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Conserved domains on  [gi|1678297255|ref|NP_001356053|]
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adenosine kinase isoform f [Homo sapiens]

Protein Classification

carbohydrate kinase family protein( domain architecture ID 399)

carbohydrate kinase family protein that accepts a wide variety of substrates, including carbohydrates and aromatic small molecules, all being phosphorylated at a hydroxyl group; belongs to the ribokinase/pfkB sugar kinase superfamily

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ribokinase_pfkB_like super family cl00192
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 12-287 2.74e-144

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).


The actual alignment was detected with superfamily member PLN02548:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 332  Bit Score: 408.33  E-value: 2.74e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  12 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 91
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  92 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA--- 168
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAgff 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 169 ------------------------------------------------------EAATFAREQGFETKDIKEIAKKTQAL 194
Cdd:PLN02548  159 ltvspesimlvaehaaannktfmmnlsapficeffkdqlmealpyvdflfgnetEARTFAKVQGWETEDVEEIALKISAL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 195 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 274
Cdd:PLN02548  239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318

                         330
                  ....*....|...
gi 1678297255 275 RRTGCTFPEKPDF 287
Cdd:PLN02548  319 QRSGCTYPEKPDF 331
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
 12-287 2.74e-144

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 408.33  E-value: 2.74e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  12 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 91
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  92 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA--- 168
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAgff 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 169 ------------------------------------------------------EAATFAREQGFETKDIKEIAKKTQAL 194
Cdd:PLN02548  159 ltvspesimlvaehaaannktfmmnlsapficeffkdqlmealpyvdflfgnetEARTFAKVQGWETEDVEEIALKISAL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 195 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 274
Cdd:PLN02548  239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318

                         330
                  ....*....|...
gi 1678297255 275 RRTGCTFPEKPDF 287
Cdd:PLN02548  319 QRSGCTYPEKPDF 331
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 6-282 1.99e-95

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: 283.74  E-value: 1.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255   6 ENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAAT 85
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  86 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekNWMLVEKARV 164
Cdd:cd01168    74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 165 CYIA------------EAATFAREQGF------------------------------------------ETKDIKEIAKK 190
Cdd:cd01168   149 LYLEgylltvppeailLAAEHAKENGVkialnlsapfivqrfkeallellpyvdilfgneeeaealaeaETTDDLEAALK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 191 TQALpkmnskRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAA 270
Cdd:cd01168   229 LLAL------RCRIVVITQGAKGAVVVEGGEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300

                         330
                  ....*....|..
gi 1678297255 271 SIIIRRTGCTFP 282
Cdd:cd01168   301 AEVIQQLGPRLP 312
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 27-281 1.34e-48

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 163.28  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  27 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 106
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 107 HVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEKARVCYIA-------------EAA 171
Cdd:pfam00294  74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISgslplglpeatleELI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 172 TFAREQGFET------------------------------------KDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTI 215
Cdd:pfam00294 151 EAAKNGGTFDpnlldplgaareallellpladllkpneeelealtgAKLDDIEEALAALHKLLAKGIKTVIVTLGADGAL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678297255 216 MATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTF 281
Cdd:pfam00294 231 VVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 84-280 2.43e-20

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: 88.40  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  84 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 161
Cdd:COG0524    53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 162 ARVCYI--------------AEAATFAREQG-----------------------------------------FETKDIKE 186
Cdd:COG0524   128 ADILHLggitlasepprealLAALEAARAAGvpvsldpnyrpalweparellrellalvdilfpneeeaellTGETDPEE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 187 IAKKTQALPKmnskrqRIVIFTQGRDDTIMATESE---VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECI 263
Cdd:COG0524   208 AAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEGLDLEEAL 275

                         250
                  ....*....|....*..
gi 1678297255 264 RAGHYAASIIIRRTGCT 280
Cdd:COG0524   276 RFANAAAALVVTRPGAQ 292
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 234-280 1.35e-07

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: 51.83  E-value: 1.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1678297255 234 EIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 280
Cdd:TIGR04382 250 EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
 
Name Accession Description Interval E-value
PLN02548 PLN02548
adenosine kinase
 12-287 2.74e-144

