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Conserved domains on  [gi|1519643992|gb|RPG16072|]
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MAG: adenosine kinase [Opitutales bacterium TMED207]

Protein Classification

adenosine kinase( domain architecture ID 10100220)

adenosine kinase catalyzes the phosphorylation of adenosine or other ribofuranosyl-containing nucleoside analogs at the 5'-hydroxyl using ATP or GTP as the phosphate donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 1-309 4.13e-84

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


:

Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 256.39  E-value: 4.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   1 MKRIIGLGSPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEINqeLVQITGGSAGNTIFALARLGIQTSFIGKI 80
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILADMEEQEELLAKLP--VKYIAGGSAANTIRGAAALGGSAAFIGRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  81 GNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHLHIEGFLI-L 159
Cdd:cd01168    79 GDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYLLtV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 160 NKDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILkNHVDMVFANEDEAAAFTQLPPAQS-EESVKILNELCETA 238
Cdd:cd01168   159 PPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELL-PYVDILFGNEEEAEALAEAETTDDlEAALKLLALRCRIV 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519643992 239 VVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:cd01168   238 VITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
 
Name Accession Description Interval E-value
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 1-309 4.13e-84

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 256.39  E-value: 4.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   1 MKRIIGLGSPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEINqeLVQITGGSAGNTIFALARLGIQTSFIGKI 80
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILADMEEQEELLAKLP--VKYIAGGSAANTIRGAAALGGSAAFIGRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  81 GNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHLHIEGFLI-L 159
Cdd:cd01168    79 GDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYLLtV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 160 NKDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILkNHVDMVFANEDEAAAFTQLPPAQS-EESVKILNELCETA 238
Cdd:cd01168   159 PPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELL-PYVDILFGNEEEAEALAEAETTDDlEAALKLLALRCRIV 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519643992 239 VVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:cd01168   238 VITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 3-320 2.13e-68

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 215.90  E-value: 2.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   3 RIIGLGSPIIDEIAFVDdafleniSGSKGGMELLAESelesikseinqeLVQITGGSAGNTIFALARLGIQTSFIGKIGN 82
Cdd:COG0524     1 DVLVIGEALVDLVARVD-------RLPKGGETVLAGS------------FRRSPGGAAANVAVALARLGARVALVGAVGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  83 CASGDFYKESLAQ*GGSTQSFKI-GNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHLHIEGFLILN- 160
Cdd:COG0524    62 DPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASe 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 161 --KDVLHKSLDLAKSNNLTVSFDLAS-FEIVNQSKSELKEILKnHVDMVFANEDEAAAFTQLPPAqsEESVKILNEL-CE 236
Cdd:COG0524   142 ppREALLAALEAARAAGVPVSLDPNYrPALWEPARELLRELLA-LVDILFPNEEEAELLTGETDP--EEAAAALLARgVK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 237 TAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG*ALSHRQ 316
Cdd:COG0524   219 LVVVTLGAEGALLYTGGEVVHVPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297


                  ....
gi 1519643992 317 WDDI 320
Cdd:COG0524   298 REEV 301
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 4-325 7.25e-63

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 203.87  E-value: 7.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   4 IIGLG-SPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEINQ----------ELVQITGGSAGNTIFALAR-LG 71
Cdd:PLN02379   22 VLGLQpVALVDHVARVDWSLLDQIPGDRGGSIRVTIEELEHILREVNAhilpspddlsPIKTMAGGSVANTIRGLSAgFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  72 IQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHL 151
Cdd:PLN02379  102 VSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLVDALGNRTMRPCLSSAVKLQADELTKEDFKGSKWL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 152 hIEGFLILNKDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILKN-HVDMVFANEDEAAAFTQLPP-AQSEESVK 229
Cdd:PLN02379  182 -VLRYGFYNLEVIEAAIRLAKQEGLSVSLDLASFEMVRNFRSPLLQLLESgKIDLCFANEDEARELLRGEQeSDPEAALE 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 230 ILNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:PLN02379  261 FLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340

                         330
                  ....*....|....*.
gi 1519643992 310 *ALSHRQWDDILKSIQ 325
Cdd:PLN02379  341 GEVTPENWQWMYKQMQ 356
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 50-309 1.93e-51

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 171.76  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  50 QELVQITGGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKI-GNIPNGKCLSLVTPDGQRTMRTS 128
Cdd:pfam00294  27 STVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIdEDTRTGTALIEVDGDGERTIVFN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 129 LGAA--MTLAEDELNP*DFQDYDHLHIEGFLI--LNKDVLHKSLDLAKSNNLtvsFDLASFEIVNQSKSELKEILkNHVD 204
Cdd:pfam00294 107 RGAAadLTPEELEENEDLLENADLLYISGSLPlgLPEATLEELIEAAKNGGT---FDPNLLDPLGAAREALLELL-PLAD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 205 MVFANEDEAAAFTQLPPAQSEESVKILNELC----ETAVVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGF 280
Cdd:pfam00294 183 LLKPNEEELEALTGAKLDDIEEALAALHKLLakgiKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGF 262

                         250       260
                  ....*....|....*....|....*....
gi 1519643992 281 LHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:pfam00294 263 LAGLLAGKSLEEALRFANAAAALVVQKSG 291
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 50-309 3.34e-28

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 110.77  E-value: 3.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  50 QELVQITGGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQS-FKIGNIPNGKCLSLVTPDGQRTMRTS 128
Cdd:TIGR02152  24 HSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYvGTVKDTPTGTAFITVDDTGENRIVVV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 129 LGAAMtlaedELNP*DFQDYDHLHIEG-FLILNKDVLHKS----LDLAKSNNLTVSFDLASfeivnqSKSELKEILKNHV 203
Cdd:TIGR02152 104 AGANA-----ELTPEDIDAAEALIAESdIVLLQLEIPLETvleaAKIAKKHGVKVILNPAP------AIKDLDDELLSLV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 204 DMVFANEDEAAAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTTGAGDFWAAG 279
Cdd:TIGR02152 173 DIITPNETEAEILTGIEVTDEEDAEKAAEKLlekgVKNVIITLGSKGALLVSKDESKLIPAFKVK-AVDTTAAGDTFNGA 251

                         250       260       270
                  ....*....|....*....|....*....|
gi 1519643992 280 FLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:TIGR02152 252 FAVALAEGKSLEDAIRFANAAAAISVTRKG 281
 
Name Accession Description Interval E-value
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 1-309 4.13e-84

Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.


