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Conserved domains on  [gi|755511713|ref|XP_011239073|]
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ribokinase isoform X1 [Mus musculus]

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 ...
 23-266 8.81e-119

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: 342.66  E-value: 8.81e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713   23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  183 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 262
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238


                  ....
gi 755511713  263 VDTT 266
Cdd:TIGR02152 239 VDTT 242
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 23-266 8.81e-119

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: 342.66  E-value: 8.81e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713   23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  183 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 262
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238


                  ....
gi 755511713  263 VDTT 266
Cdd:TIGR02152 239 VDTT 242
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 23-266 3.48e-108

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: 315.64  E-value: 3.48e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01174    6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:cd01174   86 VGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILNPAPA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 183 MADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSqaEPVPKHIPTEAVKA 262
Cdd:cd01174  166 RPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS--GGEVEHVPAFKVKA 242


                 ....
gi 755511713 263 VDTT 266
Cdd:cd01174  243 VDTT 246
PTZ00292 PTZ00292
ribokinase; Provisional
 23-266 6.68e-85

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 257.74  E-value: 6.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:PTZ00292  22 GSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNE-GQNIIVIVAGANLFLNSEDLKKAASVI-SRAKVMICQLEISPAASLEALTMARRSGVKTLFNPA 180
Cdd:PTZ00292 102 ENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYTVFNPA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 181 PAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQaEPVPKHIP 256
Cdd:PTZ00292 182 PAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEK-ENEPVHVP 260

                        250
                 ....*....|
gi 755511713 257 TEAVKAVDTT 266
Cdd:PTZ00292 261 GKRVKAVDTT 270
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 23-266 1.16e-65

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: 207.81  E-value: 1.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:COG0524    6 GEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGVRRD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAAsvISRAKVMICQL-----EISPAASLEALTMARRSGVKTLF 177
Cdd:COG0524   86 PGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAGVPVSL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 178 NPA------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPV 251
Cdd:COG0524  164 DPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238

                        250
                 ....*....|....*
gi 755511713 252 pkHIPTEAVKAVDTT 266
Cdd:COG0524  239 --HVPAFPVEVVDTT 251
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 23-266 9.19e-49

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 164.05  E-value: 9.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713   23 GSCMTDLVSLTSRLPktGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:pfam00294   6 GEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVM----ICQLEiSPAASLEALTMARRSGVKT--- 175
Cdd:pfam00294  84 EDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLG-LPEATLEELIEAAKNGGTFdpn 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  176 LFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHI 255
Cdd:pfam00294 163 LLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV-HVP 241

                         250
                  ....*....|.
gi 755511713  256 PTEAVKAVDTT 266
Cdd:pfam00294 242 AVPKVKVVDTT 252
 
Name Accession Description Interval E-value
D_ribokin_bact TIGR02152
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ...
 23-266 8.81e-119

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: 342.66  E-value: 8.81e-119
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713   23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:TIGR02152   1 GSINMDLVLRTDRLPKPGETVHGHSFQIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTV 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:TIGR02152  81 KDTPTGTAFITVDDTGENRIVVVAGANAELTPEDIDAAEALIAESDIVLLQLEIPLETVLEAAKIAKKHGVKVILNPAPA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  183 MADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKA 262
Cdd:TIGR02152 161 IKDLDDELLSLVDIITPNETEAEILTGIEVTDEEDAEKAAEKLLEKGVKNVIITLGSKGALLVSKDE--SKLIPAFKVKA 238


                  ....
gi 755511713  263 VDTT 266
Cdd:TIGR02152 239 VDTT 242
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 23-266 3.48e-108

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: 315.64  E-value: 3.48e-108
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01174    6 GSINVDLVTRVDRLPKPGETVLGSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:cd01174   86 VGAPTGTAVITVDESGENRIVVVPGANGELTPADVDAALELIAAADVLLLQLEIPLETVLAALRAARRAGVTVILNPAPA 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 183 MADLDPqFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSqaEPVPKHIPTEAVKA 262
Cdd:cd01174  166 RPLPAE-LLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLAS--GGEVEHVPAFKVKA 242


                 ....
gi 755511713 263 VDTT 266
Cdd:cd01174  243 VDTT 246
PTZ00292 PTZ00292
ribokinase; Provisional
 23-266 6.68e-85

