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Conserved domains on  [gi|75426049|sp|O24767|]
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RecName: Full=Guanosine-inosine kinase; AltName: Full=ATP:guanosine 5'-phosphotransferase; AltName: Full=Guanosine kinase; Short=GKase

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 ...
 3-289 6.36e-80

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 cd01947:

Pssm-ID: 469648 [Multi-domain]  Cd Length: 265  Bit Score: 243.09  E-value: 6.36e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGTSFAPLHKD-AKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANvD 81
Cdd:cd01947   1 KIAVVGHVEWDIFLSLDAPPQPGgISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDK-H 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  82 HVEMlEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAIlrqsiyaLDGVDAVAIDldlSVTVLERLIHLCRKMELPLF 161
Cdd:cd01947  80 TVAW-RDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPI-------LDEGDGVFIT---AAAVDKEAIRKCRETKLVIL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 162 GVCGHLSVIERNrHLLQGFTGFICSREEAEILSdlsivtvedaihVANELAKKGAPFTVVTMSELGAVYVDrrTATSGHV 241
Cdd:cd01947 149 QVTPRVRVDELN-QALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYP--GGRYNHV 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75426049 242 GTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:cd01947 214 PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
 
Name Accession Description Interval E-value
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 3-289 6.36e-80

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: 243.09  E-value: 6.36e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGTSFAPLHKD-AKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANvD 81
Cdd:cd01947   1 KIAVVGHVEWDIFLSLDAPPQPGgISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDK-H 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  82 HVEMlEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAIlrqsiyaLDGVDAVAIDldlSVTVLERLIHLCRKMELPLF 161
Cdd:cd01947  80 TVAW-RDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPI-------LDEGDGVFIT---AAAVDKEAIRKCRETKLVIL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 162 GVCGHLSVIERNrHLLQGFTGFICSREEAEILSdlsivtvedaihVANELAKKGAPFTVVTMSELGAVYVDrrTATSGHV 241
Cdd:cd01947 149 QVTPRVRVDELN-QALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYP--GGRYNHV 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75426049 242 GTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:cd01947 214 PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 3-294 2.65e-62

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 199.11  E-value: 2.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049     3 KIAVIGKVFVDIKGTSFAPLhKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDH 82
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP-GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049    83 VEMLEDHGMGMWLAVMDNEGDlQTSISKQPDAKLLEEAILRQSIYALDGVDAVAID----LDLSVTVLERLIHLCRKMEL 158
Cdd:pfam00294  80 VVIDEDTRTGTALIEVDGDGE-RTIVFNRGAAADLTPEELEENEDLLENADLLYISgslpLGLPEATLEELIEAAKNGGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   159 PLFGVCGHL-SVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDrRTAT 237
Cdd:pfam00294 159 FDPNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVE-GDGE 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 75426049   238 SGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIASTENGL 294
Cdd:pfam00294 238 VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 3-289 3.85e-44

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: 152.35  E-value: 3.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGT-SFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVD 81
Cdd:COG0524   1 DVLVIGEALVDLVARvDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  82 HVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQsiyALDGVDAV-----AIDLDLSVTVLERLIHLCRKM 156
Cdd:COG0524  81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEA---LLAGADILhlggiTLASEPPREALLAALEAARAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 157 ELPLF-----GVCGHLSVIERNRHLLQGFTGFICSREEAEILSDLsivtvEDAIHVANELAKKGAPFTVVTMSELGAVYV 231
Cdd:COG0524 158 GVPVSldpnyRPALWEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLY 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75426049 232 DRrtATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:COG0524 233 TG--GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTR 288
PRK09850 PRK09850
pseudouridine kinase; Provisional
 4-264 1.16e-26

