|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
13-273 |
4.21e-108 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 313.64 E-value: 4.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 13 SHLMEPLTALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFR--DSF 90
Cdd:COG1218 2 EALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKswDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 91 FLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERVRFDGtsigAAEPVRTRTLPtQGEP 170
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGG----ERQPIRVRDRP-PAEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 171 WIAAVSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGELR 250
Cdd:COG1218 157 LRVVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLR 236
|
250 260
....*....|....*....|...
gi 742482147 251 FGQRGDtgFIIPEFIAWGDPRAA 273
Cdd:COG1218 237 YNKKED--LLNPGFIASGDHAAI 257
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
15-266 |
2.94e-90 |
|
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: 267.55 E-value: 2.94e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 15 LMEPLTALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDSFFLID 94
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDRFWLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 95 PLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERvrfdgtsIGAAEPVRTRTLPTQGEPWIAA 174
Cdd:cd01638 81 PLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYK-------NGRPGAVSLQARPPPLQPLRVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 175 VSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGELRFGQr 254
Cdd:cd01638 154 ASRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNR- 232
|
250
....*....|..
gi 742482147 255 gdTGFIIPEFIA 266
Cdd:cd01638 233 --EDFLNPDFIA 242
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-268 |
9.16e-74 |
|
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: 225.79 E-value: 9.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 15 LMEPLTALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERtqlASPPF--RD---S 89
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEED---ASIPLtpRQtwqR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 90 FFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERvrfDGTSIGAAEPVRTRTLPTqgE 169
Cdd:TIGR01331 78 FWLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKR---EGDGQALKAPIHVRPWPS--G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 170 PWIAAVSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGEL 249
Cdd:TIGR01331 153 PLLVVISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPL 232
|
250
....*....|....*....
gi 742482147 250 RFGQRGDtgFIIPEFIAWG 268
Cdd:TIGR01331 233 LYGKRES--FRNPNFVALG 249
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
15-264 |
1.53e-62 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 197.22 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 15 LMEPLTALVVKAGEAILAV--NRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEErtqlaSPPFRD---- 88
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVydGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEE-----DPPAWEvrqh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 89 --SFFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAErvrfdgTSIGAAEPVRTRtlpt 166
Cdd:PRK10931 76 wqRYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWK------EECGVRKQIQVR---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 167 QGEPWIAAVSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKG 246
Cdd:PRK10931 146 DARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQG 225
|
250
....*....|....*...
gi 742482147 247 GELRFGQRgdTGFIIPEF 264
Cdd:PRK10931 226 KTLDYTPR--ESFLNPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
13-255 |
2.91e-44 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 150.96 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 13 SHLMEPLTALVVKAGEAILAVNRAAMRVDGK---HDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDS 89
Cdd:pfam00459 3 EEVLKVAVELAAKAGEILREAFSNKLTIEEKgksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 90 ---FFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAErvrFDGTSIgaaePVRTRTLPT 166
Cdd:pfam00459 83 dgpTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAF---LNGQPL----PVSRAPPLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 167 QGEPWIAAVSRSHGDLRSEAFIDGRPNAVRKT----VGSA-VKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKV 241
Cdd:pfam00459 156 EALLVTLFGVSSRKDTSEASFLAKLLKLVRAPgvrrVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVV 235
|
250
....*....|....
gi 742482147 242 TDGKGGELRFGQRG 255
Cdd:pfam00459 236 TDADGGPFDLLAGR 249
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
13-273 |
4.21e-108 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 313.64 E-value: 4.21e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 13 SHLMEPLTALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFR--DSF 90
Cdd:COG1218 2 EALLEAAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKswDRF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 91 FLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERVRFDGtsigAAEPVRTRTLPtQGEP 170
Cdd:COG1218 82 WLVDPLDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGG----ERQPIRVRDRP-PAEP 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 171 WIAAVSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGELR 250
Cdd:COG1218 157 LRVVASRSHRDEETEALLARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLR 236
|
250 260
....*....|....*....|...