Pssm-ID: 238573 [Multi-domain]  Cd Length: 312  Bit Score: 256.39  E-value: 4.13e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   1 MKRIIGLGSPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEINqeLVQITGGSAGNTIFALARLGIQTSFIGKI 80
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILADMEEQEELLAKLP--VKYIAGGSAANTIRGAAALGGSAAFIGRV 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  81 GNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHLHIEGFLI-L 159
Cdd:cd01168    79 GDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYLLtV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 160 NKDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILkNHVDMVFANEDEAAAFTQLPPAQS-EESVKILNELCETA 238
Cdd:cd01168   159 PPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELL-PYVDILFGNEEEAEALAEAETTDDlEAALKLLALRCRIV 237

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1519643992 239 VVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:cd01168   238 VITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLG 308
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 3-320 2.13e-68

Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis


Pssm-ID: 440290 [Multi-domain]  Cd Length: 301  Bit Score: 215.90  E-value: 2.13e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   3 RIIGLGSPIIDEIAFVDdafleniSGSKGGMELLAESelesikseinqeLVQITGGSAGNTIFALARLGIQTSFIGKIGN 82
Cdd:COG0524     1 DVLVIGEALVDLVARVD-------RLPKGGETVLAGS------------FRRSPGGAAANVAVALARLGARVALVGAVGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  83 CASGDFYKESLAQ*GGSTQSFKI-GNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHLHIEGFLILN- 160
Cdd:COG0524    62 DPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASe 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 161 --KDVLHKSLDLAKSNNLTVSFDLAS-FEIVNQSKSELKEILKnHVDMVFANEDEAAAFTQLPPAqsEESVKILNEL-CE 236
Cdd:COG0524   142 ppREALLAALEAARAAGVPVSLDPNYrPALWEPARELLRELLA-LVDILFPNEEEAELLTGETDP--EEAAAALLARgVK 218

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 237 TAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG*ALSHRQ 316
Cdd:COG0524   219 LVVVTLGAEGALLYTGGEVVHVPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297


                  ....
gi 1519643992 317 WDDI 320
Cdd:COG0524   298 REEV 301
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 4-325 7.25e-63

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 203.87  E-value: 7.25e-63
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   4 IIGLG-SPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEINQ----------ELVQITGGSAGNTIFALAR-LG 71
Cdd:PLN02379   22 VLGLQpVALVDHVARVDWSLLDQIPGDRGGSIRVTIEELEHILREVNAhilpspddlsPIKTMAGGSVANTIRGLSAgFG 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  72 IQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHL 151
Cdd:PLN02379  102 VSTGIIGACGDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLVDALGNRTMRPCLSSAVKLQADELTKEDFKGSKWL 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 152 hIEGFLILNKDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILKN-HVDMVFANEDEAAAFTQLPP-AQSEESVK 229
Cdd:PLN02379  182 -VLRYGFYNLEVIEAAIRLAKQEGLSVSLDLASFEMVRNFRSPLLQLLESgKIDLCFANEDEARELLRGEQeSDPEAALE 260

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 230 ILNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:PLN02379  261 FLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340

                         330
                  ....*....|....*.
gi 1519643992 310 *ALSHRQWDDILKSIQ 325
Cdd:PLN02379  341 GEVTPENWQWMYKQMQ 356
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 50-309 1.93e-51

pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 171.76  E-value: 1.93e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  50 QELVQITGGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKI-GNIPNGKCLSLVTPDGQRTMRTS 128
Cdd:pfam00294  27 STVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIdEDTRTGTALIEVDGDGERTIVFN 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 129 LGAA--MTLAEDELNP*DFQDYDHLHIEGFLI--LNKDVLHKSLDLAKSNNLtvsFDLASFEIVNQSKSELKEILkNHVD 204
Cdd:pfam00294 107 RGAAadLTPEELEENEDLLENADLLYISGSLPlgLPEATLEELIEAAKNGGT---FDPNLLDPLGAAREALLELL-PLAD 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 205 MVFANEDEAAAFTQLPPAQSEESVKILNELC----ETAVVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGF 280
Cdd:pfam00294 183 LLKPNEEELEALTGAKLDDIEEALAALHKLLakgiKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGF 262

                         250       260
                  ....*....|....*....|....*....
gi 1519643992 281 LHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:pfam00294 263 LAGLLAGKSLEEALRFANAAAALVVQKSG 291
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 57-309 1.09e-50

Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238917 [Multi-domain]  Cd Length: 279  Bit Score: 169.41  E-value: 1.09e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFK-IGNIPNGKCLSLVTPDGQRTMRTSLGAAMTL 135
Cdd:cd01942    36 GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRvVDEDSTGVAFILTDGDDNQIAYFYPGAMDEL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 136 AEDELNP*DFqDYDHLHIEGF--LILNKDVLHKsldlaksNNLTVSFDLASfEIVNQSKSELKEILkNHVDMVFANEDEA 213
Cdd:cd01942   116 EPNDEADPDG-LADIVHLSSGpgLIELARELAA-------GGITVSFDPGQ-ELPRLSGEELEEIL-ERADILFVNDYEA 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 214 AAFTQLppaqSEESVKILNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDS 293
Cdd:cd01942   186 ELLKER----TGLSEAELASGVRVVVVTLGPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEES 261

                         250
                  ....*....|....*.
gi 1519643992 294 AQLGALMGASVIQNHG 309
Cdd:cd01942   262 LRLGNLAASLKVERRG 277
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 57-309 2.10e-48

2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.


Pssm-ID: 238571 [Multi-domain]  Cd Length: 294  Bit Score: 163.90  E-value: 2.10e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFK-IGNIPNGKCLSLVTPDGQRTM----RTSlgA 131
Cdd:cd01166    31 GGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRvDPGRPTGLYFLEIGAGGERRVlyyrAGS--A 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 132 AMTLAEDELNP*DFQDYDHLHIEG--FLIL--NKDVLHKSLDLAKSNNLTVSFDL---ASFEIVNQSKSELKEILKnHVD 204
Cdd:cd01166   109 ASRLTPEDLDEAALAGADHLHLSGitLALSesAREALLEALEAAKARGVTVSFDLnyrPKLWSAEEAREALEELLP-YVD 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 205 MVFANEDEAAAFTQL-PPAQSEESVKILNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHG 283
Cdd:cd01166   188 IVLPSEEEAEALLGDeDPTDAAERALALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPV-EVVDTTGAGDAFAAGFLAG 266

