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Conserved domains on  [gi|1958698200|ref|XP_038951270|]
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fructose-1,6-bisphosphatase 1 isoform X1 [Rattus norvegicus]

Protein Classification

fructose-1,6-bisphosphatase (domain architecture ID 10086071)

class 1 fructose-1,6-bisphosphatase I catalyzes the conversion of D-fructose 1,6-bisphosphate to D-fructose 6-phosphate in gluconeogenesis and the Calvin cycle, which are both anabolic pathways

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
1-248 3.14e-156

Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle).


:

Pssm-ID: 238214  Cd Length: 315  Bit Score: 437.75  E-value: 3.14e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAG 80
Cdd:cd00354    68 ALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  81 YALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGAR 160
Cdd:cd00354   148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLR 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 161 YVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTED 240
Cdd:cd00354   228 YIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEE 307

                  ....*...
gi 1958698200 241 VQEFLEIY 248
Cdd:cd00354   308 VERVEEYL 315
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
1-248 3.14e-156

Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle).


Pssm-ID: 238214  Cd Length: 315  Bit Score: 437.75  E-value: 3.14e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAG 80
Cdd:cd00354    68 ALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  81 YALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGAR 160
Cdd:cd00354   148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLR 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 161 YVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTED 240
Cdd:cd00354   228 YIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEE 307

                  ....*...
gi 1958698200 241 VQEFLEIY 248
Cdd:cd00354   308 VERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-254 1.80e-131

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 376.07  E-value: 1.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAG 80
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  81 YALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGAR 160
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 161 YVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTED 240
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326
                         250
                  ....*....|....
gi 1958698200 241 VQEFLEIYNKDKAK 254
Cdd:PLN02262  327 VEEIKALYAAEAAK 340
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
2-250 1.10e-114

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 223236  Cd Length: 326  Bit Score: 332.74  E-value: 1.10e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   2 LKSSYATCVLVSEEDTHAIIIEPEKrGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSAnEPSEKDALQPGRNLVAAGY 81
Cdd:COG0158    77 LKARGNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGS-PGTEEDFLQPGNKQVAAGY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  82 ALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYI---QRKKfpPDNSAPYG 158
Cdd:COG0158   155 VVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIkdcFAED--KGTRRPYN 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 159 ARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGST 238
Cdd:COG0158   233 MRYIGSMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSK 312
                         250
                  ....*....|..
gi 1958698200 239 EDVQEFLEIYNK 250
Cdd:COG0158   313 EEVEKLERFIKE 324
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
122-249 4.83e-64

Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of Fructose-1-6-bisphosphatase enzymes. According to ECOD this domain has a Rossmann-like fold.


Pssm-ID: 408683 [Multi-domain]  Cd Length: 125  Bit Score: 196.68  E-value: 4.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 122 KGNIYSINEGYAKDFDPAINEYIQRKKFPPdnsAPYGARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPI 201
Cdd:pfam18913   1 EGKIYAINEGNARHWNAPYRAYIDDLKSGG---KGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958698200 202 AYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTEDVQEFLEIYN 249
Cdd:pfam18913  78 AFLIEQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYLK 125
 
Name Accession Description Interval E-value
FBPase cd00354
Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1, ...
1-248 3.14e-156

Fructose-1,6-bisphosphatase, an enzyme that catalyzes the hydrolysis of fructose-1,6-biphosphate into fructose-6-phosphate and is critical in gluconeogenesis pathway. The alignment model also includes chloroplastic FBPases and sedoheptulose-1,7-biphosphatases that play a role in pentose phosphate pathway (Calvin cycle).


Pssm-ID: 238214  Cd Length: 315  Bit Score: 437.75  E-value: 3.14e-156
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAG 80
Cdd:cd00354    68 ALKSSGVVAVLASEEEEEPVPVEESKDGKYLVAFDPLDGSSNIDANVSVGTIFSIYPGPSGADATEKDFLQPGRNQVAAG 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  81 YALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGAR 160
Cdd:cd00354   148 YALYGPSTMLVLTLGQGVHGFTLDPSLGEFILTHPNVKIPKKGKIYSINEGNYRYWDEPVKKYIDDCKAGEDGGKPYNLR 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 161 YVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTED 240
Cdd:cd00354   228 YIGSMVADVHRILVRGGIFLYPADKKSPKGKLRLLYEANPMAFLVEQAGGKATDGKERILDIVPTSLHQRVPVILGSKEE 307

