|
Name |
Accession |
Description |
Interval |
E-value |
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
11-268 |
1.83e-107 |
|
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: 311.50 E-value: 1.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 11 DINLAEQLADISGEIIRRYFRQPhLRAETKlgQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSRSGRYWVL 90
Cdd:cd01641 1 DLAFALELADAAGQITLPYFRTR-LQVETK--ADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYVWVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 91 DPIDGTSSFVKGLPIFGTLIGLVDLEQnlPLLGVVNQPILQQRWLGIRGKPTYYNhQPVVNPYANDDQSKLEDAcLTSTT 170
Cdd:cd01641 78 DPIDGTKSFIRGLPVWGTLIALLHDGR--PVLGVIDQPALGERWIGARGGGTFLN-GAGGRPLRVRACADLAEA-VLSTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 171 PLMFITDRQQQIAKKLQQICVRTAFGGDCYNYVALASGWCAMPMiilEADLNFYDFCAIIPIIQGAGGIITDWSGNTLVP 250
Cdd:cd01641 154 DPHFFTPGDRAAFERLARAVRLTRYGGDCYAYALVASGRVDLVV---EAGLKPYDVAALIPIIEGAGGVITDWDGGPLTG 230
|
250
....*....|....*...
gi 501596824 251 QSTEVIACSTSSLWEQAL 268
Cdd:cd01641 231 GSGRVVAAGDAELHEALL 248
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
8-272 |
2.63e-83 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 251.95 E-value: 2.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQLADISGEIIRRYFRQPhLRAETKLGqvSSIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSRSGR 86
Cdd:PLN02911 33 LDRFVDVAHKLADAAGEVTRKYFRTK-FEIIDKED--LSPVTIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEGSSD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 87 Y-WVLDPIDGTSSFVKGLPIFGTLIGLvdLEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVvnpyANDDQSKLEDAC 165
Cdd:PLN02911 110 YvWVLDPIDGTKSFITGKPLFGTLIAL--LYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEI----STRSCASLKDAY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 166 LTSTTPLMFITDRQQQIaKKLQQICVRTAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSG 245
Cdd:PLN02911 184 LYTTSPHMFSGDAEDAF-ARVRDKVKVPLYGCDCYAYGLLASGHVD---LVVESGLKPYDYLALVPVVEGAGGVITDWKG 259
|
250 260 270
....*....|....*....|....*....|....*
gi 501596824 246 NTL--------VPQSTEVIACSTSSLWEQALQEIE 272
Cdd:PLN02911 260 RKLrwepspgsLATSFNVVAAGDARLHKQALDILE 294
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
14-268 |
7.83e-81 |
|
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: 243.75 E-value: 7.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 14 LAEQLADISGEIIRRYFRQPHLRAETKLGQvsSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSRSGRY-WVLDP 92
Cdd:TIGR02067 4 FAEDLADAAGETILPFFRASLLVVDKKSDK--TPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERvWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 93 IDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVVnpyaNDDQSKLEDACLTSTTPL 172
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALV--EGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLR----VSSCANLSDAVLFTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 173 MFITDRQQQIAKKLQQICVRTAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSGNTLvPQS 252
Cdd:TIGR02067 156 LLDDPGNRPAFERLRRAARLTRYGGDCYAYLMVAGGAVD---IVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDG 231
|
250
....*....|....*.
gi 501596824 253 TEVIACSTSSLWEQAL 268
Cdd:TIGR02067 232 GGAVAAGNAMLHDEAL 247
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
9-273 |
3.60e-74 |
|
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: 227.04 E-value: 3.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 9 DQDINLAEQLADISGEIIRRYFRQPHLRAETKlgQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSRSGRY 87
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDLEVETK--GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEEsGASEGRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 88 WVLDPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVvnpyANDDQSKLEDACLT 167
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALV--RDGEPVAGVVYDPALGELFTAARGGGAFLNGRRL----RVSARTDLEDALVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 168 STTPLMFITDRQQQIAKKLQQICVR-TAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSGN 246
Cdd:COG0483 153 TGFPYLRDDREYLAALAALLPRVRRvRRLGSAALDLAYVAAGRLD---AFVEAGLKPWDIAAGALIVREAGGVVTDLDGE 229
|
250 260
....*....|....*....|....*..