                         250       260
                  ....*....|....*....|....*.
gi 1519643992 284 WANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:cd01166   267 LLEGWDLEEALRFANAAAALVVTRPG 292
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 4-324 1.43e-39

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 144.18  E-value: 1.43e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   4 IIGLGSPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEINQELVQIT-GGSAGNTIFALARLGIQTS------- 75
Cdd:PLN02813   72 VLGLGQAMVDFSGMVDDEFLERLGLEKGTRKVINHEERGKVLRALDGCSYKASaGGSLSNTLVALARLGSQSAagpalnv 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  76 -FIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DFQDYDHLHIE 154
Cdd:PLN02813  152 aMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVLVVE 231

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 155 GFLILNKDV---LHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILKNHVDMVFANEDEAAAFTQLPPAQSEESV-KI 230
Cdd:PLN02813  232 GYLWELPQTieaIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGNYADILFANSDEARALCGLGSEESPESAtRY 311

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 231 LNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVKEViDTTGAGDFWAAGFLHGWANNQS-IEDSAQLGALMGASVIQNHG 309
Cdd:PLN02813  312 LSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPV-DTCGAGDAYAAGILYGLLRGVSdLRGMGELAARVAATVVGQQG 390

                         330
                  ....*....|....*
gi 1519643992 310 *ALSHRQWDDILKSI 324
Cdd:PLN02813  391 TRLRVEDAVELAESF 405
PTZ00247 PTZ00247
adenosine kinase; Provisional
 2-309 9.00e-31

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 118.59  E-value: 9.00e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   2 KRIIGLGSPIIDEIAFVDDAFLENIsGSKGGMELLAESELESIKSEI--NQELVQITGGSAGNTifalARLG-------- 71
Cdd:PTZ00247    6 KKLLGFGNPLLDISAHVSDEFLEKY-GLELGSAILAEEKQLPIFEELesIPNVSYVPGGSALNT----ARVAqwmlqapk 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  72 IQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTpDGQRTMRTSLGAAMTLAEDELNP*DFQDY--- 148
Cdd:PTZ00247   81 GFVCYVGCVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVC-GKERSLVANLGAANHLSAEHMQSHAVQEAikt 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 149 -DHLHIEGFLiLNKDVLH--KSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILKnHVDMVFANEDEAAAFTQ---LPPA 222
Cdd:PTZ00247  160 aQLYYLEGFF-LTVSPNNvlQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLP-YVDILFGNEEEAKTFAKamkWDTE 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 223 QSEESV-KILNELCET------AVVKLGAQGSLIAKD*TIIHSEAIPV--KEVIDTTGAGDFWAAGFLHGWANNQSIEDS 293
Cdd:PTZ00247  238 DLKEIAaRIAMLPKYSgtrprlVVFTQGPEPTLIATKDGVTSVPVPPLdqEKIVDTNGAGDAFVGGFLAQYANGKDIDRC 317

                         330
                  ....*....|....*.
gi 1519643992 294 AQLGALMGASVIQNHG 309
Cdd:PTZ00247  318 VEAGHYSAQVIIQHNG 333
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 66-313 1.02e-30

Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.


Pssm-ID: 238579 [Multi-domain]  Cd Length: 292  Bit Score: 117.27  E-value: 1.02e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  66 ALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQS-FKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*- 143
Cdd:cd01174    45 AAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYvEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAAl 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 144 -DFQDYDhlhiegFLIL----NKDVLHKSLDLAKSNNLTVSFDLASFeivnqsKSELKEILKnHVDMVFANEDEAAAFTQ 218
Cdd:cd01174   125 eLIAAAD------VLLLqleiPLETVLAALRAARRAGVTVILNPAPA------RPLPAELLA-LVDILVPNETEAALLTG 191

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 219 LP---PAQSEESVKILNEL-CETAVVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTTGAGDFWAAGFLHGWANNQSIEDSA 294
Cdd:cd01174   192 IEvtdEEDAEKAARLLLAKgVKNVIVTLGAKGALLASGGEVEHVPAFKVK-AVDTTGAGDTFIGALAAALARGLSLEEAI 270

                         250
                  ....*....|....*....
gi 1519643992 295 QLGALMGASVIQNHG*ALS 313
Cdd:cd01174   271 RFANAAAALSVTRPGAQPS 289
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 50-309 3.34e-28

ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]


Pssm-ID: 274000 [Multi-domain]  Cd Length: 293  Bit Score: 110.77  E-value: 3.34e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  50 QELVQITGGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQS-FKIGNIPNGKCLSLVTPDGQRTMRTS 128
Cdd:TIGR02152  24 HSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYvGTVKDTPTGTAFITVDDTGENRIVVV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 129 LGAAMtlaedELNP*DFQDYDHLHIEG-FLILNKDVLHKS----LDLAKSNNLTVSFDLASfeivnqSKSELKEILKNHV 203
Cdd:TIGR02152 104 AGANA-----ELTPEDIDAAEALIAESdIVLLQLEIPLETvleaAKIAKKHGVKVILNPAP------AIKDLDDELLSLV 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 204 DMVFANEDEAAAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTTGAGDFWAAG 279
Cdd:TIGR02152 173 DIITPNETEAEILTGIEVTDEEDAEKAAEKLlekgVKNVIITLGSKGALLVSKDESKLIPAFKVK-AVDTTAAGDTFNGA 251

                         250       260       270
                  ....*....|....*....|....*....|
gi 1519643992 280 FLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:TIGR02152 252 FAVALAEGKSLEDAIRFANAAAAISVTRKG 281
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 47-311 5.19e-28

5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]


Pssm-ID: 275175 [Multi-domain]  Cd Length: 309  Bit Score: 110.38  E-value: 5.19e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  47 EINQELVQIT------GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTqSFkignipngkclsLVTPD 120
Cdd:TIGR04382  18 QIGVPLEDVTsfakylGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDT-SH------------VVTDP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 121 GQRTMRTSLG----------------AAMTLAEDELNP*DFQDYdhlhieGFLILNKDVL---------HKSLDLAKSNN 175
Cdd:TIGR04382  85 GRRTSLVFLEikppdefpllfyrenaADLALTPDDVDEDYIASA------RALLVSGTALsqepsreavLKALEYARAAG 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 176 LTVSFDLaSFEIVNQSKSE-----LKEILKnHVDMVFANEDE--AAAftqlPPAQSEESVKILNELC-ETAVVKLGAQGS 247
Cdd:TIGR04382 159 VRVVLDI-DYRPYLWKSPEeagiyLRLVLP-LVDVIIGTREEfdIAG----GEGDDEAAARALLDAGvEILVVKRGPEGS 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1519643992 248 L-IAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG*A 311
Cdd:TIGR04382 233 LvYTGDGEGVEVPGFPV-EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 57-283 3.72e-23

Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 96.94  E-value: 3.72e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKI-GNIPNGkcLSLVT--PDGQRT---MRTSlg 130
Cdd:cd01167    28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFdPAAPTT--LAFVTldADGERSfefYRGP-- 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 131 AAMTLAEDELNP*DFQDYDHLHIeGFLIL----NKDVLHKSLDLAKSNNLTVSFD----LASFEIVNQSKSELKEILKnH 202
Cdd:cd01167   104 AADLLLDTELNPDLLSEADILHF-GSIALasepSRSALLELLEAAKKAGVLISFDpnlrPPLWRDEEEARERIAELLE-L 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 203 VDMVFANEDEAAAFT-QLPPAQSEESVKILNelCETAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFL 281
Cdd:cd01167   182 ADIVKLSDEELELLFgEEDPEEIAALLLLFG--LKLVLVTRGADGALLYTKGGVGEVPGIPV-EVVDTTGAGDAFVAGLL 258


                  ..
gi 1519643992 282 HG 283
Cdd:cd01167   259 AQ 260
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 58-309 1.44e-22

YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 95.18  E-value: 1.44e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  58 GSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTLAE 137
Cdd:cd01944    36 GGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDGERSFISISGAEQDWST 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 138 DELNP*DFQDYDHLHIEGFLILNK---DVLHKSLDLAKSNNLTVSFDlASFEIVNQSKSELKEILKNHVdMVFANEDEAA 214
Cdd:cd01944   116 EWFATLTVAPYDYVYLSGYTLASEnasKVILLEWLEALPAGTTLVFD-PGPRISDIPDTILQALMAKRP-IWSCNREEAA 193

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 215 AFTQ-LPPAQSEESVKILNELCETAVVKLGAQGSLI-AKD*TIIHSEAIPVKeVIDTTGAGDFWAAGFLHGWANNQSIED 292
Cdd:cd01944   194 IFAErGDPAAEASALRIYAKTAAPVVVRLGSNGAWIrLPDGNTHIIPGFKVK-AVDTIGAGDTHAGGMLAGLAKGMSLAD 272

                         250
                  ....*....|....*..
gi 1519643992 293 SAQLGALMGASVIQNHG 309
Cdd:cd01944   273 AVLLANAAAAIVVTRSG 289
PTZ00292 PTZ00292
ribokinase; Provisional
 1-320 1.59e-22

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 95.96  E-value: 1.59e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   1 MKRIIGLGSPIIDEIAFVDDAflenisgSKGGmellaeselESIKSEinqELVQITGGSAGNTIFALARLGIQTSFIGKI 80
Cdd:PTZ00292   15 EPDVVVVGSSNTDLIGYVDRM-------PQVG---------ETLHGT---SFHKGFGGKGANQAVMASKLGAKVAMVGMV 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  81 GNCASGDFYKESLAQ*GGSTQS-FKIGNIPNGKCLSLV-TPDGQRTMRTSLGAamtlaEDELNP*DFQDY--DHLHIEGF 156
Cdd:PTZ00292   76 GTDGFGSDTIKNFKRNGVNTSFvSRTENSSTGLAMIFVdTKTGNNEIVIIPGA-----NNALTPQMVDAQtdNIQNICKY 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 157 LILNKDV-LHKSLD---LAKSNNLTVSFDLASfeIVNQSKSE-LKEILKnHVDMVFANEDEAAAFTQLPPAQSEESVKIL 231
Cdd:PTZ00292  151 LICQNEIpLETTLDalkEAKERGCYTVFNPAP--APKLAEVEiIKPFLK-YVSLFCVNEVEAALITGMEVTDTESAFKAS 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 232 NEL----CETAVVKLGAQGSLIA-KD*TIIHSEAIPVKeVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQ 306
Cdd:PTZ00292  228 KELqqlgVENVIITLGANGCLIVeKENEPVHVPGKRVK-AVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVT 306

                         330
                  ....*....|....
gi 1519643992 307 NHG*ALSHRQWDDI 320
Cdd:PTZ00292  307 RHGTQSSYPHPSEL 320
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 57-309 2.03e-21

Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238922 [Multi-domain]  Cd Length: 265  Bit Score: 91.71  E-value: 2.03e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLaQ*GGSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMtla 136
Cdd:cd01947    36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL-ESGGDKHTVAWRDKPTRKTLSFIDPNGERTITVPGERLE--- 111

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 137 eDELNP*DFQDYDHLHIEGFLILNKdVLHKSlDLAKSNNLTVSFDlASFEIVNQSKselkeilkNHVDMVFANEDEaaaf 216
Cdd:cd01947   112 -DDLKWPILDEGDGVFITAAAVDKE-AIRKC-RETKLVILQVTPR-VRVDELNQAL--------IPLDILIGSRLD---- 175

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 217 tqlPPAQSEESVKILNELcETAVVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTTGAGDFWAAGFLHGWANNQSIEDSAQL 296
Cdd:cd01947   176 ---PGELVVAEKIAGPFP-RYLIVTEGELGAILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALEL 250

                         250
                  ....*....|...
gi 1519643992 297 GALMGASVIQNHG 309
Cdd:cd01947   251 GAQCGAICVSHFG 263
PLN02548 PLN02548
adenosine kinase
 7-309 1.06e-20

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 90.93  E-value: 1.06e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   7 LGSPIIDEIAFVDDAFLENIsGSKGGMELLAESELESIKSE-INQELVQ-ITGGSAGNTI-FALARLGI--QTSFIGKIG 81
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKY-DVKLNNAILAEEKHLPMYDElASKYNVEyIAGGATQNSIrVAQWMLQIpgATSYMGCIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  82 NCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTpDGQRTMRTSLGAAMTLAEDEL----NP*DFQDYDHLHIEGF- 156
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVV-GGERSLVANLSAANCYKVEHLkkpeNWALVEKAKFYYIAGFf 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 157 LILNKDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILKnHVDMVFANEDEAAAFTQLPPAQSEESVKILNELCE 236
Cdd:PLN02548  159 LTVSPESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALP-YVDFLFGNETEARTFAKVQGWETEDVEEIALKISA 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 237 ----------TAVVKLGAQGSLIAKD*TIIHSEAIPV-KE-VIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASV 304
Cdd:PLN02548  238 lpkasgthkrTVVITQGADPTVVAEDGKVKEFPVIPLpKEkLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVI 317