                  ....*...
gi 1958698200 241 VQEFLEIY 248
Cdd:cd00354   308 VERVEEYL 315
PLN02262 PLN02262
fructose-1,6-bisphosphatase
1-254 1.80e-131

fructose-1,6-bisphosphatase


Pssm-ID: 215147  Cd Length: 340  Bit Score: 376.07  E-value: 1.80e-131
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAG 80
Cdd:PLN02262   87 ALVSSGRTNVLVSEEDEEAIFVEPSKRGRYCVVFDPLDGSSNIDCGVSIGTIFGIYMLKDGGEGTVEDVLQPGKEMVAAG 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  81 YALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQRKKFPPDNSAPYGAR 160
Cdd:PLN02262  167 YCMYGSSCTLVLSTGGGVNGFTLDPSLGEFILTHPDIKIPKKGKIYSVNEGNAKNWDGPTAKYVEKCKFPKDGSSPKSLR 246
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 161 YVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTED 240
Cdd:PLN02262  247 YIGSMVADVHRTLLYGGIFLYPADKKSPNGKLRVLYEVFPMSFLVEQAGGQAFTGKQRALDLVPTKIHERSPIFLGSYDD 326
                         250
                  ....*....|....
gi 1958698200 241 VQEFLEIYNKDKAK 254
Cdd:PLN02262  327 VEEIKALYAAEAAK 340
PRK09293 PRK09293
class 1 fructose-bisphosphatase;
2-252 9.85e-127

class 1 fructose-bisphosphatase;


Pssm-ID: 236458  Cd Length: 327  Bit Score: 363.40  E-value: 9.85e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   2 LKSSYATCVLVSEEDTHAIIIePEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSaNEPSEKDALQPGRNLVAAGY 81
Cdd:PRK09293   78 LKARGHVAGLASEEEDEIVPI-PENEGKYLVAYDPLDGSSNIDVNVSVGTIFSIYRAPV-GTPTEEDFLQPGNNQVAAGY 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  82 ALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYI---QRKKFPPDnsAPYG 158
Cdd:PRK09293  156 VLYGPSTMLVLTTGDGVHGFTLDPSLGEFVLTHENIRIPEDGKEYAINEGNQRHWEPGVKKYIellAGKDGPRG--RPYN 233
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 159 ARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGST 238
Cdd:PRK09293  234 MRYIGSMVADVHRILLKGGIFLYPADEPYPNGKLRLLYEANPMAFLVEQAGGAASDGKQRILDIEPESLHQRVPLFLGSK 313
                         250
                  ....*....|....
gi 1958698200 239 EDVQEFLEIYNKDK 252
Cdd:PRK09293  314 EEVERVEEYHAEAP 327
Fbp COG0158
Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];
2-250 1.10e-114

Fructose-1,6-bisphosphatase [Carbohydrate transport and metabolism];


Pssm-ID: 223236  Cd Length: 326  Bit Score: 332.74  E-value: 1.10e-114
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   2 LKSSYATCVLVSEEDTHAIIIEPEKrGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSAnEPSEKDALQPGRNLVAAGY 81
Cdd:COG0158    77 LKARGNVAGIASEEEDEPVTFPENN-GSYAVAYDPLDGSSNIDVNVSVGTIFSIYRRPGS-PGTEEDFLQPGNKQVAAGY 154
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  82 ALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYI---QRKKfpPDNSAPYG 158
Cdd:COG0158   155 VVYGPSTMLVYTLGEGVHGFTLDPSLGEFILTHENIRIPEKGKIYAINEGNQRHWEEGVKKYIkdcFAED--KGTRRPYN 232
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 159 ARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGST 238
Cdd:COG0158   233 MRYIGSMVADVHRILLKGGIFLYPSDKRAPNGKLRLLYEANPMAFLVEQAGGKATDGKQRILDIVPEKLHQRVPLFLGSK 312
                         250
                  ....*....|..
gi 1958698200 239 EDVQEFLEIYNK 250
Cdd:COG0158   313 EEVEKLERFIKE 324
PLN02542 PLN02542
fructose-1,6-bisphosphatase
2-248 3.64e-81