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 408.33  E-value: 2.74e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  12 MGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHkAATFFGCIG 91
Cdd:PLN02548    1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIRVAQWMLQIPG-ATSYMGCIG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  92 IDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA--- 168
Cdd:PLN02548   80 KDKFGEEMKKCATAAGVNVHYYEDESTPTGTCAVLVVGGERSLVANLSAANCYKVE-HLKKPENWALVEKAKFYYIAgff 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 169 ------------------------------------------------------EAATFAREQGFETKDIKEIAKKTQAL 194
Cdd:PLN02548  159 ltvspesimlvaehaaannktfmmnlsapficeffkdqlmealpyvdflfgnetEARTFAKVQGWETEDVEEIALKISAL 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 195 PKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIII 274
Cdd:PLN02548  239 PKASGTHKRTVVITQGADPTVVAEDGKVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVII 318

                         330
                  ....*....|...
gi 1678297255 275 RRTGCTFPEKPDF 287
Cdd:PLN02548  319 QRSGCTYPEKPDF 331
PTZ00247 PTZ00247
adenosine kinase; Provisional
 9-287 1.25e-118

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 343.93  E-value: 1.25e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255   9 LFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAEDKHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQPHKAATFFG 88
Cdd:PTZ00247    8 LLGFGNPLLDISAHVSDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQWMLQAPKGFVCYVG 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  89 CIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGDNRSLIANLAAANCYKKEkHLDLEKNWMLVEKARVCYIA 168
Cdd:PTZ00247   88 CVGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVCGKERSLVANLGAANHLSAE-HMQSHAVQEAIKTAQLYYLE 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 169 ---------------------------------------------------------EAATFAREQGFETKDIKEIAKKT 191
Cdd:PTZ00247  167 gffltvspnnvlqvakharesgklfclnlsapfisqffferllqvlpyvdilfgneeEAKTFAKAMKWDTEDLKEIAARI 246

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 192 QALPKMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAAS 271
Cdd:PTZ00247  247 AMLPKYSGTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQ 326

                         330
                  ....*....|....*.
gi 1678297255 272 IIIRRTGCTFPEKPDF 287
Cdd:PTZ00247  327 VIIQHNGCTYPEKPPF 342
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 6-282 1.99e-95

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: 283.74  E-value: 1.99e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255   6 ENILFGMGNPLLDISAVVDKDFLDKYSLKPNDQILAedkHKELFDELVKKFKVEYHAGGSTQNSIKVAQWMiqqpHKAAT 85
Cdd:cd01168     1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILA---DMEEQEELLAKLPVKYIAGGSAANTIRGAAAL----GGSAA 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  86 FFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTGTCAACITGD-NRSLIANLAAANCYKKEKHldlekNWMLVEKARV 164
Cdd:cd01168    74 FIGRVGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDaERTMCTYLGAANELSPDDL-----DWSLLAKAKY 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 165 CYIA------------EAATFAREQGF------------------------------------------ETKDIKEIAKK 190
Cdd:cd01168   149 LYLEgylltvppeailLAAEHAKENGVkialnlsapfivqrfkeallellpyvdilfgneeeaealaeaETTDDLEAALK 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 191 TQALpkmnskRQRIVIFTQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAA 270
Cdd:cd01168   229 LLAL------RCRIVVITQGAKGAVVVEGGEVYPVPAIPVE--KIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAA 300

                         330
                  ....*....|..
gi 1678297255 271 SIIIRRTGCTFP 282
Cdd:cd01168   301 AEVIQQLGPRLP 312
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 27-281 1.34e-48

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 163.28  E-value: 1.34e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  27 FLDKYSLKPNDQILAEDKHkelFDELVKKFKVEYHAGGSTQNSIKVAQWMIQQphkaATFFGCIGIDKFGEILKRKAAEA 106
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGL---PGELVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKE 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 107 HVDAHYYEQNEQ-PTGTCAACITGD-NRSLIANLAAANCYKKEKhldLEKNWMLVEKARVCYIA-------------EAA 171
Cdd:pfam00294  74 GVDTDYVVIDEDtRTGTALIEVDGDgERTIVFNRGAAADLTPEE---LEENEDLLENADLLYISgslplglpeatleELI 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 172 TFAREQGFET------------------------------------KDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTI 215
Cdd:pfam00294 151 EAAKNGGTFDpnlldplgaareallellpladllkpneeelealtgAKLDDIEEALAALHKLLAKGIKTVIVTLGADGAL 230

