|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
1-246 |
0e+00 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 535.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDGAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHWQRYW 80
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHSD 160
Cdd:PRK10931 81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 161 SELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESFLNPG 240
Cdd:PRK10931 161 AELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFLNPG 240
|
....*.
gi 505385386 241 FRVSLY 246
Cdd:PRK10931 241 FRVSIY 246
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-244 |
3.89e-134 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 377.96 E-value: 3.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYdgAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQS-WDERQHWQRY 79
Cdd:COG1218 4 LLEAAIEIAREAGEAILEIY--RADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIpYEERKSWDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 80 WLVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEECGV-RKQIQVR---DARPPLVVI 154
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQgAFKETGGGeRQPIRVRdrpPAEPLRVVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 155 SRSHSDSELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTaaghavaaaagahvHDWQGKPLDYTPRE 234
Cdd:COG1218 162 SRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTaagqaileaaggrvTDLDGKPLRYNKKE 241
|
250
....*....|
gi 505385386 235 SFLNPGFRVS 244
Cdd:COG1218 242 DLLNPGFIAS 251
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
1-244 |
5.22e-132 |
|
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: 372.55 E-value: 5.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDgaKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEE-APQSWDERQHWQRY 79
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQ--KELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEdASIPLTPRQTWQRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 80 WLVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGKAWKEE-CG--VRKQIQVR--DARPPLVVI 154
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREgDGqaLKAPIHVRpwPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 155 SRSHSDSELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRE 234
Cdd:TIGR01331 159 SRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKRE 238
|
250
....*....|
gi 505385386 235 SFLNPGFRVS 244
Cdd:TIGR01331 239 SFRNPNFVAL 248
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
1-243 |
9.49e-108 |
|
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: 310.70 E-value: 9.49e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDGakPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWdERQHWQRYW 80
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRG--GFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDP-LRLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEG-KAWKEECGVRKQIQVR--DARPPLVVISRS 157
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGgGAYKNGRPGAVSLQARppPLQPLRVVASRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 158 HSDSELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTpRESFL 237
Cdd:cd01638 158 HPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-REDFL 236
|
....*.
gi 505385386 238 NPGFRV 243
Cdd:cd01638 237 NPDFIA 242
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-206 |
2.67e-46 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 155.20 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 6 CQLARDAGDAIMQVYdgAKPMDVVSKADDS---PVTAADIAAHAVILKGLQALTPDIPVLSEE--APQSWDERQHWQRYW 80
Cdd:pfam00459 10 VELAAKAGEILREAF--SNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEggAKGDQTELTDDGPTW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEEcgvrKQIQVRDARP----PLVVIS 155
Cdd:pfam00459 88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKgAFLNG----QPLPVSRAPPlseaLLVTLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505385386 156 RSHSD------SELEEYLQQLGEHQTTSIGSS-LKFCLVAEGQAQLYPRFGPTNVWDT 206
Cdd:pfam00459 164 GVSSRkdtseaSFLAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDH 221
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
1-246 |
0e+00 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 535.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDGAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHWQRYW 80
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVYDGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHSD 160
Cdd:PRK10931 81 LVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWKEECGVRKQIQVRDARPPLVVISRSHAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 161 SELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESFLNPG 240
Cdd:PRK10931 161 AELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRESFLNPG 240
|
....*.
gi 505385386 241 FRVSLY 246
Cdd:PRK10931 241 FRVSIY 246
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
1-244 |
3.89e-134 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 377.96 E-value: 3.89e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYdgAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQS-WDERQHWQRY 79
Cdd:COG1218 4 LLEAAIEIAREAGEAILEIY--RADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIpYEERKSWDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 80 WLVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEECGV-RKQIQVR---DARPPLVVI 154
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQgAFKETGGGeRQPIRVRdrpPAEPLRVVA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 155 SRSHSDSELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTaaghavaaaagahvHDWQGKPLDYTPRE 234
Cdd:COG1218 162 SRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTaagqaileaaggrvTDLDGKPLRYNKKE 241
|
250
....*....|
gi 505385386 235 SFLNPGFRVS 244
Cdd:COG1218 242 DLLNPGFIAS 251
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
1-244 |
5.22e-132 |
|
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: 372.55 E-value: 5.22e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDgaKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEE-APQSWDERQHWQRY 79
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQ--KELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEdASIPLTPRQTWQRF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 80 WLVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGKAWKEE-CG--VRKQIQVR--DARPPLVVI 154
Cdd:TIGR01331 79 WLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREgDGqaLKAPIHVRpwPSGPLLVVI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 155 SRSHSDSELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRE 234
Cdd:TIGR01331 159 SRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKRE 238
|
250
....*....|
gi 505385386 235 SFLNPGFRVS 244
Cdd:TIGR01331 239 SFRNPNFVAL 248
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
1-243 |
9.49e-108 |
|
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: 310.70 E-value: 9.49e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDGakPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWdERQHWQRYW 80
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRG--GFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDP-LRLGWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEG-KAWKEECGVRKQIQVR--DARPPLVVISRS 157
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGgGAYKNGRPGAVSLQARppPLQPLRVVASRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 158 HSDSELEEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTpRESFL 237
Cdd:cd01638 158 HPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYN-REDFL 236
|
....*.