gi 742482147 251 FGQRGDtgFIIPEFIAWGDPRAA 273
Cdd:COG1218 237 YNKKED--LLNPGFIASGDHAAI 257
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
15-266 |
2.94e-90 |
|
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: 267.55 E-value: 2.94e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 15 LMEPLTALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDSFFLID 94
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRLGWDRFWLVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 95 PLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERvrfdgtsIGAAEPVRTRTLPTQGEPWIAA 174
Cdd:cd01638 81 PLDGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYK-------NGRPGAVSLQARPPPLQPLRVV 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 175 VSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGELRFGQr 254
Cdd:cd01638 154 ASRSHPDEELEALLAALGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTYNR- 232
|
250
....*....|..
gi 742482147 255 gdTGFIIPEFIA 266
Cdd:cd01638 233 --EDFLNPDFIA 242
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
15-268 |
9.16e-74 |
|
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: 225.79 E-value: 9.16e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 15 LMEPLTALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERtqlASPPF--RD---S 89
Cdd:TIGR01331 1 MLDDVIKIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEED---ASIPLtpRQtwqR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 90 FFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERvrfDGTSIGAAEPVRTRTLPTqgE 169
Cdd:TIGR01331 78 FWLVDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKR---EGDGQALKAPIHVRPWPS--G 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 170 PWIAAVSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGEL 249
Cdd:TIGR01331 153 PLLVVISRSHAEEKTTEYLANLGYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPL 232
|
250
....*....|....*....
gi 742482147 250 RFGQRGDtgFIIPEFIAWG 268
Cdd:TIGR01331 233 LYGKRES--FRNPNFVALG 249
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
15-264 |
1.53e-62 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 197.22 E-value: 1.53e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 15 LMEPLTALVVKAGEAILAV--NRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEErtqlaSPPFRD---- 88
Cdd:PRK10931 1 MLEQICQLARNAGDAIMQVydGTKPLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEE-----DPPAWEvrqh 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 89 --SFFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAErvrfdgTSIGAAEPVRTRtlpt 166
Cdd:PRK10931 76 wqRYWLVDPLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSAAEGKAWK------EECGVRKQIQVR---- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 167 QGEPWIAAVSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKG 246
Cdd:PRK10931 146 DARPPLVVISRSHADAELKEYLQQLGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQG 225
|
250
....*....|....*...
gi 742482147 247 GELRFGQRgdTGFIIPEF 264
Cdd:PRK10931 226 KTLDYTPR--ESFLNPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
13-255 |
2.91e-44 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 150.96 E-value: 2.91e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 13 SHLMEPLTALVVKAGEAILAVNRAAMRVDGK---HDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDS 89
Cdd:pfam00459 3 EEVLKVAVELAAKAGEILREAFSNKLTIEEKgksGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQTELTD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 90 ---FFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAErvrFDGTSIgaaePVRTRTLPT 166
Cdd:pfam00459 83 dgpTWIIDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAF---LNGQPL----PVSRAPPLS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 167 QGEPWIAAVSRSHGDLRSEAFIDGRPNAVRKT----VGSA-VKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKV 241
Cdd:pfam00459 156 EALLVTLFGVSSRKDTSEASFLAKLLKLVRAPgvrrVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVV 235
|
250
....*....|....