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1678297255 216 MATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCTF 281
Cdd:pfam00294 231 VVEGDGE--VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 85-278 1.09e-20

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: 89.15  E-value: 1.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  85 TFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTcaACIT----GDNRslIANLAAANcykkeKHL---DLEKNW 156
Cdd:cd01174    54 AMIGAVGDDAFGDELLENLREEGIDVSYVEVvVGAPTGT--AVITvdesGENR--IVVVPGAN-----GELtpaDVDAAL 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 157 MLVEKARVCY---------IAEAATFAREQGFET--------KDIKEIAKKT-------------------------QAL 194
Cdd:cd01174   125 ELIAAADVLLlqleipletVLAALRAARRAGVTVilnpaparPLPAELLALVdilvpneteaalltgievtdeedaeKAA 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 195 PKMNSKRQRIVIFTQGRDDTIMATESEVT---AFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAAS 271
Cdd:cd01174   205 RLLLAKGVKNVIVTLGAKGALLASGGEVEhvpAFKV------KAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAA 278


                  ....*..
gi 1678297255 272 IIIRRTG 278
Cdd:cd01174   279 LSVTRPG 285
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 84-280 2.43e-20

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: 88.40  E-value: 2.43e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  84 ATFFGCIGIDKFGEILKRKAAEAHVDAHYYEQ-NEQPTGTCAACITGD-NRSLIANLAAANCYKKEkHLDLEknwmLVEK 161
Cdd:COG0524    53 VALVGAVGDDPFGDFLLAELRAEGVDTSGVRRdPGAPTGLAFILVDPDgERTIVFYRGANAELTPE-DLDEA----LLAG 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 162 ARVCYI--------------AEAATFAREQG-----------------------------------------FETKDIKE 186
Cdd:COG0524   128 ADILHLggitlasepprealLAALEAARAAGvpvsldpnyrpalweparellrellalvdilfpneeeaellTGETDPEE 207

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 187 IAKKTQALPKmnskrqRIVIFTQGRDDTIMATESE---VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECI 263
Cdd:COG0524   208 AAAALLARGV------KLVVVTLGAEGALLYTGGEvvhVPAFPV------EVVDTTGAGDAFAAGFLAGLLEGLDLEEAL 275

                         250
                  ....*....|....*..
gi 1678297255 264 RAGHYAASIIIRRTGCT 280
Cdd:COG0524   276 RFANAAAALVVTRPGAQ 292
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 9-254 4.29e-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: 74.82  E-value: 4.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255   9 LFGMGNPLLDISAVVDKDFLDkyslkpndqilaedkhkelfDELVKKFKVEYHAGGSTQNSIKVAQWMIQqphkAATFFG 88
Cdd:cd00287     2 VLVVGSLLVDVILRVDALPLP--------------------GGLVRPGDTEERAGGGAANVAVALARLGV----SVTLVG 57

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  89 CIGIDKFGEILKRKAAEAHVdahyyeqneqptgtcAACITGdNRSLIANLAAANCYKKEKhldleknwMLVEKARVCYI- 167
Cdd:cd00287    58 ADAVVISGLSPAPEAVLDAL---------------EEARRR-GVPVVLDPGPRAVRLDGE--------ELEKLLPGVDIl 113

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 168 ----AEAATFAREQGFETKDIkeiakkTQALPKMNSKRQRIVIFTQGRDDTIMATEsEVTAFAVLDQDqKEIIDTNGAGD 243
Cdd:cd00287   114 tpneEEAEALTGRRDLEVKEA------AEAAALLLSKGPKVVIVTLGEKGAIVATR-GGTEVHVPAFP-VKVVDTTGAGD 185

                         250
                  ....*....|.
gi 1678297255 244 AFVGGFLSQLV 254
Cdd:cd00287   186 AFLAALAAGLA 196
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 84-279 8.96e-15

