|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
10-243 |
2.67e-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: 249.54 E-value: 2.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 10 DEYICQWIRGLDDIIPRLVEKMET-STKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPYEGHLWIMD 88
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTvETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 89 PIDGTSNLVKQQEDYCIIIGYFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISFKPQVLKE-- 166
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSnr 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747944 167 -ETVQSLFQSAFDFRSIGSCGLDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSKAGPFIIS 243
Cdd:cd01637 161 aAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
37-257 |
3.10e-56 |
|
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: 181.20 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 37 KDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPyEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFIDGEPK 116
Cdd:COG0483 32 KGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD-SGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 117 LSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISF-----KPQVLKEETVQSLFQSAFDFRSIGSCGLDSIR 191
Cdd:COG0483 111 AGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATgfpylRDDREYLAALAALLPRVRRVRRLGSAALDLAY 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747944 192 VIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSKaGPFIISNPGCYDDMIRILNE 257
Cdd:COG0483 191 VAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGS-GSLVAANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
32-252 |
1.28e-37 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 133.62 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 32 ETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEE---KDNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIG 108
Cdd:pfam00459 31 EEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggaKGDQTELTDDGPTWIIDPIDGTKNFVHGIPQFAVSIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 109 YFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAII--SFKPQVLKEETVQSLFQSAF------DFR 180
Cdd:pfam00459 111 LAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLvtLFGVSSRKDTSEASFLAKLLklvrapGVR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747944 181 SIGSCGLDSIRVIKGQFGAHIN-TNPKPWDISAQFLFARELGLIMTQINGEPLDFSKAGPfIISNPGCYDDMI 252
Cdd:pfam00459 191 RVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAGRV-IAANPKVLHELL 262
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
29-257 |
7.70e-22 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 91.79 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 29 EKMETSTKKDRfDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEK-----DNSDITpyeghlWIMDPIDGTSNLVKQQEDY 103
Cdd:PRK10757 27 DAVEASQKGSN-DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESgelegEDQDVQ------WVIDPLDGTTNFIKRLPHF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 104 CIIIGYFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIIS----FKpqvLKEET------VQSLF 173
Cdd:PRK10757 100 AVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILAtgfpFK---AKQHAttyiniVGKLF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 174 QSAFDFRSIGSCGLDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPlDFSKAGPFIISNPGCYDDMIR 253
Cdd:PRK10757 177 TECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGH-NYMLTGNIVAGNPRVVKAMLA 255
|
....
gi 487747944 254 ILNE 257
Cdd:PRK10757 256 NMRD 259
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
36-235 |
5.31e-06 |
|
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: 46.53 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 36 KKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEkDNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFIDGEP 115
Cdd:TIGR02067 29 KKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE-FGHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 116 KLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISF-KPQVLKEETVQSLFQSAFD----FRSIGSCGlDSI 190
Cdd:TIGR02067 108 VLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTtSPDLLDDPGNRPAFERLRRaarlTRYGGDCY-AYL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487747944 191 RVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFS 235
Cdd:TIGR02067 187 MVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDG 231
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
10-243 |
2.67e-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: 249.54 E-value: 2.67e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 10 DEYICQWIRGLDDIIPRLVEKMET-STKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPYEGHLWIMD 88
Cdd:cd01637 1 LELALKAVREAGALILEAFGEELTvETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 89 PIDGTSNLVKQQEDYCIIIGYFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISFKPQVLKE-- 166
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLSKDTPLNDALLSTNASMLRSnr 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 487747944 167 -ETVQSLFQSAFDFRSIGSCGLDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSKAGPFIIS 243
Cdd:cd01637 161 aAVLASLVNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGIIAA 238
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
37-257 |
3.10e-56 |
|