gi 501596824 247 TLVPQSTEVIAcSTSSLWEQALQEIES 273
Cdd:COG0483 230 PLDLGSGSLVA-ANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
8-274 |
2.96e-52 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 171.37 E-value: 2.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQLADISGEIIRRYFRQPHLRAETKLGQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSR---- 83
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQtelt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 84 -SGRYWVLDPIDGTSSFVKGLPIFGTLIGLvdLEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQ--PVVNPYaNDDQSK 160
Cdd:pfam00459 82 dDGPTWIIDPIDGTKNFVHGIPQFAVSIGL--AVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQplPVSRAP-PLSEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 161 LEDACLTSTTPLMFITDRQQQIAKKLQQICVRtAFGGDCYNYVALASGWCAmpmIILEAD-LNFYDFCAIIPIIQGAGGI 239
Cdd:pfam00459 159 LVTLFGVSSRKDTSEASFLAKLLKLVRAPGVR-RVGSAALKLAMVAAGKAD---AYIEFGrLKPWDHAAGVAILREAGGV 234
|
250 260 270
....*....|....*....|....*....|....*
gi 501596824 240 ITDWSGNTLVPQSTEVIACSTSSLWEQALQEIESI 274
Cdd:pfam00459 235 VTDADGGPFDLLAGRVIAANPKVLHELLAAALEEI 269
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Bacterial_IMPase_like_1 |
cd01641 |
Predominantly bacterial family of Mg++ dependend phosphatases, related to inositol ... |
11-268 |
1.83e-107 |
|
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: 311.50 E-value: 1.83e-107
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 11 DINLAEQLADISGEIIRRYFRQPhLRAETKlgQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSRSGRYWVL 90
Cdd:cd01641 1 DLAFALELADAAGQITLPYFRTR-LQVETK--ADFSPVTEADRAAEAAMRELIAAAFPDHGILGEEFGNEGGDAGYVWVL 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 91 DPIDGTSSFVKGLPIFGTLIGLVDLEQnlPLLGVVNQPILQQRWLGIRGKPTYYNhQPVVNPYANDDQSKLEDAcLTSTT 170
Cdd:cd01641 78 DPIDGTKSFIRGLPVWGTLIALLHDGR--PVLGVIDQPALGERWIGARGGGTFLN-GAGGRPLRVRACADLAEA-VLSTT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 171 PLMFITDRQQQIAKKLQQICVRTAFGGDCYNYVALASGWCAMPMiilEADLNFYDFCAIIPIIQGAGGIITDWSGNTLVP 250
Cdd:cd01641 154 DPHFFTPGDRAAFERLARAVRLTRYGGDCYAYALVASGRVDLVV---EAGLKPYDVAALIPIIEGAGGVITDWDGGPLTG 230
|
250
....*....|....*...
gi 501596824 251 QSTEVIACSTSSLWEQAL 268
Cdd:cd01641 231 GSGRVVAAGDAELHEALL 248
|
|
| PLN02911 |
PLN02911 |
inositol-phosphate phosphatase |
8-272 |
2.63e-83 |
|
inositol-phosphate phosphatase
Pssm-ID: 178499 [Multi-domain] Cd Length: 296 Bit Score: 251.95 E-value: 2.63e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQLADISGEIIRRYFRQPhLRAETKLGqvSSIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSRSGR 86
Cdd:PLN02911 33 LDRFVDVAHKLADAAGEVTRKYFRTK-FEIIDKED--LSPVTIADRAAEEAMRSIILENFPSHAIFGEEhGLRCGEGSSD 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 87 Y-WVLDPIDGTSSFVKGLPIFGTLIGLvdLEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVvnpyANDDQSKLEDAC 165
Cdd:PLN02911 110 YvWVLDPIDGTKSFITGKPLFGTLIAL--LYKGKPVLGIIDQPVLKERWVGVAGRATTLNGEEI----STRSCASLKDAY 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 166 LTSTTPLMFITDRQQQIaKKLQQICVRTAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSG 245
Cdd:PLN02911 184 LYTTSPHMFSGDAEDAF-ARVRDKVKVPLYGCDCYAYGLLASGHVD---LVVESGLKPYDYLALVPVVEGAGGVITDWKG 259
|
250 260 270
....*....|....*....|....*....|....*
gi 501596824 246 NTL--------VPQSTEVIACSTSSLWEQALQEIE 272
Cdd:PLN02911 260 RKLrwepspgsLATSFNVVAAGDARLHKQALDILE 294
|
|
| his_9_HisN |
TIGR02067 |
histidinol-phosphatase, inositol monophosphatase family; This subfamily belongs to the ... |
14-268 |
7.83e-81 |
|
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: 243.75 E-value: 7.83e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 14 LAEQLADISGEIIRRYFRQPHLRAETKLGQvsSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSRSGRY-WVLDP 92
Cdd:TIGR02067 4 FAEDLADAAGETILPFFRASLLVVDKKSDK--TPVTEADRAAEEAMRELIAAFFPDHGILGEEFGHNEEGDAERvWVLDP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 93 IDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVVnpyaNDDQSKLEDACLTSTTPL 172
Cdd:TIGR02067 82 IDGTKSFIRGVPVWGTLIALV--EGGMPVLGVIFQPATGERWWAAGGGAAFLGGRRLR----VSSCANLSDAVLFTTSPD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 173 MFITDRQQQIAKKLQQICVRTAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSGNTLvPQS 252
Cdd:TIGR02067 156 LLDDPGNRPAFERLRRAARLTRYGGDCYAYLMVAGGAVD---IVVEPGLSPWDIAALIPVIEEAGGCFTDWDGKPA-PDG 231
|
250
....*....|....*.
