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Conserved domains on  [gi|981689685|ref|WP_059886045|]
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ribokinase [Burkholderia stagnalis]

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 ...
19-312 3.40e-106

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 TIGR02152:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 293  Bit Score: 311.46  E-value: 3.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   19 GSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATS 98
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   99 AAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVLNPAPA 178
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  179 VAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNaARHYPAPAVQAV 258
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE-SKLIPAFKVKAV 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 981689685  259 DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAELA 312
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
19-312 3.40e-106

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: 311.46  E-value: 3.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   19 GSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATS 98
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   99 AAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVLNPAPA 178
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  179 VAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNaARHYPAPAVQAV 258
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE-SKLIPAFKVKAV 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 981689685  259 DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAELA 312
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
14-307 3.22e-105

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: 308.71  E-value: 3.22e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01174    1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVL 173
Cdd:cd01174   81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 NPAPAVAPLPAgWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADnAARHYPAP 253
Cdd:cd01174  161 NPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGG-EVEHVPAF 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPT 307
Cdd:cd01174  239 KVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
8-311 1.10e-76

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 237.33  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   8 GAPRAGRVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEA 87
Cdd:PTZ00292  11 GGEAEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  88 EGIDCAGLATSAAASTGVALIVVDDA-SQNAIVIVAGGNGEVTP-DTIARHDAAIAAADVLICQLETPADAVFAALAAGR 165
Cdd:PTZ00292  91 NGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPqMVDAQTDNIQNICKYLICQNEIPLETTLDALKEAK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 166 RLGRTVVLNPAPAVAPLPAG----WLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLAL 241
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIV 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 242 TADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:PTZ00292 251 EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
14-311 3.01e-67

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: 212.44  E-value: 3.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:COG0524    1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL---ICQLETPADAVFAALAAGRRLGRT 170
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLggiTLASEPPREALLAALEAARAAGVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLN------PAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPirdpaDAEAAARALQAGGARNVLVTLGARGVLALTAD 244
Cdd:COG0524  161 VSLDpnyrpaLWEPARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981689685 245 NAArHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:COG0524  236 EVV-HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
14-302 2.04e-57

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 186.78  E-value: 2.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   14 RVTVVGSLNMDLVVRAPRLPlpGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL----ICQLETPADAVFAALAAGRRLGR 169
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  170 T--VVLNPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAA 247
Cdd:pfam00294 159 FdpNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 981689685  248 RHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:pfam00294 239 HVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
19-312 3.40e-106

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: 311.46  E-value: 3.40e-106
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   19 GSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATS 98
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   99 AAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVLNPAPA 178
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  179 VAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNaARHYPAPAVQAV 258
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE-SKLIPAFKVKAV 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 981689685  259 DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAELA 312
Cdd:TIGR02152 240 DTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKGAQSSIPYLEEVE 293
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
14-307 3.22e-105

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: 308.71  E-value: 3.22e-105
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01174    1 KVVVVGSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTVVL 173
Cdd:cd01174   81 YVEVVVGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVIL 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 NPAPAVAPLPAgWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADnAARHYPAP 253
Cdd:cd01174  161 NPAPARPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGG-EVEHVPAF 238
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPT 307
Cdd:cd01174  239 KVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
PTZ00292 PTZ00292
ribokinase; Provisional
8-311 1.10e-76

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 237.33  E-value: 1.10e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   8 GAPRAGRVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEA 87
Cdd:PTZ00292  11 GGEAEPDVVVVGSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKR 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  88 EGIDCAGLATSAAASTGVALIVVDDA-SQNAIVIVAGGNGEVTP-DTIARHDAAIAAADVLICQLETPADAVFAALAAGR 165
Cdd:PTZ00292  91 NGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPqMVDAQTDNIQNICKYLICQNEIPLETTLDALKEAK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 166 RLGRTVVLNPAPAVAPLPAG----WLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLAL 241
Cdd:PTZ00292 171 ERGCYTVFNPAPAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIV 250
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 242 TADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:PTZ00292 251 EKENEPVHVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
PRK11142 PRK11142
ribokinase; Provisional
12-311 3.11e-76

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 235.53  E-value: 3.11e-76
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  12 AGRVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGID 91
Cdd:PRK11142   2 MGKLVVLGSINADHVLNLESFPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  92 CAGLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRTV 171
Cdd:PRK11142  82 TAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKV 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 172 VLNPAPAVAPLPAgWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARhYP 251
Cdd:PRK11142 162 ILNPAPARELPDE-LLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVWLSENGEGQR-VP 239
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 252 APAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:PRK11142 240 GFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEI 299
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
14-311 3.01e-67