gi 742482147 242 TDGKGGELRFGQRG 255
Cdd:pfam00459 236 TDADGGPFDLLAGR 249
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
19-256 |
8.98e-41 |
|
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: 140.91 E-value: 8.98e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 19 LTALVVKAGEAILAVNRAAMRVDGK-HDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDSFFLIDPLD 97
Cdd:cd01637 4 ALKAVREAGALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGGSGNVSDGGRVWVIDPID 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 98 GTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAervrfdgTSIGAAEPVRTRTLPtqGEPWIAAVSR 177
Cdd:cd01637 84 GTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGA-------FLNGKKLPLSKDTPL--NDALLSTNAS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 178 SHGDLRSEAFID--GRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCeWDVGAGCAVVTAAGGKVTDGKGGELRFGQRG 255
Cdd:cd01637 155 MLRSNRAAVLASlvNRALGIRIYGSAGLDLAYVAAGRLDAYLSSGLNP-WDYAAGALIVEEAGGIVTDLDGEPLDTLNRS 233
|
.
gi 742482147 256 D 256
Cdd:cd01637 234 G 234
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
13-255 |
2.30e-36 |
|
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: 129.96 E-value: 2.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 13 SHLMEPLTALVVKAGEAIL-AVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPfRDSFF 91
Cdd:COG0483 1 HPLLELALRAARAAGALILrRFRELDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRD-SGYVW 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 92 LIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAervRFDGtsigaaEPVRTRTLPTQGEPW 171
Cdd:COG0483 80 VIDPIDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGA---FLNG------RRLRVSARTDLEDAL 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 172 IAA----VSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGpTCEWDVGAGCAVVTAAGGKVTDGKGG 247
Cdd:COG0483 151 VATgfpyLRDDREYLAALAALLPRVRRVRRLGSAALDLAYVAAGRLDAFVEAG-LKPWDIAAGALIVREAGGVVTDLDGE 229
|
....*...
gi 742482147 248 ELRFGQRG 255
Cdd:COG0483 230 PLDLGSGS 237
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
19-261 |
1.07e-32 |
|
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: 120.88 E-value: 1.07e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 19 LTALVVKAGEA-ILAVNRAAMRVDG---KHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPpfrdsFFLID 94
Cdd:cd01517 4 VAILAVRAAASlTLPVFRNLGAGDVvwkKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSAALGR-----FWVLD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 95 PLDGTKEFVAGrDEFTVNLALVTKGVPLLGIVAAPAL-------GLLWRGIVGRGAERVRFDGTSigaAEPVRTRTLP-T 166
Cdd:cd01517 79 PIDGTKGFLRG-DQFAVALALIEDGEVVLGVIGCPNLplddgggGDLFSAVRGQGAWLRPLDGSS---LQPLSVRQLTnA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 167 QGEPWIAAVSRSHGDLRSEAFIDGRPNAVR-KTVGSAVKFGRIAEGSADIYPRFG-----PTCEWDVGAGCAVVTAAGGK 240
Cdd:cd01517 155 ARASFCESVESAHSSHRLQAAIKALGGTPQpVRLDSQAKYAAVARGAADFYLRLPlsmsyREKIWDHAAGVLIVEEAGGK 234
|
250 260
....*....|....*....|....*
gi 742482147 241 VTDGKGGELRFGQ----RGDTGFII 261
Cdd:cd01517 235 VTDADGKPLDFGKgrklLNNGGLIA 259
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
25-249 |
2.75e-24 |
|
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: 97.71 E-value: 2.75e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 25 KAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTqlASPPFRDSFFLIDPLDGTKEFVA 104
Cdd:cd01641 11 AAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFG--NEGGDAGYVWVLDPIDGTKSFIR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 105 GRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAervRFDGtsiGAAEPVRTRTLPTQGEPWIAAVSRSHGDLRS 184
Cdd:cd01641 89 GLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGT---FLNG---AGGRPLRVRACADLAEAVLSTTDPHFFTPGD 162
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 742482147 185 EAFIDGRPNAVRKTV--GSAVKFGRIAEGSADIYPRFG--PtceWDVGAGCAVVTAAGGKVTDGKGGEL 249
Cdd:cd01641 163 RAAFERLARAVRLTRygGDCYAYALVASGRVDLVVEAGlkP---YDVAALIPIIEGAGGVITDWDGGPL 228
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
22-254 |
4.49e-21 |
|
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: 89.13 E-value: 4.49e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 22 LVVKAGEAIL-AVNRAAMRVDGK-HDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPfrDSF-FLIDPLDG 98
Cdd:cd01639 8 AARKAGEILLeAYEKLGLNVEEKgSPVDLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLT--DEPtWIIDPLDG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 99 TKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGA----ERVRFDGT-----SIGAAEpvrtrtLPTQGE 169
Cdd:cd01639 86 TTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAflngRRIRVSGRkelkdALVATG------FPYDRG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 170 PWIAAVSRSHGDLRSEAFIDgrpnaVRKTVGSAVKFGRIAEGSADIYPRFGptC-EWDVGAGCAVVTAAGGKVTDGKGGE 248
Cdd:cd01639 160 DNFDRYLNNFAKLLAKAVRG-----VRRLGSAALDLAYVAAGRLDGYWERG--LkPWDVAAGALIVREAGGLVTDFDGGP 232
|
....*.