gi 505385386 238 NPGFRV 243
Cdd:cd01638 237 NPDFIA 242
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
2-206 |
2.51e-51 |
|
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: 167.11 E-value: 2.51e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 2 LDKICQLARDAGDAIMQVYdGAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERqHWQRYWL 81
Cdd:cd01637 1 LELALKAVREAGALILEAF-GEELTVETKKGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVS-DGGRVWV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 82 VDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEECGVRKQIQVRDARPPLVVISRSHSD 160
Cdd:cd01637 79 IDPIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKgAFLNGKKLPLSKDTPLNDALLSTNASMLRS 158
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 505385386 161 SELEEYLQQLGEHQTT-SIGS-SLKFCLVAEGQAQLYPRFGPtNVWDT 206
Cdd:cd01637 159 NRAAVLASLVNRALGIrIYGSaGLDLAYVAAGRLDAYLSSGL-NPWDY 205
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
6-206 |
2.67e-46 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 155.20 E-value: 2.67e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 6 CQLARDAGDAIMQVYdgAKPMDVVSKADDS---PVTAADIAAHAVILKGLQALTPDIPVLSEE--APQSWDERQHWQRYW 80
Cdd:pfam00459 10 VELAAKAGEILREAF--SNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEggAKGDQTELTDDGPTW 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEEcgvrKQIQVRDARP----PLVVIS 155
Cdd:pfam00459 88 IIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKgAFLNG----QPLPVSRAPPlseaLLVTLF 163
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 505385386 156 RSHSD------SELEEYLQQLGEHQTTSIGSS-LKFCLVAEGQAQLYPRFGPTNVWDT 206
Cdd:pfam00459 164 GVSSRkdtseaSFLAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDH 221
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
2-206 |
9.41e-42 |
|
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: 140.61 E-value: 9.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 2 LDKICQLARDAGDAIMQVYDGAKPMDVVS-KADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSW-DERQHWQRY 79
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKVKItKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEeVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 80 WLVDPLDGTKEFIKRNGEFTVNIALIekgkavlgvvyapvmkVMYSAAEgkawkeecgvrkqiqvrdarpplvvisRSHS 159
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY----------------VILILAE---------------------------PSHK 117
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 505385386 160 DSELEEYLQQLGEHQTTSIGSS--LKFCLVAEGQAQLYPRFGPT-NVWDT 206
Cdd:cd01636 118 RVDEKKAELQLLAVYRIRIVGSavAKMCLVALGLADIYYEPGGKrRAWDV 167
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
1-205 |
1.02e-40 |
|
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: 140.37 E-value: 1.02e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYdGAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPqsWDERQHWQRYW 80
Cdd:COG0483 3 LLELALRAARAAGALILRRF-RELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESG--ASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEEcgvrKQIQVRDARPP---LVVISR 156
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGgAFLNG----RRLRVSARTDLedaLVATGF 155
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 505385386 157 SHSDSElEEYLQQLGE-----HQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNVWD 205
Cdd:COG0483 156 PYLRDD-REYLAALAAllprvRRVRRLGSaALDLAYVAAGRLDAFVEAG-LKPWD 208
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
28-241 |
1.09e-33 |
|
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: 122.42 E-value: 1.09e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 28 VVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDerqhwqRYWLVDPLDGTKEFIkRNGEFTVNIALIEK 107
Cdd:cd01517 29 VWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAALG------RFWVLDPIDGTKGFL-RGDQFAVALALIED 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 108 GKAVLGVVYAPVMKV-------MYSAAEGK-AW--KEECGVRKQIQVRDARPP-----LVVISRSHSDSELEEYLQQLGE 172
Cdd:cd01517 102 GEVVLGVIGCPNLPLddggggdLFSAVRGQgAWlrPLDGSSLQPLSVRQLTNAarasfCESVESAHSSHRLQAAIKALGG 181
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 505385386 173 H-QTTSIGSSLKFCLVAEGQAQLYPRFG-----PTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYT-PRESFLNPGF 241
Cdd:cd01517 182 TpQPVRLDSQAKYAAVARGAADFYLRLPlsmsyREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGkGRKLLNNGGL 257
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
1-205 |
8.89e-30 |
|