gi 501596824 253 TEVIACSTSSLWEQAL 268
Cdd:TIGR02067 232 GGAVAAGNAMLHDEAL 247
|
|
| SuhB |
COG0483 |
Archaeal fructose-1,6-bisphosphatase or related enzyme, inositol monophosphatase family ... |
9-273 |
3.60e-74 |
|
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: 227.04 E-value: 3.60e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 9 DQDINLAEQLADISGEIIRRYFRQPHLRAETKlgQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSRSGRY 87
Cdd:COG0483 1 HPLLELALRAARAAGALILRRFRELDLEVETK--GDGDLVTEADRAAEAAIRERLRAAFPDHGILGEEsGASEGRDSGYV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 88 WVLDPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVvnpyANDDQSKLEDACLT 167
Cdd:COG0483 79 WVIDPIDGTTNFVHGLPLFAVSIALV--RDGEPVAGVVYDPALGELFTAARGGGAFLNGRRL----RVSARTDLEDALVA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 168 STTPLMFITDRQQQIAKKLQQICVR-TAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSGN 246
Cdd:COG0483 153 TGFPYLRDDREYLAALAALLPRVRRvRRLGSAALDLAYVAAGRLD---AFVEAGLKPWDIAAGALIVREAGGVVTDLDGE 229
|
250 260
....*....|....*....|....*..
gi 501596824 247 TLVPQSTEVIAcSTSSLWEQALQEIES 273
Cdd:COG0483 230 PLDLGSGSLVA-ANPALHDELLALLRE 255
|
|
| Inositol_P |
pfam00459 |
Inositol monophosphatase family; |
8-274 |
2.96e-52 |
|
Inositol monophosphatase family;
Pssm-ID: 459820 [Multi-domain] Cd Length: 271 Bit Score: 171.37 E-value: 2.96e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQLADISGEIIRRYFRQPHLRAETKLGQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSR---- 83
Cdd:pfam00459 2 LEEVLKVAVELAAKAGEILREAFSNKLTIEEKGKSGANDLVTAADKAAEELILEALAALFPSHKIIGEEGGAKGDQtelt 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 84 -SGRYWVLDPIDGTSSFVKGLPIFGTLIGLvdLEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQ--PVVNPYaNDDQSK 160
Cdd:pfam00459 82 dDGPTWIIDPIDGTKNFVHGIPQFAVSIGL--AVNGEPVLGVIYQPFAGQLYSAAKGKGAFLNGQplPVSRAP-PLSEAL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 161 LEDACLTSTTPLMFITDRQQQIAKKLQQICVRtAFGGDCYNYVALASGWCAmpmIILEAD-LNFYDFCAIIPIIQGAGGI 239
Cdd:pfam00459 159 LVTLFGVSSRKDTSEASFLAKLLKLVRAPGVR-RVGSAALKLAMVAAGKAD---AYIEFGrLKPWDHAAGVAILREAGGV 234
|
250 260 270
....*....|....*....|....*....|....*
gi 501596824 240 ITDWSGNTLVPQSTEVIACSTSSLWEQALQEIESI 274
Cdd:pfam00459 235 VTDADGGPFDLLAGRVIAANPKVLHELLAAALEEI 269
|
|
| IMPase_like |
cd01637 |
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ... |
13-257 |
2.10e-50 |
|
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: 165.57 E-value: 2.10e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 13 NLAEQLADISGEIIRRYFRQpHLRAETKLGqVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEG--ENIPSRSGRYWVL 90
Cdd:cd01637 2 ELALKAVREAGALILEAFGE-ELTVETKKG-DGDLVTEADLAAEELIVDVLKALFPDDGILGEEGggSGNVSDGGRVWVI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 91 DPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVVNPyanddQSKLEDACLTSTT 170
Cdd:cd01637 80 DPIDGTTNFVAGLPNFAVSIALY--EDGKPVLGVIYDPMLDELYYAGRGKGAFLNGKKLPLS-----KDTPLNDALLSTN 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 171 PLMFITDRQQQIAKKLQQICVRTAFGGDCYNYVALASGWCAmpmIILEADLNFYDFCAIIPIIQGAGGIITDWSGNTLVP 250
Cdd:cd01637 153 ASMLRSNRAAVLASLVNRALGIRIYGSAGLDLAYVAAGRLD---AYLSSGLNPWDYAAGALIVEEAGGIVTDLDGEPLDT 229
|
....*..