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: 212.44  E-value: 3.01e-67
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:COG0524    1 DVLVIGEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL---ICQLETPADAVFAALAAGRRLGRT 170
Cdd:COG0524   81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLggiTLASEPPREALLAALEAARAAGVP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLN------PAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPirdpaDAEAAARALQAGGARNVLVTLGARGVLALTAD 244
Cdd:COG0524  161 VSLDpnyrpaLWEPARELLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVTLGAEGALLYTGG 235
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981689685 245 NAArHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPTLAEL 311
Cdd:COG0524  236 EVV-HVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPTREEV 301
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
14-302 2.04e-57

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 186.78  E-value: 2.04e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   14 RVTVVGSLNMDLVVRAPRLPlpGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTD 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL----ICQLETPADAVFAALAAGRRLGR 169
Cdd:pfam00294  79 YVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNGGT 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  170 T--VVLNPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAA 247
Cdd:pfam00294 159 FdpNLLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV 238
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 981689685  248 RHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:pfam00294 239 HVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
14-307 2.35e-37

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: 134.34  E-value: 2.35e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01945    1 RVLGVGLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 GLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQLETpadaVFAALAAGRRLGRTVVL 173
Cdd:cd01945   81 FIVVAPGARSPISSITDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPEA----ALHLAQEARARGIPIPL 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 NPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAAralqagGARNVLVTLGARGVLALTADNAARHYPAP 253
Cdd:cd01945  157 DLDGGGLRVLEELLPLADHAICSENFLRPNTGSADDEALELLASL------GIPFVAVTLGEAGCLWLERDGELFHVPAF 230
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIPT 307
Cdd:cd01945  231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
14-302 5.70e-33

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: 122.80  E-value: 5.70e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLP-LPGETLAGHAFaQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDC 92
Cdd:cd01942    1 DVAVVGHLNYDIILKVESFPgPFESVLVKDLR-REFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDT 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  93 AGLATSAAASTGVALIVVDDaSQNAIVIVA-GGNGEVTPDTIARHDAAIAaadvlICQLETPADAVFAALAAGRRlGRTV 171
Cdd:cd01942   80 SHVRVVDEDSTGVAFILTDG-DDNQIAYFYpGAMDELEPNDEADPDGLAD-----IVHLSSGPGLIELARELAAG-GITV 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 172 VL----NPAPAVAPLPAGWLPLVDYLIPNEVEAAAL---TGLPirdpadaeaaaRALQAGGARNVLVTLGARGVLALTAD 244
Cdd:cd01942  153 SFdpgqELPRLSGEELEEILERADILFVNDYEAELLkerTGLS-----------EAELASGVRVVVVTLGPKGAIVFEDG 221
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 981689685 245 NAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:cd01942  222 EEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
14-301 1.27e-28

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: 111.51  E-value: 1.27e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETlaghaFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01166    1 DVVTIGEVMVDLSPPGGGRLEQADS-----FRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTS 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 GLATSAAASTGVALIVVDDASQNAIVIVAGGN--GEVTPDtIARHDAAIAAADVLIC-----QLETPADAVFAALAAGRR 166
Cdd:cd01166   76 HVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSaaSRLTPE-DLDEAALAGADHLHLSgitlaLSESAREALLEALEAAKA 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 167 LGRTVV--------LNPAPAVAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALqagGARNVLVTLGARGV 238
Cdd:cd01166  155 RGVTVSfdlnyrpkLWSAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALAL---GVKAVVVKLGAEGA 231
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 981689685 239 LALTADnAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:cd01166  232 LVYTGG-GRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGD 293
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
34-301 7.33e-27

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: 106.95  E-value: 7.33e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  34 LPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSAAASTGVALIVVDDA 113
Cdd:cd01167   13 IPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDAD 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 114 SQNAIVIVAGGNGEVTPDTIARHDAAIAAADVLICQL----ETPADAVFAALAAGRRLGRTVVL---------NPAPAVA 180
Cdd:cd01167   93 GERSFEFYRGPAADLLLDTELNPDLLSEADILHFGSIalasEPSRSALLELLEAAKKAGVLISFdpnlrpplwRDEEEAR 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 181 PLPAGWLPLVDYLIPNEVEAAALTGLpirdpADAEAAARALQAGGARNVLVTLGARGVLALTADNAArHYPAPAVQAVDT 260
Cdd:cd01167  173 ERIAELLELADIVKLSDEELELLFGE-----EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGVG-EVPGIPVEVVDT 246
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 981689685 261 TAAGDTFIGGFAAQLAAG-------ADVDAAIRFAQRAAALSVTRAGA 301
Cdd:cd01167  247 TGAGDAFVAGLLAQLLSRgllaldeDELAEALRFANAVGALTCTKAGA 294
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
15-296 2.22e-26

