|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
8-261 |
1.35e-133 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 377.96 E-value: 1.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 8 ELVALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWRRWWLVDP 87
Cdd:COG1218 7 AAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRAQPISVR-LEPEEAFTVVASKRHG 166
Cdd:COG1218 87 LDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGERQPIRVRdRPPAEPLRVVASRSHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 167 SPAQERLLdglsERFGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEPRED 246
Cdd:COG1218 167 DEETEALL----ARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNKKED 242
|
250
....*....|....*
gi 489190673 247 YLNGSFLALPRAAEW 261
Cdd:COG1218 243 LLNPGFIASGDHAAI 257
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
6-255 |
1.54e-104 |
|
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: 303.99 E-value: 1.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 6 WGELVA-LVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWRRWWL 84
Cdd:TIGR01331 1 MLDDVIkIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 85 VDPLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRAQ-PISVRLEPEEAFTVVASK 163
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKaPIHVRPWPSGPLLVVISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 164 RHGSPAQERLLDGLserfGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEP 243
Cdd:TIGR01331 161 SHAEEKTTEYLANL----GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
|
250
....*....|..
gi 489190673 244 REDYLNGSFLAL 255
Cdd:TIGR01331 237 RESFRNPNFVAL 248
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
9-254 |
3.42e-103 |
|
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: 300.30 E-value: 3.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPlsERGHWRRWWLVDPL 88
Cdd:cd01638 5 LIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDP--LRLGWDRFWLVDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 89 DGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRAQPISVRLEPEEAfTVVASKRHGSP 168
Cdd:cd01638 83 DGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPL-RVVASRSHPDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 169 AQERLLDGlserFGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYePREDYL 248
Cdd:cd01638 162 ELEALLAA----LGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTY-NREDFL 236
|
....*.
gi 489190673 249 NGSFLA 254
Cdd:cd01638 237 NPDFIA 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
11-252 |
3.24e-87 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 260.01 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 11 ALVRRAGEAILPHWRAD--VAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDceiP--LSERGHWRRWWLVD 86
Cdd:PRK10931 7 QLARNAGDAIMQVYDGTkpLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEED---PpaWEVRQHWQRYWLVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 87 PLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGgAGLGAWREEaDGRAQPISVRlePEEAFTVVASKRHG 166
Cdd:PRK10931 84 PLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSA-AEGKAWKEE-CGVRKQIQVR--DARPPLVVISRSHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 167 SpaqERLLDGLSErFGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEPRED 246
Cdd:PRK10931 160 D---AELKEYLQQ-LGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRES 235
|
....*.
gi 489190673 247 YLNGSF 252
Cdd:PRK10931 236 FLNPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
9-244 |
2.66e-50 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 166.37 E-value: 2.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRADVAVRSKADES---PVTAADLAAHHILEAGLRALAPDIPVLSEEDCE-IPLSERGHWRRWWL 84
Cdd:pfam00459 9 AVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGAkGDQTELTDDGPTWI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 85 VDPLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEadgraQPISVRLEPE----EAFTVV 160
Cdd:pfam00459 89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNG-----QPLPVSRAPPlseaLLVTLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 161 ASKRHGSPAQERLLDGLSERFGDLRRASIGSS-LKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPF 239
Cdd:pfam00459 164 GVSSRKDTSEASFLAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDADGGPF 243
|
....*
gi 489190673 240 TYEPR 244
Cdd:pfam00459 244 DLLAG 248
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
8-261 |
1.35e-133 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 377.96 E-value: 1.35e-133
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 8 ELVALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWRRWWLVDP 87
Cdd:COG1218 7 AAIEIAREAGEAILEIYRADFEVEEKADDSPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPYEERKSWDRFWLVDP 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRAQPISVR-LEPEEAFTVVASKRHG 166
Cdd:COG1218 87 LDGTKEFIKRNGEFTVNIALIEDGRPVLGVVYAPALGRLYYAAKGQGAFKETGGGERQPIRVRdRPPAEPLRVVASRSHR 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 167 SPAQERLLdglsERFGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEPRED 246
Cdd:COG1218 167 DEETEALL----ARLGVAELVSVGSSLKFCLVAEGEADLYPRLGPTMEWDTAAGQAILEAAGGRVTDLDGKPLRYNKKED 242
|
250
....*....|....*
gi 489190673 247 YLNGSFLALPRAAEW 261
Cdd:COG1218 243 LLNPGFIASGDHAAI 257
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
6-255 |
1.54e-104 |
|
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: 303.99 E-value: 1.54e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 6 WGELVA-LVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWRRWWL 84
Cdd:TIGR01331 1 MLDDVIkIARAAGEEILPVYQKELAVAQKADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPLTPRQTWQRFWL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 85 VDPLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRAQ-PISVRLEPEEAFTVVASK 163
Cdd:TIGR01331 81 VDPLDGTKEFINRNGDFTVNIALVEHGVPVLGVVYAPATGVTYFATAGKAAKREGDGQALKaPIHVRPWPSGPLLVVISR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 164 RHGSPAQERLLDGLserfGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEP 243
Cdd:TIGR01331 161 SHAEEKTTEYLANL----GYDLRTSGGSSLKFCLVAEGSADIYPRLGPTGEWDTAAGHAVLAAAGGAIFDLDGSPLLYGK 236
|
250
....*....|..