gi 501596824 251 QSTEVIA 257
Cdd:cd01637 230 LNRSGII 236
|
|
| IMPase |
cd01639 |
IMPase, inositol monophosphatase and related domains. A family of Mg++ dependent phosphatases, ... |
13-259 |
2.82e-38 |
|
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: 134.59 E-value: 2.82e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 13 NLAEQLADISGEIIRRYFRQPHLRAETKLGQVSsIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSRSGRYWVLD 91
Cdd:cd01639 3 NIAIEAARKAGEILLEAYEKLGLNVEEKGSPVD-LVTEVDKAVEKLIIEILKKAYPDHGFLGEEsGAAGGLTDEPTWIID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 92 PIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPV-VNpyandDQSKLEDACLTSTT 170
Cdd:cd01639 82 PLDGTTNFVHGFPHFAVSIALA--VKGEPVVGVVYDPIRNELFTAVRGQGAFLNGRRIrVS-----GRKELKDALVATGF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 171 PLMF--ITDRQQQIAKKLQQICVRtafGGDCYNYVALASGWCAMPMI--ILEADLNFYDFCAIIPIIQGAGGIITDWSGN 246
Cdd:cd01639 155 PYDRgdNFDRYLNNFAKLLAKAVR---GVRRLGSAALDLAYVAAGRLdgYWERGLKPWDVAAGALIVREAGGLVTDFDGG 231
|
250
....*....|...
gi 501596824 247 TLVPQSTEVIACS 259
Cdd:cd01639 232 PFDLMSGNILAGN 244
|
|
| Bacterial_IMPase_like_2 |
cd01643 |
Bacterial family of Mg++ dependent phosphatases, related to inositol monophosphatases. These ... |
12-254 |
3.24e-36 |
|
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: 128.99 E-value: 3.24e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 12 INLAEQLADISGEIIRRYFRQpHLRAETKLGQvsSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSRSGRYWVLD 91
Cdd:cd01643 1 LSLAEAIAQEAGDRALADFGN-SLSAETKADG--SLVTAADRWVEQLIRARLAAQFPDDGVLGEEGGGIFPSSGWYWVID 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 92 PIDGTSSFVKGLPIFGTLIGLvdLEQNLPLLGVVNQPILQQRWLGIRGKPTYYNhqpvvNPYANDDQSKLEDACLTSTTP 171
Cdd:cd01643 78 PIDGTTNFARGIPIWAISIAL--LYRGEPVFGVIALPALNQTFVAFKGGGAFLN-----GKPLALHPPLQLPDCNVGFNR 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 172 LMFITDRQQQIAKKLQQICVRTAFGGDCYNYVALASGWCAMPMiilEADLNFYDFCAIIPIIQGAGGIITdWSGNTLVPQ 251
Cdd:cd01643 151 SSRASARAVLRVILRRFPGKIRMLGSASLNLASVAAGQTLGYV---EATPKIWDIAAAWVILREAGGSWT-ILDEEPAFL 226
|
...
gi 501596824 252 STE 254
Cdd:cd01643 227 QTK 229
|
|
| CysQ |
cd01638 |
CysQ, a 3'-Phosphoadenosine-5'-phosphosulfate (PAPS) 3'-phosphatase, is a bacterial member of ... |
11-257 |
7.69e-29 |
|
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: 109.62 E-value: 7.69e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 11 DINLAEQLADISGEIIRRYFRQPHLRAETKLGqvsSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSR--SGRYW 88
Cdd:cd01638 1 LLELLIRIAREAGDAILEVYRGGFTVERKEDG---SPVTAADLAANAFIVEGLAALRPDIPVLSEESADDPLRlgWDRFW 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 89 VLDPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVVNPYANDDQSKLEDACLTS 168
Cdd:cd01638 78 LVDPLDGTREFIKGNGEFAVNIALV--EDGRPVLGVVYAPALGELYYALRGGGAYKNGRPGAVSLQARPPPLQPLRVVAS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 169 TTplmFITDRQQQIAKKLQQICVRTAfgGDCYNYVALASGwcampmiilEADL-------NFYDFCAIIPIIQGAGGIIT 241
Cdd:cd01638 156 RS---HPDEELEALLAALGVAEVVSI--GSSLKFCLVAEG---------EADIyprlgptMEWDTAAGDAVLRAAGGAVS 221
|
250
....*....|....*.