fructose-1,6-bisphosphatase


Pssm-ID: 215298  Cd Length: 412  Bit Score: 250.18  E-value: 3.64e-81
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   2 LKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYrktSANEPSEKD------------- 68
Cdd:PLN02542  151 LRSSGRTGIIASEEEDVPVAVEESYSGNYIVVFDPLDGSSNIDAAVSTGSIFGIY---SPNDECLADigddstldsveqr 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  69 ----ALQPGRNLVAAGYALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYI 144
Cdd:PLN02542  228 civnVCQPGSNLLAAGYCMYSSSVIFVLTIGTGVFSFTLDPMYGEFVLTQENIQIPKAGKIYSFNEGNYQLWDDKLKKYI 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 145 QRKKFPPDNSAPYGARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVP 224
Cdd:PLN02542  308 DDLKDPGPSGKPYSARYIGSLVGDFHRTLLYGGIYGYPRDKKSKNGKLRLLYECAPMSFIVEQAGGKGSDGHQRILDIQP 387
                         250       260
                  ....*....|....*....|....
gi 1958698200 225 TEIHQKAPVIMGSTEDVqEFLEIY 248
Cdd:PLN02542  388 TEIHQRVPLYIGSVEEV-EKLEKY 410
PLN02628 PLN02628
fructose-1,6-bisphosphatase family protein
2-257 2.31e-77

fructose-1,6-bisphosphatase family protein


Pssm-ID: 215337  Cd Length: 351  Bit Score: 238.54  E-value: 2.31e-77
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   2 LKSSYATCVLVSEEDTHAIIIEPEkrGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANE--PSEKDA----LQPGRN 75
Cdd:PLN02628   94 LRNSGKVAVMASEEDDAPIWIGDD--GPYVVVFDPLDGSRNIDASIPTGTIFGIYNRLVEADhlPVEEKAqlnvLQRGSR 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  76 LVAAGYALYGSATMLVLAMNCGVNCFMLDPSIGEFILVDRDVKIKKKGNIYSINEGYAKDFDPAINEYIQR-KKFPPDNS 154
Cdd:PLN02628  172 LVAAGYVLYSSATILCISFGSGTHGFTLDHSTGEFVLTHPDIKIPERGQIYSVNDARYFDWPEGLRKYIDTvRQGKGQYP 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 155 APYGARYVGSMVADVHRTLVYGGIFLypankkNPSGKLRLLYECNPIAYVMEKAGGLATTGNEDILDIVPTEIHQKAPVI 234
Cdd:PLN02628  252 KKYSARYICSLVADLHRTILYGGIAM------NPRSHLRLVYEANPLSFLVEQAGGRGSDGKRRILSIQPVKLHQRLPLF 325
                         250       260
                  ....*....|....*....|...
gi 1958698200 235 MGSTEDVQEfLEIYNKDKAKSRP 257
Cdd:PLN02628  326 LGSSEDVLE-LESYGDVQQKVNP 347
FBPase_C pfam18913
Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of ...
122-249 4.83e-64

Fructose-1-6-bisphosphatase, C-terminal domain; This entry represents the C-terminal domain of Fructose-1-6-bisphosphatase enzymes. According to ECOD this domain has a Rossmann-like fold.


Pssm-ID: 408683 [Multi-domain]  Cd Length: 125  Bit Score: 196.68  E-value: 4.83e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 122 KGNIYSINEGYAKDFDPAINEYIQRKKFPPdnsAPYGARYVGSMVADVHRTLVYGGIFLYPANKKNPSGKLRLLYECNPI 201
Cdd:pfam18913   1 EGKIYAINEGNARHWNAPYRAYIDDLKSGG---KGYTLRYVGSMVADVHRILLKGGIFLYPADKRAPNGKLRLLYECAPL 77
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1958698200 202 AYVMEKAGGLATTGNEDILDIVPTEIHQKAPVIMGSTEDVQEFLEIYN 249
Cdd:pfam18913  78 AFLIEQAGGKASDGKQRILDIVPDSLHQRTPIFLGSREEVERVEAYLK 125
FBPase pfam00316
Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this ...
1-114 1.05e-63

Fructose-1-6-bisphosphatase, N-terminal domain; This family represents the N-terminus of this protein family.


Pssm-ID: 395249  Cd Length: 189  Bit Score: 198.02  E-value: 1.05e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYRKTSANEPSEKDALQPGRNLVAAG 80
Cdd:pfam00316  75 ALKASGIVAVLVSEEEEELIVFEGNKRGKYVVAFDPLDGSSNIDTNVSVGTIFSIYRRVSTDSPTTIDFLQPGNEQVAAG 154
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1958698200  81 YALYGSATMLVLAMNCGVNCFMLDPSIGEFILVD 114
Cdd:pfam00316 155 YVVYGSSTMLVLTTGCGVHGFTLDPSLGEFILTH 188
PLN02462 PLN02462
sedoheptulose-1,7-bisphosphatase
2-246 3.54e-38

