|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
12-271 |
1.21e-124 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 355.24 E-value: 1.21e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 12 YGSLLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLGDR 91
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 92 FYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPD-GAKEVTLDHsggiiSSRSISCRKAPDQ- 169
Cdd:COG1218 81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGqGAFKETGGG-----ERQPIRVRDRPPAe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 170 -MIAVASRSHRTPETDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELL 248
Cdd:COG1218 156 pLRVVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPL 235
|
250 260
....*....|....*....|...
gi 495404163 249 TYGRRnqaddADFANPGFVARGR 271
Cdd:COG1218 236 RYNKK-----EDLLNPGFIASGD 253
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-270 |
4.50e-103 |
|
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: 300.14 E-value: 4.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLGDRFYL 94
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 95 VDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPD-GAKEvtldHSGGIISSRSISCRKAPDQMIAV 173
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGkAAKR----EGDGQALKAPIHVRPWPSGPLLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 174 A-SRSHRTPETDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGR 252
Cdd:TIGR01331 157 ViSRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
|
250
....*....|....*...
gi 495404163 253 RNqaddaDFANPGFVARG 270
Cdd:TIGR01331 237 RE-----SFRNPNFVALG 249
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
15-268 |
2.69e-101 |
|
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: 295.29 E-value: 2.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGdlGDRFYL 94
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLG--WDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 95 VDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGakEVTLDhsGGIISSRSISCRKAPDQMIAVA 174
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGG--GAYKN--GRPGAVSLQARPPPLQPLRVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 175 SRSHRTPETDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGRrn 254
Cdd:cd01638 155 SRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNR-- 232
|
250
....*....|....
gi 495404163 255 qaddADFANPGFVA 268
Cdd:cd01638 233 ----EDFLNPDFIA 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
26-266 |
1.35e-70 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 217.64 E-value: 1.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 26 AGLEILRIY--EEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLgDRFYLVDPLDGTRE 103
Cdd:PRK10931 12 AGDAIMQVYdgTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHW-QRYWLVDPLDGTKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 104 FVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGA-KEvtldhSGGiiSSRSISCRKAPDQMIaVASRSHRTPE 182
Cdd:PRK10931 91 FIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAwKE-----ECG--VRKQIQVRDARPPLV-VISRSHADAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 183 TDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGRRNQaddadFA 262
Cdd:PRK10931 163 LKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRES-----FL 237
|
....
gi 495404163 263 NPGF 266
Cdd:PRK10931 238 NPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
11-251 |
3.27e-50 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 165.98 E-value: 3.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 11 DYGSLLSVFETTAIAAGLEILRIYEEGCDVALKDDKS---PVTAADHAAEAIILEALRRATPDIPVVAEEEV-SGGHVPG 86
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGaKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 87 DLGDRFYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTggpdGAKEVTLDHSGGIIssRSISCRKA 166
Cdd:pfam00459 81 TDDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYS----AAKGKGAFLNGQPL--PVSRAPPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 167 PDQMIAVASRSHRTPET------DAHLEDFDIEECVSVGSS-IKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGV 239
Cdd:pfam00459 155 SEALLVTLFGVSSRKDTseasflAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGV 234
|
250
....*....|..
gi 495404163 240 TLTLDGELLTYG 251
Cdd:pfam00459 235 VTDADGGPFDLL 246
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
12-271 |
1.21e-124 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 355.24 E-value: 1.21e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 12 YGSLLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLGDR 91
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 92 FYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPD-GAKEVTLDHsggiiSSRSISCRKAPDQ- 169
Cdd:COG1218 81 FWLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGqGAFKETGGG-----ERQPIRVRDRPPAe 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 170 -MIAVASRSHRTPETDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELL 248
Cdd:COG1218 156 pLRVVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPL 235
|
250 260
....*....|....*....|...
gi 495404163 249 TYGRRnqaddADFANPGFVARGR 271
Cdd:COG1218 236 RYNKK-----EDLLNPGFIASGD 253
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-270 |
4.50e-103 |
|
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: 300.14 E-value: 4.50e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLGDRFYL 94
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 95 VDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPD-GAKEvtldHSGGIISSRSISCRKAPDQMIAV 173
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGkAAKR----EGDGQALKAPIHVRPWPSGPLLV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 174 A-SRSHRTPETDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGR 252
Cdd:TIGR01331 157 ViSRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
|
250
....*....|....*...