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: 111.47 E-value: 8.89e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDGAkPMDVVSKADDS-PVTAADIAAHAVILKGLQALTPDIPVLSEE--APQSWDErqhwQ 77
Cdd:cd01639 1 LLNIAIEAARKAGEILLEAYEKL-GLNVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEEsgAAGGLTD----E 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 78 RYWLVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEEcgvrKQIQVRDARPP---LVV 153
Cdd:cd01639 76 PTWIIDPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQgAFLNG----RRIRVSGRKELkdaLVA 151
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 154 ISRSHS-----DSELEEYLQQLGE--HQTTSIGS-SLKFCLVAEGQAQLYPRFGpTNVWD 205
Cdd:cd01639 152 TGFPYDrgdnfDRYLNNFAKLLAKavRGVRRLGSaALDLAYVAAGRLDGYWERG-LKPWD 210
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
7-229 |
1.73e-26 |
|
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: 103.10 E-value: 1.73e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 7 QLARDAGDAIMQVYdgAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPqswDERQHWQRYWLVDPLD 86
Cdd:cd01641 7 ELADAAGQITLPYF--RTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFG---NEGGDAGYVWVLDPID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 87 GTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGKAWKEECGVRKQIQVRDARPP---LVVISRSHSDSEL 163
Cdd:cd01641 82 GTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVRACADLaeaVLSTTDPHFFTPG 161
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505385386 164 EE--YLQQLGEHQTTSIGSS-LKFCLVAEGQAQLYPRFGpTNVWDTAAGHAVAAAAGAHVHDWQGKPLD 229
Cdd:cd01641 162 DRaaFERLARAVRLTRYGGDcYAYALVASGRVDLVVEAG-LKPYDVAALIPIIEGAGGVITDWDGGPLT 229
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
7-205 |
2.88e-20 |
|
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: 86.23 E-value: 2.88e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 7 QLARDAGDaiMQVYDGAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHwqrYWLVDPLD 86
Cdd:cd01643 6 AIAQEAGD--RALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGW---YWVIDPID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 87 GTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEecGVRKQIQVRDARPPLVV-ISRSHSdSELE 164
Cdd:cd01643 81 GTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGgAFLN--GKPLALHPPLQLPDCNVgFNRSSR-ASAR 157
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 505385386 165 EYLQQLGEHQTTSI---GS-SLKFCLVAEGQAQLYPRFGPtNVWD 205
Cdd:cd01643 158 AVLRVILRRFPGKIrmlGSaSLNLASVAAGQTLGYVEATP-KIWD 201
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
24-230 |
3.00e-18 |
|
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: 82.61 E-value: 3.00e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 24 KPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDER---------------QHWQ----------- 77
Cdd:TIGR01330 31 KDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSGLSEAdftlgrvnelvnetlVYAKnykkddqfplk 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 78 --------------------RYWLVDPLDGTKEFIkRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGKAWKEECG 137
Cdd:TIGR01330 111 sledvlqiidfgnyeggrkgRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIGCPNLPLSSYGAQNLKGSESKG 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 138 -----VRK----------------QIQVRDARPPLVVI-----SRSHSDSELEEYL-QQLG-EHQTTSIGSSLKFCLVAE 189
Cdd:TIGR01330 190 cifraVRGsgafmyslssdaesptKVHVSSVKDTKDAIfcegvEKGHSSHDEQTAIaNKLGiSKSPLRLDSQAKYAALAR 269
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 505385386 190 GQAQLYPRFgPTN------VWDTAAGHAVAAAAGAHVHDWQGKPLDY 230
Cdd:TIGR01330 270 GDADVYLRL-PIKlsyqekIWDHAAGNVIVEEAGGIVTDAMGKPLDF 315
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
31-240 |
5.50e-18 |
|
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: 80.83 E-value: 5.50e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 31 KADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHWQRY-------------------------WlVDPL 85
Cdd:cd01640 36 EGANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRDVdldeeileescpspskdlpeedlgvW-VDPL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 86 DGTKEFIKRNGEF-TVNIALIEKGKAVLGVVYAP-VMKVMYSAAEGKAWKEE---CGVRKQIQVRDARPPLVVISRSHSD 160
Cdd:cd01640 115 DATQEYTEGLLEYvTVLIGVAVKGKPIAGVIHQPfYEKTAGAGAWLGRTIWGlsgLGAHSSDFKEREDAGKIIVSTSHSH 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 161 SELEEYLQQLGEHQT--TSIGSSLKFCLVAEGQAQLYpRF--GPTNVWDTAAGHAVAAAAGAHVHDWQGKPLDYTPRESF 236
Cdd:cd01640 195 SVKEVQLITAGNKDEvlRAGGAGYKVLQVLEGLADAY-VHstGGIKKWDICAPEAILRALGGDMTDLHGEPLSYSKAVKP 273
|
....
