|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
10-255 |
1.68e-122 |
|
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: 349.53 E-value: 1.68e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 10 CLEVASNLVSEAGRLIARNNEQR-QDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGAEGvkKLTDEP 88
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLgLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEE--SGAAG--GLTDEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEFGT 168
Cdd:cd01639 77 TWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 169 TRDEaKMKVVHENFEKM-AKKAHGLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFDI 247
Cdd:cd01639 157 DRGD-NFDRYLNNFAKLlAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDL 235
|
....*...
gi 21357329 248 MSRRVLAA 255
Cdd:cd01639 236 MSGNILAG 243
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
1-270 |
4.37e-106 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 308.93 E-value: 4.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 1 MSHNVDVEKCLEVASNLVSEAGRLIARNNEQRQDfVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEeSSGAEG 80
Cdd:PLN02553 1 MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKH-VEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEE-TTAASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 81 VKKLTDEPTWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKA 160
Cdd:PLN02553 79 GTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 161 LVTSEFGTTRDEAKMKVVHENFEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFGIHA-WDVCAGDLIVREAGGVVID 239
Cdd:PLN02553 159 LLATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAGGLVFD 238
|
250 260 270
....*....|....*....|....*....|.
gi 21357329 240 PAGGEFDIMSRRVlAAATPELAQEISKVLTQ 270
Cdd:PLN02553 239 PSGGPFDIMSRRV-AASNGHLKDAFVEALRQ 268
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
11-268 |
1.90e-89 |
|
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: 265.94 E-value: 1.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGAEGVKklTDEPTW 90
Cdd:COG0483 4 LELALRAARAAGALILRRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEE--SGASEGR--DSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEFGTTR 170
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 171 DEAKMkvvHENFEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFDIMSR 250
Cdd:COG0483 160 DDREY---LAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSG 236
|
250
....*....|....*...
gi 21357329 251 RVlAAATPELAQEISKVL 268
Cdd:COG0483 237 SL-VAANPALHDELLALL 253
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-268 |
8.55e-86 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 257.27 E-value: 8.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 6 DVEKCLEVASNLVSEAGRLI--ARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEESSGAEGVKK 83
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILreAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 84 LTDEPTWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVT 163
Cdd:pfam00459 81 TDDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 164 SEFGTTRDEA-KMKVVHENFEKmAKKAHGLRVLGSAALNMSMVALGAADANYEFG-IHAWDVCAGDLIVREAGGVVIDPA 241
Cdd:pfam00459 161 TLFGVSSRKDtSEASFLAKLLK-LVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|....*..
gi 21357329 242 GGEFDIMSRRVLAAATPELAQEISKVL 268
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKVLHELLAAAL 266
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
11-268 |
4.75e-41 |
|
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273949 [Multi-domain] Cd Length: 251 Bit Score: 142.06 E-value: 4.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEessgAEGVKKLTDEPTW 90
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE----FGHNEEGDAERVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVtseFGTTR 170
Cdd:TIGR02067 78 VLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVL---FTTSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 171 DEAKMKVVHENFEKMAKKAHgLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFdIMSR 250
Cdd:TIGR02067 155 DLLDDPGNRPAFERLRRAAR-LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGG 232
|
250
....*....|....*...
gi 21357329 251 RVLAAATPELAQEISKVL 268
Cdd:TIGR02067 233 GAVAAGNAMLHDEALEIL 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
10-255 |
1.68e-122 |
|
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: 349.53 E-value: 1.68e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 10 CLEVASNLVSEAGRLIARNNEQR-QDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGAEGvkKLTDEP 88
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKLgLNVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEE--SGAAG--GLTDEP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEFGT 168
Cdd:cd01639 77 TWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPY 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 169 TRDEaKMKVVHENFEKM-AKKAHGLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFDI 247
Cdd:cd01639 157 DRGD-NFDRYLNNFAKLlAKAVRGVRRLGSAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDL 235
|
....*...