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: 181.20 E-value: 3.10e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 37 KDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPyEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFIDGEPK 116
Cdd:COG0483 32 KGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD-SGYVWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 117 LSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISF-----KPQVLKEETVQSLFQSAFDFRSIGSCGLDSIR 191
Cdd:COG0483 111 AGVVYDPALGELFTAARGGGAFLNGRRLRVSARTDLEDALVATgfpylRDDREYLAALAALLPRVRRVRRLGSAALDLAY 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747944 192 VIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSKaGPFIISNPGCYDDMIRILNE 257
Cdd:COG0483 191 VAAGRLDAFVEAGLKPWDIAAGALIVREAGGVVTDLDGEPLDLGS-GSLVAANPALHDELLALLRE 255
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
32-236 |
3.65e-38 |
|
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: 134.20 E-value: 3.65e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 32 ETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKdNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFI 111
Cdd:cd01639 26 NVEEKGSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEES-GAAGGLTDEPTWIIDPLDGTTNFVHGFPHFAVSIALAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 112 DGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISFKPQVLKEETVQS--------LFQSAFDFRSIG 183
Cdd:cd01639 105 KGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIRVSGRKELKDALVATGFPYDRGDNFDRylnnfaklLAKAVRGVRRLG 184
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 487747944 184 SCGLDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSK 236
Cdd:cd01639 185 SAALDLAYVAAGRLDGYWERGLKPWDVAAGALIVREAGGLVTDFDGGPFDLMS 237
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
32-252 |
1.28e-37 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 133.62 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 32 ETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEE---KDNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIG 108
Cdd:pfam00459 31 EEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEggaKGDQTELTDDGPTWIIDPIDGTKNFVHGIPQFAVSIG 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 109 YFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAII--SFKPQVLKEETVQSLFQSAF------DFR 180
Cdd:pfam00459 111 LAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPLPVSRAPPLSEALLvtLFGVSSRKDTSEASFLAKLLklvrapGVR 190
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747944 181 SIGSCGLDSIRVIKGQFGAHIN-TNPKPWDISAQFLFARELGLIMTQINGEPLDFSKAGPfIISNPGCYDDMI 252
Cdd:pfam00459 191 RVGSAALKLAMVAAGKADAYIEfGRLKPWDHAAGVAILREAGGVVTDADGGPFDLLAGRV-IAANPKVLHELL 262
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
33-236 |
1.23e-26 |
|
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: 103.95 E-value: 1.23e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 33 TSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEkdNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFID 112
Cdd:cd01643 24 SAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE--GGGIFPSSGWYWVIDPIDGTTNFARGIPIWAISIALLYR 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 113 GEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISF-KPQVLKEETVQSLFQSAF--DFRSIGSCGLDS 189
Cdd:cd01643 102 GEPVFGVIALPALNQTFVAFKGGGAFLNGKPLALHPPLQLPDCNVGFnRSSRASARAVLRVILRRFpgKIRMLGSASLNL 181
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487747944 190 IRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSK 236
Cdd:cd01643 182 ASVAAGQTLGYVEATPKIWDIAAAWVILREAGGSWTILDEEPAFLQT 228
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
32-246 |
4.61e-22 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 92.15 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 32 ETSTKKDRfDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPYEGH--LWIMDPIDGTSNLVKQQEDYCIIIGY 109
Cdd:COG1218 28 EVEEKADD-SPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWdrFWLVDPLDGTKEFIKRNGEFTVNIAL 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 110 FIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTmPKRIGLREAIISFKPQVL-----KEETVQSLFQS--AFDFRSI 182
Cdd:COG1218 107 IEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGE-RQPIRVRDRPPAEPLRVVasrshRDEETEALLARlgVAELVSV 185
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 487747944 183 GScGLDSIRVIKGQFGAHINTNPK-PWDISA-QFLfARELGLIMTQINGEPLDFSKAGPFIisNPG 246
Cdd:COG1218 186 GS-SLKFCLVAEGEADLYPRLGPTmEWDTAAgQAI-LEAAGGRVTDLDGKPLRYNKKEDLL--NPG 247
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
29-257 |
7.70e-22 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 91.79 E-value: 7.70e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 29 EKMETSTKKDRfDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEK-----DNSDITpyeghlWIMDPIDGTSNLVKQQEDY 103
Cdd:PRK10757 27 DAVEASQKGSN-DFVTNVDKAAEAVIIDTIRKSYPQHTIITEESgelegEDQDVQ------WVIDPLDGTTNFIKRLPHF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 104 CIIIGYFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIIS----FKpqvLKEET------VQSLF 173
Cdd:PRK10757 100 AVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARDLDGTILAtgfpFK---AKQHAttyiniVGKLF 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 174 QSAFDFRSIGSCGLDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPlDFSKAGPFIISNPGCYDDMIR 253
Cdd:PRK10757 177 TECADFRRTGSAALDLAYVAAGRVDGFFEIGLKPWDFAAGELLVREAGGIVSDFTGGH-NYMLTGNIVAGNPRVVKAMLA 255
|
....
