|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
5-253 |
4.81e-130 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 368.33 E-value: 4.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 5 PQQLCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVT-DR 83
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSwDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 84 FWLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGV-RSAITCR-RAPLEGCTVV 161
Cdd:COG1218 81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGeRQPIRVRdRPPAEPLRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 162 SSRSHGSEApLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAK 241
Cdd:COG1218 161 ASRSHRDEE-TEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNK 239
|
250
....*....|...
gi 1423782289 242 P-GLDNPHFVASG 253
Cdd:COG1218 240 KeDLLNPGFIASG 252
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
8-251 |
1.31e-107 |
|
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: 1.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 8 LCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPdVTDRFWLV 87
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRL-GWDRFWLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 88 DPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAITCRRAPLEGCTVVSSRSHG 167
Cdd:cd01638 80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRSHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 168 SEaPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAKPGLDNP 247
Cdd:cd01638 160 DE-ELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDFLNP 238
|
....
gi 1423782289 248 HFVA 251
Cdd:cd01638 239 DFIA 242
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
8-253 |
1.03e-95 |
|
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: 280.88 E-value: 1.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 8 LCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIP-DVTDRFWL 86
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPrQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 87 VDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKG--VRSAITCRRAPLEGCTVVSSR 164
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGqaLKAPIHVRPWPSGPLLVVISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 165 SHgSEAPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAK-PG 243
Cdd:TIGR01331 161 SH-AEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKrES 239
|
250
....*....|
gi 1423782289 244 LDNPHFVASG 253
Cdd:TIGR01331 240 FRNPNFVALG 249
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
10-252 |
6.30e-89 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 263.48 E-value: 6.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 10 EEIAAVAREAGKVILDVY--ATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVTDRFWLV 87
Cdd:PRK10931 3 EQICQLARNAGDAIMQVYdgTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYWLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 88 DPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAgAYVEEKGVRSAITCRRA--PLegctVVSSRS 165
Cdd:PRK10931 83 DPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKEECGVRKQIQVRDArpPL----VVISRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 166 HGsEAPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYA-KPGL 244
Cdd:PRK10931 158 HA-DAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTpRESF 236
|
....*...
gi 1423782289 245 DNPHFVAS 252
Cdd:PRK10931 237 LNPGFRVS 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
4-244 |
1.12e-58 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 187.17 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 4 DPQQLCEEIAAVAREAGKVILDVYATDFTVDNKADAS---PVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDV 80
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 81 TD--RFWLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKG--VRSAITCRRAPLE 156
Cdd:pfam00459 81 TDdgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPlpVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 157 GCTVVSSRSHGSEAPLAD-FLAGRRVARSVFAGSS-LKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEG 234
Cdd:pfam00459 161 TLFGVSSRKDTSEASFLAkLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDADG 240
|
250
....*....|
gi 1423782289 235 SELRYAKPGL 244
Cdd:pfam00459 241 GPFDLLAGRV 250
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
5-253 |
4.81e-130 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 368.33 E-value: 4.81e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 5 PQQLCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVT-DR 83
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSwDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 84 FWLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGV-RSAITCR-RAPLEGCTVV 161
Cdd:COG1218 81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGeRQPIRVRdRPPAEPLRVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 162 SSRSHGSEApLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAK 241
Cdd:COG1218 161 ASRSHRDEE-TEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNK 239
|
250
....*....|...
gi 1423782289 242 P-GLDNPHFVASG 253
Cdd:COG1218 240 KeDLLNPGFIASG 252
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
8-251 |
1.31e-107 |
|
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: 1.31e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 8 LCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPdVTDRFWLV 87
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRL-GWDRFWLV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 88 DPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAITCRRAPLEGCTVVSSRSHG 167
Cdd:cd01638 80 DPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVASRSHP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 168 SEaPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAKPGLDNP 247
Cdd:cd01638 160 DE-ELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNREDFLNP 238
|
....