gi 489190673 244 REDYLNGSFLAL 255
Cdd:TIGR01331 237 RESFRNPNFVAL 248
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
9-254 |
3.42e-103 |
|
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: 300.30 E-value: 3.42e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPlsERGHWRRWWLVDPL 88
Cdd:cd01638 5 LIRIAREAGDAILEVYRGGFTVERKEDGSPVTAADLAANAFIVEGLAALRPDIPVLSEESADDP--LRLGWDRFWLVDPL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 89 DGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRAQPISVRLEPEEAfTVVASKRHGSP 168
Cdd:cd01638 83 DGTREFIKGNGEFAVNIALVEDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPL-RVVASRSHPDE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 169 AQERLLDGlserFGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYePREDYL 248
Cdd:cd01638 162 ELEALLAA----LGVAEVVSIGSSLKFCLVAEGEADIYPRLGPTMEWDTAAGDAVLRAAGGAVSDLDGSPLTY-NREDFL 236
|
....*.
gi 489190673 249 NGSFLA 254
Cdd:cd01638 237 NPDFIA 242
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
11-252 |
3.24e-87 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 260.01 E-value: 3.24e-87
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 11 ALVRRAGEAILPHWRAD--VAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDceiP--LSERGHWRRWWLVD 86
Cdd:PRK10931 7 QLARNAGDAIMQVYDGTkpLDVASKADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEED---PpaWEVRQHWQRYWLVD 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 87 PLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGgAGLGAWREEaDGRAQPISVRlePEEAFTVVASKRHG 166
Cdd:PRK10931 84 PLDGTKEFIKRNGEFTVNIALIEQGKPVLGVVYAPVMNVMYSA-AEGKAWKEE-CGVRKQIQVR--DARPPLVVISRSHA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 167 SpaqERLLDGLSErFGDLRRASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEPRED 246
Cdd:PRK10931 160 D---AELKEYLQQ-LGEHQTTSIGSSLKFCLVAEGQAQLYPRFGPTNIWDTAAGHAVAIAAGAHVHDWQGKTLDYTPRES 235
|
....*.