gi 487747944 254 ILNE 257
Cdd:PRK10757 256 NMRD 259
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
32-244 |
2.71e-20 |
|
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: 87.37 E-value: 2.71e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 32 ETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDitpyeGHLWIMDPIDGTSNLVKQQEdYCIIIGYFI 111
Cdd:cd01517 27 DVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAAL-----GRFWVLDPIDGTKGFLRGDQ-FAVALALIE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 112 DGEPKLSYIYD--YPHQ-----RLYRAIAGIGAYennqlmTMPKRIGLREAIISFKPQVLKEETVQS---------LFQS 175
Cdd:cd01517 101 DGEVVLGVIGCpnLPLDdggggDLFSAVRGQGAW------LRPLDGSSLQPLSVRQLTNAARASFCEsvesahsshRLQA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 176 AFDFRSI--GSCGLDS----IRVIKGQ------FGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFSK------A 237
Cdd:cd01517 175 AIKALGGtpQPVRLDSqakyAAVARGAadfylrLPLSMSYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKgrkllnN 254
|
....*..
gi 487747944 238 GPFIISN 244
Cdd:cd01517 255 GGLIAAP 261
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
35-246 |
4.16e-19 |
|
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of the inositol monophosphatase family. It has been proposed that CysQ helps control intracellular levels of PAPS, which is an intermediate in cysteine biosynthesis (a principal route of sulfur assimilation).
Pssm-ID: 238816 [Multi-domain] Cd Length: 242 Bit Score: 83.81 E-value: 4.16e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 35 TKKDRfDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEkdnSDITPYE---GHLWIMDPIDGTSNLVKQQEDYCIIIGYFI 111
Cdd:cd01638 28 RKEDG-SPVTAADLAANAFIVEGLAALRPDIPVLSEE---SADDPLRlgwDRFWLVDPLDGTREFIKGNGEFAVNIALVE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 112 DGEPKLSYIYDYPHQRLYRAIAGIGAYENN-----QLMTMPKRIGLREAIISFKpqVLKEETVQSLFQ-SAFDFRSIGSc 185
Cdd:cd01638 104 DGRPVLGVVYAPALGELYYALRGGGAYKNGrpgavSLQARPPPLQPLRVVASRS--HPDEELEALLAAlGVAEVVSIGS- 180
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 487747944 186 GLDSIRVIKGQFGAHIN-TNPKPWDISAQFLFARELGLIMTQINGEPLDFSKAGPfiiSNPG 246
Cdd:cd01638 181 SLKFCLVAEGEADIYPRlGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDF---LNPD 239
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
37-233 |
8.25e-18 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 80.50 E-value: 8.25e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 37 KDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEK----DNSDITpyEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFID 112
Cdd:PLN02553 38 KGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaasGGTELT--DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 113 GEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISFKPQVLK-EETVQSLFQS----AFDFRSI---GS 184
Cdd:PLN02553 116 KVPVVGVVYNPILDELFTAVKGKGAFLNGKPIKASSQSELGKALLATEVGTKRdKATVDATTNRinalLYKVRSLrmsGS 195
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 487747944 185 CGLDSIRVIKGQFGAHINTN-PKPWDISAQFLFARELGLIMTQINGEPLD 233
Cdd:PLN02553 196 CALNLCGVACGRLDIFYEIGfGGPWDVAAGAVIVKEAGGLVFDPSGGPFD 245
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
67-235 |
1.73e-15 |
|
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: 73.95 E-value: 1.73e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 67 LLAEE---KDNSDITPYeghLWIMDPIDGTSNLVKQQEDY--CIIIGYFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENN 141
Cdd:cd01515 61 IVSEEigvIDNGDEPEY---TVVLDPLDGTYNAINGIPFYsvSVAVFKIDKSDPYYGYVYNLATGDLYYAIKGKGAYLNG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 142 QLMTMPKRIGLREAIISFKPQVLKEETVQSLFQSAFDFRSIGSCGLDSIRVIKGQFGAHINTNPK--PWDISAQFLFARE 219
Cdd:cd01515 138 KRIKVSDFSSLKSISVSYYIYGKNHDRTFKICRKVRRVRIFGSVALELCYVASGALDAFVDVRENlrLVDIAAGYLIAEE 217
|
170
....*....|....*.