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 257.74  E-value: 6.68e-85
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:PTZ00292  22 GSSNTDLIGYVDRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRT 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNE-GQNIIVIVAGANLFLNSEDLKKAASVI-SRAKVMICQLEISPAASLEALTMARRSGVKTLFNPA 180
Cdd:PTZ00292 102 ENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIqNICKYLICQNEIPLETTLDALKEAKERGCYTVFNPA 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 181 PAMADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQaEPVPKHIP 256
Cdd:PTZ00292 182 PAPKLAEVEiikpFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANGCLIVEK-ENEPVHVP 260

                        250
                 ....*....|
gi 755511713 257 TEAVKAVDTT 266
Cdd:PTZ00292 261 GKRVKAVDTT 270
PRK11142 PRK11142
ribokinase; Provisional
 36-266 1.96e-66

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 209.73  E-value: 1.96e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  36 LPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVN 115
Cdd:PRK11142  22 FPRPGETLTGRHYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVN 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 116 NEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVMICQLEiSPAAS-LEALTMARRSGVKTLFNPAPAMAdLDPQFYTLS 194
Cdd:PRK11142 102 DEGENSIGIHAGANAALTPALVEAHRELIANADALLMQLE-TPLETvLAAAKIAKQHGTKVILNPAPARE-LPDELLALV 179

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511713 195 SIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGcVILSQAEPvPKHIPTEAVKAVDTT 266
Cdd:PRK11142 180 DIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRG-VWLSENGE-GQRVPGFRVQAVDTI 249
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 23-266 1.16e-65

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: 207.81  E-value: 1.16e-65
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:COG0524    6 GEALVDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSGVRRD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAAsvISRAKVMICQL-----EISPAASLEALTMARRSGVKTLF 177
Cdd:COG0524   86 PGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEAL--LAGADILHLGGitlasEPPREALLAALEAARAAGVPVSL 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 178 NPA------PAMADLDPQFYTLSSIFCCNESEAEILTGHavsdpTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPV 251
Cdd:COG0524  164 DPNyrpalwEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLYTGGEVV 238

                        250
                 ....*....|....*
gi 755511713 252 pkHIPTEAVKAVDTT 266
Cdd:COG0524  239 --HVPAFPVEVVDTT 251
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 23-266 9.19e-49

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 164.05  E-value: 9.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713   23 GSCMTDLVSLTSRLPktGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:pfam00294   6 GEANIDLIGNVEGLP--GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVID 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  103 RDAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLKKAASVISRAKVM----ICQLEiSPAASLEALTMARRSGVKT--- 175
Cdd:pfam00294  84 EDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLENADLLyisgSLPLG-LPEATLEELIEAAKNGGTFdpn 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  176 LFNPAPAMADLDPQFYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHI 255
Cdd:pfam00294 163 LLDPLGAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGEV-HVP 241

                         250
                  ....*....|.
gi 755511713  256 PTEAVKAVDTT 266
Cdd:pfam00294 242 AVPKVKVVDTT 252
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 23-266 8.69e-27

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: 106.12  E-value: 8.69e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVsltsrlPKTGETIHGHEFF-IGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQ 101
Cdd:cd01166    6 GEVMVDLS------PPGGGRLEQADSFrKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 102 TRDAATGTASIIV--NNEGQNIIVIVAGANLFLNSEDLKKAAsvISRAK-VMICqlEISPAAS-------LEALTMARRS 171
Cdd:cd01166   80 DPGRPTGLYFLEIgaGGERRVLYYRAGSAASRLTPEDLDEAA--LAGADhLHLS--GITLALSesarealLEALEAAKAR 155

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 172 GVKTLF--NPAPAMADLD------PQFYTLSSIFCCNESEAEILTGHAvSDPTTAGKAAMilLERGCQVVVITLGASGCV 243
Cdd:cd01166  156 GVTVSFdlNYRPKLWSAEearealEELLPYVDIVLPSEEEAEALLGDE-DPTDAAERALA--LALGVKAVVVKLGAEGAL 232

                        250       260
                 ....*....|....*....|...
gi 755511713 244 ILSQAEPVpkHIPTEAVKAVDTT 266
Cdd:cd01166  233 VYTGGGRV--FVPAYPVEVVDTT 253
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 53-266 1.74e-26