gi 495404163 253 RNqaddaDFANPGFVARG 270
Cdd:TIGR01331 237 RE-----SFRNPNFVALG 249
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
15-268 |
2.69e-101 |
|
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: 295.29 E-value: 2.69e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGdlGDRFYL 94
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLG--WDRFWL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 95 VDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGakEVTLDhsGGIISSRSISCRKAPDQMIAVA 174
Cdd:cd01638 79 VDPLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGG--GAYKN--GRPGAVSLQARPPPLQPLRVVA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 175 SRSHRTPETDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGRrn 254
Cdd:cd01638 155 SRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNR-- 232
|
250
....*....|....
gi 495404163 255 qaddADFANPGFVA 268
Cdd:cd01638 233 ----EDFLNPDFIA 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
26-266 |
1.35e-70 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 217.64 E-value: 1.35e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 26 AGLEILRIY--EEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLgDRFYLVDPLDGTRE 103
Cdd:PRK10931 12 AGDAIMQVYdgTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEEDPPAWEVRQHW-QRYWLVDPLDGTKE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 104 FVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGA-KEvtldhSGGiiSSRSISCRKAPDQMIaVASRSHRTPE 182
Cdd:PRK10931 91 FIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAwKE-----ECG--VRKQIQVRDARPPLV-VISRSHADAE 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 183 TDAHLEDFDIEECVSVGSSIKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGRRNQaddadFA 262
Cdd:PRK10931 163 LKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRES-----FL 237
|
....
gi 495404163 263 NPGF 266
Cdd:PRK10931 238 NPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
11-251 |
3.27e-50 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 165.98 E-value: 3.27e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 11 DYGSLLSVFETTAIAAGLEILRIYEEGCDVALKDDKS---PVTAADHAAEAIILEALRRATPDIPVVAEEEV-SGGHVPG 86
Cdd:pfam00459 1 DLEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGaKGDQTEL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 87 DLGDRFYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTggpdGAKEVTLDHSGGIIssRSISCRKA 166
Cdd:pfam00459 81 TDDGPTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYS----AAKGKGAFLNGQPL--PVSRAPPL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 167 PDQMIAVASRSHRTPET------DAHLEDFDIEECVSVGSS-IKFGLLARGEADIYPRLSRTMEWDTAAGDAVLRAAGGV 239
Cdd:pfam00459 155 SEALLVTLFGVSSRKDTseasflAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGV 234
|
250
....*....|..
gi 495404163 240 TLTLDGELLTYG 251
Cdd:pfam00459 235 VTDADGGPFDLL 246
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
15-254 |
3.20e-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: 139.98 E-value: 3.20e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYEEGC-DVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEevsGGHVPGDLGDRFY 93
Cdd:COG0483 3 LLELALRAARAAGALILRRFRELDlEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEE---SGASEGRDSGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 94 LVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGAkeVTLDHsggiissRSISCRKAPD--QMI 171
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGG--AFLNG-------RRLRVSARTDleDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 172 AVASRSHRTPEtDAHLEDFD--IEECVSV----GSSIKFGLLARGEADIY--PRLSrtmEWDTAAGDAVLRAAGGVTLTL 243
Cdd:COG0483 151 VATGFPYLRDD-REYLAALAalLPRVRRVrrlgSAALDLAYVAAGRLDAFveAGLK---PWDIAAGALIVREAGGVVTDL 226
|
250
....*....|.