                  ....*
gi 1519643992 305 IQNHG 309
Cdd:PLN02548  318 IQRSG 322
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
66-325 4.89e-20

1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 88.65  E-value: 4.89e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  66 ALARLGIQTS---FIGKigncASGDFYKESLAQ*GGSTQSFKI-GNIPNgkCLSLVTPDGQRTmrTSL-GAAMTLAEDEL 140
Cdd:COG1105    44 VLKALGVDVTalgFLGG----FTGEFIEELLDEEGIPTDFVPIeGETRI--NIKIVDPSDGTE--TEInEPGPEISEEEL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 141 Np*DFQDY--DHLHIEGFLIL--------NKDVLHKSLDLAKSNNLTVSFDLasfeivnqSKSELKEILKNHVDMVFANE 210
Cdd:COG1105   116 E--ALLERleELLKEGDWVVLsgslppgvPPDFYAELIRLARARGAKVVLDT--------SGEALKAALEAGPDLIKPNL 185

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 211 DEAAAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHGWAN 286
Cdd:COG1105   186 EELEELLGRPLETLEDIIAAARELlergAENVVVSLGADGALLVTEDGVYRAKPPKV-EVVSTVGAGDSMVAGFLAGLAR 264

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1519643992 287 NQSIEDSAQLGALMGASVIQNHG*ALSHR-QWDDILKSIQ 325
Cdd:COG1105   265 GLDLEEALRLAVAAGAAAALSPGTGLPDReDVEELLAQVE 304
1-PFK TIGR03168
hexose kinase, 1-phosphofructokinase family; This family consists largely of ...
 57-325 2.58e-19

hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.


Pssm-ID: 274464 [Multi-domain]  Cd Length: 303  Bit Score: 86.48  E-value: 2.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNcASGDFYKESLAQ*GGSTQSFKIgnipNGK---CLSLVTPDGQRTMRTSLGAam 133
Cdd:TIGR03168  35 GGKGINVARVLARLGAEVVATGFLGG-FTGEFIEALLAEEGIKNDFVEV----KGEtriNVKIKESSGEETELNEPGP-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 134 TLAEDELN------P*DFQDYDHLHIEGFLI--LNKDVLHKSLDLAKSNNLTVsfdlasfeIVNQSKSELKEILKNHVDM 205
Cdd:TIGR03168 108 EISEEELEqlleklRELLASGDIVVISGSLPpgVPPDFYAQLIAIARKKGAKV--------ILDTSGEALREALAAKPFL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 206 VFANEDEAAAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFL 281
Cdd:TIGR03168 180 IKPNHEELEELFGRELKTLEEIIEAARELldrgAENVLVSLGADGALLVTKEGALKATPPKV-EVVNTVGAGDSMVAGFL 258

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1519643992 282 HGWANNQSIEDSAQLGALMGASVIQNHG*ALSHRQ-WDDILKSIQ 325
Cdd:TIGR03168 259 AGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEdVEELLDQVT 303
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 65-311 3.97e-19

1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.


Pssm-ID: 238570 [Multi-domain]  Cd Length: 289  Bit Score: 85.66  E-value: 3.97e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  65 FALARLGIQTSFIGKIGNcASGDFYKESLAQ*GGSTQSFKI-GNIPNgkCLSLVTPDGQRTMrtSLGAAMTLAEDELNp* 143
Cdd:cd01164    44 RVLKDLGVEVTALGFLGG-FTGDFFEALLKEEGIPDDFVEVaGETRI--NVKIKEEDGTETE--INEPGPEISEEELE-- 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 144 DFQDY--------DHLHIEGFL--ILNKDVLHKSLDLAKSNNLTVsfdlasfeIVNQSKSELKEILKNHVDMVFANEDEA 213
Cdd:cd01164   117 ALLEKlkallkkgDIVVLSGSLppGVPADFYAELVRLAREKGARV--------ILDTSGEALLAALAAKPFLIKPNREEL 188

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 214 AAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTTGAGDFWAAGFLHGWANNQS 289
Cdd:cd01164   189 EELFGRPLGDEEDVIAAARKLiergAENVLVSLGADGALLVTKDGVYRASPPKVK-VVSTVGAGDSMVAGFVAGLAQGLS 267

                         250       260
                  ....*....|....*....|..
gi 1519643992 290 IEDSAQLGALMGASVIQNHG*A 311
Cdd:cd01164   268 LEEALRLAVAAGSATAFSPGTG 289
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 57-309 7.82e-19

Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.


Pssm-ID: 238915 [Multi-domain]  Cd Length: 264  Bit Score: 84.33  E-value: 7.82e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGkCLSLVTPDGQRT-MRTSLGAAMTL 135
Cdd:cd01940    22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENA-VADVELVDGDRIfGLSNKGGVARE 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 136 AEDELNP*DFQDYDHLHIEgfliLNKDVLH--KSLDLAKSNNLTVSFDLAsfeivNQSKSELKEILKNHVDMVFANEDEA 213
Cdd:cd01940   101 HPFEADLEYLSQFDLVHTG----IYSHEGHleKALQALVGAGALISFDFS-----DRWDDDYLQLVCPYVDFAFFSASDL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 214 AaftqlPPAQSEESVKILNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHGW-ANNQSIED 292
Cdd:cd01940   172 S-----DEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPV-EVVDTLGAGDSFIAGFLLSLlAGGTAIAE 245

                         250
                  ....*....|....*..
gi 1519643992 293 SAQLGALMGASVIQNHG 309
Cdd:cd01940   246 AMRQGAQFAAKTCGHEG 262
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 57-309 5.88e-18

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 82.09  E-value: 5.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNgkclslvtpdgqrtmrtslgaAMTLA 136
Cdd:PRK09813   23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVT---------------------AQTQV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 137 EDELNP*DFQDYDHLHIEGFLILNKDV--------LHKSL------DLAK--SNNLTVSFDLAsfeivNQSKSELKEILK 200
Cdd:PRK09813   82 ELHDNDRVFGDYTEGVMADFALSEEDYawlaqydiVHAAIwghaedAFPQlhAAGKLTAFDFS-----DKWDSPLWQTLV 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 201 NHVDMVFANEDEAAAFTQlppaqseesvKILNELCE----TAVVKLGAQGSLiAKD*TIIHSEAIPVKEVIDTTGAGDFW 276
Cdd:PRK09813  157 PHLDYAFASAPQEDEFLR----------LKMKAIVArgagVVIVTLGENGSI-AWDGAQFWRQAPEPVTVVDTMGAGDSF 225