gi 21357329 248 MSRRVLAA 255
Cdd:cd01639 236 MSGNILAG 243
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
1-270 |
4.37e-106 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 308.93 E-value: 4.37e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 1 MSHNVDVEKCLEVASNLVSEAGRLIARNNEQRQDfVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEeSSGAEG 80
Cdd:PLN02553 1 MAQNDDLEQFLEVAVDAAKAAGQIIRKGFYQTKH-VEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEE-TTAASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 81 VKKLTDEPTWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKA 160
Cdd:PLN02553 79 GTELTDEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 161 LVTSEFGTTRDEAKMKVVHENFEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFGIHA-WDVCAGDLIVREAGGVVID 239
Cdd:PLN02553 159 LLATEVGTKRDKATVDATTNRINALLYKVRSLRMSGSCALNLCGVACGRLDIFYEIGFGGpWDVAAGAVIVKEAGGLVFD 238
|
250 260 270
....*....|....*....|....*....|.
gi 21357329 240 PAGGEFDIMSRRVlAAATPELAQEISKVLTQ 270
Cdd:PLN02553 239 PSGGPFDIMSRRV-AASNGHLKDAFVEALRQ 268
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
11-268 |
1.90e-89 |
|
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: 265.94 E-value: 1.90e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGAEGVKklTDEPTW 90
Cdd:COG0483 4 LELALRAARAAGALILRRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEE--SGASEGR--DSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEFGTTR 170
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATGFPYLR 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 171 DEAKMkvvHENFEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFDIMSR 250
Cdd:COG0483 160 DDREY---LAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGSG 236
|
250
....*....|....*...
gi 21357329 251 RVlAAATPELAQEISKVL 268
Cdd:COG0483 237 SL-VAANPALHDELLALL 253
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-268 |
8.55e-86 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 257.27 E-value: 8.55e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 6 DVEKCLEVASNLVSEAGRLI--ARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEESSGAEGVKK 83
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILreAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 84 LTDEPTWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVT 163
Cdd:pfam00459 81 TDDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 164 SEFGTTRDEA-KMKVVHENFEKmAKKAHGLRVLGSAALNMSMVALGAADANYEFG-IHAWDVCAGDLIVREAGGVVIDPA 241
Cdd:pfam00459 161 TLFGVSSRKDtSEASFLAKLLK-LVRAPGVRRVGSAALKLAMVAAGKADAYIEFGrLKPWDHAAGVAILREAGGVVTDAD 239
|
250 260
....*....|....*....|....*..
gi 21357329 242 GGEFDIMSRRVLAAATPELAQEISKVL 268
Cdd:pfam00459 240 GGPFDLLAGRVIAANPKVLHELLAAAL 266
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
11-256 |
3.02e-70 |
|
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: 216.41 E-value: 3.02e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEessGAEGVKKLTDEPTW 90
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEE---GGGSGNVSDGGRVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEFGTTR 170
Cdd:cd01637 78 VIDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 171 DEAkmkvvHENFEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFDIMSR 250
Cdd:cd01637 158 SNR-----AAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNR 232
|
....*.
gi 21357329 251 RVLAAA 256
Cdd:cd01637 233 SGIIAA 238
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
11-261 |
4.72e-52 |
|
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: 170.21 E-value: 4.72e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLiarnneQRQDF-----VCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGAEgvkKLT 85
Cdd:cd01643 1 LSLAEAIAQEAGDR------ALADFgnslsAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE--GGGI---FPS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 86 DEPTWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRI--HVSGQKELGKALvt 163
Cdd:cd01643 70 SGWYWVIDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLNGKPLalHPPLQLPDCNVG-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 164 seFGTTRDEAKMKVVHENFEKMAKKahgLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGG 243
Cdd:cd01643 148 --FNRSSRASARAVLRVILRRFPGK---IRMLGSASLNLASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEE 222
|
250
....*....|....*...