gi 1423782289 248 HFVA 251
Cdd:cd01638 239 DFIA 242
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
8-253 |
1.03e-95 |
|
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: 280.88 E-value: 1.03e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 8 LCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIP-DVTDRFWL 86
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPrQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 87 VDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKG--VRSAITCRRAPLEGCTVVSSR 164
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGqaLKAPIHVRPWPSGPLLVVISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 165 SHgSEAPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAK-PG 243
Cdd:TIGR01331 161 SH-AEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGKrES 239
|
250
....*....|
gi 1423782289 244 LDNPHFVASG 253
Cdd:TIGR01331 240 FRNPNFVALG 249
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
10-252 |
6.30e-89 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 263.48 E-value: 6.30e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 10 EEIAAVAREAGKVILDVY--ATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVTDRFWLV 87
Cdd:PRK10931 3 EQICQLARNAGDAIMQVYdgTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHWQRYWLV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 88 DPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAgAYVEEKGVRSAITCRRA--PLegctVVSSRS 165
Cdd:PRK10931 83 DPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGK-AWKEECGVRKQIQVRDArpPL----VVISRS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 166 HGsEAPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEGSELRYA-KPGL 244
Cdd:PRK10931 158 HA-DAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTpRESF 236
|
....*...
gi 1423782289 245 DNPHFVAS 252
Cdd:PRK10931 237 LNPGFRVS 244
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
4-244 |
1.12e-58 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 187.17 E-value: 1.12e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 4 DPQQLCEEIAAVAREAGKVILDVYATDFTVDNKADAS---PVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDV 80
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 81 TD--RFWLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKG--VRSAITCRRAPLE 156
Cdd:pfam00459 81 TDdgPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQPlpVSRAPPLSEALLV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 157 GCTVVSSRSHGSEAPLAD-FLAGRRVARSVFAGSS-LKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGGHVRTLEG 234
Cdd:pfam00459 161 TLFGVSSRKDTSEASFLAkLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDADG 240
|
250
....*....|
gi 1423782289 235 SELRYAKPGL 244
Cdd:pfam00459 241 GPFDLLAGRV 250
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
6-244 |
1.51e-49 |
|
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: 163.48 E-value: 1.51e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 6 QQLCEEIAAVAREAGKVILDVYAT-DFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGriPDVTDRF 84
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRElDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASE--GRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 85 WLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAitcRRAPLEGCTV-VSS 163
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFLNGRRLRVS---ARTDLEDALVaTGF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 164 RSHGSEAPLADFLAG--RRVARSVFAGS-SLKLCLIAACEADIYPRFGrTMEWDIAAGHAVVRAAGGHVRTLEGSELRYA 240
Cdd:COG0483 156 PYLRDDREYLAALAAllPRVRRVRRLGSaALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGEPLDLG 234
|
....
gi 1423782289 241 KPGL 244
Cdd:COG0483 235 SGSL 238
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
10-243 |
3.79e-48 |
|
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: 159.02 E-value: 3.79e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 10 EEIAAVAREAGKVILDVYATDFTVDNK-ADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDvTDRFWLVD 88
Cdd:cd01637 2 ELALKAVREAGALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSD-GGRVWVID 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 89 PLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAitcRRAPLEGCTVVSSRSHGS 168
Cdd:cd01637 81 PIDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLS---KDTPLNDALLSTNASMLR 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423782289 169 EAPLADFLAGRRVARSV--FAGSSLKLCLIAACEADIYPRFGrTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAKPG 243
Cdd:cd01637 158 SNRAAVLASLVNRALGIriYGSAGLDLAYVAAGRLDAYLSSG-LNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRS 233
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
12-244 |
5.41e-42 |
|
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: 144.38 E-value: 5.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 12 IAAVAREAGKVILDVYATDFTVDnKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAgripdvTDRFWLVDPLD 91
Cdd:cd01517 9 VRAAASLTLPVFRNLGAGDVVWK-KSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAA------LGRFWVLDPID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 92 GTKEFIgRNGEFTVNIALVEHGEPVLGVVFAPAL-------DRLFAGVVGAGAYVEEKGVRSAITCR------RAPLEGC 158
Cdd:cd01517 82 GTKGFL-RGDQFAVALALIEDGEVVLGVIGCPNLplddgggGDLFSAVRGQGAWLRPLDGSSLQPLSvrqltnAARASFC 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 159 TVVSSrSHGSEAPLADFLAGRRVARSVFAGSSLKLCLIAACEADIYPRFG-----RTMEWDIAAGHAVVRAAGGHVRTLE 233
Cdd:cd01517 161 ESVES-AHSSHRLQAAIKALGGTPQPVRLDSQAKYAAVARGAADFYLRLPlsmsyREKIWDHAAGVLIVEEAGGKVTDAD 239
|
250
....*....|.