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: 105.77  E-value: 1.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTrDAATGTASIIVNNEGQNIIVIVAGANLFL 132
Cdd:cd01168   55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRYQVQP-DGPTGTCAVLVTPDAERTMCTYLGAANEL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 133 NSEDLKKAAsvISRAKVMIC---QLEISPAASLEALTMARRSGVKTLFN-PAPAMadldPQFYT--LSSIFC------CN 200
Cdd:cd01168  134 SPDDLDWSL--LAKAKYLYLegyLLTVPPEAILLAAEHAKENGVKIALNlSAPFI----VQRFKeaLLELLPyvdilfGN 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755511713 201 ESEAEILTGHAVSDPTTAGKAamiLLERGCQVVVITLGASGCVILSQAE--PVPkhiPTEAVKAVDTT 266
Cdd:cd01168  208 EEEAEALAEAETTDDLEAALK---LLALRCRIVVITQGAKGAVVVEGGEvyPVP---AIPVEKIVDTN 269
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 53-266 3.27e-23

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


Pssm-ID: 238572 [Multi-domain]  Cd Length: 295  Bit Score: 96.55  E-value: 3.27e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAG--ANL 130
Cdd:cd01167   28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDPAAPTTLAFVTLDADGERSFEFYRGpaADL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 131 FLNSEDLKkaaSVISRAK-VMICQL----EISPAASLEALTMARRSGVKTLF----------NPAPAMADLdPQFYTLSS 195
Cdd:cd01167  108 LLDTELNP---DLLSEADiLHFGSIalasEPSRSALLELLEAAKKAGVLISFdpnlrpplwrDEEEARERI-AELLELAD 183

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755511713 196 IFCCNESEAEILTGHavSDPTtagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTT 266
Cdd:cd01167  184 IVKLSDEELELLFGE--EDPE---EIAALLLLFGLKLVLVTRGADGALLYTKGGVG--EVPGIPVEVVDTT 247
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 23-266 1.81e-21

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: 91.60  E-value: 1.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01942    6 GHLNYDIILKVESFPGPFESVLVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVV 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNEGQNIIVIVAGANLFLnseDLKKAASVISRAKVmicqLEISPAASLEALTMARRSGVKTL-FNPAP 181
Cdd:cd01942   86 DEDSTGVAFILTDGDDNQIAYFYPGAMDEL---EPNDEADPDGLADI----VHLSSGPGLIELARELAAGGITVsFDPGQ 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 182 AMADLD----PQFYTLSSIFCCNESEAEIL---TGhaVSDPTTAgkaamilleRGCQVVVITLGASGCVILSQAEPVpKH 254
Cdd:cd01942  159 ELPRLSgeelEEILERADILFVNDYEAELLkerTG--LSEAELA---------SGVRVVVVTLGPKGAIVFEDGEEV-EV 226

                        250
                 ....*....|..
gi 755511713 255 IPTEAVKAVDTT 266
Cdd:cd01942  227 PAVPAVKVVDTT 238
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 23-266 2.86e-19

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: 85.42  E-value: 2.86e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQT 102
Cdd:cd01945    6 GLAVLDLIYLVASFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVA 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 RDAATGTASIIVNNEGQNIIVIVAG----ANLFLNSEDLKKAASVI--SRAkvmicqleisPAASLEALTMARRSGVktl 176
Cdd:cd01945   86 PGARSPISSITDITGDRATISITAIdtqaAPDSLPDAILGGADAVLvdGRQ----------PEAALHLAQEARARGI--- 152

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 177 fnpaPAMADLDPQF-------YTLSSIFCCNESEAEILTGhaVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAE 249
Cdd:cd01945  153 ----PIPLDLDGGGlrvleelLPLADHAICSENFLRPNTG--SADD----EALELLASLGIPFVAVTLGEAGCLWLERDG 222

                        250
                 ....*....|....*..
gi 755511713 250 PVpKHIPTEAVKAVDTT 266
Cdd:cd01945  223 EL-FHVPAFPVEVVDTT 238
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 52-263 5.19e-18

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: 81.98  E-value: 5.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  52 FGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQ---NHISTEFtyqtRDAATGTASIIVNNEGqNIIVIVAGA 128
Cdd:cd01941   34 PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKaglNVRGIVF----EGRSTASYTAILDKDG-DLVVALADM 108