gi 21357329 244 EFDIMSRRVLAAATPELA 261
Cdd:cd01643 223 PAFLQTKDYLSAGFPTLI 240
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
11-268 |
1.63e-50 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 166.91 E-value: 1.63e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQrQDFVCKSN--DIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEE--ESSGAEgvkkltD 86
Cdd:PRK10757 5 LNIAVRAARKAGNLIAKNYET-PDAVEASQkgSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEEsgELEGED------Q 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 87 EPTWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEF 166
Cdd:PRK10757 78 DVQWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILATGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 167 ---GTTRDEAKMKVVHENFEKMAKkahgLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGG 243
Cdd:PRK10757 158 pfkAKQHATTYINIVGKLFTECAD----FRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGG 233
|
250 260 270
....*....|....*....|....*....|..
gi 21357329 244 EFDIMS-------RRVLAAATPELAQEISKVL 268
Cdd:PRK10757 234 HNYMLTgnivagnPRVVKAMLANMRDELSDAL 265
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
43-255 |
2.70e-48 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 164.20 E-value: 2.70e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 43 DLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGAEGvkKLTDEPTWIIDPVDGTMNFVHAFPHSCISVGL--KVNKV- 119
Cdd:PLN02737 111 DLVTDTDKASEAAILEVVRKNFPDHLILGEE--GGVIG--DSSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVlfRGTPAa 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 120 -TELGLVYNPIL--EQRFTARRGHGAFYNGRRIHVSGQKELGKALVTSEFGTTRDEAKMKVVhENFEKMAKKAHGLRVLG 196
Cdd:PLN02737 187 aTVVEFVGGPMCwnTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHDDAWATNI-ELFKEFTDVSRGVRRLG 265
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 21357329 197 SAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFDIMSRRVLAA 255
Cdd:PLN02737 266 AAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGKFSVFDRSVLVS 324
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
11-264 |
3.28e-47 |
|
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: 157.80 E-value: 3.28e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSnDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEEssGAEGvkkLTDEPTW 90
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKA-DFSPVTEADRAAEAAMRELIAAAFPDHGILGEEF--GNEG---GDAGYVW 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYN---GRRIHVSGQKELGKALV---TS 164
Cdd:cd01641 76 VLDPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNgagGRPLRVRACADLAEAVLsttDP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 165 EFGTTRDEAKmkvvhenFEKMAKKAhGLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGE 244
Cdd:cd01641 156 HFFTPGDRAA-------FERLARAV-RLTRYGGDCYAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGP 227
|
250 260
....*....|....*....|
gi 21357329 245 FDIMSRRVLAAATPELAQEI 264
Cdd:cd01641 228 LTGGSGRVVAAGDAELHEAL 247
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
11-268 |
4.75e-41 |
|
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273949 [Multi-domain] Cd Length: 251 Bit Score: 142.06 E-value: 4.75e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEessgAEGVKKLTDEPTW 90
Cdd:TIGR02067 2 LAFAEDLADAAGETILPFFRASLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE----FGHNEEGDAERVW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVtseFGTTR 170
Cdd:TIGR02067 78 VLDPIDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVL---FTTSP 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 171 DEAKMKVVHENFEKMAKKAHgLRVLGSAALNMSMVALGAADANYEFGIHAWDVCAGDLIVREAGGVVIDPAGGEFdIMSR 250
Cdd:TIGR02067 155 DLLDDPGNRPAFERLRRAAR-LTRYGGDCYAYLMVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDGG 232
|
250
....*....|....*...