                         250       260       270
                  ....*....|....*....|....*....|...
gi 1519643992 277 AAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:PRK09813  226 IAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 57-306 1.97e-17

YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238916 [Multi-domain]  Cd Length: 288  Bit Score: 80.82  E-value: 1.97e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDGQrtmrTSLGAAMTLA 136
Cdd:cd01941    35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYTAILDKDGD----LVVALADMDI 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 137 EDELNP*DFQdydhlHIEGFLI----------LNKDVLHKSLDLAKSNNLTVSFdlasfEIVNQSKSELKEILKNHVDMV 206
Cdd:cd01941   111 YELLTPDFLR-----KIREALKeakpivvdanLPEEALEYLLALAAKHGVPVAF-----EPTSAPKLKKLFYLLHAIDLL 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 207 FANEDEAAAFTQLPPAQSEESVKILNELC----ETAVVKLGAQGSLIA-KD*TIIHSEAIP--VKEVIDTTGAGDFWAAG 279
Cdd:cd01941   181 TPNRAELEALAGALIENNEDENKAAKILLlpgiKNVIVTLGAKGVLLSsREGGVETKLFPApqPETVVNVTGAGDAFVAG 260

                         250       260
                  ....*....|....*....|....*..
gi 1519643992 280 FLHGWANNQSIEDSAQLGALMGASVIQ 306
Cdd:cd01941   261 LVAGLLEGMSLDDSLRFAQAAAALTLE 287
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 3-305 6.64e-17

Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .


Pssm-ID: 238920 [Multi-domain]  Cd Length: 284  Bit Score: 79.26  E-value: 6.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   3 RIIGLGSPIIDEIAFVDDAflenisgSKGGMELLAESelesikseinqeLVQITGGSAGNTIFALARLGIQTSFIGKIGN 82
Cdd:cd01945     1 RVLGVGLAVLDLIYLVASF-------PGGDGKIVATD------------YAVIGGGNAANAAVAVARLGGQARLIGVVGD 61

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  83 CASGDFYKESLAQ*GGSTQSFKIGniPNGK----CLSLVTPDGQRTMRTSLGAamTLAEDELNP*DFQDYDHLHIEGFLI 158
Cdd:cd01945    62 DAIGRLILAELAAEGVDTSFIVVA--PGARspisSITDITGDRATISITAIDT--QAAPDSLPDAILGGADAVLVDGRQP 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 159 lnkDVLHKSLDLAKSNNLTVSFDlasfeiVNQSKSELKEILKNHVDMVFANEDEAAAFTqlpPAQSEESVKILNEL-CET 237
Cdd:cd01945   138 ---EAALHLAQEARARGIPIPLD------LDGGGLRVLEELLPLADHAICSENFLRPNT---GSADDEALELLASLgIPF 205

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1519643992 238 AVVKLGAQGSL-IAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFLHGWANNQSIEDsaqlgALMGASVI 305
Cdd:cd01945   206 VAVTLGEAGCLwLERDGELFHVPAFPV-EVVDTTGAGDVFHGAFAHALAEGMPLRE-----ALRFASAA 268
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 148-285 1.01e-16

ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).


Pssm-ID: 238177 [Multi-domain]  Cd Length: 196  Bit Score: 77.14  E-value: 1.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 148 YDHLHIEGfLILNKDVLHKSLDLAKSNNLTVSFDLASFEIVNqsKSELKEILKNHVDMVFANEDEAAAFTQLPPAQSEES 227
Cdd:cd00287    58 ADAVVISG-LSPAPEAVLDALEEARRRGVPVVLDPGPRAVRL--DGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEA 134

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1519643992 228 VK----ILNELCETAVVKLGAQGSLIA-KD*TIIHSEAIPVKeVIDTTGAGDFWAAGFLHGWA 285
Cdd:cd00287   135 AEaaalLLSKGPKVVIVTLGEKGAIVAtRGGTEVHVPAFPVK-VVDTTGAGDAFLAALAAGLA 196
pfkB TIGR03828
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ...
 57-316 3.53e-15

1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).


Pssm-ID: 274804 [Multi-domain]  Cd Length: 304  Bit Score: 74.55  E-value: 3.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNcASGDFYKESLAQ*GGSTQSFKIgnipNGK---CLSLVTPDGQRTMRTSLGAam 133
Cdd:TIGR03828  35 GGKGINVSRVLKNLGVDVVALGFLGG-FTGDFIEALLREEGIKTDFVRV----PGEtriNVKIKEPSGTETKLNGPGP-- 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 134 TLAEDELN------P*DFQDYDHLHIEGFLI--LNKDVLHKSLDLAKSNNLTVSFDLasfeivnqSKSELKEILKNHVDM 205
Cdd:TIGR03828 108 EISEEELEalleklRAQLAEGDWLVLSGSLPpgVPPDFYAELIALAREKGAKVILDT--------SGEALRDGLKAKPFL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 206 VFANEDEAAAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TIIHSEAIPVkEVIDTTGAGDFWAAGFL 281
Cdd:TIGR03828 180 IKPNDEELEELFGRELKTLEEIIEAARELldlgAENVLISLGADGALLVTKEGALFAQPPKG-EVVSTVGAGDSMVAGFL 258

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1519643992 282 HGWANNQSIEDSAQLGALMGASVIQNHG*ALSHRQ 316
Cdd:TIGR03828 259 AGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPE 293
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 57-309 6.81e-14

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 72.17  E-value: 6.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAgNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTqsfkIGNIPNGK-------------CLSLVTPDGqr 123
Cdd:PLN02341  120 GGNC-NFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV----VGLIEGTDagdsssasyetllCWVLVDPLQ-- 192

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 124 tmRTSLGAAMTLAEDELNP*DFQDYDH-----------LHIEGFLI--LNKDVLHKSLDLAKSNNLTVSFD-----LASF 185
Cdd:PLN02341  193 --RHGFCSRADFGPEPAFS-WISKLSAeakmairqskaLFCNGYVFdeLSPSAIASAVDYAIDVGTAVFFDpgprgKSLL 269

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 186 EIVNQSKSELKEILKNHvDMVFANEDEAAAFTQL-PPAQSEESVKILNELCETAVVKLGAQGS-LIAKD*tiIHSEAIPV 263
Cdd:PLN02341  270 VGTPDERRALEHLLRMS-DVLLLTSEEAEALTGIrNPILAGQELLRPGIRTKWVVVKMGSKGSiLVTRSS--VSCAPAFK 346