gi 489190673 247 YLNGSF 252
Cdd:PRK10931 236 FLNPGF 241
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
9-244 |
2.66e-50 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 166.37 E-value: 2.66e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRADVAVRSKADES---PVTAADLAAHHILEAGLRALAPDIPVLSEEDCE-IPLSERGHWRRWWL 84
Cdd:pfam00459 9 AVELAAKAGEILREAFSNKLTIEEKGKSGandLVTAADKAAEELILEALAALFPSHKIIGEEGGAkGDQTELTDDGPTWI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 85 VDPLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEadgraQPISVRLEPE----EAFTVV 160
Cdd:pfam00459 89 IDPIDGTKNFVHGIPQFAVSIGLAVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNG-----QPLPVSRAPPlseaLLVTLF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 161 ASKRHGSPAQERLLDGLSERFGDLRRASIGSS-LKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPF 239
Cdd:pfam00459 164 GVSSRKDTSEASFLAKLLKLVRAPGVRRVGSAaLKLAMVAAGKADAYIEFGRLKPWDHAAGVAILREAGGVVTDADGGPF 243
|
....*
gi 489190673 240 TYEPR 244
Cdd:pfam00459 244 DLLAG 248
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
9-242 |
2.72e-50 |
|
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: 165.79 E-value: 2.72e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRA-DVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGhwrRWWLVDP 87
Cdd:COG0483 7 ALRAARAAGALILRRFRElDLEVETKGDGDLVTEADRAAEAAIRERLRAAFPDHGILGEESGASEGRDSG---YVWVIDP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWReeaDGRAQPISVRLEPEEAFTVVASKRHGS 167
Cdd:COG0483 84 IDGTTNFVHGLPLFAVSIALVRDGEPVAGVVYDPALGELFTAARGGGAFL---NGRRLRVSARTDLEDALVATGFPYLRD 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489190673 168 PAQER-LLDGLSERFGDLRRasIGS-SLKFCLLAEGAADCY--PRLTPtsqWDTAAAQGVLEGAGGEVLDLHGAPFTYE 242
Cdd:COG0483 161 DREYLaALAALLPRVRRVRR--LGSaALDLAYVAAGRLDAFveAGLKP---WDIAAGALIVREAGGVVTDLDGEPLDLG 234
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
9-248 |
1.72e-49 |
|
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: 163.25 E-value: 1.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRADVAVRSK-ADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEipLSERGHWRRWWLVDP 87
Cdd:cd01637 4 ALKAVREAGALILEAFGEELTVETKkGDGDLVTEADLAAEELIVDVLKALFPDDGILGEEGGG--SGNVSDGGRVWVIDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWReeaDGRAQPISVRLEPEEA--FTVVASKRH 165
Cdd:cd01637 82 IDGTTNFVAGLPNFAVSIALYEDGKPVLGVIYDPMLDELYYAGRGKGAFL---NGKKLPLSKDTPLNDAllSTNASMLRS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 166 GSPAqerLLDGLSERFGDLRRasIGS-SLKFCLLAEGAAD--CYPRLTPtsqWDTAAAQGVLEGAGGEVLDLHGAPFTYE 242
Cdd:cd01637 159 NRAA---VLASLVNRALGIRI--YGSaGLDLAYVAAGRLDayLSSGLNP---WDYAAGALIVEEAGGIVTDLDGEPLDTL 230
|
....*.
gi 489190673 243 PREDYL 248
Cdd:cd01637 231 NRSGII 236
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
11-258 |
1.57e-38 |
|
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: 135.90 E-value: 1.57e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 11 ALVRRAGEAILPHWR---ADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEiPLSerghwrRWWLVDP 87
Cdd:cd01517 7 LAVRAAASLTLPVFRnlgAGDVVWKKSDKSPVTVADYGAQALITAALARLFPSDPIVGEEDSA-ALG------RFWVLDP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGsEEFTVNVALVEDGRVLFGLVGVPVS-------GRCYYGGAGLGAW-REEADGRAQPISVRLEP---EEA 156
Cdd:cd01517 80 IDGTKGFLRG-DQFAVALALIEDGEVVLGVIGCPNLplddgggGDLFSAVRGQGAWlRPLDGSSLQPLSVRQLTnaaRAS 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 157 FTVVASKRHGSPAQERLLDGLSERFGDLRrasIGSSLKFCLLAEGAADCYPRLtPTSQ------WDTAAAQGVLEGAGGE 230
Cdd:cd01517 159 FCESVESAHSSHRLQAAIKALGGTPQPVR---LDSQAKYAAVARGAADFYLRL-PLSMsyrekiWDHAAGVLIVEEAGGK 234
|
250 260
....*....|....*....|....*....