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 129 NLF--LNSEDLKKAASVISRAKVMICQLEISPAASLEALTMARRSGVKTLFNPA-----PAMADLDPQFYTLSsifcCNE 201
Cdd:cd01941  109 DIYelLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAFEPTsapklKKLFYLLHAIDLLT----PNR 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511713 202 SEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPV-PKHIPTEAVKAV 263
Cdd:cd01941  185 AELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVeTKLFPAPQPETV 247
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 54-266 2.34e-14

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: 71.82  E-value: 2.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  54 GKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEF-TYQTRDAATGTAsiivnnegqniiVIVAGANLF- 131
Cdd:cd01172   40 GGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGiVDEGRPTTTKTR------------VIARNQQLLr 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 132 LNSED------------LKKAASVISRAKVMIcqLE------ISPAASLEALTMARRSGVKTLFNPAPamadLDPQFYTL 193
Cdd:cd01172  108 VDREDdsplsaeeeqrlIERIAERLPEADVVI--LSdygkgvLTPRVIEALIAAARELGIPVLVDPKG----RDYSKYRG 181

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511713 194 SSIFCCNESEAEILTGHAVSDPTTAGKAAMILLER-GCQVVVITLGASGCVILSQAEPvPKHIPTEAVKAVDTT 266
Cdd:cd01172  182 ATLLTPNEKEAREALGDEINDDDELEAAGEKLLELlNLEALLVTLGEEGMTLFERDGE-VQHIPALAKEVYDVT 254
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 23-266 5.42e-13

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: 66.35  E-value: 5.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVckvgndsfgndyienlkqnhisteftyqt 102
Cdd:cd00287    6 GSLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLV----------------------------- 56

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 rdaatgTASIIVNNEGQniivivaganlflnsedlkkaasvisrakvmicqleISPAASLEALTMARRSGVKTLFNPAPA 182
Cdd:cd00287   57 ------GADAVVISGLS------------------------------------PAPEAVLDALEEARRRGVPVVLDPGPR 94

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 183 MADLDPQ----FYTLSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpKHIPTE 258
Cdd:cd00287   95 AVRLDGEelekLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTE-VHVPAF 173


                 ....*...
gi 755511713 259 AVKAVDTT 266
Cdd:cd00287  174 PVKVVDTT 181
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 23-265 4.48e-11

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: 62.05  E-value: 4.48e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  23 GSCMTDLVSLTSRLPKTGETIHGHEFFIGFGGkGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHIstEFTYQT 102
Cdd:cd01944    6 GAAVVDIVLDVDKLPASGGDIEAKSKSYVIGG-GFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGI--EILLPP 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 103 R-DAATGTASIIVNNEGQNIIVIVAGANLFLNSEDLkKAASVISRAKVMICQLEI-SPAASLEALT---MARRSGVKTLF 177
Cdd:cd01944   83 RgGDDGGCLVALVEPDGERSFISISGAEQDWSTEWF-ATLTVAPYDYVYLSGYTLaSENASKVILLewlEALPAGTTLVF 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 178 NPAPAMADLDPQFYT----LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGcqvVVITLGASGCVILSQAEPvPK 253
Cdd:cd01944  162 DPGPRISDIPDTILQalmaKRPIWSCNREEAAIFAERGDPAAEASALRIYAKTAAP---VVVRLGSNGAWIRLPDGN-TH 237

                        250
                 ....*....|..
gi 755511713 254 HIPTEAVKAVDT 265
Cdd:cd01944  238 IIPGFKVKAVDT 249
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 53-266 8.17e-11

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 61.49  E-value: 8.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQtrDAATGTASIIV--NNEGQN--IIVIVAGA 128
Cdd:PRK09434  28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRL--DPAHRTSTVVVdlDDQGERsfTFMVRPSA 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 129 NLFLNSEDLK--KAASVISRAKVMICQlEISPAASLEALTMARRSGVKTLFNP---------APAMADLDPQFYTLSSIF 197
Cdd:PRK09434 106 DLFLQPQDLPpfRQGEWLHLCSIALSA-EPSRSTTFEAMRRIKAAGGFVSFDPnlredlwqdEAELRECLRQALALADVV 184

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511713 198 CCNESEAEILTGhavSDPTTAGKAAmILLERGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKAVDTT 266
Cdd:PRK09434 185 KLSEEELCFLSG---TSQLEDAIYA-LADRYPIALLLVTLGAEGVLVHTRGQ--VQHFPAPSVDPVDTT 247
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 54-265 2.29e-10