gi 742482147 249 LRFGQR 254
Cdd:cd01639 233 FDLMSG 238
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
21-259 |
5.92e-21 |
|
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: 88.93 E-value: 5.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 21 ALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLAspPFRDSFFLIDPLDGTK 100
Cdd:cd01643 6 AIAQEAGDRALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIF--PSSGWYWVIDPIDGTT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 101 EFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAERvrfDGTSIGAAEPvrtRTLPTQGEpWIAAVSRSHG 180
Cdd:cd01643 84 NFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFL---NGKPLALHPP---LQLPDCNV-GFNRSSRASA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 181 DLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTCeWDVGAGCAVVTAAGGKVT--DGKGGELRFGQRGDTG 258
Cdd:cd01643 157 RAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYVEATPKI-WDIAAAWVILREAGGSWTilDEEPAFLQTKDYLSAG 235
|
.
gi 742482147 259 F 259
Cdd:cd01643 236 F 236
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
16-244 |
3.23e-19 |
|
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: 82.83 E-value: 3.23e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 16 MEPLTALVVKAGEAILAVNRAAMRVD---GKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDS--F 90
Cdd:cd01636 1 LEELCRVAKEAGLAILKAFGRELSGKvkiTKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDeyT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 91 FLIDPLDGTKEFVAGRDEFTVNLALvtkgvpllgivaapalgllwrgivgrgaervrfdGTSIGAAEPVRTRTLPTQGEP 170
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAV----------------------------------YVILILAEPSHKRVDEKKAEL 126
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 742482147 171 WIAAVSRshgdlrseafidgrpnaVRKTVGSAVKFGRIAEGSADIYPRFGPTCE-WDVGAGCAVVTAAGGKVTDG 244
Cdd:cd01636 127 QLLAVYR-----------------IRIVGSAVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIMTDW 184
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
23-251 |
1.38e-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: 83.14 E-value: 1.38e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 23 VVKAGEAILAVNRAAMRvdGKHDgsPVTEADLAADRVIADGLARLAADVPTLSEERTQLAS------PPFRDSFFL---- 92
Cdd:cd01640 20 VKKGRLLILLVEGKTKE--GAND--FKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEFENqedesrDVDLDEEILeesc 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 93 ---------------IDPLDGTKEFVAGRDEF-TVNLALVTKGVPLLGIVAAP-------ALGLLWR---GIVGRGAErv 146
Cdd:cd01640 96 pspskdlpeedlgvwVDPLDATQEYTEGLLEYvTVLIGVAVKGKPIAGVIHQPfyektagAGAWLGRtiwGLSGLGAH-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 147 rfdGTSIGAAEPVRTRTLPTqgepwiaavSRSHGDLRSEAFIDGRPNAVRKTVGSAVKFGRIAEGSADIYPRFGPTC-EW 225
Cdd:cd01640 174 ---SSDFKEREDAGKIIVST---------SHSHSVKEVQLITAGNKDEVLRAGGAGYKVLQVLEGLADAYVHSTGGIkKW 241
|
250 260
....*....|....*....|....*.
