 197
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 247 HGIRSVGTAAVNMCLVATGGADAYYEM--GIHCWDVAGAGIIVTEAGGVLMDVTGGP----FDLMSRRVIAANNRILAER 320
Cdd:PRK14076 198 RRIRLFGSIALEMCYVASGALDAFINVneTTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKK 277
|
.
gi 221625487 321 I 321
Cdd:PRK14076 278 L 278
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
74-307 |
1.68e-14 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 72.03 E-value: 1.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 74 LARQAGEVVCEAIKNE--MNVMLKS--SPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEEsvaageksiltDNPTW--- 146
Cdd:PRK10931 8 LARNAGDAIMQVYDGTkpLDVASKAddSPV---TAADIAAHTVIKDGLRTLTPDIPVLSEE-----------DPPAWevr 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 147 -------IIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKgAF--CNGQKLQVsQQEDITKSL 217
Cdd:PRK10931 74 qhwqrywLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWkeECGVRKQI-QVRDARPPL 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 218 LVTelgsSRTPETVRMvlsnMEKLFCIPVHGIRSVGTaAVNMCLVATGGADAYYEMG-IHCWDVAGAGIIVTEAGGVLMD 296
Cdd:PRK10931 152 VVI----SRSHADAEL----KEYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHD 222
|
250
....*....|.
gi 221625487 297 VTGGPFDLMSR 307
Cdd:PRK10931 223 WQGKTLDYTPR 233
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
69-317 |
9.60e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 70.52 E-value: 9.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 69 DYAVTLARQAGEVVCEAIKNEMNVMLK--SSPVdlvTATDQKVEKMLISSIKEKYPSHSFIGEE-SVAAGEKSiltDNPT 145
Cdd:PLN02911 38 DVAHKLADAAGEVTRKYFRTKFEIIDKedLSPV---TIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEGS---SDYV 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 146 WIIDPIDGTTNFVHRFPFVAVSIGFAVNKKIEFGVVYSCVEGKMYTARKGKGAFCNGQKLQVSQQEDITKSLLVTElgss 225
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKDAYLYTT---- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 226 rTPEtvrMVLSNMEKLFC-------IPVHGIRSVGTAavnmcLVATGGADAYYEMGIHCWDVAGAGIIVTEAGGVLMDVT 298
Cdd:PLN02911 188 -SPH---MFSGDAEDAFArvrdkvkVPLYGCDCYAYG-----LLASGHVDLVVESGLKPYDYLALVPVVEGAGGVITDWK 258
|
250 260
....*....|....*....|....*..
gi 221625487 299 GGPFDL--------MSRRVIAANNRIL 317
Cdd:PLN02911 259 GRKLRWepspgslaTSFNVVAAGDARL 285
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
106-283 |
5.13e-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: 59.00 E-value: 5.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 106 DQKVEKMLISSIKEKYPSHSFIGEESvaaGEKSILTDNPTWIIDPIDGTTNFVHRFPFVAVSIGFA-------------V 172
Cdd:cd01642 40 DLKAEEIILKLLREEGVFGQIISEES---GEIRKGSGEYIAVLDPLDGSTNYLSGIPFYSVSVALAdprskvkaatldnF 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 173 NKKIEFGVVYSCVEGKMYTARKGKGAFCNGQklqvsqqediTKSLLVTELGSSRTPETVRMVLSNMEKlfcipvhgIRSV 252
Cdd:cd01642 117 VSGEGGLKVYSPPTRFSYISVPKLGPPLVPE----------VPSKIGIYEGSSRNPEKFLLLSRNGLK--------FRSL 178
|
170 180 190
....*....|....*....|....*....|...
gi 221625487 253 GTAAVNMCLVATGGADAYYEM--GIHCWDVAGA 283
Cdd:cd01642 179 GSAALELAYTCEGSFVLFLDLrgKLRNFDVAAA 211
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
71-304 |
1.64e-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: 51.94 E-value: 1.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 71 AVTLARQAGEVVCEAIKNEMNVML------KSSPVDLVTATDQKVEKMLISSIKEKYPSHSFIGEESVAAGE-------- 136
Cdd:cd01640 5 LLAVAEKAGGIARDVVKKGRLLILlvegktKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENqedesrdv 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 137 -----------KSILTDNP-----TWIiDPIDGTTNFVH-RFPFVAVSIGFAVNKKIEFGVVY----------SCVEGKM 189
Cdd:cd01640 85 dldeeileescPSPSKDLPeedlgVWV-DPLDATQEYTEgLLEYVTVLIGVAVKGKPIAGVIHqpfyektagaGAWLGRT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 221625487 190 YTARKGKGAFCNgqklQVSQQEDiTKSLLVTELGSSRTPETVRMVLSNMEKLFcipvhgirSVGTAAVNMCLVATGGADA 269
Cdd:cd01640 164 IWGLSGLGAHSS----DFKERED-AGKIIVSTSHSHSVKEVQLITAGNKDEVL--------RAGGAGYKVLQVLEGLADA 230
|
250 260 270
....*....|....*....|....*....|....*..
gi 221625487 270 YY--EMGIHCWDVAGAGIIVTEAGGVLMDVTGGPFDL 304
Cdd:cd01640 231 YVhsTGGIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
|
|
| |
