|
Name |
Accession |
Description |
Interval |
E-value |
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
10-261 |
6.00e-137 |
|
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: 386.04 E-value: 6.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYEKkDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQWDRYW 89
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQK-ELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 90 LVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPDlNDSVKIKTHRHELPNQSIAMAI 169
Cdd:TIGR01331 80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGD-GQALKAPIHVRPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 170 SRRQDINRITNRMsSAWNYDLVPLGSAALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSYNER 249
Cdd:TIGR01331 159 SRSHAEEKTTEYL-ANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237
|
250
....*....|..
gi 1327167620 250 ETLENPNFIVLG 261
Cdd:TIGR01331 238 ESFRNPNFVALG 249
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
7-264 |
2.06e-132 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 374.88 E-value: 2.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 7 LSHLLPSIIEIARSAGQLILEIYEKkDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQWD 86
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRA-DFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 87 RYWLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPDLNDSVKIKThRHELPNQSIA 166
Cdd:COG1218 80 RFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGERQPIRV-RDRPPAEPLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 167 MAISRRQDINRITNRMSSAWNYDLVPLGSaALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSY 246
Cdd:COG1218 159 VVASRSHRDEETEALLARLGVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRY 237
|
250
....*....|....*...
gi 1327167620 247 NERETLENPNFIVLGDAD 264
Cdd:COG1218 238 NKKEDLLNPGFIASGDHA 255
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
10-259 |
8.36e-106 |
|
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: 306.84 E-value: 8.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYeKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLeqRSQWDRYW 89
Cdd:cd01638 1 LLELLIRIAREAGDAILEVY-RGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 90 LVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPdlnDSVKIKTHRHELPNQSIAMAI 169
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNG---RPGAVSLQARPPPLQPLRVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 170 SRRQDINRITNRMSSAWNYDLVPLGSaALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSYNeR 249
Cdd:cd01638 155 SRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-R 232
|
250
....*....|
gi 1327167620 250 ETLENPNFIV 259
Cdd:cd01638 233 EDFLNPDFIA 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
10-259 |
6.16e-80 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 241.52 E-value: 6.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYE-KKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADiSLEQRSQWDRY 88
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDgTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPP-AWEVRQHWQRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 89 WLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKgAWKipDLNDSVK-IKTHRHELPnqsiAM 167
Cdd:PRK10931 80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWK--EECGVRKqIQVRDARPP----LV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 168 AISRRQDINRITNRMSSAWNYDLVPLGSaALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSYN 247
Cdd:PRK10931 153 VISRSHADAELKEYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
250
....*....|..
gi 1327167620 248 ERETLENPNFIV 259
Cdd:PRK10931 232 PRESFLNPGFRV 243
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-249 |
5.09e-54 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 176.00 E-value: 5.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 6 DLSHLLPSIIEIARSAGQLILEIY-EKKDYEEFTKSDDT-PVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRS 83
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFsNKLTIEEKGKSGANdLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 84 QWDRY-WLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKipdlnDSVKIKTHR-HELP 161
Cdd:pfam00459 81 TDDGPtWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFL-----NGQPLPVSRaPPLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 162 NQSIAMAI--SRRQDINR--ITNRMSSAWNYDLVP-LGSAALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRI 236
Cdd:pfam00459 156 EALLVTLFgvSSRKDTSEasFLAKLLKLVRAPGVRrVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVV 235
|
250
....*....|...
gi 1327167620 237 LSTQLEPLSYNER 249
Cdd:pfam00459 236 TDADGGPFDLLAG 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
10-261 |
6.00e-137 |
|
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: 386.04 E-value: 6.00e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYEKkDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQWDRYW 89
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQK-ELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 90 LVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPDlNDSVKIKTHRHELPNQSIAMAI 169
Cdd:TIGR01331 80 LVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGD-GQALKAPIHVRPWPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 170 SRRQDINRITNRMsSAWNYDLVPLGSAALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSYNER 249
Cdd:TIGR01331 159 SRSHAEEKTTEYL-ANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKR 237
|
250
....*....|..