gi 505385386 237 LNPG 240
Cdd:cd01640 274 VNKG 277
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
1-130 |
9.08e-18 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 79.85 E-value: 9.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQLARDAGDAIMQVYDGAKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHWQryW 80
Cdd:PRK10757 4 MLNIAVRAARKAGNLIAKNYETPDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQDVQ--W 81
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK 130
Cdd:PRK10757 82 VIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQ 131
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
2-121 |
2.93e-15 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 73.22 E-value: 2.93e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 2 LDKICQLARDAGDAIMQVYDG--AKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSW-DERQHWqr 78
Cdd:PLN02911 33 LDRFVDVAHKLADAAGEVTRKyfRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCgEGSSDY-- 110
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 505385386 79 YWLVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMK 121
Cdd:PLN02911 111 VWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLK 153
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
9-130 |
1.76e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 70.87 E-value: 1.76e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 9 ARDAGDAIMQVYDGAKpmDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEE------APQSWDERQhwqryWLV 82
Cdd:PLN02553 18 AKAAGQIIRKGFYQTK--HVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEEttaasgGTELTDEPT-----WIV 90
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 505385386 83 DPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK 130
Cdd:PLN02553 91 DPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGK 138
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
9-115 |
7.25e-07 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 49.41 E-value: 7.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 9 ARDAGDAIMQVYDgaKPMDVVSKADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHWqrYWLVDPLDGT 88
Cdd:PLN02737 87 AKTGAEVVMEAVN--KPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSDY--LWCIDPLDGT 162
|
90 100
....*....|....*....|....*..
gi 505385386 89 KEFIKRNGEFTVNIALIEKGKAVLGVV 115
Cdd:PLN02737 163 TNFAHGYPSFAVSVGVLFRGTPAAATV 189
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
3-149 |
9.25e-07 |
|
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: 48.53 E-value: 9.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 3 DKIC-QLARDAGDAIMQVYDGAKPMDVVS-KADDSPVTAADIAAHAVILKGLQALTPdIPVLSEEAPQSwDERQHWQRYW 80
Cdd:cd01515 2 LEIArNIAKEIEKAIKPLFGTEDASEVVKiGADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVI-DNGDEPEYTV 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 505385386 81 LVDPLDGTKEFIKRNGEFTVNIAL--IEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEecgvRKQIQVRDARP 149
Cdd:cd01515 80 VLDPLDGTYNAINGIPFYSVSVAVfkIDKSDPYYGYVYNLATGDLYYAIKGKgAYLN----GKRIKVSDFSS 147
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
1-229 |
1.65e-03 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 38.74 E-value: 1.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 1 MLDKICQ-LARDAGDAIMQVYDGAKPMDVVSK-ADDSPVTAADIAAHAVILKGLQALTPDIPVLSEEAPQSWDERQHWQR 78
Cdd:PRK12676 5 EWLEICDdMAKEVEKAIMPLFGTPDAGETVGMgADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPEYTV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505385386 79 YwlVDPLDGTKEFIKRNGEFTVNIALIEKGKAVLGVVYAPVMKVMYSAAEGK-AWKEEcgvrKQIQV---RDARPPLVVI 154
Cdd:PRK12676 85 V--LDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKgAYLNG----KPIKVsktSELNESAVSI 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 505385386 155 SRSHSDselEEYLQQLGEH--QTTSIGSS-LKFCLVAEGQAQLYPRFGPT-NVWDTAAGHAVAAAAGAHVHDWQGKPLD 229
Cdd:PRK12676 159 YGYRRG---KERTVKLGRKvrRVRILGAIaLELCYVASGRLDAFVDVRNYlRVTDIAAGKLICEEAGGIVTDEDGNELK 234
|
|
| |