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: 105.47  E-value: 2.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  15 VTVVGSLNMDLVVRAPRLPLPGETLAGHAFaQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAG 94
Cdd:cd01941    2 IVVIGAANIDLRGKVSGSLVPGTSNPGHVK-QSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  95 LATSAAaSTGVALIVVDdasQNAIVIVAGGN----GEVTPDTIARHDAAIAAADVLICQLETPADAVFAALAAGRRLGRT 170
Cdd:cd01941   81 IVFEGR-STASYTAILD---KDGDLVVALADmdiyELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLNPAPAV-APLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLA--LTADNAA 247
Cdd:cd01941  157 VAFEPTSAPkLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLssREGGVET 236
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 981689685 248 RHYPAPAVQAV-DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSV 296
Cdd:cd01941  237 KLFPAPQPETVvNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTL 286
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
48-313 9.17e-23

ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 96.03  E-value: 9.17e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  48 AGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSAAASTGVALIVVDDASQnaIVIVAGGNGE 127
Cdd:COG2870   55 PGG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTKTRVIAGGQQ--LLRLDFEDRF 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 128 VTPDTIARHDAAIAAAD-----VLICQ-----LETPADAVFAALAAgRRLGRTVVLNPAPAVAPLPAGwlplVDYLIPNE 197
Cdd:COG2870  132 PLSAELEARLLAALEAAlpevdAVILSdygkgVLTPELIQALIALA-RAAGKPVLVDPKGRDFSRYRG----ATLLTPNL 206
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 198 VEAAALTGLPIRDPADAEAAARAL-QAGGARNVLVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLA 276
Cdd:COG2870  207 KEAEAAVGIPIADEEELVAAAAELlERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIATLALALA 286
                        250       260       270
                 ....*....|....*....|....*....|....*..
gi 981689685 277 AGADVDAAIRFAQRAAALSVTRAGAQPsiPTLAELAD 313
Cdd:COG2870  287 AGASLEEAAELANLAAGIVVGKLGTAT--VSPEELLA 321
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
36-304 3.94e-21

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: 91.52  E-value: 3.94e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  36 GETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDcAGLATSAAASTGVALIVVDDASQ 115
Cdd:cd01168   42 EELLAKLPVKYIAGGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVD-TRYQVQPDGPTGTCAVLVTPDAE 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 116 NAIVIVAGGNGEVTPDTIARHDAAIAAadvlICQLE-----TPADAVFAALAAGRRLGRTVVLNPAPAVAP-----LPAG 185
Cdd:cd01168  121 RTMCTYLGAANELSPDDLDWSLLAKAK----YLYLEgylltVPPEAILLAAEHAKENGVKIALNLSAPFIVqrfkeALLE 196
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 186 WLPLVDYLIPNEVEAAALTGLpirDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGD 265
Cdd:cd01168  197 LLPYVDILFGNEEEAEALAEA---ETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGD 273
                        250       260       270
                 ....*....|....*....|....*....|....*....
gi 981689685 266 TFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPS 304
Cdd:cd01168  274 AFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
24-313 2.94e-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: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  24 DLVVRAPRLpLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAhGAALRAGLEAEGIDCAGLATsaAAST 103
Cdd:COG1105   11 DRTYEVDEL-EPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLGGFT-GEFIEELLDEEGIPTDFVPI--EGET 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 104 GVALIVVDDASQNAIVIVAGGNgEVTPDTIAR-----HDAAIAAADVLIC---QLETPADAVFAALAAGRRLGRTVVLNP 175
Cdd:COG1105   87 RINIKIVDPSDGTETEINEPGP-EISEEELEAllerlEELLKEGDWVVLSgslPPGVPPDFYAELIRLARARGAKVVLDT 165
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 176 APAVAPLPAGWLPlvdYLI-PNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADnAARHYPAPA 254
Cdd:COG1105  166 SGEALKAALEAGP---DLIkPNLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTED-GVYRAKPPK 241
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 981689685 255 VQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQpsIPTLAELAD 313
Cdd:COG1105  242 VEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTG--LPDREDVEE 298
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
14-300 1.20e-16