gi 501596824 242 DWSGNTLVPQSTEVIA 257
Cdd:cd01638 222 DLDGSPLTYNREDFLN 237
|
|
| CysQ |
COG1218 |
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and ... |
8-248 |
5.04e-28 |
|
3'-Phosphoadenosine 5'-phosphosulfate (PAPS) 3'-phosphatase [Inorganic ion transport and metabolism];
Pssm-ID: 440831 [Multi-domain] Cd Length: 260 Bit Score: 107.94 E-value: 5.04e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQLADISGEIIRRYFRQPhLRAETKLGQvsSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIP----SR 83
Cdd:COG1218 1 LEALLEAAIEIAREAGEAILEIYRAD-FEVEEKADD--SPVTEADLAAHAIILAGLAALTPDIPVLSEESAAIPyeerKS 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 84 SGRYWVLDPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNH-----QPV-VNPYANDD 157
Cdd:COG1218 78 WDRFWLVDPLDGTKEFIKRNGEFTVNIALI--EDGRPVLGVVYAPALGRLYYAAKGQGAFKETgggerQPIrVRDRPPAE 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 158 qskledacltsttPLMFITDR------QQQIAKKLQQICVRTAfgGDCYNYVALASGwcampmiilEADLnfY------- 224
Cdd:COG1218 156 -------------PLRVVASRshrdeeTEALLARLGVAELVSV--GSSLKFCLVAEG---------EADL--Yprlgptm 209
|
250 260
....*....|....*....|....*.
gi 501596824 225 --DFCAIIPIIQGAGGIITDWSGNTL 248
Cdd:COG1218 210 ewDTAAGQAILEAAGGRVTDLDGKPL 235
|
|
| FIG |
cd01636 |
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ... |
13-243 |
5.49e-24 |
|
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: 95.54 E-value: 5.49e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 13 NLAEQLADISGEIIRRYFRQpHLRAETKLGQVS-SIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPS----RSGRY 87
Cdd:cd01636 2 EELCRVAKEAGLAILKAFGR-ELSGKVKITKSDnDPVTTADVAAETLIRNMLKSSFPDVKIVGEESGVAEEvmgrRDEYT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 88 WVLDPIDGTSSFVKGLPIFGTLIGLVDleqnlpllgvvnqpilqqrwlgirgkptyynhqpvvnpyanddqskledaCLT 167
Cdd:cd01636 81 WVIDPIDGTKNFINGLPFVAVVIAVYV--------------------------------------------------ILI 110
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 501596824 168 STTPLMFITDRQQQiakKLQQICVRTAF--GGDCYNYVALASGWcAMPMIILEADLNFYDFCAIIPIIQGAGGIITDW 243
Cdd:cd01636 111 LAEPSHKRVDEKKA---ELQLLAVYRIRivGSAVAKMCLVALGL-ADIYYEPGGKRRAWDVAASAAIVREAGGIMTDW 184
|
|
| PLN02553 |
PLN02553 |
inositol-phosphate phosphatase |
6-272 |
1.08e-20 |
|
inositol-phosphate phosphatase
Pssm-ID: 178168 [Multi-domain] Cd Length: 270 Bit Score: 88.59 E-value: 1.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 6 HPLDQDINLAEQLADISGEIIRRYFRQPHlRAETKlGQVSsIVTIADQQAEEAMVKMILTHAPDDGIIreeGENIPSRSG 85
Cdd:PLN02553 5 DDLEQFLEVAVDAAKAAGQIIRKGFYQTK-HVEHK-GQVD-LVTETDKACEDLIFNHLKQAFPSHKFI---GEETTAASG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 86 -------RYWVLDPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVvnpyANDDQ 158
Cdd:PLN02553 79 gteltdePTWIVDPLDGTTNFVHGFPFVCVSIGLT--IGKVPVVGVVYNPILDELFTAVKGKGAFLNGKPI----KASSQ 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 159 SKLEDACLTS-------TTPLMFITDRQQQIAKKLQQicVRtaFGGDCynyvalASGWCAMPMIILEA--DLNF---YDF 226
Cdd:PLN02553 153 SELGKALLATevgtkrdKATVDATTNRINALLYKVRS--LR--MSGSC------ALNLCGVACGRLDIfyEIGFggpWDV 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 501596824 227 CAIIPIIQGAGGIITDWSGNTLVPQSTEViACSTSSLWEQ---ALQEIE 272
Cdd:PLN02553 223 AAGAVIVKEAGGLVFDPSGGPFDIMSRRV-AASNGHLKDAfveALRQTE 270
|
|
| bisphos_cysQ |
TIGR01331 |
3'(2'),5'-bisphosphate nucleotidase, bacterial; Sulfate is incorporated into ... |
8-248 |
2.22e-19 |
|
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: 84.81 E-value: 2.22e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQladiSGEIIRRYFRQPhLRAETKlgQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIP----SR 83