gi 495404163 244 DGELLTYGRRN 254
Cdd:COG0483 227 DGEPLDLGSGS 237
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
43-268 |
9.16e-39 |
|
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: 136.67 E-value: 9.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 43 KDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSgghvpgDLGdRFYLVDPLDGTREFVnRNGDFTVNIALIEHGI 122
Cdd:cd01517 32 KSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA------ALG-RFWVLDPIDGTKGFL-RGDQFAVALALIEDGE 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 123 PVLGVVYAPVRGWLFTGGPD--------GAKEVTLDHSGGI-ISSRSISCRKAPDQMIAVASRSHRTPETDAHLEDFDIE 193
Cdd:cd01517 104 VVLGVIGCPNLPLDDGGGGDlfsavrgqGAWLRPLDGSSLQpLSVRQLTNAARASFCESVESAHSSHRLQAAIKALGGTP 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 194 ECVSVGSSIKFGLLARGEADIYPRL-----SRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGRRNQADDadfaNPGFVA 268
Cdd:cd01517 184 QPVRLDSQAKYAAVARGAADFYLRLplsmsYREKIWDHAAGVLIVEEAGGKVTDADGKPLDFGKGRKLLN----NGGLIA 259
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
25-254 |
1.26e-37 |
|
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: 132.44 E-value: 1.26e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 25 AAGLEILRIYEEGCDVALK-DDKSPVTAADHAAEAIILEALRRATPDIPVVAEEevSGGHVPGDLGDRFYLVDPLDGTRE 103
Cdd:cd01637 10 EAGALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEE--GGGSGNVSDGGRVWVIDPIDGTTN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 104 FVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGAkeVTLDHSGgiisSRSISCRKAPDQMIAVASRSHRTPET 183
Cdd:cd01637 88 FVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKG--AFLNGKK----LPLSKDTPLNDALLSTNASMLRSNRA 161
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495404163 184 DAhleDFDIEECV----SVGS-SIKFGLLARGEADIYPRlSRTMEWDTAAGDAVLRAAGGVTLTLDGELLTYGRRN 254
Cdd:cd01637 162 AV---LASLVNRAlgirIYGSaGLDLAYVAAGRLDAYLS-SGLNPWDYAAGALIVEEAGGIVTDLDGEPLDTLNRS 233
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
23-246 |
1.16e-26 |
|
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: 104.16 E-value: 1.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 23 AIAAGLEILRIYEE-GCDVALKDD-KSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGhvpgDLGDRFY-LVDPLD 99
Cdd:cd01639 9 ARKAGEILLEAYEKlGLNVEEKGSpVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAG----GLTDEPTwIIDPLD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 100 GTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTggpdGAKevtldHSGGIISSRSISCRKAP---DQMIAV--- 173
Cdd:cd01639 85 GTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFT----AVR-----GQGAFLNGRRIRVSGRKelkDALVATgfp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 174 ASRSHRTPETDAHLEDFDIEECVSV---GS-SIKFGLLARGEADIYprlsrtME-----WDTAAGDAVLRAAGGVTLTLD 244
Cdd:cd01639 156 YDRGDNFDRYLNNFAKLLAKAVRGVrrlGSaALDLAYVAAGRLDGY------WErglkpWDVAAGALIVREAGGLVTDFD 229
|
..
gi 495404163 245 GE 246
Cdd:cd01639 230 GG 231
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
16-249 |
5.88e-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: 102.33 E-value: 5.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 16 LSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEvsGGHVPGdlGDRFYLV 95
Cdd:cd01641 2 LAFALELADAAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEF--GNEGGD--AGYVWVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 96 DPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGGPDGAKevTLDHSGGiissRSISCRKAPDQMIAVAS 175
Cdd:cd01641 78 DPIDGTKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGT--FLNGAGG----RPLRVRACADLAEAVLS 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 176 RS---HRTPETDAHLEDF--DIEECVSVGSSIKFGLLARGEADIY--PRLSrtmEWDTAAGDAVLRAAGGVTLTLDGELL 248
Cdd:cd01641 152 TTdphFFTPGDRAAFERLarAVRLTRYGGDCYAYALVASGRVDLVveAGLK---PYDVAALIPIIEGAGGVITDWDGGPL 228
|
.