gi 1423782289 234 GSELRYAKPGL 244
Cdd:cd01517 240 GKPLDFGKGRK 250
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
11-252 |
1.41e-35 |
|
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: 126.88 E-value: 1.41e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 11 EIAA-VAREAGKVILDVYA-TDFTVDNKADAS-PVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDvtDRFWLV 87
Cdd:cd01639 3 NIAIeAARKAGEILLEAYEkLGLNVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTD--EPTWII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 88 DPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRsaiTCRRAPLEGCTVVSSRSHG 167
Cdd:cd01639 81 DPLDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIR---VSGRKELKDALVATGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 168 SEAPLADFLAG-RRVARSVFAG------SSLKLCLIAACEADIYPRFGrTMEWDIAAGHAVVRAAGGHVRTLEGSELrya 240
Cdd:cd01639 158 RGDNFDRYLNNfAKLLAKAVRGvrrlgsAALDLAYVAAGRLDGYWERG-LKPWDVAAGALIVREAGGLVTDFDGGPF--- 233
|
250
....*....|..
gi 1423782289 241 kpGLDNPHFVAS 252
Cdd:cd01639 234 --DLMSGNILAG 243
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
12-237 |
1.70e-33 |
|
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: 121.59 E-value: 1.70e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 12 IAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEaasAGRIPDVTDRFWLVDPLD 91
Cdd:cd01641 5 ALELADAAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEE---FGNEGGDAGYVWVLDPID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 92 GTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAITCRRAPLEGCTVVSSRSH-GSEA 170
Cdd:cd01641 82 GTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGRPLRVRACADLAEAVLSTTDPHfFTPG 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1423782289 171 PLADFLAGRRVAR-SVFAGSSLKLCLIAACEADIyprfgrTME-----WDIAAGHAVVRAAGGHVRTLEGSEL 237
Cdd:cd01641 162 DRAAFERLARAVRlTRYGGDCYAYALVASGRVDL------VVEaglkpYDVAALIPIIEGAGGVITDWDGGPL 228
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
7-236 |
5.36e-33 |
|
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: 120.13 E-value: 5.36e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 7 QLCEEIAavaREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAasaGRIPDVTDRFWL 86
Cdd:cd01643 2 SLAEAIA---QEAGDRALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEG---GGIFPSSGWYWV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 87 VDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEekGVRSAITcRRAPLEGCTVVSSRSH 166
Cdd:cd01643 76 IDPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFLN--GKPLALH-PPLQLPDCNVGFNRSS 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423782289 167 GSEA------PLADFLAGRRVARSvfagSSLKLCLIAACEADIYprFGRTME-WDIAAGHAVVRAAGGHVRTLEGSE 236
Cdd:cd01643 153 RASAravlrvILRRFPGKIRMLGS----ASLNLASVAAGQTLGY--VEATPKiWDIAAAWVILREAGGSWTILDEEP 223
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
10-232 |
4.04e-28 |
|
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: 105.94 E-value: 4.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 10 EEIAAVAREAGKVILDVYATDFTVDN---KADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVTD-RFW 85
Cdd:cd01636 2 EELCRVAKEAGLAILKAFGRELSGKVkitKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDeYTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 86 LVDPLDGTKEFIGRNGEFTVNIAlvehgepvlgvvfapaldrLFAGVVGAGAyveekgvrsaitcrraplegctvvSSRS 165
Cdd:cd01636 82 VIDPIDGTKNFINGLPFVAVVIA-------------------VYVILILAEP------------------------SHKR 118
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423782289 166 HGSEAPLADFLAGRRVARsvFAGSSLKLCLIAACEADIYPRFGRTME-WDIAAGHAVVRAAGGHVRTL 232
Cdd:cd01636 119 VDEKKAELQLLAVYRIRI--VGSAVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
9-229 |
1.38e-27 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 106.70 E-value: 1.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 9 CEEIAA-VAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVTD-RFWL 86
Cdd:PLN02553 10 FLEVAVdAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTELTDePTWI 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 87 VDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRsaitcrraplegctvVSSRSH 166
Cdd:PLN02553 90 VDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPIK---------------ASSQSE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 167 GSEAPLA------------DFLAGR-----RVARSV-FAGS-SLKLCLIAACEADIYPRFGRTMEWDIAAGHAVVRAAGG 227
Cdd:PLN02553 155 LGKALLAtevgtkrdkatvDATTNRinallYKVRSLrMSGScALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGG 234
|
..