gi 1327167620 250 ETLENPNFIVLG 261
Cdd:TIGR01331 238 ESFRNPNFVALG 249
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
7-264 |
2.06e-132 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 374.88 E-value: 2.06e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 7 LSHLLPSIIEIARSAGQLILEIYEKkDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQWD 86
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRA-DFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 87 RYWLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPDLNDSVKIKThRHELPNQSIA 166
Cdd:COG1218 80 RFWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGERQPIRV-RDRPPAEPLR 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 167 MAISRRQDINRITNRMSSAWNYDLVPLGSaALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSY 246
Cdd:COG1218 159 VVASRSHRDEETEALLARLGVAELVSVGS-SLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRY 237
|
250
....*....|....*...
gi 1327167620 247 NERETLENPNFIVLGDAD 264
Cdd:COG1218 238 NKKEDLLNPGFIASGDHA 255
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
10-259 |
8.36e-106 |
|
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: 306.84 E-value: 8.36e-106
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYeKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLeqRSQWDRYW 89
Cdd:cd01638 1 LLELLIRIAREAGDAILEVY-RGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPL--RLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 90 LVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPdlnDSVKIKTHRHELPNQSIAMAI 169
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNG---RPGAVSLQARPPPLQPLRVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 170 SRRQDINRITNRMSSAWNYDLVPLGSaALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSYNeR 249
Cdd:cd01638 155 SRSHPDEELEALLAALGVAEVVSIGS-SLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-R 232
|
250
....*....|
gi 1327167620 250 ETLENPNFIV 259
Cdd:cd01638 233 EDFLNPDFIA 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
10-259 |
6.16e-80 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 241.52 E-value: 6.16e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYE-KKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADiSLEQRSQWDRY 88
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDgTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPP-AWEVRQHWQRY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 89 WLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKgAWKipDLNDSVK-IKTHRHELPnqsiAM 167
Cdd:PRK10931 80 WLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWK--EECGVRKqIQVRDARPP----LV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 168 AISRRQDINRITNRMSSAWNYDLVPLGSaALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRILSTQLEPLSYN 247
Cdd:PRK10931 153 VISRSHADAELKEYLQQLGEHQTTSIGS-SLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYT 231
|
250
....*....|..
gi 1327167620 248 ERETLENPNFIV 259
Cdd:PRK10931 232 PRESFLNPGFRV 243
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
8-272 |
1.11e-55 |
|
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: 179.66 E-value: 1.11e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 8 SHLLPSIIEIARSAGQLILEIYEKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRsqwDR 87
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDS---GY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 88 YWLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWkipdLNDsVKIKT-HRHELPNQSIA 166
Cdd:COG0483 78 VWVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAF----LNG-RRLRVsARTDLEDALVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 167 MAISRRQDINRITNRMSSAWN--YDLVPLGSAALKACLVAEGAVDCYLRIGpTGEWDTAATQCIVEEAGGRILSTQLEPL 244
Cdd:COG0483 153 TGFPYLRDDREYLAALAALLPrvRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPL 231
|
250 260
....*....|....*....|....*...
gi 1327167620 245 SYNEREtlenpnfIVLGDADLpWAEILQ 272
Cdd:COG0483 232 DLGSGS-------LVAANPAL-HDELLA 251
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
14-252 |
5.39e-55 |
|
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: 177.51 E-value: 5.39e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 14 IIEIARSAGQLILEIYEKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDAdiSLEQRSQWDRYWLVDP 93
Cdd:cd01637 4 ALKAVREAGALILEAFGEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGG--GSGNVSDGGRVWVIDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 94 LDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKIPdlNDSVKIKTHRhelPNQSIAMAISRRQ 173
Cdd:cd01637 82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNG--KKLPLSKDTP---LNDALLSTNASML 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 174 DINRITNRMSSAWNYDLVP-LGSAALKACLVAEGAVDCYLRIGPtGEWDTAATQCIVEEAGGRILSTQLEPLSYNERETL 252
Cdd:cd01637 157 RSNRAAVLASLVNRALGIRiYGSAGLDLAYVAAGRLDAYLSSGL-NPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRSGI 235
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-249 |
5.09e-54 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 176.00 E-value: 5.09e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 6 DLSHLLPSIIEIARSAGQLILEIY-EKKDYEEFTKSDDT-PVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRS 83
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFsNKLTIEEKGKSGANdLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 84 QWDRY-WLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWKipdlnDSVKIKTHR-HELP 161
Cdd:pfam00459 81 TDDGPtWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFL-----NGQPLPVSRaPPLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 162 NQSIAMAI--SRRQDINR--ITNRMSSAWNYDLVP-LGSAALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAGGRI 236
Cdd:pfam00459 156 EALLVTLFgvSSRKDTSEasFLAKLLKLVRAPGVRrVGSAALKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVV 235
|
250
....*....|...