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: 78.62  E-value: 1.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCA 93
Cdd:cd01944    1 KVLVIGAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEIL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 gLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAAdVLIC--QLETPADAVFAALAAGRRL--GR 169
Cdd:cd01944   80 -LPPRGGDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYDY-VYLSgyTLASENASKVILLEWLEALpaGT 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 170 TVVLNPAPAVAPLPAGWLPLVDYLIP----NEVEAAALTGlpiRDPADAEAAARALQAGGARNVLVTLGARGVLALTADN 245
Cdd:cd01944  158 TLVFDPGPRISDIPDTILQALMAKRPiwscNREEAAIFAE---RGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDG 234
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 246 AARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:cd01944  235 NTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
229-312 1.46e-15

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 75.74  E-value: 1.46e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 229 VLVTLGARGVLALTADNAaRHYPAPAVQAVDTTAAGDTFIGGFAAQLAAG------ADVDAAIRFAQRAAALSVTRAGAQ 302
Cdd:PRK09434 216 LLVTLGAEGVLVHTRGQV-QHFPAPSVDPVDTTGAGDAFVAGLLAGLSQAglwtdeAELAEIIAQAQACGALATTAKGAM 294
                         90
                 ....*....|
gi 981689685 303 PSIPTLAELA 312
Cdd:PRK09434 295 TALPNRQELE 304
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
48-306 2.33e-15

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: 74.90  E-value: 2.33e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  48 AGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLaTSAAASTGVALIVVDDASQ------------ 115
Cdd:cd01172   39 LGG-AANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGI-VDEGRPTTTKTRVIARNQQllrvdreddspl 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 116 -------------------NAIVIVAGGNGEVTPDTIArhdaaiaaadvLICQLetpadavfaalaaGRRLGRTVVLNPA 176
Cdd:cd01172  117 saeeeqrlieriaerlpeaDVVILSDYGKGVLTPRVIE-----------ALIAA-------------ARELGIPVLVDPK 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 177 PAVAPLPAGwlplVDYLIPNEVEAAALTGLPIRDPADAEAAARALQ-AGGARNVLVTLGARGVLALTADNAARHYPAPAV 255
Cdd:cd01172  173 GRDYSKYRG----ATLLTPNEKEAREALGDEINDDDELEAAGEKLLeLLNLEALLVTLGEEGMTLFERDGEVQHIPALAK 248
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 981689685 256 QAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGAQPSIP 306
Cdd:cd01172  249 EVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
14-276 3.57e-15

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: 72.51  E-value: 3.57e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  14 RVTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGcvgadahgaalragleaegIDCA 93
Cdd:cd00287    1 RVLVVGSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG-------------------ADAV 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  94 gLATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTPDTIARHDAAiaaadvlicqletpadavfaalaagrrlgrtvvl 173
Cdd:cd00287   62 -VISGLSPAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGEELEKL---------------------------------- 106
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 174 npapavaplpagwLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPAP 253
Cdd:cd00287  107 -------------LPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAF 173
                        250       260
                 ....*....|....*....|...
gi 981689685 254 AVQAVDTTAAGDTFIGGFAAQLA 276
Cdd:cd00287  174 PVKVVDTTGAGDAFLAALAAGLA 196
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
23-300 2.06e-14

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: 72.18  E-value: 2.06e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  23 MDLVVRAPRLpLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADaHGAALRAGLEAEGID----------- 91
Cdd:cd01164   11 IDLTIELDQL-QPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPddfvevagetr 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  92 ----------------CAGLATSAAASTGVALIVVDDASQNAIVIVAGgngEVTPDTiarhdaaiaaadvlicqletPAD 155
Cdd:cd01164   89 invkikeedgteteinEPGPEISEEELEALLEKLKALLKKGDIVVLSG---SLPPGV--------------------PAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 156 AVFAALAAGRRLGRTVVLNPAPAVAPLPAGWLPlvdYLI-PNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLG 234
Cdd:cd01164  146 FYAELVRLAREKGARVILDTSGEALLAALAAKP---FLIkPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLG 222
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981689685 235 ARGVLALTADNAArHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:cd01164  223 ADGALLVTKDGVY-RASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
49-301 7.78e-12