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 106.61  E-value: 1.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049    4 IAVIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHV 83
Cdd:PRK09850   7 VVIIGSANIDVAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   84 EMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSVTVLERLIHlcRKMELPLF-- 161
Cdd:PRK09850  87 LIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILD--NAANVPVFvd 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  162 ----GVCGHLsviernRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGaVYVDRRTAT 237
Cdd:PRK09850 165 pvsaWKCVKV------RDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG-VYYSDISGE 237

                        250       260
                 ....*....|....*....|....*..
gi 75426049  238 SGHVGTKKVKVVDSTGAGDSFFSAVLS 264
Cdd:PRK09850 238 SGWSAPIKTNVINVTGAGDAMMAGLAS 264
 
Name Accession Description Interval E-value
Guanosine_kinase_like cd01947
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ...
 3-289 6.36e-80

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: 243.09  E-value: 6.36e-80
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGTSFAPLHKD-AKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANvD 81
Cdd:cd01947   1 KIAVVGHVEWDIFLSLDAPPQPGgISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDK-H 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  82 HVEMlEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAIlrqsiyaLDGVDAVAIDldlSVTVLERLIHLCRKMELPLF 161
Cdd:cd01947  80 TVAW-RDKPTRKTLSFIDPNGERTITVPGERLEDDLKWPI-------LDEGDGVFIT---AAAVDKEAIRKCRETKLVIL 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 162 GVCGHLSVIERNrHLLQGFTGFICSREEAEILSdlsivtvedaihVANELAKKGAPFTVVTMSELGAVYVDrrTATSGHV 241
Cdd:cd01947 149 QVTPRVRVDELN-QALIPLDILIGSRLDPGELV------------VAEKIAGPFPRYLIVTEGELGAILYP--GGRYNHV 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*...
gi 75426049 242 GTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:cd01947 214 PAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
PfkB pfam00294
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ...
 3-294 2.65e-62

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


Pssm-ID: 425587 [Multi-domain]  Cd Length: 294  Bit Score: 199.11  E-value: 2.65e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049     3 KIAVIGKVFVDIKGTSFAPLhKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDH 82
Cdd:pfam00294   1 KVVVIGEANIDLIGNVEGLP-GELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049    83 VEMLEDHGMGMWLAVMDNEGDlQTSISKQPDAKLLEEAILRQSIYALDGVDAVAID----LDLSVTVLERLIHLCRKMEL 158
Cdd:pfam00294  80 VVIDEDTRTGTALIEVDGDGE-RTIVFNRGAAADLTPEELEENEDLLENADLLYISgslpLGLPEATLEELIEAAKNGGT 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   159 PLFGVCGHL-SVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDrRTAT 237
Cdd:pfam00294 159 FDPNLLDPLgAAREALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVE-GDGE 237

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 75426049   238 SGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIASTENGL 294
Cdd:pfam00294 238 VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
RbsK COG0524
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ...
 3-289 3.85e-44

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: 152.35  E-value: 3.85e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGT-SFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVD 81
Cdd:COG0524   1 DVLVIGEALVDLVARvDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  82 HVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQsiyALDGVDAV-----AIDLDLSVTVLERLIHLCRKM 156
Cdd:COG0524  81 GVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEA---LLAGADILhlggiTLASEPPREALLAALEAARAA 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 157 ELPLF-----GVCGHLSVIERNRHLLQGFTGFICSREEAEILSDLsivtvEDAIHVANELAKKGAPFTVVTMSELGAVYV 231
Cdd:COG0524 158 GVPVSldpnyRPALWEPARELLRELLALVDILFPNEEEAELLTGE-----TDPEEAAAALLARGVKLVVVTLGAEGALLY 232

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75426049 232 DRrtATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:COG0524 233 TG--GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTR 288
YeiC_kinase_like cd01941
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ...
 3-289 5.32e-42

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: 146.30  E-value: 5.32e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANvDH 82
Cdd:cd01941   1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLN-VR 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  83 VEMLEDHGMGMWLAVMDNEGDLQTSISkqpDAKLLE---EAILRQSIYALDGVDAVAIDLDLSVTVLERLIHLCRKMELP 159
Cdd:cd01941  80 GIVFEGRSTASYTAILDKDGDLVVALA---DMDIYElltPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVP 156