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1519643992 264 KEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:PLN02341  347 VNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGAATAMGCG 392
PRK15074 PRK15074
inosine/guanosine kinase; Provisional
 4-217 2.89e-12

inosine/guanosine kinase; Provisional


Pssm-ID: 185033  Cd Length: 434  Bit Score: 66.96  E-value: 2.89e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992   4 IIGLGSPIIDEIAFVDDAFLENISGSKGGMELLAESELESIKSEI-NQELV--QITGGSAGNT-----IFALAR---LGI 72
Cdd:PRK15074   36 IVGIDQTLVDIEAKVDDEFLERYGLSKGHSLVIEDDVAEALYQELkQNNLIthEFAGGTIGNTlhnysVLADDRsvlLGV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  73 QTSFIgKIGNCA-------SGDFYKESLAQ*GGstqsfkigniPNGKCLSLVTPDGQRTMRTSLGAAMTLAEDELNP*DF 145
Cdd:PRK15074  116 MSSNI-EIGSYAyrylcntSSRTDLNYLQGVDG----------PIGRCFTLISEDGERTFAISPGHMNQLRPESIPEDVI 184

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1519643992 146 QDYDHLHIEGFLILNK------DVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEILKNHVDMVFANEDEAAAFT 217
Cdd:PRK15074  185 AGASALVLTAYLVRCKpgepmpEATMKAIEYAKKHNVPVVLTLGTKFVIEDNPQWWQEFLKEHVSILAMNEDEAEALT 262
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 52-296 3.23e-12

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 66.11  E-value: 3.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  52 LVQITGGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGniPNGKCLSLV---TPDGQRT---- 124
Cdd:PRK09434   23 YLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLD--PAHRTSTVVvdlDDQGERSftfm 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 125 MRTSlgaamtlAEDELNP*D---FQDYDHLHIEGFLILN---KDVLHKSLDLAKSNNLTVSFDLASFEIVNQSKSELKEI 198
Cdd:PRK09434  101 VRPS-------ADLFLQPQDlppFRQGEWLHLCSIALSAepsRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEAELREC 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 199 LKNHV---DMVFANEDEaaaFTQLPPAQS-EESVKILNELCETA--VVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTTGA 272
Cdd:PRK09434  174 LRQALalaDVVKLSEEE---LCFLSGTSQlEDAIYALADRYPIAllLVTLGAEGVLVHTRGQVQHFPAPSVD-PVDTTGA 249

                         250       260
                  ....*....|....*....|....
gi 1519643992 273 GDFWAAGFLHGWANNQSIEDSAQL 296
Cdd:PRK09434  250 GDAFVAGLLAGLSQAGLWTDEAEL 273
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 58-306 3.49e-12

RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 66.04  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  58 GSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGNIP-NGKCLSLVtpDGQRTMR------TSLG 130
Cdd:cd01172    40 GGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDEGRPtTTKTRVIA--RNQQLLRvdreddSPLS 117

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 131 AAMTLAEDELNP*DFQDYDHLHIEGFL--ILNKDVLHKSLDLAKSNNLTVSFDLASfeiVNQSKSElkeilknHVDMVFA 208
Cdd:cd01172   118 AEEEQRLIERIAERLPEADVVILSDYGkgVLTPRVIEALIAAARELGIPVLVDPKG---RDYSKYR-------GATLLTP 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 209 NEDEAAAFTQLPPAQSEESVKILNEL-----CETAVVKLGAQG-SLIAKD*TIIHseaIPV--KEVIDTTGAGDFWAAGF 280
Cdd:cd01172   188 NEKEAREALGDEINDDDELEAAGEKLlellnLEALLVTLGEEGmTLFERDGEVQH---IPAlaKEVYDVTGAGDTVIATL 264

                         250       260
                  ....*....|....*....|....*.
gi 1519643992 281 LHGWANNQSIEDSAQLGALMGASVIQ 306
Cdd:cd01172   265 ALALAAGADLEEAAFLANAAAGVVVG 290
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 48-305 3.58e-09

Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238912 [Multi-domain]  Cd Length: 254  Bit Score: 56.64  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  48 INQELVQITGGSAGNTIFALARLGIQTSFIGKIG------NCASGDFYKESLAQ*GGSTQSFKIGNIPNGKCLSLVTPDG 121
Cdd:cd01937    15 TNGSGVVKPGGPATYASLTLSRLGLTVKLVTKVGrdypdkWSDLFDNGIEVISLLSTETTTFELNYTNEGRTRTLLAKCA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 122 QRTMRTSLGAAMTLAEDELNP*dfqdYDHLHIEGFLILNKdvlhksldlaksnnltVSFDLASF-EIVNQSKSELKEILK 200
Cdd:cd01937    95 AIPDTESPLSTITAEIVILGPV----PEEISPSLFRKFAF----------------ISLDAQGFlRRANQEKLIKCVILK 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 201 NHvDMVFANEDEAAAFTQLppaqsEESVKILNEL-CETAVVKLGAQGSLIAKD*TIIHSEAIPVKEViDTTGAGDFWAAG 279
Cdd:cd01937   155 LH-DVLKLSRVEAEVISTP-----TELARLIKETgVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVV-DPTGAGDVFLAA 227

                         250       260
                  ....*....|....*....|....*.
gi 1519643992 280 FLHGWANNQSIEDSAQLGALMGASVI 305
Cdd:cd01937   228 FLYSRLSGKDIKEAAEFAAAAAAKFI 253
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 178-308 5.42e-09

Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.


Pssm-ID: 238921 [Multi-domain]  Cd Length: 277  Bit Score: 56.32  E-value: 5.42e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 178 VSFDLASFEIvNQSKSELKEILKNhVDMVFANEDEAAAFTQLPPAQSEeSVKILNELCETAVVKLGAQGSLIAKD*TIIH 257
Cdd:cd01946   141 VVMDTMNFWI-SIKPEKLKKVLAK-VDVVIINDGEARQLTGAANLVKA-ARLILAMGPKALIIKRGEYGALLFTDDGYFA 217

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519643992 258 SEAIPVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNH 308
Cdd:cd01946   218 APAYPLESVFDPTGAGDTFAGGFIGYLASQKDTSEANMRRAIIYGSAMASF 268
PRK11142 PRK11142
ribokinase; Provisional
 57-293 5.66e-09