Cdd:TIGR01331 2 LDDVIKIARA----AGEEILPVYQKE-LAVAQK--ADNSPVTEADRAAHRFILEGLRALTPDIPVLSEEDASIPltprQT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 84 SGRYWVLDPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHqpvvnpyanDDQS---K 160
Cdd:TIGR01331 75 WQRFWLVDPLDGTKEFINRNGDFTVNIALV--EHGVPVLGVVYAPATGVTYFATAGKAAKREG---------DGQAlkaP 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 161 LEDACLTSTTPLMFITDRQ--QQIAKKLQQicvrtafggdcYNYVALASGWCAMPMIIL---EADL-------NFYDFCA 228
Cdd:TIGR01331 144 IHVRPWPSGPLLVVISRSHaeEKTTEYLAN-----------LGYDLRTSGGSSLKFCLVaegSADIyprlgptGEWDTAA 212
|
250 260
....*....|....*....|
gi 501596824 229 IIPIIQGAGGIITDWSGNTL 248
Cdd:TIGR01331 213 GHAVLAAAGGAIFDLDGSPL 232
|
|
| PAP_phosphatase |
cd01517 |
PAP-phosphatase_like domains. PAP-phosphatase is a member of the inositol monophosphatase ... |
46-270 |
1.55e-18 |
|
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: 82.75 E-value: 1.55e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 46 SIVTIADQQAEEAMVKMILTHAPDDGIIREEGEnipSRSGRYWVLDPIDGTSSFVKGLPiFGTLIGLVdlEQNLPLLGVV 125
Cdd:cd01517 36 SPVTVADYGAQALITAALARLFPSDPIVGEEDS---AALGRFWVLDPIDGTKGFLRGDQ-FAVALALI--EDGEVVLGVI 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 126 NQPILQQ------RWL-GIRGKPTYYNHQPVVNPYANDDQSKLEDACLTSTTPLmfitDRQQQIAKKLQQICVRTAFGGD 198
Cdd:cd01517 110 GCPNLPLddggggDLFsAVRGQGAWLRPLDGSSLQPLSVRQLTNAARASFCESV----ESAHSSHRLQAAIKALGGTPQP 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 199 C-----YNYVALASGwcampmiileaDLNFYDFCAIIP--------------IIQGAGGIITDWSGNTL-------VPQS 252
Cdd:cd01517 186 VrldsqAKYAAVARG-----------AADFYLRLPLSMsyrekiwdhaagvlIVEEAGGKVTDADGKPLdfgkgrkLLNN 254
|
250 260
....*....|....*....|.
gi 501596824 253 TEVIACSTS---SLWEqALQE 270
Cdd:cd01517 255 GGLIAAPGEiheQVLE-ALRE 274
|
|
| Arch_FBPase_1 |
cd01515 |
Archaeal fructose-1,6-bisphosphatase and related enzymes of inositol monophosphatase family ... |
49-257 |
6.40e-13 |
|
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: 67.02 E-value: 6.40e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 49 TIADQQAEEAMVKMILTHAPDDGIIREEGE-NIPSRSGRYWVLDPIDGTSSFVKGLPIFGTLIGLVDLEQNLPLLGVVNQ 127
Cdd:cd01515 39 KLIDKVAEDAAIEILKKLGSVNIVSEEIGViDNGDEPEYTVVLDPLDGTYNAINGIPFYSVSVAVFKIDKSDPYYGYVYN 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 128 PILQQRWLGIRGKPTYYNHQPVvnpyANDDQSKLEDACLTSTTPLmFITDRQQQIAKKLQQICVRTAFGGD-CYnyvaLA 206
Cdd:cd01515 119 LATGDLYYAIKGKGAYLNGKRI----KVSDFSSLKSISVSYYIYG-KNHDRTFKICRKVRRVRIFGSVALElCY----VA 189
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 501596824 207 SGWCAMPMIILEAdLNFYDFCAIIPIIQGAGGIITDWSGNTL-----VPQSTEVIA 257
Cdd:cd01515 190 SGALDAFVDVREN-LRLVDIAAGYLIAEEAGGIVTDENGKELklklnVTERVNIIA 244
|
|
| PRK12676 |
PRK12676 |
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase; |
14-272 |
3.68e-12 |
|
bifunctional fructose-bisphosphatase/inositol-phosphate phosphatase;
Pssm-ID: 183673 [Multi-domain] Cd Length: 263 Bit Score: 64.54 E-value: 3.68e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 14 LAEQLADISGEIIRRYFRQPHLRAETKLGQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSRSGRYWVLDP 92
Cdd:PRK12676 9 ICDDMAKEVEKAIMPLFGTPDAGETVGMGADGTPTKLIDKVAEDIILEVLKPLGRCVNIISEElGEIVGNGPEYTVVLDP 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 93 IDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGKPTYYNHQPVvnpyANDDQSKLEDACLtSTTPL 172
Cdd:PRK12676 89 LDGTYNAINGIPFYAISIAVF--KGGKPVYGYVYNLATGDFYEAIPGKGAYLNGKPI----KVSKTSELNESAV-SIYGY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 173 MFITDRQQQIAKKLQQICVRTAFGGD-CYnyvaLASGwcampmiILEA--DLNFY----DFCAIIPIIQGAGGIITDWSG 245
Cdd:PRK12676 162 RRGKERTVKLGRKVRRVRILGAIALElCY----VASG-------RLDAfvDVRNYlrvtDIAAGKLICEEAGGIVTDEDG 230
|
250 260 270
....*....|....*....|....*....|..