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 61.00  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  54 GKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTeftyQTRDAATGTASIiVNNEGQNIIVIV----AGAN 129
Cdd:PLN02341 120 GGNCNFAIAAARLGLRCSTIGHVGDEIYGKFLLDVLAEEGISV----VGLIEGTDAGDS-SSASYETLLCWVlvdpLQRH 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 130 LFLNSEDLKK-------------AASVISRAKVMICQ----LEISPAASLEALTMARRSGVKTLFNPAP---AMADLDP- 188
Cdd:PLN02341 195 GFCSRADFGPepafswisklsaeAKMAIRQSKALFCNgyvfDELSPSAIASAVDYAIDVGTAVFFDPGPrgkSLLVGTPd 274

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 189 ------QFYTLSSIFCCNESEAEILTGhaVSDPTTAGKAamiLLERGC--QVVVITLGASGCVILSQAEPVPKhiPTEAV 260
Cdd:PLN02341 275 erraleHLLRMSDVLLLTSEEAEALTG--IRNPILAGQE---LLRPGIrtKWVVVKMGSKGSILVTRSSVSCA--PAFKV 347


                 ....*
gi 755511713 261 KAVDT 265
Cdd:PLN02341 348 NVVDT 352
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 28-266 6.16e-10

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: 58.58  E-value: 6.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  28 DLVSLTSRLPKTGETIHGHEFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHIstEFTYQTRDAAT 107
Cdd:cd01947   11 DIFLSLDAPPQPGGISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGD--KHTVAWRDKPT 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 108 GTASIIVNNEGQNIIVIVAGanlflNSEDLKKAASVISRAKVMIcqleISPAASLEALTMARRSGVKTLFNPAPAMADLD 187
Cdd:cd01947   89 RKTLSFIDPNGERTITVPGE-----RLEDDLKWPILDEGDGVFI----TAAAVDKEAIRKCRETKLVILQVTPRVRVDEL 159

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511713 188 PQFYTLSSIFCCNESEAEILtghavsdpTTAGKAAMilleRGCQVVVITLGASGCVILSQAEpvPKHIPTEAVKAVDTT 266
Cdd:cd01947  160 NQALIPLDILIGSRLDPGEL--------VVAEKIAG----PFPRYLIVTEGELGAILYPGGR--YNHVPAKKAKVPDST 224
PLN02323 PLN02323
probable fructokinase
 53-266 1.00e-09

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 58.48  E-value: 1.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIV--AGANL 130
Cdd:PLN02323  43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYrnPSADM 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 131 FLNSEDLKKaaSVISRAKV-------MICqlEISPAASLEALTMARRSGVKTLFNP---------APAMADLDPQFYTLS 194
Cdd:PLN02323 123 LLRESELDL--DLIRKAKIfhygsisLIT--EPCRSAHLAAMKIAKEAGALLSYDPnlrlplwpsAEAAREGIMSIWDEA 198

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511713 195 SIFCCNESEAEILTGhavSDPTTaGKAAMILLERGCQVVVITLGASGCVILSQAepVPKHIPTEAVKAVDTT 266
Cdd:PLN02323 199 DIIKVSDEEVEFLTG---GDDPD-DDTVVKLWHPNLKLLLVTEGEEGCRYYTKD--FKGRVEGFKVKAVDTT 264
PRK09850 PRK09850
pseudouridine kinase; Provisional
 53-241 5.10e-07

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 50.37  E-value: 5.10e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIV-AGANLF 131
Cdd:PRK09850  40 GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINdMNISNA 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 132 LNSEDLKKAASVISRAKVMICQLEISPAASLEALTMArrSGVKTLFNPAPA-----MADLDPQFYTLSSifccNESEAEI 206
Cdd:PRK09850 120 ITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNA--ANVPVFVDPVSAwkcvkVRDRLNQIHTLKP----NRLEAET 193

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755511713 207 LTGHAVSDPTTAGKAAMILLERGCQVVVITLGASG 241
Cdd:PRK09850 194 LSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG 228
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
200-266 1.73e-06