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: 64.30  E-value: 7.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  49 GGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATsAAASTGVALIVVDDASQNAIVIVAGGNGEV 128
Cdd:cd01940   22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV-KEGENAVADVELVDGDRIFGLSNKGGVARE 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 129 TPDTIARHdaaiaaadvLICQLETPADAVFAALAAGRRLGRTVVLNPAPAVAPLPAGW-LPLVDYLIPNeVEAAALTGlP 207
Cdd:cd01940  101 HPFEADLE---------YLSQFDLVHTGIYSHEGHLEKALQALVGAGALISFDFSDRWdDDYLQLVCPY-VDFAFFSA-S 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 208 IRDPADAEAAARALQAGGARNVLVTLGARGVLALtADNAARHYPAPAVQAVDTTAAGDTFIGGF-AAQLAAGADVDAAIR 286
Cdd:cd01940  170 DLSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DGAVFYSVAPRPVEVVDTLGAGDSFIAGFlLSLLAGGTAIAEAMR 248
                        250
                 ....*....|....*
gi 981689685 287 FAQRAAALSVTRAGA 301
Cdd:cd01940  249 QGAQFAAKTCGHEGA 263
PLN02323 PLN02323
probable fructokinase
230-310 2.85e-09

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 57.32  E-value: 2.85e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 230 LVTLGARGVLALTADNAARhYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADV-------DAAIRFAQRAAALSVTRAGAQ 302
Cdd:PLN02323 234 LVTEGEEGCRYYTKDFKGR-VEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLledeerlREALRFANACGAITTTERGAI 312

                 ....*...
gi 981689685 303 PSIPTLAE 310
Cdd:PLN02323 313 PALPTKEA 320
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
224-297 3.41e-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: 3.41e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981689685 224 GGARNVLVTLGARGVLALTaDNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVT 297
Cdd:cd01937  182 TGVKEIIVTDGEEGGYIFD-GNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFIE 254
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
187-313 9.81e-09

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: 55.81  E-value: 9.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIR-------DPADAEAAARALQAGGARNVLVT-LGARGVLALTADNA-ARHYPA---PA 254
Cdd:cd01943  178 LPRVDVFSPNLEEAARLLGLPTSepssdeeKEAVLQALLFSGILQDPGGGVVLrCGKLGCYVGSADSGpELWLPAyhtKS 257
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 981689685 255 VQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGaqpsIPTLAELAD 313
Cdd:cd01943  258 TKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG----LPRLTKVEG 312
PLN02548 PLN02548
adenosine kinase
187-300 1.25e-08

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 55.49  E-value: 1.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALT------GLPIRDPADAEAAARALQAGGARNVLVTLGARGVLaLTADNAARHYPA---PAVQA 257
Cdd:PLN02548 201 LPYVDFLFGNETEARTFAkvqgweTEDVEEIALKISALPKASGTHKRTVVITQGADPTV-VAEDGKVKEFPViplPKEKL 279
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 981689685 258 VDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:PLN02548 280 VDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSG 322
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
15-301 1.63e-08

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: 54.73  E-value: 1.63e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  15 VTVVGSLNMDLVVRAPRLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIdcAG 94
Cdd:cd01947    2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KH 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  95 LATSAAASTGVALIVVDDASQNAIVIVAGGNGEVTP-------DTIARHDAAIAAADVLICqletpadavfaalaagrRL 167
Cdd:cd01947   80 TVAWRDKPTRKTLSFIDPNGERTITVPGERLEDDLKwpildegDGVFITAAAVDKEAIRKC-----------------RE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 168 GRTVVLNPAPAVAPLPAGW-LPLVDYLIPNEVEAAALTglpirdpadaeaAARALQAGGARNVLVTLGARGVLALTAdNA 246
Cdd:cd01947  143 TKLVILQVTPRVRVDELNQaLIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYPG-GR 209
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 247 ARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:cd01947  210 YNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGP 264
Ketohexokinase cd01939
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ...
229-300 1.95e-08

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: 54.72  E-value: 1.95e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 981689685 229 VLVTLGARGVLALTADNAARHYPA-PAVQAVDTTAAGDTFIGGFAAQLA-AGADVDAAIRFAQRAAALSVTRAG 300
Cdd:cd01939  215 LVCTWGDQGAGALGPDGEYVHSPAhKPIRVVDTLGAGDTFNAAVIYALNkGPDDLSEALDFGNRVASQKCTGVG 288
ribokinase_group_C cd01946
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ...
187-284 2.06e-08