gi 21357329 251 RVLAAATPELAQEISKVL 268
Cdd:TIGR02067 233 GAVAAGNAMLHDEALEIL 250
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
11-245 |
4.47e-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: 128.88 E-value: 4.47e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIaRNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEessGAEGVKKLTDEPTW 90
Cdd:cd01638 2 LELLIRIAREAGDAI-LEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEE---SADDPLRLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQ----KELGKALVTSEf 166
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQarppPLQPLRVVASR- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 167 gtTRDEAKMKVVHenfekMAKKAHGLRVLGSaALNMSMVALGAADANYEFG-IHAWDVCAGDLIVREAGGVVIDPAGGEF 245
Cdd:cd01638 157 --SHPDEELEALL-----AALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGpTMEWDTAAGDAVLRAAGGAVSDLDGSPL 228
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
11-239 |
1.69e-35 |
|
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: 125.58 E-value: 1.69e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLI--ARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEeSSGAEGVKKLTDEP 88
Cdd:cd01636 1 LEELCRVAKEAGLAIlkAFGRELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEE-SGVAEEVMGRRDEY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TWIIDPVDGTMNFVHAFPHSCISVGlkvnkvtelglvynpileqrftarrghgafyngrrihvsgqkeLGKALVTSEFGT 168
Cdd:cd01636 80 TWVIDPIDGTKNFINGLPFVAVVIA-------------------------------------------VYVILILAEPSH 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 21357329 169 TRDEAKMkvvhenFEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFGI--HAWDVCAGDLIVREAGGVVID 239
Cdd:cd01636 117 KRVDEKK------AELQLLAVYRIRIVGSAVAKMCLVALGLADIYYEPGGkrRAWDVAASAAIVREAGGIMTD 183
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
11-268 |
1.59e-33 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 122.71 E-value: 1.59e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIA--RNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEEssgaeGVKKLtDEP 88
Cdd:PRK12676 7 LEICDDMAKEVEKAIMplFGTPDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEEL-----GEIVG-NGP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TW--IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELgKALVTSEF 166
Cdd:PRK12676 81 EYtvVLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSEL-NESAVSIY 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 167 GTTRDEakmkvvhENFEKMAKKAHGLRVLGSAALNMSMVALGAADA-----NYefgIHAWDVCAGDLIVREAGGVVIDPA 241
Cdd:PRK12676 160 GYRRGK-------ERTVKLGRKVRRVRILGAIALELCYVASGRLDAfvdvrNY---LRVTDIAAGKLICEEAGGIVTDED 229
|
250 260 270
....*....|....*....|....*....|..
gi 21357329 242 GGEFDI-----MSRRVLAAATPELAQEISKVL 268
Cdd:PRK12676 230 GNELKLplnvtERTNLIAANGEELHKKILELL 261
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
11-246 |
4.47e-32 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 118.72 E-value: 4.47e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARnnEQRQDF-VCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEeSSGAEGVKKLTDEPT 89
Cdd:COG1218 5 LEAAIEIAREAGEAILE--IYRADFeVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEE-SAAIPYEERKSWDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 90 WIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFY-----NGRRIHVSgqkelgkalvts 164
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKetgggERQPIRVR------------ 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 165 efgTTRDEAKMKVV----HEN--FEKMAKK--AHGLRVLGSaALNMSMVALGAADANYEFG-IHAWDVCAGDLIVREAGG 235
Cdd:COG1218 150 ---DRPPAEPLRVVasrsHRDeeTEALLARlgVAELVSVGS-SLKFCLVAEGEADLYPRLGpTMEWDTAAGQAILEAAGG 225
|
250
....*....|.
gi 21357329 236 VVIDPAGGEFD 246
Cdd:COG1218 226 RVTDLDGKPLR 236
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
11-270 |
6.46e-32 |
|
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: 118.95 E-value: 6.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIAR--NNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEESSgaegvkklTDEP 88
Cdd:cd01517 2 LEVAILAVRAAASLTLPvfRNLGAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA--------ALGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TWIIDPVDGTMNFVHAFPHsCISVGLKVNKVTELGLVYNPILEQR-------FTARRGHGAFYngRRIHVSGQKELGKAL 161
Cdd:cd01517 74 FWVLDPIDGTKGFLRGDQF-AVALALIEDGEVVLGVIGCPNLPLDdggggdlFSAVRGQGAWL--RPLDGSSLQPLSVRQ 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 162 VTSEFGTTRDEAkmkVVHENFEKMAKKAHGLRVLGSAALNMS------MVALGAADANYEFGIH------AWDVCAGDLI 229
Cdd:cd01517 151 LTNAARASFCES---VESAHSSHRLQAAIKALGGTPQPVRLDsqakyaAVARGAADFYLRLPLSmsyrekIWDHAAGVLI 227
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 21357329 230 VREAGGVVIDPAGGEFDIMSRRVLA------AATPELAQEISKVLTQ 270
Cdd:cd01517 228 VEEAGGKVTDADGKPLDFGKGRKLLnnggliAAPGEIHEQVLEALRE 274
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
11-268 |
4.31e-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: 4.31e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIAR--NNEQRQDFVCKSNDIDLVTQTDKDVEQLLMdGIRRHFPEHKFIGEEEssgaeGVKKLTDEP 88
Cdd:cd01515 2 LEIARNIAKEIEKAIKPlfGTEDASEVVKIGADGTPTKLIDKVAEDAAI-EILKKLGSVNIVSEEI-----GVIDNGDEP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TW--IIDPVDGTMNFVHAFPHSCISVGLKVNKVTEL--GLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGKALVTS 164
Cdd:cd01515 76 EYtvVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPyyGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDFSSLKSISVSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 165 EFGTTRDEAKMKVVhENFEKMakkahglRVLGSAALNMSMVALGAADA--NYEFGIHAWDVCAGDLIVREAGGVVIDPAG 242
Cdd:cd01515 156 YIYGKNHDRTFKIC-RKVRRV-------RIFGSVALELCYVASGALDAfvDVRENLRLVDIAAGYLIAEEAGGIVTDENG 227
|
250 260 270
....*....|....*....|....*....|
gi 21357329 243 GE----FDIMSRRVLAAATPELAQEISKVL 268
Cdd:cd01515 228 KElklkLNVTERVNIIAANSELHKKLLELL 257
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
11-246 |
3.45e-27 |
|
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: 105.61 E-value: 3.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSnDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEESSgAEGVKKLTDEPTW 90
Cdd:TIGR01331 2 LDDVIKIARAAGEEILPVYQKELAVAQKA-DNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDAS-IPLTPRQTWQRFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNG------RRIHVsGQKELGKALVTS 164
Cdd:TIGR01331 80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGdgqalkAPIHV-RPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 165 efGTTRDEAKMKvvhenfEKMAKKAHGLRVLGSAALNMSMVALGAADANYEFG-IHAWDVCAGDLIVREAGGVVIDPAGG 243
Cdd:TIGR01331 159 --SRSHAEEKTT------EYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGpTGEWDTAAGHAVLAAAGGAIFDLDGS 230
|
...
gi 21357329 244 EFD 246
Cdd:TIGR01331 231 PLL 233
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
5-268 |
1.83e-19 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 85.93 E-value: 1.83e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 5 VDVEKCLEVASNLVSEAGRLIARNNEQRQDFVCKSnDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEE-----SSGAE 79
Cdd:PLN02911 31 AVLDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKE-DLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHglrcgEGSSD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 80 GVkkltdeptWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHGAFYNGRRIHVSGQKELGK 159
Cdd:PLN02911 110 YV--------WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEISTRSCASLKD 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 160 ALV--TSEFGTTRDEAkmkvvhENFEKMAKK-----------AHGLrvlgsaalnmsmVALGAADANYEFGIHAWDVCAG 226
Cdd:PLN02911 182 AYLytTSPHMFSGDAE------DAFARVRDKvkvplygcdcyAYGL------------LASGHVDLVVESGLKPYDYLAL 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 21357329 227 DLIVREAGGVVID---------PAGGEFDImSRRVLAAATPELAQEISKVL 268
Cdd:PLN02911 244 VPVVEGAGGVITDwkgrklrwePSPGSLAT-SFNVVAAGDARLHKQALDIL 293