gi 489190673 231 VLDLHGAPFTY-EPREDYLNGSFLALPRA 258
Cdd:cd01517 235 VTDADGKPLDFgKGRKLLNNGGLIAAPGE 263
|
|
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
11-240 |
5.09e-37 |
|
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: 131.22 E-value: 5.09e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 11 ALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEiplsERGHWRRWWLVDPLDG 90
Cdd:cd01641 7 ELADAAGQITLPYFRTRLQVETKADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGN----EGGDAGYVWVLDPIDG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 91 TKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEADGRaqPISVR--LEPEEAFTVVASKRHGSP 168
Cdd:cd01641 83 TKSFIRGLPVWGTLIALLHDGRPVLGVIDQPALGERWIGARGGGTFLNGAGGR--PLRVRacADLAEAVLSTTDPHFFTP 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 489190673 169 AQERLLDGLSE-----RFGdlrrasiGSSLKFCLLAEGAAD--CYPRLTPtsqWDTAAAQGVLEGAGGEVLDLHGAPFT 240
Cdd:cd01641 161 GDRAAFERLARavrltRYG-------GDCYAYALVASGRVDlvVEAGLKP---YDVAALIPIIEGAGGVITDWDGGPLT 229
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
9-252 |
1.64e-32 |
|
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: 119.36 E-value: 1.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWrrwwLVDPL 88
Cdd:cd01643 4 AEAIAQEAGDRALADFGNSLSAETKADGSLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWYW----VIDPI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 89 DGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWReeaDGRAQPISVRLePEEAFTVVASKRHGSP 168
Cdd:cd01643 80 DGTTNFARGIPIWAISIALLYRGEPVFGVIALPALNQTFVAFKGGGAFL---NGKPLALHPPL-QLPDCNVGFNRSSRAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 169 AQERLLDGLSERFGDLRRasIGS-SLKFCLLAEGAADCYPRLTPtSQWDTAAAQGVLEGAGGEVLDLHGAPFTYEPREDY 247
Cdd:cd01643 156 ARAVLRVILRRFPGKIRM--LGSaSLNLASVAAGQTLGYVEATP-KIWDIAAAWVILREAGGSWTILDEEPAFLQTKDYL 232
|
....*
gi 489190673 248 LNGSF 252
Cdd:cd01643 233 SAGFP 237
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
9-240 |
1.42e-29 |
|
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the inositol monophosphatase family (pfam00459). The members of this family consist of no more than one per species and are found only in species in which histidine is synthesized de novo but no histidinol phosphatase can be found in either of the two described families (TIGR01261, TIGR01856). In at least one species, the member of this family is found near known histidine biosynthesis genes. The role as histidinol-phosphatase wsa first proven in Corynebacterium glutamicum. [Amino acid biosynthesis, Histidine family]
Pssm-ID: 273949 [Multi-domain] Cd Length: 251 Bit Score: 112.01 E-value: 1.42e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 9 LVALVRRAGEAILPHWRA-DVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEiplSERGHWRRWWLVDP 87
Cdd:TIGR02067 5 AEDLADAAGETILPFFRAsLLVVDKKSDKTPVTEADRAAEEAMRELIAAFFPDHGILGEEFGH---NEEGDAERVWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWReeadgRAQPISVRLEPEEAFTVVASkrhgs 167
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALVEGGMPVLGVIFQPATGERWWAAGGGAAFL-----GGRRLRVSSCANLSDAVLFT----- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 168 pAQERLLD--GLSERFGDLRRASI-----GSSLKFCLLAEGAADCY--PRLTPtsqWDTAAAQGVLEGAGGEVLDLHGAP 238
Cdd:TIGR02067 152 -TSPDLLDdpGNRPAFERLRRAARltrygGDCYAYLMVAGGAVDIVvePGLSP---WDIAALIPVIEEAGGCFTDWDGKP 227
|
..
gi 489190673 239 FT 240
Cdd:TIGR02067 228 AP 229
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
10-244 |
1.63e-27 |
|
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: 106.08 E-value: 1.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 10 VALVRRAGEAILPHW-RADVAVRSKADES-PVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWrrwWLVDP 87
Cdd:cd01639 6 IEAARKAGEILLEAYeKLGLNVEEKGSPVdLVTEVDKAVEKLIIEILKKAYPDHGFLGEESGAAGGLTDEPT---WIIDP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 88 LDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEadgraQPISV--RLEPEEAF--TVVASK 163
Cdd:cd01639 83 LDGTTNFVHGFPHFAVSIALAVKGEPVVGVVYDPIRNELFTAVRGQGAFLNG-----RRIRVsgRKELKDALvaTGFPYD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 164 RHG--SPAQERLLDGLSERFGDLRRasIGS-SLKFCLLAEGAADCY--PRLTPtsqWDTAAAQGVLEGAGGEVLDLHGAP 238
Cdd:cd01639 158 RGDnfDRYLNNFAKLLAKAVRGVRR--LGSaALDLAYVAAGRLDGYweRGLKP---WDVAAGALIVREAGGLVTDFDGGP 232
|
....*.