sedoheptulose-1,7-bisphosphatase


Pssm-ID: 215256  Cd Length: 304  Bit Score: 136.01  E-value: 3.54e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   2 LKSSYATCVLVSEEDTHAIIIEPEKRGKYVVCFDPLDGSSNIDCLASIGTIFGIYrktsanePSEKDALQPGRNLVAAGY 81
Cdd:PLN02462   66 LKYSHVCKYACSEEVPEVQDMGGPVEGGFSVAFDPLDGSSIVDTNFAVGTIFGVW-------PGDKLTGVTGRDQVAAAM 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  82 ALYGSATMLVLAMNCGVNCFmldpsigEFILVDRDVKIKKKGNIySINEGyaKDFDPA--------------INEYIQRK 147
Cdd:PLN02462  139 GIYGPRTTYVVALKDGPGTH-------EFLLLDDGKWQHVKETT-EIGEG--KIFSPGnlratfdnpgyeklINYYVSEK 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200 148 kfppdnsapYGARYVGSMVADVHRTLVY-GGIFLYPANKKNPSgKLRLLYECNPIAYVMEKAGGLATTGNED--ILDIVP 224
Cdd:PLN02462  209 ---------YTLRYTGGMVPDVYQIIVKeKGVFTNVTSPKSKA-KLRLLFEVAPLGLLVEKAGGKSSDGVQGgsVLDKQI 278
                         250       260
                  ....*....|....*....|..
gi 1958698200 225 TEIHQKAPVIMGSTEDVQEFLE 246
Cdd:PLN02462  279 NNLDQRTQVAYGSKNEVIRFEE 300
FIG cd01636
FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with ...
1-215 1.53e-23

FIG, FBPase/IMPase/glpX-like domain. A superfamily of metal-dependent phosphatases with various substrates. Fructose-1,6-bisphospatase (both the major and the glpX-encoded variant) hydrolyze fructose-1,6,-bisphosphate to fructose-6-phosphate in gluconeogenesis. Inositol-monophosphatases and inositol polyphosphatases play vital roles in eukaryotic signalling, as they participate in metabolizing the messenger molecule Inositol-1,4,5-triphosphate. Many of these enzymes are inhibited by Li+.


Pssm-ID: 238814 [Multi-domain]  Cd Length: 184  Bit Score: 94.38  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIIEpEKRGKYVVCFDPLDGSSNID-CLASIGTIFGIYRKTSANEPSEkdalqpgrnlvaa 79
Cdd:cd01636    51 MLKSSFPDVKIVGEESGVAEEVM-GRRDEYTWVIDPIDGTKNFInGLPFVAVVIAVYVILILAEPSH------------- 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  80 gyalygsatmlvlamncgvncfmldpsigefilvdrdvkikkkgniysinegyaKDFDPaineyiqrKKFPPDNSAPYGA 159
Cdd:cd01636   117 ------------------------------------------------------KRVDE--------KKAELQLLAVYRI 134
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958698200 160 RYVGSMVADVHRTLV-YGGIFLYPANKKNPsgklrllYECNPIAYVMEKAGGLATTG 215
Cdd:cd01636   135 RIVGSAVAKMCLVALgLADIYYEPGGKRRA-------WDVAASAAIVREAGGIMTDW 184
IMPase_like cd01637
Inositol-monophosphatase-like domains. This family of phosphatases is dependent on bivalent ...
1-223 1.24e-14

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: 71.19  E-value: 1.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200   1 MLKSSYATCVLVSEEDTHAIIiepEKRGKYVVCFDPLDGSSN-IDCLASIGTIFGIYRKtsaNEPsekdalqpgrnlVAA 79
Cdd:cd01637    49 VLKALFPDDGILGEEGGGSGN---VSDGGRVWVIDPIDGTTNfVAGLPNFAVSIALYED---GKP------------VLG 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958698200  80 GYALYGsATMLVLAM-NCGVNCFMLDPSIgefilvdrdVKIKKKGNIYSINEGYAKDFDPAineyiqrKKFPPDNSAPYG 158
Cdd:cd01637   111 VIYDPM-LDELYYAGrGKGAFLNGKKLPL---------SKDTPLNDALLSTNASMLRSNRA-------AVLASLVNRALG 173
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958698200 159 ARYVGSMVADVHRTLVY-GGIFLYPANKknpsgklrlLYECNPIAYVMEKAGGLATTGNEDILDIV 223
Cdd:cd01637   174 IRIYGSAGLDLAYVAAGrLDAYLSSGLN---------PWDYAAGALIVEEAGGIVTDLDGEPLDTL 230
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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