gi 501596824 246 NTL-----VPQSTEVIACSTSSLWEQALQEIE 272
Cdd:PRK12676 231 NELklplnVTERTNLIAANGEELHKKILELLE 262
|
|
| PRK10757 |
PRK10757 |
inositol-1-monophosphatase; |
5-246 |
1.60e-11 |
|
inositol-1-monophosphatase;
Pssm-ID: 236753 [Multi-domain] Cd Length: 267 Bit Score: 62.90 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 5 LHPLdqdINLAEQLADISGEIIRRYFRQPHlRAETKLGQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREE-GENIPSR 83
Cdd:PRK10757 1 MHPM---LNIAVRAARKAGNLIAKNYETPD-AVEASQKGSNDFVTNVDKAAEAVIIDTIRKSYPQHTIITEEsGELEGED 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 84 SGRYWVLDPIDGTSSFVKGLPIFGTLIGlVDLEQNLPlLGVVNQPILQQRWLGIRGKPTYYNHQPVVNPYANDdqskLED 163
Cdd:PRK10757 77 QDVQWVIDPLDGTTNFIKRLPHFAVSIA-VRIKGRTE-VAVVYDPMRNELFTATRGQGAQLNGYRLRGSTARD----LDG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 164 ACLTSTTPLmfitdRQQQ-------IAKKLQQICV---RTAFGGDCYNYVALA--SGWcampmiiLEADLNFYDFCAIIP 231
Cdd:PRK10757 151 TILATGFPF-----KAKQhattyinIVGKLFTECAdfrRTGSAALDLAYVAAGrvDGF-------FEIGLKPWDFAAGEL 218
|
250
....*....|....*
gi 501596824 232 IIQGAGGIITDWSGN 246
Cdd:PRK10757 219 LVREAGGIVSDFTGG 233
|
|
| PLN02737 |
PLN02737 |
inositol monophosphatase family protein |
7-113 |
8.99e-10 |
|
inositol monophosphatase family protein
Pssm-ID: 215392 [Multi-domain] Cd Length: 363 Bit Score: 58.27 E-value: 8.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 7 PLDQDINLAEQLADISGEIIRRYFRQPhlRAETKLGqVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEGENIPSRSGR 86
Cdd:PLN02737 75 PAEELLAVAELAAKTGAEVVMEAVNKP--RNISYKG-LTDLVTDTDKASEAAILEVVRKNFPDHLILGEEGGVIGDSSSD 151
|
90 100
....*....|....*....|....*...
gi 501596824 87 Y-WVLDPIDGTSSFVKGLPIFGTLIGLV 113
Cdd:PLN02737 152 YlWCIDPLDGTTNFAHGYPSFAVSVGVL 179
|
|
| PRK10931 |
PRK10931 |
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional |
17-140 |
1.74e-08 |
|
adenosine-3'(2'),5'-bisphosphate nucleotidase; Provisional
Pssm-ID: 182848 [Multi-domain] Cd Length: 246 Bit Score: 53.93 E-value: 1.74e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 17 QLADISGE-IIRRYFRQPHLRAETKlgQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREEgeNIPSRS-----GRYWVL 90
Cdd:PRK10931 7 QLARNAGDaIMQVYDGTKPLDVASK--ADDSPVTAADIAAHTVIKDGLRTLTPDIPVLSEE--DPPAWEvrqhwQRYWLV 82
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 501596824 91 DPIDGTSSFVKGLPIFGTLIGLVdlEQNLPLLGVVNQPILQQRWLGIRGK 140
Cdd:PRK10931 83 DPLDGTKEFIKRNGEFTVNIALI--EQGKPVLGVVYAPVMNVMYSAAEGK 130
|
|
| IPPase |
cd01640 |
IPPase; Inositol polyphosphate-1-phosphatase, a member of the Mg++ dependent family of ... |
12-248 |
4.04e-07 |
|
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: 50.01 E-value: 4.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 12 INLAEQladiSGEIIRRYFRQPHLRAETKLGQ----VSSIVTIADQQAEEAMVKMILTHAPDDGIIREEG---------- 77
Cdd:cd01640 6 LAVAEK----AGGIARDVVKKGRLLILLVEGKtkegANDFKTLADRLSQRVIKHSLQKQFPKLKIIGEEDnefenqedes 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 78 ------------------ENIPSRSGRYWVlDPIDGTSSFVKG-LPIFGTLIGLVdlEQNLPLLGVVNQPIL-QQRWLGI 137
Cdd:cd01640 82 rdvdldeeileescpspsKDLPEEDLGVWV-DPLDATQEYTEGlLEYVTVLIGVA--VKGKPIAGVIHQPFYeKTAGAGA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 138 RGKPTYYNhqpVVNPYA-NDDQSKLEDAcltsttPLMFITDRQQQIAKKLQQIcvrTAFGGDCYNYVALAsGWCAMPMII 216
Cdd:cd01640 159 WLGRTIWG---LSGLGAhSSDFKEREDA------GKIIVSTSHSHSVKEVQLI---TAGNKDEVLRAGGA-GYKVLQVLE 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 501596824 217 LEADLNFY--------DFCAIIPIIQGAGGIITDWSGNTL 248
Cdd:cd01640 226 GLADAYVHstggikkwDICAPEAILRALGGDMTDLHGEPL 265
|
|
| Arch_FBPase_2 |
cd01642 |
Putative fructose-1,6-bisphosphatase or related enzymes of inositol monophosphatase family. ... |
21-118 |
2.66e-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: 47.44 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 21 ISGEIIRRYFRQPHLRAETKLGQVSSIVTI-ADQQAEEAMVKMiLTHAPDDG-IIREEGENIPSRSGRY-WVLDPIDGTS 97
Cdd:cd01642 8 ITKEIILLLNEKNRQGLVKLIRGAGGDVTRvADLKAEEIILKL-LREEGVFGqIISEESGEIRKGSGEYiAVLDPLDGST 86
|
90 100
....*....|....*....|.