gi 495404163 249 T 249
Cdd:cd01641 229 T 229
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
16-243 |
3.03e-23 |
|
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: 93.23 E-value: 3.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 16 LSVFETTAIAAGLEILRIYEE---GCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDLGDRF 92
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRelsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 93 YLVDPLDGTREFVNRNGDFTVNIALIehgipVLGVVYAPvrgwlftggpdgakevtldhsggiiSSRSISCRKAPDQMIA 172
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVY-----VILILAEP-------------------------SHKRVDEKKAELQLLA 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495404163 173 VASRSHrtpetdahledfdieecvsVGS-SIKFGLLARGEADIYPRLSRTME-WDTAAGDAVLRAAGGVTLTL 243
Cdd:cd01636 131 VYRIRI-------------------VGSaVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIMTDW 184
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
16-268 |
1.22e-22 |
|
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: 93.17 E-value: 1.22e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 16 LSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEevSGGHVPGDlgDRFYLV 95
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEE--GGGIFPSS--GWYWVI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 96 DPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRG---WLFTGGPDGA--KEVTLDHSGGIISSRSIScrkapdqm 170
Cdd:cd01643 77 DPIDGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNqtfVAFKGGGAFLngKPLALHPPLQLPDCNVGF-------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 171 iavaSRSHRTPETDAHLEDFDIEECVSVG---SSIKFGLLARGEADIYprLSRTME-WDTAAGDAVLRAAGGVTLTLDGE 246
Cdd:cd01643 149 ----NRSSRASARAVLRVILRRFPGKIRMlgsASLNLASVAAGQTLGY--VEATPKiWDIAAAWVILREAGGSWTILDEE 222
|
250 260
....*....|....*....|..
gi 495404163 247 LLTYGRRnqaDDADFANPGFVA 268
Cdd:cd01643 223 PAFLQTK---DYLSAGFPTLIA 241
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
15-250 |
3.24e-19 |
|
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: 85.07 E-value: 3.24e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYEEGCDVALKDDKS------PVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPGDL 88
Cdd:cd01640 2 LRSLLAVAEKAGGIARDVVKKGRLLILLVEGKTkegandFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENQEDES 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 89 GDRFY-----------------------LVDPLDGTREFV-NRNGDFTVNIALIEHGIPVLGVVYAPvrgwlFTGGPDGA 144
Cdd:cd01640 82 RDVDLdeeileescpspskdlpeedlgvWVDPLDATQEYTeGLLEYVTVLIGVAVKGKPIAGVIHQP-----FYEKTAGA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 145 KEVTLDHSGGIISSRSISC--RKAPDQMIAVASRSHRTPETDAHLEDFDIEECV--SVGSSIKFGLLARGEADIYPRLSR 220
Cdd:cd01640 157 GAWLGRTIWGLSGLGAHSSdfKEREDAGKIIVSTSHSHSVKEVQLITAGNKDEVlrAGGAGYKVLQVLEGLADAYVHSTG 236
|
250 260 270
....*....|....*....|....*....|.
gi 495404163 221 -TMEWDTAAGDAVLRAAGGVTLTLDGELLTY 250
Cdd:cd01640 237 gIKKWDICAPEAILRALGGDMTDLHGEPLSY 267
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
11-241 |
5.22e-19 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 83.97 E-value: 5.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 11 DYGSLLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEVSGGHVPgDLGD 90
Cdd:PLN02553 6 DLEQFLEVAVDAAKAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGT-ELTD 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 91 -RFYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFTGgpdgakevtLDHSGGIISSRSISCRKAPD- 168
Cdd:PLN02553 85 ePTWIVDPLDGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTA---------VKGKGAFLNGKPIKASSQSEl 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 169 --QMIAVASRSHRTPET-DAHLEdfDIEECVSVGSSIK------FGL--LARGEADIYPRLSRTMEWDTAAGDAVLRAAG 237
Cdd:PLN02553 156 gkALLATEVGTKRDKATvDATTN--RINALLYKVRSLRmsgscaLNLcgVACGRLDIFYEIGFGGPWDVAAGAVIVKEAG 233
|
....
gi 495404163 238 GVTL 241
Cdd:PLN02553 234 GLVF 237
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
1-250 |
9.33e-16 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 75.53 E-value: 9.33e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 1 MTVNSALPTLDYGSLLSVFETTAIAAGLEILRIYEEGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEEvs 80
Cdd:PLN02911 22 MDAASALSDAVLDRFVDVAHKLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEH-- 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 81 GGHVPGDLGDRFYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRG--WLftgGPDGaKEVTLDhsGGIISS 158
Cdd:PLN02911 100 GLRCGEGSSDYVWVLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKerWV---GVAG-RATTLN--GEEIST 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 159 RsiSCRKAPDQMIAVasrshrtpeTDAHLEDFDIEEC-VSVGSSIK----------FGLLARG------EADIYPrlsrt 221
Cdd:PLN02911 174 R--SCASLKDAYLYT---------TSPHMFSGDAEDAfARVRDKVKvplygcdcyaYGLLASGhvdlvvESGLKP----- 237
|
250 260
....*....|....*....|....*....