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: 72.73  E-value: 8.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  84 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTcaACIT---GDNRSLIANLAAANCYKKEKHLDLEKNW--- 156
Cdd:cd01942    53 PGLVAAVGEDFHGRLYLEELREEGVDtSHVRVVDEDSTGV--AFILtdgDDNQIAYFYPGAMDELEPNDEADPDGLAdiv 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 157 ------MLVEKARVCYiAEAATFA-----REQGFETKDIKEIAKKTQALpKMN------------------SKRQRIVIF 207
Cdd:cd01942   131 hlssgpGLIELARELA-AGGITVSfdpgqELPRLSGEELEEILERADIL-FVNdyeaellkertglseaelASGVRVVVV 208

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678297255 208 TQGRDDTIMATESEVTAFAVLDQDqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGC 279
Cdd:cd01942   209 TLGPKGAIVFEDGEEVEVPAVPAV--KVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 61-280 4.77e-12

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: 64.90  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  61 HAGGSTQNsikVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQ-PTGTcAACITGDNRS---LIA 136
Cdd:cd01166    29 FFGGAEAN---VAVGLARLGHRVA-LVTAVGDDPFGRFILAELRREGVDTSHVRVDPGrPTGL-YFLEIGAGGErrvLYY 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 137 NLAAANCYKKEKHLDLEknwmLVEKARVCYIA---------------EAATFAREQG----F------------ETKD-I 184
Cdd:cd01166   104 RAGSAASRLTPEDLDEA----ALAGADHLHLSgitlalsesareallEALEAAKARGvtvsFdlnyrpklwsaeEAREaL 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 185 KEIAKKTQ-ALP---------------------KMNSKRQRIVIFTQGRDDTIMATESEVTAFAVLdqdQKEIIDTNGAG 242
Cdd:cd01166   180 EELLPYVDiVLPseeeaeallgdedptdaaeraLALALGVKAVVVKLGAEGALVYTGGGRVFVPAY---PVEVVDTTGAG 256

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1678297255 243 DAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 280
Cdd:cd01166   257 DAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 68-273 1.56e-10

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: 60.06  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  68 NSIKVAQWMIQQPHKAAtFFGCIGIDKFGEILKRKAAEAHVDAHYYEQNEQPTG-TCAACITGDNRSLIAN--------- 137
Cdd:cd01940    24 NALNVAVYAKRLGHESA-YIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAvADVELVDGDRIFGLSNkggvarehp 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 138 ------------LAAANCYKKEKHL----------------DLEKNWMLVEKARVCYIAEAATFAREqGFETKDIKEIAK 189
Cdd:cd01940   103 feadleylsqfdLVHTGIYSHEGHLekalqalvgagalisfDFSDRWDDDYLQLVCPYVDFAFFSAS-DLSDEEVKAKLK 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 190 KTQalpkmnSKRQRIVIFTQGRDDTIMATESEVTAFAVLdqdQKEIIDTNGAGDAFVGGFL-SQLVSDKPLTECIRAG-H 267
Cdd:cd01940   182 EAV------SRGAKLVIVTRGEDGAIAYDGAVFYSVAPR---PVEVVDTLGAGDSFIAGFLlSLLAGGTAIAEAMRQGaQ 252


                  ....*.
gi 1678297255 268 YAASII 273
Cdd:cd01940   253 FAAKTC 258
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 84-278 9.03e-10

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: 58.42  E-value: 9.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255  84 ATFFGCIGIDKFGEILKRKAAEAHVD-AHYYEQNEQPTGTCAACITGD-NRS-LIANLAAANCykkekHLDLEKNWMLVE 160
Cdd:cd01167    45 AAFIGKVGDDEFGDFLLETLKEAGVDtRGIQFDPAAPTTLAFVTLDADgERSfEFYRGPAADL-----LLDTELNPDLLS 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 161 KARVCY--------------IAEAATFAREQG--------------------------------------------FETK 182
Cdd:cd01167   120 EADILHfgsialasepsrsaLLELLEAAKKAGvlisfdpnlrpplwrdeeeareriaelleladivklsdeelellFGEE 199