gi 742482147 226 DVGAGCAVVTAAGGKVTDGKGGELRF 251
Cdd:cd01640 242 DICAPEAILRALGGDMTDLHGEPLSY 267
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
21-271 |
1.97e-18 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 82.85 E-value: 1.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 21 ALVVKAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDSFFLIDPLDGTK 100
Cdd:PLN02911 42 KLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEEHGLRCGEGSSDYVWVLDPIDGTK 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 101 EFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRgaeRVRFDGtsigaaEPVRTRTLPTQGEPWIAAVSrSHg 180
Cdd:PLN02911 122 SFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAGR---ATTLNG------EEISTRSCASLKDAYLYTTS-PH- 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 181 dlrseaFIDGRPNAVRKTVGSAVK----------FGRIAEGSAD--IYPRFGPtceWDVGAGCAVVTAAGGKVTDGKGGE 248
Cdd:PLN02911 191 ------MFSGDAEDAFARVRDKVKvplygcdcyaYGLLASGHVDlvVESGLKP---YDYLALVPVVEGAGGVITDWKGRK 261
|
250 260
....*....|....*....|...
gi 742482147 249 LRFGQRGDTGFIIPEFIAWGDPR 271
Cdd:PLN02911 262 LRWEPSPGSLATSFNVVAAGDAR 284
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
25-249 |
5.11e-16 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 75.88 E-value: 5.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 25 KAGEAILAVNRAAMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPF--RDSFFLIDPLDGTKEF 102
Cdd:PLN02553 20 AAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETTAASGGTEltDEPTWIVDPLDGTTNF 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 103 VAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAervRFDGTSIGAAepvrtrtlpTQGEPWIAAVSRSHGDL 182
Cdd:PLN02553 100 VHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGA---FLNGKPIKAS---------SQSELGKALLATEVGTK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 742482147 183 RSEAFID---GRPNA-------VRKTVGSAVKFGRIAEGSADIYPRFGPTCEWDVGAGCAVVTAAGGKVTDGKGGEL 249
Cdd:PLN02553 168 RDKATVDattNRINAllykvrsLRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPF 244
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
45-251 |
3.12e-11 |
|
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: 62.01 E-value: 3.12e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 45 DGSPVTEADLAADRVIADGLARLAAdVPTLSEERTQLASPPFRDSFFLIDPLDGTKEFVAGRDEFTVNLALVT--KGVPL 122
Cdd:cd01515 34 DGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIDNGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVFKidKSDPY 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 123 LGIVAAPALGLLWRGIVGRGAervRFDGTSIgaaepvRTRTLPTQGEPWIAAVSRSHGDLRSEAfIDGRPNAVRkTVGS- 201
Cdd:cd01515 113 YGYVYNLATGDLYYAIKGKGA---YLNGKRI------KVSDFSSLKSISVSYYIYGKNHDRTFK-ICRKVRRVR-IFGSv 181
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 742482147 202 AVKFGRIAEGS----ADIYPRFGPTcewDVGAGCAVVTAAGGKVTDGKGGELRF 251
Cdd:cd01515 182 ALELCYVASGAldafVDVRENLRLV---DIAAGYLIAEEAGGIVTDENGKELKL 232
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
16-247 |
7.08e-11 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 60.98 E-value: 7.08e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 16 MEPLTALVV----KAGEAILAVNRAAMRVDGKHDGSP--VTEADLAADRVIADGLARLAADVPTLSEERTQLASPPfRDS 89
Cdd:PRK10757 1 MHPMLNIAVraarKAGNLIAKNYETPDAVEASQKGSNdfVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGED-QDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 90 FFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALGLLWRGIVGRGAE----RVR------FDGTSIGAAEPV 159
Cdd:PRK10757 80 QWVIDPLDGTTNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQGAQlngyRLRgstardLDGTILATGFPF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 160 RTRTLPTqgePWIAAVsrshGDLRSEAfidgrpNAVRKTVGSAVKFGRIAEGSADIYPRFGPTcEWDVGAGCAVVTAAGG 239
Cdd:PRK10757 160 KAKQHAT---TYINIV----GKLFTEC------ADFRRTGSAALDLAYVAAGRVDGFFEIGLK-PWDFAAGELLVREAGG 225
|
....*...