gi 501596824 98 SFVKGLPIFGTLIGLVDLEQN 118
Cdd:cd01642 87 NYLSGIPFYSVSVALADPRSK 107
|
|
| bisphos_HAL2 |
TIGR01330 |
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into ... |
8-130 |
5.31e-06 |
|
3'(2'),5'-bisphosphate nucleotidase, HAL2 family; Sulfate is incorporated into 3-phosphoadenylylsulfate, PAPS, for utilization in pathways such as methionine biosynthesis. Transfer of sulfate from PAPS to an acceptor leaves adenosine 3'-5'-bisphosphate, APS. This model describes a form found in plants of the enzyme 3'(2'),5'-bisphosphate nucleotidase, which removes the 3'-phosphate from APS to regenerate AMP and help drive the cycle. Sensitivity of this essential enzyme to sodium and other metal ions results is responsible for characterization of this enzyme as a salt tolerance protein. Some members of this family are active also as inositol 1-monophosphatase.
Pssm-ID: 273558 [Multi-domain] Cd Length: 353 Bit Score: 47.17 E-value: 5.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 8 LDQDINLAEQLADISGEIIRRYFRQPHL--RAETKLGQVSSIVTIADQQAEEAMVKMILTHAPDDGIIREE--------- 76
Cdd:TIGR01330 2 LERELDVATQAVRLASLLTKKVQSELIShkDSTVITKDDKSPVTVGDYGAQAIVINVLKSNFPDDPIVGEEdssglsead 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 77 ----------------------------------------GENIPSRSGRYWVLDPIDGTSSFVKGlPIFGTLIGLvdLE 116
Cdd:TIGR01330 82 ftlgrvnelvnetlvyaknykkddqfplksledvlqiidfGNYEGGRKGRHWVLDPIDGTKGFLRG-DQYAVCLAL--IE 158
|
170
....*....|....
gi 501596824 117 QNLPLLGVVNQPIL 130
Cdd:TIGR01330 159 NGKVVLGVIGCPNL 172
|
|
| pnk |
PRK14076 |
bifunctional NADP phosphatase/NAD kinase; |
57-248 |
1.04e-03 |
|
bifunctional NADP phosphatase/NAD kinase;
Pssm-ID: 237601 [Multi-domain] Cd Length: 569 Bit Score: 40.10 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 57 EAMVKMILTHAPDDGIIREE------GENIPsrsgRY-WVLDPIDGTSSFVKGLPIFGTLIGLVDLE-----------QN 118
Cdd:PRK14076 50 ENIAINSLEKFCSGILISEEigfkkiGKNKP----EYiFVLDPIDGTYNALKDIPIYSASIAIAKIDgfdkkikefigKN 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 119 LPL----LGVVNQPILQQRWLGIRGKPTYYNHQPVVNPYANDDQSKLEDACLT------STTPLMFITDRqqqiakKLQQ 188
Cdd:PRK14076 126 LTIndleVGVVKNIATGDTYYAEKGEGAYLLKKGEKKKIEISNISNLKDASIGlfayglSLDTLKFIKDR------KVRR 199
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 501596824 189 ICVrtaFGGD----CYnyvaLASGwcampmiILEADLN------FYDFCAIIPIIQGAGGIITDWSGNTL 248
Cdd:PRK14076 200 IRL---FGSIalemCY----VASG-------ALDAFINvnettrLCDIAAGYVICKEAGGIITNKNGKPL 255
|
|
| |