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
6-268 |
2.66e-17 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 81.31 E-value: 2.66e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 6 DVEKCLEVASNLVSEAGRLIAR--NNEQRQDFVCKSND------IDLVTqtdkdvEQLLMDGIRRhFPEHKFIGEEEssg 77
Cdd:PRK14076 1 MAMDMLKIALKVAKEIEKKIKPliGWEKAGEVVKIGADgtptkrIDLIA------ENIAINSLEK-FCSGILISEEI--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 78 aeGVKKLTDE-PTWI--IDPVDGTMNFVHAFPHSCISVGL-KVNKVT----------------ELGLVYNPILEQRFTAR 137
Cdd:PRK14076 71 --GFKKIGKNkPEYIfvLDPIDGTYNALKDIPIYSASIAIaKIDGFDkkikefigknltindlEVGVVKNIATGDTYYAE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 138 RGHGAFY----NGRRIHVSGQKELGKALVTS-EFGTTRDEAKmkvvhenFEKmAKKAHGLRVLGSAALNMSMVALGAADA 212
Cdd:PRK14076 149 KGEGAYLlkkgEKKKIEISNISNLKDASIGLfAYGLSLDTLK-------FIK-DRKVRRIRLFGSIALEMCYVASGALDA 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 21357329 213 --NYEFGIHAWDVCAGDLIVREAGGVVIDPAGGE----FDIMSRRVLAAATPELAQEISKVL 268
Cdd:PRK14076 221 fiNVNETTRLCDIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSVICSNEILHKKLVGIF 282
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
11-211 |
2.55e-12 |
|
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: 65.16 E-value: 2.55e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIARNNEQRQDFVCKSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEesSGaeGVKKLTDEPTW 90
Cdd:cd01642 2 LEVLEKITKEIILLLNEKNRQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEE--SG--EIRKGSGEYIA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 91 IIDPVDGTMNFVHAFPHSCISVGL-KVNKVTELGLVYNpileqrFTARRGHGAFYN----GRRIHVSGQKELGKALVTSE 165
Cdd:cd01642 78 VLDPLDGSTNYLSGIPFYSVSVALaDPRSKVKAATLDN------FVSGEGGLKVYSpptrFSYISVPKLGPPLVPEVPSK 151
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 21357329 166 ----FGTTRDEAKMKVVHENFEKmakkahgLRVLGSAALNMSMVALGAAD 211
Cdd:cd01642 152 igiyEGSSRNPEKFLLLSRNGLK-------FRSLGSAALELAYTCEGSFV 194
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
38-242 |
5.99e-12 |
|
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: 64.65 E-value: 5.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 38 KSNDIDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEESSGAEGVKKLTD---------EPT--------------WiIDP 94
Cdd:cd01640 35 KEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDvdldeeileESCpspskdlpeedlgvW-VDP 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 95 VDGTMNFVHAFPHSC-ISVGLKVNKVTELGLVYNPILEQrfTArrGHGAFYN-------GRRIHVSGQKEL---GKALVt 163
Cdd:cd01640 114 LDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIHQPFYEK--TA--GAGAWLGrtiwglsGLGAHSSDFKERedaGKIIV- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 164 sefgTTRDEAKMKVVHenfEKMAKKAHGLRVLGSAALNMSMVALGAADAnYEF---GIHAWDVCAGDLIVREAGGVVIDP 240
Cdd:cd01640 189 ----STSHSHSVKEVQ---LITAGNKDEVLRAGGAGYKVLQVLEGLADA-YVHstgGIKKWDICAPEAILRALGGDMTDL 260
|
..
gi 21357329 241 AG 242
Cdd:cd01640 261 HG 262
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
11-250 |
1.07e-06 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 48.54 E-value: 1.07e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 11 LEVASNLVSEAGRLIAR--NNEQRQDFVCKSNDiDLVTQTDKDVEQLLMDGIRRHFPEHKFIGEEESSGAEGVKKLtdEP 88
Cdd:PRK10931 2 LEQICQLARNAGDAIMQvyDGTKPLDVASKADD-SPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHW--QR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 89 TWIIDPVDGTMNFVHAFPHSCISVGLKVNKVTELGLVYNPILEQRFTARRGHgAFY--NGRRIHVSGQKELGKALVTSef 166
Cdd:PRK10931 79 YWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKeeCGVRKQIQVRDARPPLVVIS-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 21357329 167 gttRDEAKmkvvHENFEKMAKKA-HGLRVLGSaALNMSMVALGAADANYEFG-IHAWDVCAGDLIVREAGGVVIDPAGGE 244
Cdd:PRK10931 156 ---RSHAD----AELKEYLQQLGeHQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNIWDTAAGHAVAIAAGAHVHDWQGKT 227
|
....*.
gi 21357329 245 FDIMSR 250
Cdd:PRK10931 228 LDYTPR 233
|
|
| |