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: 54.39  E-value: 2.06e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPirdpaDAEAAARALQAGGARNVLVTLGARGVLALTADN--AARHYPAPAVqaVDTTAAG 264
Cdd:cd01946  161 LAKVDVVIINDGEARQLTGAA-----NLVKAARLILAMGPKALIIKRGEYGALLFTDDGyfAAPAYPLESV--FDPTGAG 233
                         90       100
                 ....*....|....*....|
gi 981689685 265 DTFIGGFAAQLAAGADVDAA 284
Cdd:cd01946  234 DTFAGGFIGYLASQKDTSEA 253
PTZ00247 PTZ00247
adenosine kinase; Provisional
187-301 5.48e-08

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 53.49  E-value: 5.48e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALT---GLP---IRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAaRHYPAPAVQA--- 257
Cdd:PTZ00247 212 LPYVDILFGNEEEAKTFAkamKWDtedLKEIAARIAMLPKYSGTRPRLVVFTQGPEPTLIATKDGV-TSVPVPPLDQeki 290
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 981689685 258 VDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:PTZ00247 291 VDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGC 334
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
225-301 6.88e-08

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 52.82  E-value: 6.88e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 981689685 225 GARNVLVTLGARGVLALTADNAARHYPAPaVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:PRK09813 184 GAGVVIVTLGENGSIAWDGAQFWRQAPEP-VTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
6-272 1.36e-07

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 52.53  E-value: 1.36e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685   6 TGGAPRAGR---VTVVGSLNMDLVVRAPRLPLPG--------ETLAGHAFAQAAGGKGGN--QAVAAARLGAQVAMIGCV 72
Cdd:PLN02341  63 TEVGSAAGKeidVATLGNLCVDIVLPVPELPPPSreerkaymEELAASPPDKKSWEAGGNcnFAIAAARLGLRCSTIGHV 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  73 GADAHGAALRAGLEAEGIDCAGLA--------TSAAASTGVALIVVDDASQNAIVIVAGGNGEVT----PDTIARHDAAI 140
Cdd:PLN02341 143 GDEIYGKFLLDVLAEEGISVVGLIegtdagdsSSASYETLLCWVLVDPLQRHGFCSRADFGPEPAfswiSKLSAEAKMAI 222
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 141 AAADVLICQ----LETPADAVFAALAAGRRLGRTVVLNPAPAVAPLPAG----------WLPLVDYLIPNEVEAAALTGL 206
Cdd:PLN02341 223 RQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPRGKSLLVGtpderralehLLRMSDVLLLTSEEAEALTGI 302
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981689685 207 --PIRDPADAEAAARalqagGARNVLVTLGARGVLALTADNAARhYPAPAVQAVDTTAAGDTFIGGFA 272
Cdd:PLN02341 303 rnPILAGQELLRPGI-----RTKWVVVKMGSKGSILVTRSSVSC-APAFKVNVVDTVGCGDSFAAAIA 364
PRK09954 PRK09954
sugar kinase;
17-309 3.57e-07

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 51.09  E-value: 3.57e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  17 VVGSLNMDLVVRAPrLPLPGETLAGHAFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLA 96
Cdd:PRK09954  62 VVGAINMDIRGMAD-IRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCI 140
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  97 TSAAASTGVALIVvddASQNAIVIVAGGNG----EVTPDTIARHDAAIAAADVLI--CQLeTPADAVFAALAAGrrlGRT 170
Cdd:PRK09954 141 RLHGQSTSTYLAI---ANRQDETVLAINDThilqQLTPQLLNGSRDLIRHAGVVLadCNL-TAEALEWVFTLAD---EIP 213
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 171 VVLNPAPA-VAPLPAGWLPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARH 249
Cdd:PRK09954 214 VFVDTVSEfKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFL 293
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 250 YPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSvtRAGAQPSIPTLA 309
Cdd:PRK09954 294 LTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAIS--RASGSLNNPTLS 351
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
230-301 2.32e-06

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 48.67  E-value: 2.32e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 981689685 230 LVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGA 301
Cdd:PRK11316 229 LVTRSEQGMTLLQPGKAPLHLPTQAREVYDVTGAGDTVISVLAAALAAGNSLEEACALANAAAGVVVGKLGT 300
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
187-290 3.74e-06

Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.