gi 1423782289 228 HV 229
Cdd:PLN02553 235 LV 236
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
11-243 |
3.03e-26 |
|
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: 103.56 E-value: 3.03e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 11 EIAAVAREAGKVILDVYA--TDFTVDNKA-----DASPVTLADERAEAVILAGLARIAPDIPAISEEAASAGRIPDVTD- 82
Cdd:cd01640 4 SLLAVAEKAGGIARDVVKkgRLLILLVEGktkegANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDESRd 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 83 ------------------------RFWlVDPLDGTKEFI-GRNGEFTVNIALVEHGEPVLGVVFAP----------ALDR 127
Cdd:cd01640 84 vdldeeileescpspskdlpeedlGVW-VDPLDATQEYTeGLLEYVTVLIGVAVKGKPIAGVIHQPfyektagagaWLGR 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 128 LFAGVVGAGAYVEekgVRSAITCRRaplegcTVVSSRSHGS---EAPLADFLAGRRVARsvFAGSSLK-LCLIAA-CEAD 202
Cdd:cd01640 163 TIWGLSGLGAHSS---DFKEREDAG------KIIVSTSHSHsvkEVQLITAGNKDEVLR--AGGAGYKvLQVLEGlADAY 231
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1423782289 203 IYPRFGrTMEWDIAAGHAVVRAAGGHVRTLEGSELRYAKPG 243
Cdd:cd01640 232 VHSTGG-IKKWDICAPEAILRALGGDMTDLHGEPLSYSKAV 271
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
30-241 |
1.89e-19 |
|
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: 86.07 E-value: 1.89e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 30 DFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAAS--------AGRIPDVTD------------------- 82
Cdd:TIGR01330 32 DSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEDSSglseadftLGRVNELVNetlvyaknykkddqfplks 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 83 -------------------RFWLVDPLDGTKEFIgRNGEFTVNIALVEHGEPVLGVVFAPALDR---------------- 127
Cdd:TIGR01330 112 ledvlqiidfgnyeggrkgRHWVLDPIDGTKGFL-RGDQYAVCLALIENGKVVLGVIGCPNLPLssygaqnlkgseskgc 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 128 LFAGVVGAGAYVEE----------------KGVRSAITCRraPLEGctvvSSRSHGSEAPLADFLAGRRVARSVFagSSL 191
Cdd:TIGR01330 191 IFRAVRGSGAFMYSlssdaesptkvhvssvKDTKDAIFCE--GVEK----GHSSHDEQTAIANKLGISKSPLRLD--SQA 262
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1423782289 192 KLCLIAACEADIYPRFGRTME-----WDIAAGHAVVRAAGGHVRTLEGSELRYAK 241
Cdd:TIGR01330 263 KYAALARGDADVYLRLPIKLSyqekiWDHAAGNVIVEEAGGIVTDAMGKPLDFGK 317
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
10-134 |
1.52e-18 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 82.85 E-value: 1.52e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 10 EEIAAVARE----AGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAASagRIPD-VTDRF 84
Cdd:PLN02911 34 DRFVDVAHKladaAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGL--RCGEgSSDYV 111
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1423782289 85 WLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVG 134
Cdd:PLN02911 112 WVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAG 161
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
16-234 |
1.34e-17 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 79.85 E-value: 1.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 16 AREAGKVILDVYATDFTVD--NKADASPVTLADERAEAVILAGLARIAPDIPAISEEAAS-AGRIPDVTdrfWLVDPLDG 92
Cdd:PRK10757 12 ARKAGNLIAKNYETPDAVEasQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGElEGEDQDVQ---WVIDPLDG 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 93 TKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAiTCRraPLEGcTVVSS------RSH 166
Cdd:PRK10757 89 TTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQLNGYRLRGS-TAR--DLDG-TILATgfpfkaKQH 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1423782289 167 GSE---------APLADFlagRRvarsvfAGS-SLKLCLIAACEADIYPRFGrTMEWDIAAGHAVVRAAGGHVRTLEG 234
Cdd:PRK10757 165 ATTyinivgklfTECADF---RR------TGSaALDLAYVAAGRVDGFFEIG-LKPWDFAAGELLVREAGGIVSDFTG 232