gi 1327167620 237 LSTQLEPLSYNER 249
Cdd:pfam00459 236 TDADGGPFDLLAG 248
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
15-236 |
3.39e-43 |
|
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: 147.30 E-value: 3.39e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 15 IEIARSAGQLILEIYEKKDYEEFTKSDDT-PVTSADLAAHKLILKKLSELTPDIPVLSEEDAdISLEQRSQWdrYWLVDP 93
Cdd:cd01639 6 IEAARKAGEILLEAYEKLGLNVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEESG-AAGGLTDEP--TWIIDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 94 LDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWkipdLNDSvKIKTHRHELPNQS-IAMAIS-- 170
Cdd:cd01639 83 LDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAF----LNGR-RIRVSGRKELKDAlVATGFPyd 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327167620 171 RRQDINRITNRMSSAWNY---DLVPLGSAALKACLVAEGAVDCYLRIGpTGEWDTAATQCIVEEAGGRI 236
Cdd:cd01639 158 RGDNFDRYLNNFAKLLAKavrGVRRLGSAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLV 225
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
38-259 |
1.03e-37 |
|
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: 133.98 E-value: 1.03e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 38 TKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADisleqrsQWDRYWLVDPLDGTQEFIarSGD-FATIIALIEH 116
Cdd:cd01517 31 KKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA-------ALGRFWVLDPIDGTKGFL--RGDqFAVALALIED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 117 NKPVMGVVYAPVSGVS-------YYAYSGKGAWKIPDLNDSVKIKTHRHELPNQSIAMAISRRQ---DINRITNRMSSAW 186
Cdd:cd01517 102 GEVVLGVIGCPNLPLDdggggdlFSAVRGQGAWLRPLDGSSLQPLSVRQLTNAARASFCESVESahsSHRLQAAIKALGG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 187 NYDLVPLGSAAlKACLVAEGAVDCYLRIgPTGE------WDTAATQCIVEEAGGRILSTQLEPLSY-NERETLENPNFIV 259
Cdd:cd01517 182 TPQPVRLDSQA-KYAAVARGAADFYLRL-PLSMsyrekiWDHAAGVLIVEEAGGKVTDADGKPLDFgKGRKLLNNGGLIA 259
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
11-261 |
5.81e-35 |
|
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: 125.91 E-value: 5.81e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 11 LPSIIEIARSAGQLILEIYEKKDYEEfTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADIslEQRSQWdrYWL 90
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAE-TKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGI--FPSSGW--YWV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 91 VDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWkipdLNDsVKIKTHRHE-LPNQSIAMAI 169
Cdd:cd01643 76 IDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAF----LNG-KPLALHPPLqLPDCNVGFNR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 170 SRRQDINRITNRMSSAWNYDLVPLGSAALKACLVAEGAVDCYLRIGPTgEWDTAATQCIVEEAGGRILSTQLEPLSYNER 249
Cdd:cd01643 151 SSRASARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPK-IWDIAAAWVILREAGGSWTILDEEPAFLQTK 229
|
250
....*....|..