gi 487747944 220 LGLIMTQINGEPLDFS 235
Cdd:cd01515 218 AGGIVTDENGKELKLK 233
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
7-225 |
8.12e-15 |
|
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: 70.88 E-value: 8.12e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 7 KKLDEYICQWIRGlddiiprlVEKMETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEkDNSDITPYEGH--- 83
Cdd:cd01636 9 KEAGLAILKAFGR--------ELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEE-SGVAEEVMGRRdey 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 84 LWIMDPIDGTSNLVKQQEDYCIIIGyfidgepklsyiydyphqrLYRAIAGIGAYEnnqlmtmpkrigLREAIISFKPQV 163
Cdd:cd01636 80 TWVIDPIDGTKNFINGLPFVAVVIA-------------------VYVILILAEPSH------------KRVDEKKAELQL 128
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747944 164 LKEETvqslfqsafdFRSIGSCGLDSIRVIKGQFGAHINTNPK--PWDISAQFLFARELGLIMT 225
Cdd:cd01636 129 LAVYR----------IRIVGSAVAKMCLVALGLADIYYEPGGKrrAWDVAASAAIVREAGGIMT 182
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
37-233 |
8.71e-14 |
|
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: 69.21 E-value: 8.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 37 KDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSdiTPYEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFIDGEPK 116
Cdd:cd01641 29 KADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNE--GGDAGYVWVLDPIDGTKSFIRGLPVWGTLIALLHDGRPV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 117 LSYIYDYPHQRLYRAIAGIGAYENNQLmtmPKRIG------LREAIISF-KPQVLK---EETVQSLFQSAFDFRSIGSCg 186
Cdd:cd01641 107 LGVIDQPALGERWIGARGGGTFLNGAG---GRPLRvracadLAEAVLSTtDPHFFTpgdRAAFERLARAVRLTRYGGDC- 182
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 487747944 187 LDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLD 233
Cdd:cd01641 183 YAYALVASGRVDLVVEAGLKPYDVAALIPIIEGAGGVITDWDGGPLT 229
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
22-231 |
1.63e-13 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 69.44 E-value: 1.63e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 22 DIIPRLVEKMETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPYEgHLWIMDPIDGTSNLVKQQE 101
Cdd:PLN02737 92 EVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSD-YLWCIDPLDGTTNFAHGYP 170
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 102 DYCIIIGYFIDGEPKLSYIYDY---PH---QRLYRAIAGIGAYENNQLMTMPKRIGLREAIISFKPQVLKEE---TVQSL 172
Cdd:PLN02737 171 SFAVSVGVLFRGTPAAATVVEFvggPMcwnTRTFSASAGGGAFCNGQKIHVSQTDKVERSLLVTGFGYEHDDawaTNIEL 250
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 487747944 173 FQSAFD----FRSIGSCGLDSIRVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEP 231
Cdd:PLN02737 251 FKEFTDvsrgVRRLGAAAVDMCHVALGIVEAYWEYRLKPWDMAAGVLIVEEAGGTVTRMDGGK 313
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
86-235 |
2.30e-13 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 68.01 E-value: 2.30e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 86 IMDPIDGTSNLVKQQEDYCIIIGYFIDGEPKLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLRE--AIISFKPQv 163
Cdd:PRK12676 85 VLDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKTSELNEsaVSIYGYRR- 163
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 487747944 164 lKEETVQSLFQSAFDFRSIGSCGLDSIRVIKGQFGAHINTNPK--PWDISAQFLFARELGLIMTQINGEPLDFS 235
Cdd:PRK12676 164 -GKERTVKLGRKVRRVRILGAIALELCYVASGRLDAFVDVRNYlrVTDIAAGKLICEEAGGIVTDEDGNELKLP 236
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
32-239 |
5.87e-11 |
|
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of inositol monophosphatase-like domains, hydrolyzes the 1' position phosphate from inositol 1,3,4-trisphosphate and inositol 1,4-bisphosphate. Members in this group may also exhibit 3'-phosphoadenosine 5'-phosphate phosphatase activity, and they all appear to be inhibited by lithium. IPPase is one of the proposed targets of Li+ therapy in manic-depressive illness.