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 48.59  E-value: 1.73e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755511713 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTT 266
Cdd:COG1105  184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGVY--RAKPPKVEVVSTV 248
PTZ00247 PTZ00247
adenosine kinase; Provisional
 53-275 5.51e-06

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 47.33  E-value: 5.51e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQC-VQAARLGAKAAIVCKVG---NDSFGNDYIENLKQNHISTEFTYqTRDAATGT-ASIIVNNEGQNIIVIVAG 127
Cdd:PTZ00247  62 GGSALNTArVAQWMLQAPKGFVCYVGcvgDDRFAEILKEAAEKDGVEMLFEY-TTKAPTGTcAVLVCGKERSLVANLGAA 140

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 128 ANL---FLNSEDLKKAasvISRAKVMICQ---LEISPAASLEALTMARRSGVKTLFN-PAP-AMADLDPQFYTL---SSI 196
Cdd:PTZ00247 141 NHLsaeHMQSHAVQEA---IKTAQLYYLEgffLTVSPNNVLQVAKHARESGKLFCLNlSAPfISQFFFERLLQVlpyVDI 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 197 FCCNESEAEILtGHAVSDPTT-----AGKAAMILLERGCQ--VVVITLGASGCVILSQAE----PVPkhiPTEAVKAVDT 265
Cdd:PTZ00247 218 LFGNEEEAKTF-AKAMKWDTEdlkeiAARIAMLPKYSGTRprLVVFTQGPEPTLIATKDGvtsvPVP---PLDQEKIVDT 293

                        250
                 ....*....|
gi 755511713 266 TflTLGDVLC 275
Cdd:PTZ00247 294 N--GAGDAFV 301
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 53-266 1.47e-05

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: 45.42  E-value: 1.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTyQTRDAATGTASIIVNNeGQNIIV-----IVAG 127
Cdd:cd01940   22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD-GDRIFGlsnkgGVAR 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 128 ANLFlnSEDLKKaasvISRAKVMICQLEISPAASLEALTMARRSGVKTLF----NPAPAMADLDPQFYTLSSIFCCNESE 203
Cdd:cd01940  100 EHPF--EADLEY----LSQFDLVHTGIYSHEGHLEKALQALVGAGALISFdfsdRWDDDYLQLVCPYVDFAFFSASDLSD 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755511713 204 AEIltghavsdpttaGKAAMILLERGCQVVVITLGASGCVILSQAEPVPKHIptEAVKAVDTT 266
Cdd:cd01940  174 EEV------------KAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAP--RPVEVVDTL 222
PLN02813 PLN02813
pfkB-type carbohydrate kinase family protein
 41-265 2.64e-05

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215434 [Multi-domain]  Cd Length: 426  Bit Score: 45.18  E-value: 2.64e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  41 ETIHGHEFFIGFGGKGANQCVQAARLGAKA--------AIVCKVGNDSFGNDYIENLKQNHIstEFTYQ-TRDAATGTAS 111
Cdd:PLN02813 114 RALDGCSYKASAGGSLSNTLVALARLGSQSaagpalnvAMAGSVGSDPLGDFYRTKLRRANV--HFLSQpVKDGTTGTVI 191

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 112 IIVNNEGQNIIVIVAGANLFLN-SEDLkkaASVISRAKVMIC-----QLEISPAASLEALTMARRSGVKTlfnpapAMAD 185
Cdd:PLN02813 192 VLTTPDAQRTMLSYQGTSSTVNyDSCL---ASAISKSRVLVVegylwELPQTIEAIAQACEEAHRAGALV------AVTA 262

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 186 LDP--------QFYTL----SSIFCCNESEAEILTGHAVSDpttAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpk 253
Cdd:PLN02813 263 SDVscierhrdDFWDVmgnyADILFANSDEARALCGLGSEE---SPESATRYLSHFCPLVSVTDGARGSYIGVKGEAV-- 337

                        250
                 ....*....|..
gi 755511713 254 HIPTEAVKAVDT 265
Cdd:PLN02813 338 YIPPSPCVPVDT 349
PLN02379 PLN02379
pfkB-type carbohydrate kinase family protein
 200-266 2.40e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 178005 [Multi-domain]  Cd Length: 367  Bit Score: 42.09  E-value: 2.40e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755511713 200 NESEA-EILTGHAVSDPttagKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIP-TEAVKAVDTT 266
Cdd:PLN02379 239 NEDEArELLRGEQESDP----EAALEFLAKYCNWAVVTLGSKGCIARHGKEVV--RVPaIGETNAVDAT 301
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 200-241 4.26e-04