gi 1327167620 250 ETLENPNFIVLG 261
Cdd:cd01643 230 DYLSAGFPTLIA 241
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
11-236 |
9.13e-32 |
|
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: 115.95 E-value: 9.13e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 11 LPSIIEIARSAGQLILEIY--EKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQWDRY 88
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFgrELSGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 89 WLVDPLDGTQEFIARSGDFATIIALIehnkpvmgvvyapVSGVSYYAYsgkgawkipdlndsvkiktHRHELPNqsiaMA 168
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY-------------VILILAEPS-------------------HKRVDEK----KA 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1327167620 169 ISRRQDINRITNrmssawnydlvpLGSAALKACLVAEGAVDCYLRIGPTGE-WDTAATQCIVEEAGGRI 236
Cdd:cd01636 125 ELQLLAVYRIRI------------VGSAVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIM 181
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
16-236 |
1.39e-30 |
|
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: 114.66 E-value: 1.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 16 EIARSAGQLILEiYEKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDAdislEQRSQWDRYWLVDPLD 95
Cdd:cd01641 7 ELADAAGQITLP-YFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFG----NEGGDAGYVWVLDPID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 96 GTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAW------------KIPDLNDSVKIKTHRHELPNQ 163
Cdd:cd01641 82 GTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFlngaggrplrvrACADLAEAVLSTTDPHFFTPG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327167620 164 SIAmAISRRQDINRITNRMSSAWNYdlvplgsaalkaCLVAEGAVDCYLRIG--PtgeWDTAATQCIVEEAGGRI 236
Cdd:cd01641 162 DRA-AFERLARAVRLTRYGGDCYAY------------ALVASGRVDLVVEAGlkP---YDVAALIPIIEGAGGVI 220
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
6-237 |
2.25e-29 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 112.09 E-value: 2.25e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 6 DLSHLLPSIIEIARSAGQLILE-IYEKKDYEEFTKSDdtPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQ 84
Cdd:PLN02553 6 DLEQFLEVAVDAAKAAGQIIRKgFYQTKHVEHKGQVD--LVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 85 WDRYWLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWkipdLNDSvKIKTH-RHELPNQ 163
Cdd:PLN02553 84 DEPTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAF----LNGK-PIKASsQSELGKA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 164 SIAMAISRRQD---INRITNRMSSawnydLVPL-------GSAALKACLVAEGAVDCYLRIGPTGEWDTAATQCIVEEAG 233
Cdd:PLN02553 159 LLATEVGTKRDkatVDATTNRINA-----LLYKvrslrmsGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAG 233
|
....
gi 1327167620 234 GRIL 237
Cdd:PLN02553 234 GLVF 237
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
15-236 |
2.24e-27 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 106.53 E-value: 2.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 15 IEIARSAGQLILEIYEKKDYEEFTK--SDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEdADISLEQRSQWDRYwlVD 92
Cdd:PRK12676 11 DDMAKEVEKAIMPLFGTPDAGETVGmgADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEE-LGEIVGNGPEYTVV--LD 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 93 PLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAWkipdLNDsVKIKTHRHELPNQSiAMAIS-R 171
Cdd:PRK12676 88 PLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAY----LNG-KPIKVSKTSELNES-AVSIYgY 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1327167620 172 RQDINRITNRMSSAWNYDLvpLGSAALKACLVAEGAVDC------YLRigPTgewDTAATQCIVEEAGGRI 236
Cdd:PRK12676 162 RRGKERTVKLGRKVRRVRI--LGAIALELCYVASGRLDAfvdvrnYLR--VT---DIAAGKLICEEAGGIV 225
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
15-236 |
9.85e-27 |
|
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: 104.77 E-value: 9.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 15 IEIARSAGQLILEIYEKKDYEEFTK--SDDTPVTSADLAAHKLILKKLSELTPdIPVLSEEDADISLEQRSQWdrYWLVD 92
Cdd:cd01515 6 RNIAKEIEKAIKPLFGTEDASEVVKigADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIDNGDEPEY--TVVLD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 93 PLDGTQEFIARSGDFATIIALIEHNK--PVMGVVYAPVSGVSYYAYSGKGAWkipdLNDSvKIKTHRHELPNQSIAMAIS 170
Cdd:cd01515 83 PLDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAY----LNGK-RIKVSDFSSLKSISVSYYI 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1327167620 171 RRQ------DINRITNRMSSawnydlvpLGSAALKACLVAEGAVDCYLRIGPTGE-WDTAATQCIVEEAGGRI 236
Cdd:cd01515 158 YGKnhdrtfKICRKVRRVRI--------FGSVALELCYVASGALDAFVDVRENLRlVDIAAGYLIAEEAGGIV 222
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
15-259 |
1.09e-21 |
|
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.