Pssm-ID: 430062 [Multi-domain]  Cd Length: 246  Bit Score: 47.09  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLG------ARGVLALTADNAARHYPAPAVQAVDT 260
Cdd:pfam08543 117 LPLATLITPNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhlegeeAVVTDVLYDGGGFYTLEAPRIPTKNT 196
                          90       100       110
                  ....*....|....*....|....*....|
gi 981689685  261 TAAGDTFIGGFAAQLAAGADVDAAIRFAQR 290
Cdd:pfam08543 197 HGTGCTLSAAIAANLAKGLSLPEAVREAKE 226
PLN02630 PLN02630
pfkB-type carbohydrate kinase family protein
229-308 1.61e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178237  Cd Length: 335  Bit Score: 45.95  E-value: 1.61e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 229 VLVTLGARGVLALTADNAARHYPAPAVQaVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVTRAGaqpsIPTL 308
Cdd:PLN02630 206 VIVTNGKKGCRIYWKDGEMRVPPFPAIQ-VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG----IPKF 280
fruK PRK09513
1-phosphofructokinase; Provisional
195-297 1.67e-05

1-phosphofructokinase; Provisional


Pssm-ID: 181923 [Multi-domain]  Cd Length: 312  Bit Score: 45.84  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 195 PNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPaPAVQAVDTTAAGDTFIGGFAAQ 274
Cdd:PRK09513 186 PNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISLGAEGALWVNASGEWIAKP-PACDVVSTVGAGDSMVGGLIYG 264
                         90       100
                 ....*....|....*....|...
gi 981689685 275 LAAGADVDAAIRFAQRAAALSVT 297
Cdd:PRK09513 265 LLMRESSEHTLRLATAVSALAVS 287
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
37-312 1.75e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 45.96  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  37 ETLAGHAFAQAAGGKGGNQAVAAARLGAQ--------VAMIGCVGADAHGAALRAGLEAEGIDCAGlATSAAASTGVALI 108
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQsaagpalnVAMAGSVGSDPLGDFYRTKLRRANVHFLS-QPVKDGTTGTVIV 192
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 109 VVDDASQNAIVIVAGGNGEVTPDTIARHDAAIAAADVL---ICQLETPADAVFAALAAGRRLGRTVVLNPAPAVAPL--- 182
Cdd:PLN02813 193 LTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVLVVegyLWELPQTIEAIAQACEEAHRAGALVAVTASDVSCIErhr 272
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 183 PAGWLPL---VDYLIPNEVEAAALTGLPIRDPADAEAAARALQaggARNVLVTLGARGVLALTADNAARHYPAPAVqAVD 259
Cdd:PLN02813 273 DDFWDVMgnyADILFANSDEARALCGLGSEESPESATRYLSHF---CPLVSVTDGARGSYIGVKGEAVYIPPSPCV-PVD 348
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 981689685 260 TTAAGDTFIGGFAAQLAAGA-DVDAAIRFAQRAAALSVTRAGAQPSIPTLAELA 312
Cdd:PLN02813 349 TCGAGDAYAAGILYGLLRGVsDLRGMGELAARVAATVVGQQGTRLRVEDAVELA 402
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
187-290 2.80e-05

Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase is part of the Pathway/BioSystem: Thiamine biosynthesis


Pssm-ID: 440120 [Multi-domain]  Cd Length: 254  Bit Score: 44.64  E-value: 2.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVT----LGARGVLALTADNAARHYPAPAVQAVDTTA 262
Cdd:COG0351  124 LPLATVVTPNLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVKgghlPGDEAVDVLYDGDGVREFSAPRIDTGNTHG 203
                         90       100
                 ....*....|....*....|....*...
gi 981689685 263 AGDTFIGGFAAQLAAGADVDAAIRFAQR 290
Cdd:COG0351  204 TGCTLSSAIAALLAKGLDLEEAVREAKE 231
PRK10294 PRK10294
6-phosphofructokinase 2; Provisional
195-300 5.84e-05

6-phosphofructokinase 2; Provisional


Pssm-ID: 182361 [Multi-domain]  Cd Length: 309  Bit Score: 44.00  E-value: 5.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 195 PNEVEAAALTGLPIRD-PADAEAAARALQAGGARNVLVTLGARGVLALTADNAARHYPAPaVQAVDTTAAGDTFIGGFAA 273
Cdd:PRK10294 186 PNQKELSALVNRDLTQpDDVRKAAQELVNSGKAKRVVVSLGPQGALGVDSENCIQVVPPP-VKSQSTVGAGDSMVGAMTL 264
                         90       100
                 ....*....|....*....|....*..
gi 981689685 274 QLAAGADVDAAIRFAQRAAALSVTRAG 300
Cdd:PRK10294 265 KLAENASLEEMVRFGVAAGSAATLNQG 291
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
187-311 7.58e-05

Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis


Pssm-ID: 441841 [Multi-domain]  Cd Length: 272  Bit Score: 43.60  E-value: 7.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVT--------LGARGVLALTADnAARHYPAPAVqAV 258
Cdd:COG2240  136 VPLADIITPNLTELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpADKIGNLAVTAD-GAWLVETPLL-PF 213
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 981689685 259 DTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRA--AALSVTRAGAQPSIPTLAEL 311
Cdd:COG2240  214 SPNGTGDLFAALLLAHLLRGKSLEEALERAAAFvyEVLERTAAAGSDELLLEAAL 268
PLN02323 PLN02323
probable fructokinase
43-108 8.57e-05

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 43.46  E-value: 8.57e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 981689685  43 AFAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDCAGLATSAAASTGVALI 108
Cdd:PLN02323  37 AFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFV 102
PRK09850 PRK09850
pseudouridine kinase; Provisional
15-297 1.49e-04

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 42.67  E-value: 1.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  15 VTVVGSLNMDLVvraprlplpGETLAGHAFAQA--------AGGKGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLE 86
Cdd:PRK09850   7 VVIIGSANIDVA---------GYSHESLNYADSnpgkikftPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTN 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685  87 AEGI---DC---AGLATSAAAS----TGVALIVVDDAS-----------------QNAIVIVAGGNgeVTPDTIARHDAA 139
Cdd:PRK09850  78 QSGVyvdKClivPGENTSSYLSlldnTGEMLVAINDMNisnaitaeylaqhrefiQRAKVIVADCN--ISEEALAWILDN 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 140 IAAADVLIcqleTPADAVFAALAAGRrlgrtvvlnpapavaplpagwLPLVDYLIPNEVEAAALTGLPIRDPADAEAAAR 219
Cdd:PRK09850 156 AANVPVFV----DPVSAWKCVKVRDR---------------------LNQIHTLKPNRLEAETLSGIALSGREDVAKVAA 210
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 981689685 220 ALQAGGARNVLVTLGARGVLALTADNAARHYPAPAVQAVDTTAAGDTFIGGFAAQLAAGADVDAAIRFAQRAAALSVT 297
Cdd:PRK09850 211 WFHQHGLNRLVLSMGGDGVYYSDISGESGWSAPIKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
PRK06427 PRK06427
bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed
187-288 5.27e-04

bifunctional hydroxy-methylpyrimidine kinase/ hydroxy-phosphomethylpyrimidine kinase; Reviewed


Pssm-ID: 180561 [Multi-domain]  Cd Length: 266  Bit Score: 40.88  E-value: 5.27e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAG-GARNVLVTLGARGVLALTAD-----NAARHYPAPAVQAVDT 260
Cdd:PRK06427 131 LPLATLITPNLPEAEALTGLPIADTEDEMKAAARALHAlGCKAVLIKGGHLLDGEESVDwlfdgEGEERFSAPRIPTKNT 210
                         90       100
                 ....*....|....*....|....*...
gi 981689685 261 TAAGDTFIGGFAAQLAAGADVDAAIRFA 288
Cdd:PRK06427 211 HGTGCTLSAAIAAELAKGASLLDAVQTA 238
PRK11316 PRK11316
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ...
48-92 2.23e-03

bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;


Pssm-ID: 183085 [Multi-domain]  Cd Length: 473  Bit Score: 39.43  E-value: 2.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 981689685  48 AGGkGGNQAVAAARLGAQVAMIGCVGADAHGAALRAGLEAEGIDC 92
Cdd:PRK11316  50 PGG-AANVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKC 93
PLN02543 PLN02543
pfkB-type carbohydrate kinase family protein
44-81 3.02e-03

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215299  Cd Length: 496  Bit Score: 39.12  E-value: 3.02e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 981689685  44 FAQAAGGKGGNQAVAAARLGAQVAMIGCVGADAHGAAL 81
Cdd:PLN02543 167 FARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEEL 204
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
187-289 6.87e-03

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 37.35  E-value: 6.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 981689685 187 LPLVDYLIPNEVEAAALTGLPIRDPADAEAAARALQAGGARNVLVT----LGARGVLALTADNAARHYPAPAVQAVDTTA 262
Cdd:PRK12413 127 FPYVTVITPNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKggnrLSQKKAIDLFYDGKEFVILESPVLEKNNIG 206
                         90       100
                 ....*....|....*....|....*..
gi 981689685 263 AGDTFIGGFAAQLAAGADVDAAIRFAQ 289
Cdd:PRK12413 207 AGCTFASSIASQLVKGKSPLEAVKNSK 233
 
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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