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 183 DIKEIAKKTQALPkmnskrQRIVIFTQGRDDTIMAT---ESEVTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDK-- 257
Cdd:cd01167   200 DPEEIAALLLLFG------LKLVLVTRGADGALLYTkggVGEVPGIPV------EVVDTTGAGDAFVAGLLAQLLSRGll 267

                         250       260
                  ....*....|....*....|....*.
gi 1678297255 258 -----PLTECIRAGHYAASIIIRRTG 278
Cdd:cd01167   268 aldedELAEALRFANAVGALTCTKAG 293
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 168-272 1.11e-07

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: 51.93  E-value: 1.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 168 AEAATFAREQGFETKDIKeIAKKTQALPKMNskrqrIVIFTQGRDDTI---MATESEVTAFAVLDQDqkEIIDTNGAGDA 244
Cdd:cd01941   185 AELEALAGALIENNEDEN-KAAKILLLPGIK-----NVIVTLGAKGVLlssREGGVETKLFPAPQPE--TVVNVTGAGDA 256

                          90       100
                  ....*....|....*....|....*...
gi 1678297255 245 FVGGFLSQLVSDKPLTECIRAGHYAASI 272
Cdd:cd01941   257 FVAGLVAGLLEGMSLDDSLRFAQAAAAL 284
myo_inos_iolC_N TIGR04382
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ...
 234-280 1.35e-07

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: 51.83  E-value: 1.35e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1678297255 234 EIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 280
Cdd:TIGR04382 250 EVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCS 296
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 169-278 6.55e-07

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: 49.73  E-value: 6.55e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 169 EAATFAREQGFETKD-IKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMAtesevtAFAVldqdqkEIIDTNGAGDAFVG 247
Cdd:cd01944   191 EAAIFAERGDPAAEAsALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIP------GFKV------KAVDTIGAGDTHAG 258

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1678297255 248 GFLSQLVSDKPLTECIRAGHYAASIIIRRTG 278
Cdd:cd01944   259 GMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
PTZ00292 PTZ00292
ribokinase; Provisional
 178-278 1.86e-06

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 48.58  E-value: 1.86e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 178 GFETKDIKEIAKKTQALPKMNSkrqRIVIFTQG-RDDTIMATESEVTAfavLDQDQKEIIDTNGAGDAFVGGFLSQLVSD 256
Cdd:PTZ00292  214 GMEVTDTESAFKASKELQQLGV---ENVIITLGaNGCLIVEKENEPVH---VPGKRVKAVDTTGAGDCFVGSMAYFMSRG 287

                          90       100
                  ....*....|....*....|..
gi 1678297255 257 KPLTECIRAGHYAASIIIRRTG 278
Cdd:PTZ00292  288 KDLKESCKRANRIAAISVTRHG 309
PLN02323 PLN02323
probable fructokinase
 236-261 1.19e-05

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 46.15  E-value: 1.19e-05
                          10        20
                  ....*....|....*....|....*.
gi 1678297255 236 IDTNGAGDAFVGGFLSQLVSDKPLTE 261
Cdd:PLN02323  261 VDTTGAGDAFVGGLLSQLAKDLSLLE 286
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
178-266 2.09e-05

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 45.13  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 178 GFETKDIKEIAKKTQALPKMNSkrqRIVIFTQGRDDTIMATESEVTAFAVLDQdqkEIIDTNGAGDAFVGGFLSQLVSDK 257
Cdd:COG1105   193 GRPLETLEDIIAAARELLERGA---ENVVVSLGADGALLVTEDGVYRAKPPKV---EVVSTVGAGDSMVAGFLAGLARGL 266


                  ....*....
gi 1678297255 258 PLTECIRAG 266
Cdd:COG1105   267 DLEEALRLA 275
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 178-274 3.86e-05

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 43.96  E-value: 3.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 178 GFETKDIKEIAKKTQALPKMNSKrqrIVIFTQGRDDTIMATESEVTAFAVldqDQKEIIDTNGAGDAFVGGFLSQLVSDK 257
Cdd:PRK09813  164 ASAPQEDEFLRLKMKAIVARGAG---VVIVTLGENGSIAWDGAQFWRQAP---EPVTVVDTMGAGDSFIAGFLCGWLAGM 237