Pssm-ID: 273558 [Multi-domain] Cd Length: 353 Bit Score: 92.62 E-value: 1.09e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 15 IEIARSAGQLILEIYEK----KDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDAD-------------- 76
Cdd:TIGR01330 10 TQAVRLASLLTKKVQSElishKDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSglseadftlgrvne 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 77 -----ISLEQRSQWD--------------------------RYWLVDPLDGTQEFIaRSGDFATIIALIEHNKPVMGVVY 125
Cdd:TIGR01330 90 lvnetLVYAKNYKKDdqfplksledvlqiidfgnyeggrkgRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 126 AP----------------VSGVSYYAYSGKGAWKIPDLNDS---VKIKTHRHELP--------------NQSIAMAISRR 172
Cdd:TIGR01330 169 CPnlplssygaqnlkgseSKGCIFRAVRGSGAFMYSLSSDAespTKVHVSSVKDTkdaifcegvekghsSHDEQTAIANK 248
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 173 QDINRITNRMSSAWNYdlvplgsaalkaCLVAEGAVDCYLRIGPTGE-----WDTAATQCIVEEAGGRILSTQLEPLSYN 247
Cdd:TIGR01330 249 LGISKSPLRLDSQAKY------------AALARGDADVYLRLPIKLSyqekiWDHAAGNVIVEEAGGIVTDAMGKPLDFG 316
|
330
....*....|..
gi 1327167620 248 ERETLENPNFIV 259
Cdd:TIGR01330 317 KGRTLALDKGVI 328
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
15-234 |
2.88e-21 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 90.25 E-value: 2.88e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 15 IEIARSAGQLILEIYEKKDYEEFT-KSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRsqwDRYWLVDP 93
Cdd:PRK10757 9 VRAARKAGNLIAKNYETPDAVEASqKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQ---DVQWVIDP 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 94 LDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGVSYYAYSGKGAwkipDLNDSVKIKTHRHELPNQSIAMA--ISR 171
Cdd:PRK10757 86 LDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGA----QLNGYRLRGSTARDLDGTILATGfpFKA 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1327167620 172 RQDINRITNRMSSAWNY--DLVPLGSAALKACLVAEGAVDCYLRIGpTGEWDTAATQCIVEEAGG 234
Cdd:PRK10757 162 KQHATTYINIVGKLFTEcaDFRRTGSAALDLAYVAAGRVDGFFEIG-LKPWDFAAGELLVREAGG 225
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
14-256 |
2.72e-20 |
|
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: 88.15 E-value: 2.72e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 14 IIEIARSAGQL-ILEIYEKKDyeeftKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADI--------------- 77
Cdd:cd01640 15 IARDVVKKGRLlILLVEGKTK-----EGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFenqedesrdvdldee 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 78 SLEQ--RSQWDRY-------WlVDPLDGTQEFIARSGDFATIIALIEHN-KPVMGVVYAPvsgvsyyaYSGKGAWKIPDL 147
Cdd:cd01640 90 ILEEscPSPSKDLpeedlgvW-VDPLDATQEYTEGLLEYVTVLIGVAVKgKPIAGVIHQP--------FYEKTAGAGAWL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 148 NDSV----KIKTH---RHELPNQSIAMAISRRQDINRITNRMSSAWNYDLVPLGSAALKACLVAEGAVDCYLRI-GPTGE 219
Cdd:cd01640 161 GRTIwglsGLGAHssdFKEREDAGKIIVSTSHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHStGGIKK 240
|
250 260 270
....*....|....*....|....*....|....*..