gi 489190673 239 FTYEPR 244
Cdd:cd01639 233 FDLMSG 238
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
8-234 |
1.89e-25 |
|
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: 99.39 E-value: 1.89e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 8 ELVALVRRAGEAILPHWRA---DVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGHWRRWWL 84
Cdd:cd01636 3 ELCRVAKEAGLAILKAFGRelsGKVKITKSDNDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEVMGRRDEYTWV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 85 VDPLDGTKEFISGSEEFTVNVALvedgrvlfglvgvpvsgrcyyggaglgawreeadgraQPISVRLEPeeaftvvASKR 164
Cdd:cd01636 83 IDPIDGTKNFINGLPFVAVVIAV-------------------------------------YVILILAEP-------SHKR 118
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489190673 165 HgSPAQERLLDGLSERFgdlRRASiGSSLKFCLLAEGAADCYPRLTPTSQ-WDTAAAQGVLEGAGGEVLDL 234
Cdd:cd01636 119 V-DEKKAELQLLAVYRI---RIVG-SAVAKMCLVALGLADIYYEPGGKRRaWDVAASAAIVREAGGIMTDW 184
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
27-249 |
2.51e-24 |
|
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: 98.93 E-value: 2.51e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 27 DVAVRSKADES---PVTAADLAAHHILEAGLRALAPDIPVLSEEDCE----------------------------IPLSE 75
Cdd:cd01640 27 ILLVEGKTKEGandFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDNEfenqedesrdvdldeeileescpspskdLPEED 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 76 RGHWrrwwlVDPLDGTKEFISGSEEF-TVNVALVEDGRVLFGLVGVP----------VSGRCYYGGAGLGAWREEADGRA 144
Cdd:cd01640 107 LGVW-----VDPLDATQEYTEGLLEYvTVLIGVAVKGKPIAGVIHQPfyektagagaWLGRTIWGLSGLGAHSSDFKERE 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 145 QPISVRLEPEEAFTV--VASKRHGSPaqerllDGLsERFGdlrrasiGSSLKFCLLAEGAADCYPRLTPTS-QWDTAAAQ 221
Cdd:cd01640 182 DAGKIIVSTSHSHSVkeVQLITAGNK------DEV-LRAG-------GAGYKVLQVLEGLADAYVHSTGGIkKWDICAPE 247
|
250 260
....*....|....*....|....*...
gi 489190673 222 GVLEGAGGEVLDLHGAPFTYEPREDYLN 249
Cdd:cd01640 248 AILRALGGDMTDLHGEPLSYSKAVKPVN 275
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
11-255 |
2.74e-17 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 79.76 E-value: 2.74e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 11 ALVRRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEdceiplserGHWRR------W-W 83
Cdd:PLN02911 42 KLADAAGEVTRKYFRTKFEIIDKEDLSPVTIADRAAEEAMRSIILENFPSHAIFGEE---------HGLRCgegssdYvW 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 84 LVDPLDGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGlgawrEEADGRAQPISVRLEPEEAFTVVASK 163
Cdd:PLN02911 113 VLDPIDGTKSFITGKPLFGTLIALLYKGKPVLGIIDQPVLKERWVGVAG-----RATTLNGEEISTRSCASLKDAYLYTT 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 164 rhgSPaqeRLLDGLSE-RFGDLRRAsIGSSLKFC------LLAEGAADCYPR--LTPtsqWDTAAAQGVLEGAGGEVLDL 234
Cdd:PLN02911 188 ---SP---HMFSGDAEdAFARVRDK-VKVPLYGCdcyaygLLASGHVDLVVEsgLKP---YDYLALVPVVEGAGGVITDW 257
|
250 260
....*....|....*....|.