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
8-238 |
4.27e-17 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 78.03 E-value: 4.27e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 8 LCEEIAavaREAGKVILDVYATD---FTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAasaGRIPDVTDRF 84
Cdd:PRK12676 9 ICDDMA---KEVEKAIMPLFGTPdagETVGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEEL---GEIVGNGPEY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 85 WLV-DPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAITcrRAPLEGCTVVSS 163
Cdd:PRK12676 83 TVVlDPLDGTYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPIKVSKT--SELNESAVSIYG 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1423782289 164 RSHGSEAPLAdflAGRRVAR-SVFAGSSLKLCLIAACEADIYPRFGRTME-WDIAAGHAVVRAAGGHVRTLEGSELR 238
Cdd:PRK12676 161 YRRGKERTVK---LGRKVRRvRILGAIALELCYVASGRLDAFVDVRNYLRvTDIAAGKLICEEAGGIVTDEDGNELK 234
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
15-238 |
6.62e-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: 72.02 E-value: 6.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 15 VAREAGKVILDVYATD---FTVDNKADASPVTLADERAEAVILAGLARIAPdIPAISEEAA--SAGRIPDVTdrfWLVDP 89
Cdd:cd01515 8 IAKEIEKAIKPLFGTEdasEVVKIGADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGviDNGDEPEYT---VVLDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 90 LDGTKEFIGRNGEFTVNIALVEHGE--PVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAITcrrAPLEGCTVvsSRSHG 167
Cdd:cd01515 84 LDGTYNAINGIPFYSVSVAVFKIDKsdPYYGYVYNLATGDLYYAIKGKGAYLNGKRIKVSDF---SSLKSISV--SYYIY 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1423782289 168 SEAPLADFLAGRRVARSVFAGS-SLKLCLIAA----CEADIYPRFGRTmewDIAAGHAVVRAAGGHVRTLEGSELR 238
Cdd:cd01515 159 GKNHDRTFKICRKVRRVRIFGSvALELCYVASgaldAFVDVRENLRLV---DIAAGYLIAEEAGGIVTDENGKELK 231
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
5-236 |
1.25e-13 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 69.44 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 5 PQQLCEEIAAVAREAGKVILDVYATDFTVDNKADASPVTLADERAEAVILAGLARIAPDIPAISEEAasaGRIPDV-TDR 83
Cdd:PLN02737 76 AEELLAVAELAAKTGAEVVMEAVNKPRNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEEG---GVIGDSsSDY 152
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 84 FWLVDPLDGTKEFIGRNGEFTVNIALVEHGEPVLGVV--FAPA----LDRLFAGVVGAGAYVEEKGVRSAITCRrapLEG 157
Cdd:PLN02737 153 LWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVveFVGGpmcwNTRTFSASAGGGAFCNGQKIHVSQTDK---VER 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 158 CTVVSSRSHGSEAPLAD----FLAGRRVARSV--FAGSSLKLCLIAACEADIYPRFgRTMEWDIAAGHAVVRAAGGHVRT 231
Cdd:PLN02737 230 SLLVTGFGYEHDDAWATnielFKEFTDVSRGVrrLGAAAVDMCHVALGIVEAYWEY-RLKPWDMAAGVLIVEEAGGTVTR 308
|
....*
gi 1423782289 232 LEGSE 236
Cdd:PLN02737 309 MDGGK 313
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
37-237 |
4.68e-07 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 50.11 E-value: 4.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 37 ADASPVTLADERAEAVILAGLARIAPDIpAISEEAASAgRIPDVTDRF-WLVDPLDGT---------------------- 93
Cdd:PRK14076 37 ADGTPTKRIDLIAENIAINSLEKFCSGI-LISEEIGFK-KIGKNKPEYiFVLDPIDGTynalkdipiysasiaiakidgf 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 94 ----KEFIGRNgeFTVNialvehgEPVLGVVFAPALDRLFAGVVGAGAYVEEKGVRSAITCRRAPLEGCTVVSSRSHGSE 169
Cdd:PRK14076 115 dkkiKEFIGKN--LTIN-------DLEVGVVKNIATGDTYYAEKGEGAYLLKKGEKKKIEISNISNLKDASIGLFAYGLS 185
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1423782289 170 APLADFLAGRRVAR-SVFAGSSLKLCLIAACEADIYPRFGRTMEW-DIAAGHAVVRAAGGHVRTLEGSEL 237
Cdd:PRK14076 186 LDTLKFIKDRKVRRiRLFGSIALEMCYVASGALDAFINVNETTRLcDIAAGYVICKEAGGIITNKNGKPL 255
|
|
| |