gi 1327167620 220 WDTAATQCIVEEAGGRILSTQLEPLSYNERETLENPN 256
Cdd:cd01640 241 WDICAPEAILRALGGDMTDLHGEPLSYSKAVKPVNKG 277
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
7-236 |
8.15e-15 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 73.30 E-value: 8.15e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 7 LSHLLPSIIEIARSAGQLILEIYEKK---DYEEFTKSddtpVTSADLAAHKLILKKLSELTPDIPVLSEEDADISleqRS 83
Cdd:PLN02737 76 AEELLAVAELAAKTGAEVVMEAVNKPrniSYKGLTDL----VTDTDKASEAAILEVVRKNFPDHLILGEEGGVIG---DS 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 84 QWDRYWLVDPLDGTQEFIARSGDFATIIALIEHNKPVMGVVYAPVSGV------SYYAYSGKGAW---------KIPDLN 148
Cdd:PLN02737 149 SSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGPmcwntrTFSASAGGGAFcngqkihvsQTDKVE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 149 DSVKIK--THRHELPNQSIAMAISRRQDINRITNRmssawnydlvpLGSAALKACLVAEGAVDCY--LRIGPtgeWDTAA 224
Cdd:PLN02737 229 RSLLVTgfGYEHDDAWATNIELFKEFTDVSRGVRR-----------LGAAAVDMCHVALGIVEAYweYRLKP---WDMAA 294
|
250
....*....|..
gi 1327167620 225 TQCIVEEAGGRI 236
Cdd:PLN02737 295 GVLIVEEAGGTV 306
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
16-128 |
1.88e-13 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 68.98 E-value: 1.88e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 16 EIARSAGQLILEiYEKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEDADISLEQRSQWdrYWLVDPLD 95
Cdd:PLN02911 42 KLADAAGEVTRK-YFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDY--VWVLDPID 118
|
90 100 110
....*....|....*....|....*....|...
gi 1327167620 96 GTQEFIARSGDFATIIALIEHNKPVMGVVYAPV 128
Cdd:PLN02911 119 GTKSFITGKPLFGTLIALLYKGKPVLGIIDQPV 151
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
16-252 |
5.38e-09 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 56.66 E-value: 5.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 16 EIARSAGQLILeiYEKKDyeEFTK--SDDTPVTSADLAAHKLILKKLSELTPDIpVLSEEdadISLEQ--RSQWDRYWLV 91
Cdd:PRK14076 15 EIEKKIKPLIG--WEKAG--EVVKigADGTPTKRIDLIAENIAINSLEKFCSGI-LISEE---IGFKKigKNKPEYIFVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 92 DPLDGTQEFIARSGDFATIIALIEHNKPV-----------------MGVVYAPVSGVSYYAYSGKGAW------------ 142
Cdd:PRK14076 87 DPIDGTYNALKDIPIYSASIAIAKIDGFDkkikefigknltindleVGVVKNIATGDTYYAEKGEGAYllkkgekkkiei 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 143 -KIPDLNDSvKIKTHRHELPNQSIAMAISRRqdINRItnRMssawnydlvpLGSAALKACLVAEGAVDCYLRIGPTGEW- 220
Cdd:PRK14076 167 sNISNLKDA-SIGLFAYGLSLDTLKFIKDRK--VRRI--RL----------FGSIALEMCYVASGALDAFINVNETTRLc 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1327167620 221 DTAATQCIVEEAGGRILSTQLEP----LSYNERETL 252
Cdd:PRK14076 232 DIAAGYVICKEAGGIITNKNGKPlnmkLDINEKTSV 267
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
10-224 |
1.42e-07 |
|
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: 51.29 E-value: 1.42e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 10 LLPSIIEIARSAGQLILEIYEKKDYEEFTKSDDTPVTSADLAAHKLILKKLSELTPDIPVLSEEdadiSLEQRSQWDRY- 88
Cdd:cd01642 1 MLEVLEKITKEIILLLNEKNRQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEE----SGEIRKGSGEYi 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 89 WLVDPLDGTQEFIARSGDFATIIALIEHNKPV-------------MGVVYAPVSGVSYYAYSGKGAWKIPdlndsvkikt 155
Cdd:cd01642 77 AVLDPLDGSTNYLSGIPFYSVSVALADPRSKVkaatldnfvsgegGLKVYSPPTRFSYISVPKLGPPLVP---------- 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1327167620 156 hrhELPNQSIAMAISRRqDINRITnrMSSAWNYDLVPLGSAALKACLVAEGAVDCYLRI-GPTGEWDTAA 224
Cdd:cd01642 147 ---EVPSKIGIYEGSSR-NPEKFL--LLSRNGLKFRSLGSAALELAYTCEGSFVLFLDLrGKLRNFDVAA 210
|
|
| |