gi 489190673 235 HGAPFTYEPREDYLNGSFLAL 255
Cdd:PLN02911 258 KGRKLRWEPSPGSLATSFNVV 278
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
26-238 |
1.59e-14 |
|
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: 71.25 E-value: 1.59e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 26 ADVAVRSKADESPVTAADLAAHHILEAGLRALAPdIPVLSEEDCEIPLSERGHWRrwWLVDPLDGTKEFISGSEEFTVNV 105
Cdd:cd01515 25 ASEVVKIGADGTPTKLIDKVAEDAAIEILKKLGS-VNIVSEEIGVIDNGDEPEYT--VVLDPLDGTYNAINGIPFYSVSV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 106 ALVE--DGRVLFGLVGVPVSGRCYYGGAGLGAWREEadgraQPISVR-LEPEEAFTVVASKRHGSPAQERLLDglserfG 182
Cdd:cd01515 102 AVFKidKSDPYYGYVYNLATGDLYYAIKGKGAYLNG-----KRIKVSdFSSLKSISVSYYIYGKNHDRTFKIC------R 170
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 489190673 183 DLRRASI-GS-SLKFCLLAEGAADCYPRLTPTSQ-WDTAAAQGVLEGAGGEVLDLHGAP 238
Cdd:cd01515 171 KVRRVRIfGSvALELCYVASGALDAFVDVRENLRlVDIAAGYLIAEEAGGIVTDENGKE 229
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
16-239 |
1.87e-14 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 71.09 E-value: 1.87e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 16 AGEAILPHW---RADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGhwrrwWLV--DPLDG 90
Cdd:PRK12676 17 VEKAIMPLFgtpDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEELGEIVGNGPE-----YTVvlDPLDG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 91 TKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREEadgraQPISVRLEPE-EAFTVVASkrhGSPA 169
Cdd:PRK12676 92 TYNAINGIPFYAISIAVFKGGKPVYGYVYNLATGDFYEAIPGKGAYLNG-----KPIKVSKTSElNESAVSIY---GYRR 163
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489190673 170 QERLLDGLSERfgdLRRASI--GSSLKFCLLAEGAADCY----PRLTPTsqwDTAAAQGVLEGAGGEVLDLHGAPF 239
Cdd:PRK12676 164 GKERTVKLGRK---VRRVRIlgAIALELCYVASGRLDAFvdvrNYLRVT---DIAAGKLICEEAGGIVTDEDGNEL 233
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
14-239 |
2.75e-14 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 70.87 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 14 RRAGEAILPHWRADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEED---CEIPL--SERGhwrrwWLVDPL 88
Cdd:PLN02553 19 KAAGQIIRKGFYQTKHVEHKGQVDLVTETDKACEDLIFNHLKQAFPSHKFIGEETtaaSGGTEltDEPT-----WIVDPL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 89 DGTKEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGAWREeadgrAQPISVRLEPEEAFTVVASKRhGSP 168
Cdd:PLN02553 94 DGTTNFVHGFPFVCVSIGLTIGKVPVVGVVYNPILDELFTAVKGKGAFLN-----GKPIKASSQSELGKALLATEV-GTK 167
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489190673 169 AQERLLDGLSERFGDLR------RASIGSSLKFCLLAEGAADCYPRLTPTSQWDTAAAQGVLEGAGGEVLDLHGAPF 239
Cdd:PLN02553 168 RDKATVDATTNRINALLykvrslRMSGSCALNLCGVACGRLDIFYEIGFGGPWDVAAGAVIVKEAGGLVFDPSGGPF 244
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
14-237 |
1.97e-11 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 62.52 E-value: 1.97e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 14 RRAGEAILPHWRADVAVRS--KADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIPLSERGhwrRWWLVDPLDGT 91
Cdd:PRK10757 13 RKAGNLIAKNYETPDAVEAsqKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEESGELEGEDQD---VQWVIDPLDGT 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 92 KEFISGSEEFTVNVALVEDGRVLFGLVGVPVSGRCYYGGAGLGawreeadgrAQPISVRLEPEEAF----TVVAS----- 162