gi 495404163 222 meWDTAAGDAVLRAAGGVTLTLDGELLTY 250
Cdd:PLN02911 238 --YDYLALVPVVEGAGGVITDWKGRKLRW 264
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
15-138 |
1.33e-13 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 69.07 E-value: 1.33e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAIAAGLEILRIYE--EGCDVALKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEevSGGHVpGDLGDRF 92
Cdd:PRK10757 4 MLNIAVRAARKAGNLIAKNYEtpDAVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEE--SGELE-GEDQDVQ 80
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 495404163 93 YLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYAPVRGWLFT 138
Cdd:PRK10757 81 WVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFT 126
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
15-141 |
4.03e-11 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 62.51 E-value: 4.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 15 LLSVFETTAiAAGLEILR---------IYEEGCDValkddkspVTAADHAAEAIILEALRRATPDIPVVAEEevsgGHVP 85
Cdd:PLN02737 79 LLAVAELAA-KTGAEVVMeavnkprniSYKGLTDL--------VTDTDKASEAAILEVVRKNFPDHLILGEE----GGVI 145
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 495404163 86 GD-LGDRFYLVDPLDGTREFVNRNGDFTVNIALIEHGIPVLGVVYApvrgwlFTGGP 141
Cdd:PLN02737 146 GDsSSDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVE------FVGGP 196
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
39-248 |
4.64e-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: 49.68 E-value: 4.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 39 DVALKDDKSPVTAADHAAEAIILEALRRATPdIPVVAEEevSGGHVPGDLGDRFYLVDPLDGTREFVNRNGDFTVNIALI 118
Cdd:cd01515 28 VVKIGADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEE--IGVIDNGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVF 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 119 EH--GIPVLGVVYAPVRGWLFTGGPDgakevtldhSGGIISSRSISCRKAPDQMIAVASrshRTPETDAHLEDFDIEECV 196
Cdd:cd01515 105 KIdkSDPYYGYVYNLATGDLYYAIKG---------KGAYLNGKRIKVSDFSSLKSISVS---YYIYGKNHDRTFKICRKV 172
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 495404163 197 S----VGS-SIKFGLLARGEADIYPRLSRTME-WDTAAGDAVLRAAGGVTLTLDGELL 248
Cdd:cd01515 173 RrvriFGSvALELCYVASGALDAFVDVRENLRlVDIAAGYLIAEEAGGIVTDENGKEL 230
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-144 |
5.74e-07 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 49.52 E-value: 5.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 45 DKSPVTAADHAAEAIILEALRRATPDIPVVAEEEvsgGHVPGDLGDRFYLVDPLDGTREFVNRNGDFTVNIALIEHGIPV 124
Cdd:PRK12676 39 DGTPTKLIDKVAEDIILEVLKPLGRCVNIISEEL---GEIVGNGPEYTVVLDPLDGTYNAINGIPFYAISIAVFKGGKPV 115
|
90 100
....*....|....*....|.
gi 495404163 125 LGVVYAPVRGWLFTGGPD-GA 144
Cdd:PRK12676 116 YGYVYNLATGDFYEAIPGkGA 136
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
32-229 |
6.29e-05 |
|
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: 43.21 E-value: 6.29e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 32 RIYEEGCdvaLKDDKSPVTAADHAAEAIILEALRRATPDIPVVAEEevSGGHVPGDlGDRFYLVDPLDGTREFVNRNGDF 111
Cdd:cd01642 22 QGLVKLI---RGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEE--SGEIRKGS-GEYIAVLDPLDGSTNYLSGIPFY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495404163 112 TVNIALIEHGIPV-LGVVYApvrgwlFTGGPDGAKEVTLDHSGGIISSRSISCRKAPDQ--MIAVASRSHRTPE--TDAH 186
Cdd:cd01642 96 SVSVALADPRSKVkAATLDN------FVSGEGGLKVYSPPTRFSYISVPKLGPPLVPEVpsKIGIYEGSSRNPEkfLLLS 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 495404163 187 LEDFDIEecvSVGSS-IKFGLLARGEADIYPRL-SRTMEWDTAAG 229
Cdd:cd01642 170 RNGLKFR---SLGSAaLELAYTCEGSFVLFLDLrGKLRNFDVAAA 211
|
|
| |