Pssm-ID: 238818 [Multi-domain] Cd Length: 293 Bit Score: 61.57 E-value: 5.87e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 32 ETSTKKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEKD---NSDITPYEGHL-----------------------W 85
Cdd:cd01640 31 EGKTKEGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNefeNQEDESRDVDLdeeileescpspskdlpeedlgvW 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 86 ImDPIDGTSNLVKQQEDYC-IIIGYFIDGEPKLSYIYdYPH-----------QRLYRAIAGIGAyENNQLMTMPKRiglR 153
Cdd:cd01640 111 V-DPLDATQEYTEGLLEYVtVLIGVAVKGKPIAGVIH-QPFyektagagawlGRTIWGLSGLGA-HSSDFKEREDA---G 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 154 EAIISFKPQVLKEETVQSLFQSAFDFRSIGSCGLDSIRVIKGQFGAHINTNP--KPWDISAQFLFARELGLIMTQINGEP 231
Cdd:cd01640 185 KIIVSTSHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGgiKKWDICAPEAILRALGGDMTDLHGEP 264
|
....*...
gi 487747944 232 LDFSKAGP 239
Cdd:cd01640 265 LSYSKAVK 272
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
83-256 |
1.56e-09 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 58.20 E-value: 1.56e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 83 HLWIMDPIDGTSNLVKQQEDY--CIIIGYfIDGEPK----------------LSYIYDYPHQRLYRAIAGIGAYE----N 140
Cdd:PRK14076 82 YIFVLDPIDGTYNALKDIPIYsaSIAIAK-IDGFDKkikefigknltindleVGVVKNIATGDTYYAEKGEGAYLlkkgE 160
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 141 NQLMTMPKRIGLREAIISFKPQVLKEETVQSLFQSAFD-FRSIGSCGLDSIRVIKGQFGAHINTNP--KPWDISAQFLFA 217
Cdd:PRK14076 161 KKKIEISNISNLKDASIGLFAYGLSLDTLKFIKDRKVRrIRLFGSIALEMCYVASGALDAFINVNEttRLCDIAAGYVIC 240
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 487747944 218 RELGLIMTQINGEPLD-----FSKAGpFIISNPGCYDDMIRILN 256
Cdd:PRK14076 241 KEAGGIITNKNGKPLNmkldiNEKTS-VICSNEILHKKLVGIFG 283
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
36-235 |
5.31e-06 |
|
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: 46.53 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 36 KKDRFDLVTNVDKQIQNHFQNFLQEHYPTHQLLAEEkDNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFIDGEP 115
Cdd:TIGR02067 29 KKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEE-FGHNEEGDAERVWVLDPIDGTKSFIRGVPVWGTLIALVEGGMP 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 116 KLSYIYDYPHQRLYRAIAGIGAYENNQLMTMPKRIGLREAIISF-KPQVLKEETVQSLFQSAFD----FRSIGSCGlDSI 190
Cdd:TIGR02067 108 VLGVIFQPATGERWWAAGGGAAFLGGRRLRVSSCANLSDAVLFTtSPDLLDDPGNRPAFERLRRaarlTRYGGDCY-AYL 186
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 487747944 191 RVIKGQFGAHINTNPKPWDISAQFLFARELGLIMTQINGEPLDFS 235
Cdd:TIGR02067 187 MVAGGAVDIVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPAPDG 231
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
38-124 |
2.67e-04 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 41.63 E-value: 2.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 487747944 38 DRFDL--VTNVDKQIQNHFQNFLQEHYPTHQLLAEEKDNSDITPYEGHLWIMDPIDGTSNLVKQQEDYCIIIGYFIDGEP 115
Cdd:PLN02911 63 DKEDLspVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKP 142
|
....*....
gi 487747944 116 KLSYIyDYP 124
Cdd:PLN02911 143 VLGII-DQP 150
|
|
| |