Cdd:PRK10757 90 TNFIKRLPHFAVSIAVRIKGRTEVAVVYDPMRNELFTATRGQG---------AQLNGYRLRGSTARdldgTILATgfpfk 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489190673 163 -KRHgSPAQERLLDGLSERFGDLRRASiGSSLKFCLLAEGAADCYPR--LTPtsqWDTAAAQGVLEGAGGEVLDLHGA 237
Cdd:PRK10757 161 aKQH-ATTYINIVGKLFTECADFRRTG-SAALDLAYVAAGRVDGFFEigLKP---WDFAAGELLVREAGGIVSDFTGG 233
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
3-240 |
2.71e-07 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 50.95 E-value: 2.71e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 3 PVPWGELVALVRRAGEAilphwRADVaVRSKADESP----------VTAADLAAHHILEAGLRALAPDIPVLSEEDCEIP 72
Cdd:PLN02737 73 PIPAEELLAVAELAAKT-----GAEV-VMEAVNKPRnisykgltdlVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIG 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 73 LSERGHWrrwWLVDPLDGTKEFISGSEEFTVNVALVEDGRVLFGLV----GVPV--SGRCYYGGAGLGAWreeADGraQP 146
Cdd:PLN02737 147 DSSSDYL---WCIDPLDGTTNFAHGYPSFAVSVGVLFRGTPAAATVvefvGGPMcwNTRTFSASAGGGAF---CNG--QK 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 147 ISVRL--EPEEAFTVVASKRHGSPAQERLLDgLSERFGDLRRA--SIGS-SLKFCLLAEGAADCY--PRLTPtsqWDTAA 219
Cdd:PLN02737 219 IHVSQtdKVERSLLVTGFGYEHDDAWATNIE-LFKEFTDVSRGvrRLGAaAVDMCHVALGIVEAYweYRLKP---WDMAA 294
|
250 260
....*....|....*....|.
gi 489190673 220 AQGVLEGAGGEVLDLHGAPFT 240
Cdd:PLN02737 295 GVLIVEEAGGTVTRMDGGKFS 315
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
11-238 |
1.56e-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: 45.13 E-value: 1.56e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 11 ALVRRAGEAILPHW----RADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIPVLSEEDCEIplsERGHWRRWWLVD 86
Cdd:cd01642 4 VLEKITKEIILLLNeknrQGLVKLIRGAGGDVTRVADLKAEEIILKLLREEGVFGQIISEESGEI---RKGSGEYIAVLD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 87 PLDGTKEFISGSEEFTVNVALVE-DGRVLFGLVGVPVSGRcyyGGAGLgawrEEADGRAQPISVRLEPEEAFTVVASKRH 165
Cdd:cd01642 81 PLDGSTNYLSGIPFYSVSVALADpRSKVKAATLDNFVSGE---GGLKV----YSPPTRFSYISVPKLGPPLVPEVPSKIG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 166 GSPAQERLLD--GLSERFGdLRRASIGSS-LKFCLLAEGAADCY----PRLTPTsqwDTAAAQGVLEGaggevLDLHGAP 238
Cdd:cd01642 154 IYEGSSRNPEkfLLLSRNG-LKFRSLGSAaLELAYTCEGSFVLFldlrGKLRNF---DVAAALGACKR-----LGLHGDP 224
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
25-238 |
2.11e-05 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 45.49 E-value: 2.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 25 RADVAVRSKADESPVTAADLAAHHILEAGLRALAPDIpVLSEEDCEIPLSeRGHWRRWWLVDPLDGT------------- 91
Cdd:PRK14076 28 KAGEVVKIGADGTPTKRIDLIAENIAINSLEKFCSGI-LISEEIGFKKIG-KNKPEYIFVLDPIDGTynalkdipiysas 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489190673 92 ------KEFISGSEEFTVNVALVEDgrVLFGLVGVPVSGRCYYGGAGLGAWrEEADGRAQPISVRLEPEEAFTVVASKRH 165
Cdd:PRK14076 106 iaiakiDGFDKKIKEFIGKNLTIND--LEVGVVKNIATGDTYYAEKGEGAY-LLKKGEKKKIEISNISNLKDASIGLFAY 182
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489190673 166 GSPAQerLLDGLSERfgDLRRASI-GS-SLKFCLLAEGAADCYPRLTPTSQW-DTAAAQGVLEGAGGEVLDLHGAP 238
Cdd:PRK14076 183 GLSLD--TLKFIKDR--KVRRIRLfGSiALEMCYVASGALDAFINVNETTRLcDIAAGYVICKEAGGIITNKNGKP 254
|
|
| |