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 56.42  E-value: 5.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSF-KIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTL 135
Cdd:PRK11142   39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVsVIKGESTGVALIFVNDEGENSIGIHAGANAAL 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 136 AEDELNP*dfqdydHLHiegfLILNKDVL-----------HKSLDLAKSNNLTVsfdlasfeIVN----QSKSElkEILK 200
Cdd:PRK11142  119 TPALVEA-------HRE----LIANADALlmqletpletvLAAAKIAKQHGTKV--------ILNpapaRELPD--ELLA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 201 NhVDMVFANEDEAAAFTQLPPAQSEESVKILNEL----CETAVVKLGAQGSLIAKD*TiihSEAIP---VKeVIDTTGAG 273
Cdd:PRK11142  178 L-VDIITPNETEAEKLTGIRVEDDDDAAKAAQVLhqkgIETVLITLGSRGVWLSENGE---GQRVPgfrVQ-AVDTIAAG 252

                         250       260
                  ....*....|....*....|
gi 1519643992 274 DFWAAGFLHGWANNQSIEDS 293
Cdd:PRK11142  253 DTFNGALVTALLEGKPLPEA 272
PLN02323 PLN02323
probable fructokinase
 57-296 4.74e-07

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 50.78  E-value: 4.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*GGSTQSFKIGniPNGK-CLSLVT--PDGQRTM---RTSlG 130
Cdd:PLN02323   43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD--PGARtALAFVTlrSDGEREFmfyRNP-S 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 131 AAMTLAEDELNP*dfqdydhlhiegfLILNKDVLH----------------KSLDLAKSNNLTVSFD----LASFEIVNQ 190
Cdd:PLN02323  120 ADMLLRESELDLD-------------LIRKAKIFHygsislitepcrsahlAAMKIAKEAGALLSYDpnlrLPLWPSAEA 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 191 SKSELKEILkNHVDMVFANEDEAAAFTQLPPAQSEESVKILNELCETAVVKLGAQGSLIAKD*TIIHSEAIPVKeVIDTT 270
Cdd:PLN02323  187 AREGIMSIW-DEADIIKVSDEEVEFLTGGDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVK-AVDTT 264

                         250       260
                  ....*....|....*....|....*..
gi 1519643992 271 GAGDFWAAGFLHGWANNQSI-EDSAQL 296
Cdd:PLN02323  265 GAGDAFVGGLLSQLAKDLSLlEDEERL 291
fruK PRK09513
1-phosphofructokinase; Provisional
 187-327 1.81e-06

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 48.92  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 187 IVNQSKSELKEILKNHVDMVFANEDEAAAFTQLPPAQSEESVKILNELCETA----VVKLGAQGSLIAKD*TIIHSEAiP 262
Cdd:PRK09513  165 IFDSSREALVAGLKAAPWLVKPNRRELEIWAGRKLPELKDVIEAAHALREQGiahvVISLGAEGALWVNASGEWIAKP-P 243

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1519643992 263 VKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG*ALSHR-QWDDILKSIQTT 327
Cdd:PRK09513  244 ACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVSQSNVGITDRpQLAAMMARVDLT 309
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
 57-289 2.07e-05

Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.


Pssm-ID: 238914 [Multi-domain]  Cd Length: 290  Bit Score: 45.48  E-value: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992  57 GGSAGNTIFALARLGIQTSFIGKIGNCASGDFYKESLAQ*G-GSTQSFKIGNIPNGKCLSLVTPDGQRTMRTSLGAAMTL 135
Cdd:cd01939    36 GGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGiDISHCYRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEV 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 136 AEDELNP*DFQDYDHLHIEGfliLNKDvlhKSLD-----LAKSNNLTVSFDLASFEIVNqSKSELKEiLKNHVDMVFANE 210
Cdd:cd01939   116 TYDDFSKIDLTQYGWIHFEG---RNPD---ETLRmmqhiEEHNNRRPEIRITISVEVEK-PREELLE-LAAYCDVVFVSK 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 211 DEAAAFTQLPPAQSEESVKILNELCETAVVKLGAQGSLI-AKD*TIIHSEAIPVKEVIDTTGAGDFWAAGFLHGWANNQS 289
Cdd:cd01939   188 DWAQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAGAlGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYALNKGPD 267
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
 187-312 1.93e-04

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 42.46  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 187 IVNQSKSELKEILK-NHVDMVFANEDEAAAFTQLPPAQSEESVKILNELCETA-----VVKLGAQGSLIAKD*TIIHSEA 260
Cdd:PRK10294  164 IIDSSGDALSAALAiGNIELVKPNQKELSALVNRDLTQPDDVRKAAQELVNSGkakrvVVSLGPQGALGVDSENCIQVVP 243

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1519643992 261 IPVKEvIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG*AL 312
Cdd:PRK10294  244 PPVKS-QSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGTRL 294
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 195-309 1.17e-03

MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.


Pssm-ID: 238918 [Multi-domain]  Cd Length: 328  Bit Score: 40.02  E-value: 1.17e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1519643992 195 LKEILkNHVDMVFANEDEAAAFTQLP---PAQSEESVKILNELCETA---------VVKLGAQGSLI--AKD*TIIHSEA 260
Cdd:cd01943   174 LLQAL-PRVDVFSPNLEEAARLLGLPtsePSSDEEKEAVLQALLFSGilqdpgggvVLRCGKLGCYVgsADSGPELWLPA 252

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1519643992 261 I--PVKEVIDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGASVIQNHG 309
Cdd:cd01943   253 YhtKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
TrbI_Ftype pfam09677
Type-F conjugative transfer system protein (TrbI_Ftype); This entry represents TrbI, an ...
 195-271 4.88e-03

Type-F conjugative transfer system protein (TrbI_Ftype); This entry represents TrbI, an essential component of the F-type conjugative transfer system for plasmid DNA transfer that has been shown to be localized to the periplasm.


Pssm-ID: 430747  Cd Length: 106  Bit Score: 36.25  E-value: 4.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1519643992 195 LKEILKNHVDmvfanedeAAAFTQLPPAQSEESVKILNELCETAVVKLGAQGsliakd*TIIHSEAIPVKEVIDTTG 271
Cdd:pfam09677  34 LSETLGEFVD--------AQARKKATPAQVKALSRAFNKALEASLQELGRHG------RIVLVGEAVLAGNAPDITD 96
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
 239-302 4.91e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 38.25  E-value: 4.91e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1519643992 239 VVKLGAQGSLIAKD*TIIHSEAIPVKEViDTTGAGDFWAAGFLHGWANNQSIEDSAQLGALMGA 302
Cdd:PLN02630  207 IVTNGKKGCRIYWKDGEMRVPPFPAIQV-DPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGS 269
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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