                          90
                  ....*....|....*..
gi 1678297255 258 PLTECIRAGHYAASIII 274
Cdd:PRK09813  238 TLPQAMAQGTACAAKTI 254
PRK11142 PRK11142
ribokinase; Provisional
 222-278 5.10e-05

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 44.09  E-value: 5.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1678297255 222 VTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 278
Cdd:PRK11142  238 VPGFRV------QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKG 288
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 232-280 7.01e-05

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: 43.56  E-value: 7.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1678297255 232 QKEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTGCT 280
Cdd:cd01947   217 KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 182-266 9.33e-05

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: 43.29  E-value: 9.33e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 182 KDIKEIAKKtqalpkMNSKRQRIVIFTQGRDDTIMATESEV---TAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKP 258
Cdd:cd01164   200 EDVIAAARK------LIERGAENVLVSLGADGALLVTKDGVyraSPPKV------KVVSTVGAGDSMVAGFVAGLAQGLS 267


                  ....*...
gi 1678297255 259 LTECIRAG 266
Cdd:cd01164   268 LEEALRLA 275
PRK15074 PRK15074
inosine/guanosine kinase; Provisional
 11-70 1.35e-04

inosine/guanosine kinase; Provisional


Pssm-ID: 185033  Cd Length: 434  Bit Score: 43.07  E-value: 1.35e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1678297255  11 GMGNPLLDISAVVDKDFLDKYSL-KPNDQILAEDKHKELFDELVKKFKVEYH-AGGSTQNSI 70
Cdd:PRK15074   38 GIDQTLVDIEAKVDDEFLERYGLsKGHSLVIEDDVAEALYQELKQNNLITHEfAGGTIGNTL 99
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 158-278 1.44e-04

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: 42.71  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 158 LVEKARVCYIAEAATFAREQGFETKDIkeiAKKTQALPKMNSkrqrIVIFTQGRDDTIMATESEVTAF---AVlDQDQKE 234
Cdd:cd01943   188 LEEAARLLGLPTSEPSSDEEKEAVLQA---LLFSGILQDPGG----GVVLRCGKLGCYVGSADSGPELwlpAY-HTKSTK 259

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1678297255 235 IIDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 278
Cdd:cd01943   260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 203-255 2.83e-04

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 41.85  E-value: 2.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1678297255 203 RIVIFTQGRDDTIMATESEVTAFA---VldqdqkEIIDTNGAGDAFVGGFLSQLVS 255
Cdd:PRK09434  214 ALLLVTLGAEGVLVHTRGQVQHFPapsV------DPVDTTGAGDAFVAGLLAGLSQ 263
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 236-278 5.28e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 40.93  E-value: 5.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1678297255 236 IDTNGAGDAFVGGFLSQLVSDKPLTECIRAGHYAASIIIRRTG 278
Cdd:PLN02379  298 VDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALG 340
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 191-278 6.60e-04

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: 40.35  E-value: 6.60e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 191 TQALPKMNSKRQRIVIFTQGRDDTIMATES----EVTAFAVldqdqkEIIDTNGAGDAFVGGFLSQLVSDKPLTECIRAG 266
Cdd:cd01945   192 DEALELLASLGIPFVAVTLGEAGCLWLERDgelfHVPAFPV------EVVDTTGAGDVFHGAFAHALAEGMPLREALRFA 265

                          90
                  ....*....|..
gi 1678297255 267 HYAASIIIRRTG 278
Cdd:cd01945   266 SAAAALKCRGLG 277
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
 180-261 5.15e-03

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: 37.83  E-value: 5.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1678297255 180 ETKDIKEIAKKTQALPKMNSKRQRIVIFTQGRDDTIMATESEVtaFAVLDQDQKEIIDTNGAGDAFVGGFLSQLVSDKPL 259
Cdd:cd01946   173 EARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDDGY--FAAPAYPLESVFDPTGAGDTFAGGFIGYLASQKDT 250


                  ..
gi 1678297255 260 TE 261
Cdd:cd01946   251 SE 252
 
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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