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: 41.36  E-value: 4.26e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 755511713 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVITLGASG 241
Cdd:cd01164  184 NREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADG 225
PLN02543 PLN02543
pfkB-type carbohydrate kinase family protein
 47-179 7.64e-04

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215299  Cd Length: 496  Bit Score: 40.66  E-value: 7.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  47 EFFIGFGGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIV--NNEGQNIIVI 124
Cdd:PLN02543 166 EFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIkfRDGGKMVAET 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755511713 125 VAGAnlflnSEDLKKAA----SVISRAKVMICQLEISPAASLE-----ALTMARRSGVKTLFNP 179
Cdd:PLN02543 246 VKEA-----AEDSLLASelnlAVLKEARMFHFNSEVLTSPSMQstlfrAIELSKKFGGLIFFDL 304
ThiD COG0351
Hydroxymethylpyrimidine/phosphomethylpyrimidine kinase [Coenzyme transport and metabolism]; ...
 200-236 1.33e-03

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: 39.64  E-value: 1.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 755511713 200 NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 236
Cdd:COG0351  133 NLPEAEALLGIEITTLDDMREAAKALLELGAKAVLVK 169
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 181-236 1.79e-03

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: 39.36  E-value: 1.79e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 181 PAMADLDPQFYTLSSIFCC--------------NESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 236
Cdd:COG2240  112 PVMGDNGKGYYVFPGIAEFimrrlvpladiitpNLTELALLTGRPYETLEEALAAARALLALGPKIVVVT 181
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 199-236 4.72e-03

Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.


Pssm-ID: 238578 [Multi-domain]  Cd Length: 254  Bit Score: 37.95  E-value: 4.72e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 755511713 199 CNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 236
Cdd:cd01173  142 PNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVT 179
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 203-236 4.82e-03

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: 37.85  E-value: 4.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 755511713  203 EAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 236
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIK 162
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 193-236 6.42e-03

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 37.75  E-value: 6.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 755511713 193 LSSIFCCNESEAEILTGHAVSDPTTAGKAAMILLERGCQVVVIT 236
Cdd:PTZ00344 139 YADVITPNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVIT 182
PRK09954 PRK09954
sugar kinase;
53-238 6.96e-03

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 37.60  E-value: 6.96e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVGNDSFGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAGANL-F 131
Cdd:PRK09954  93 GGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDETVLAINDTHILqQ 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 132 LNSEDLKKAASVISRAKVMICQLEISPAAsLEaltmarrsGVKTLFNPAPAMADLDPQFYT------LSSIFCC--NESE 203
Cdd:PRK09954 173 LTPQLLNGSRDLIRHAGVVLADCNLTAEA-LE--------WVFTLADEIPVFVDTVSEFKAgkikhwLAHIHTLkpTQPE 243

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 755511713 204 AEILTGHAVSDPTTAGKAAMILLERGCQVVVITLG 238
Cdd:PRK09954 244 LEILWGQAITSDADRNAAVNALHQQGVQQIFVYLP 278
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 53-275 7.32e-03

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: 37.38  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713  53 GGKGANQCVQAARLGAKAAIVCKVgndsfGNDYIENLKQNHISTEFTYQTRDAATGTASIIVNNEGQNIIVIVAGANLfl 132
Cdd:cd01937   24 GGPATYASLTLSRLGLTVKLVTKV-----GRDYPDKWSDLFDNGIEVISLLSTETTTFELNYTNEGRTRTLLAKCAAI-- 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755511713 133 nsEDLKKAASVISRAKVMICQL--EISPAASLEaltmarrsgvktlfnPAPAMadLDPQFY-----TLSSIFCCNESEAE 205
Cdd:cd01937   97 --PDTESPLSTITAEIVILGPVpeEISPSLFRK---------------FAFIS--LDAQGFlrranQEKLIKCVILKLHD 157

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755511713 206 ILTGHAVS--DPTTAGKAAMILLERGCQVVVITLGASGCVILSQAEPVpkHIPTEAVKAVDTTflTLGDVLC 275
Cdd:cd01937  158 VLKLSRVEaeVISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKY--TIPASKKDVVDPT--GAGDVFL 225
 
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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