gi 742482147 240 KVTDGKGG 247
Cdd:PRK10757 226 IVSDFTGG 233
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
45-251 |
1.89e-10 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 59.92 E-value: 1.89e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 45 DGSPVTEADLAADRVIADGLARLAADVPTLSEE--RTQLASPPFrdsFFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPL 122
Cdd:PRK12676 39 DGTPTKLIDKVAEDIILEVLKPLGRCVNIISEElgEIVGNGPEY---TVVLDPLDGTYNAINGIPFYAISIAVFKGGKPV 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 123 LGIVAAPALGLLWRGIVGRGAervRFDGTSIgaaEPVRTRTLPtqgepwiaavsrshgdlRSEAFIDGRPNAVRKTV--G 200
Cdd:PRK12676 116 YGYVYNLATGDFYEAIPGKGA---YLNGKPI---KVSKTSELN-----------------ESAVSIYGYRRGKERTVklG 172
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 742482147 201 SAVK----FGRIA-----------EGSADIYPRFGPTcewDVGAGCAVVTAAGGKVTDGKGGELRF 251
Cdd:PRK12676 173 RKVRrvriLGAIAlelcyvasgrlDAFVDVRNYLRVT---DIAAGKLICEEAGGIVTDEDGNELKL 235
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
9-248 |
3.14e-07 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 50.95 E-value: 3.14e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 9 GP-AASHLMEPLTALVVKAGEAIL-AVNRAaMRVDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEErTQLASPPF 86
Cdd:PLN02737 72 GPiPAEELLAVAELAAKTGAEVVMeAVNKP-RNISYKGLTDLVTDTDKASEAAILEVVRKNFPDHLILGEE-GGVIGDSS 149
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 87 RDSFFLIDPLDGTKEFVAGRDEFTVNLALVTKGVPLLGIVAAPALG-LLWR-----GIVGRGAervRFDGTSIGAAEPVR 160
Cdd:PLN02737 150 SDYLWCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVVEFVGGpMCWNtrtfsASAGGGA---FCNGQKIHVSQTDK 226
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 161 T-RTLPTQG------EPWIAAVsrshgDLRSEaFIDgRPNAVRKTVGSAVKFGRIAEGSADIY--PRFGPtceWDVGAGC 231
Cdd:PLN02737 227 VeRSLLVTGfgyehdDAWATNI-----ELFKE-FTD-VSRGVRRLGAAAVDMCHVALGIVEAYweYRLKP---WDMAAGV 296
|
250
....*....|....*..
gi 742482147 232 AVVTAAGGKVTDGKGGE 248
Cdd:PLN02737 297 LIVEEAGGTVTRMDGGK 313
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
19-121 |
1.56e-06 |
|
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: 48.21 E-value: 1.56e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 742482147 19 LTALVVKAGEAILAVNRAAMR----VDGKHDGSPVTEADLAADRVIADGLARLAADVPTLSEERTQLASPPFRDsFFLID 94
Cdd:cd01642 2 LEVLEKITKEIILLLNEKNRQglvkLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEIRKGSGEY-IAVLD 80
|
90 100
....*....|....*....|....*..
gi 742482147 95 PLDGTKEFVAGRDEFTVNLALVTKGVP 121
Cdd:cd01642 81 PLDGSTNYLSGIPFYSVSVALADPRSK 107
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