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 160 LFGVCGHLSVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTATSG 239
Cdd:cd01941 157 VAFEPTSAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVET 236

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|..
gi 75426049 240 HVG--TKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:cd01941 237 KLFpaPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
KdgK cd01166
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ...
 3-289 8.33e-31

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: 116.91  E-value: 8.33e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDIKGTSFAPLHkdakNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDH 82
Cdd:cd01166   1 DVVTIGEVMVDLSPPGGGRLE----QADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSH 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  83 VEMLEDHGMGMWLAVMDNEGD--LQTSISKQPDAKLLEEAILRQsiyALDGVDAV-------AIDLDLSVTVLErLIHLC 153
Cdd:cd01166  77 VRVDPGRPTGLYFLEIGAGGErrVLYYRAGSAASRLTPEDLDEA---ALAGADHLhlsgitlALSESAREALLE-ALEAA 152

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 154 RKM------------ELPLFGVCghlsvIERNRHLLQGFTGFICSREEAEILSDLSivTVEDAIHVANELAKkGAPFTVV 221
Cdd:cd01166 153 KARgvtvsfdlnyrpKLWSAEEA-----REALEELLPYVDIVLPSEEEAEALLGDE--DPTDAAERALALAL-GVKAVVV 224

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75426049 222 TMSELGAVYVDRRTATsgHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAS 289
Cdd:cd01166 225 KLGAEGALVYTGGGRV--FVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTR 290
PRK09850 PRK09850
pseudouridine kinase; Provisional
 4-264 1.16e-26

pseudouridine kinase; Provisional


Pssm-ID: 182111 [Multi-domain]  Cd Length: 313  Bit Score: 106.61  E-value: 1.16e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049    4 IAVIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHV 83
Cdd:PRK09850   7 VVIIGSANIDVAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKC 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   84 EMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSVTVLERLIHlcRKMELPLF-- 161
Cdd:PRK09850  87 LIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILD--NAANVPVFvd 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  162 ----GVCGHLsviernRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGaVYVDRRTAT 237
Cdd:PRK09850 165 pvsaWKCVKV------RDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDG-VYYSDISGE 237

                        250       260
                 ....*....|....*....|....*..
gi 75426049  238 SGHVGTKKVKVVDSTGAGDSFFSAVLS 264
Cdd:PRK09850 238 SGWSAPIKTNVINVTGAGDAMMAGLAS 264
ribokinase cd01174
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ...
 37-284 1.22e-25

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: 103.01  E-value: 1.22e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  37 GGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKL 116
Cdd:cd01174  36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGEL 115

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 117 LEEAILRQSiYALDGVDAVAIDLDLSVTVLERLIHLCRKMELPlfgvcghlsVI-------ERNRHLLQGFTGFICSREE 189
Cdd:cd01174 116 TPADVDAAL-ELIAAADVLLLQLEIPLETVLAALRAARRAGVT---------VIlnpaparPLPAELLALVDILVPNETE 185

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 190 AEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTatSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQE 269
Cdd:cd01174 186 AALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASGGE--VEHVPAFKVKAVDTTGAGDTFIGALAAALARG 263

                       250
                ....*....|....*
gi 75426049 270 KSAEEALKLGMKVAA 284
Cdd:cd01174 264 LSLEEAIRFANAAAA 278
ribokinase_group_A cd01942
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ...
 4-290 5.81e-25

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: 101.23  E-value: 5.81e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   4 IAVIGKVFVDI--KGTSFAPLHKDAkNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVD 81
Cdd:cd01942   2 VAVVGHLNYDIilKVESFPGPFESV-LVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  82 HVEMLEDHGMGMWLaVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVdavaidldlSVTVLERLIHLCRKM----- 156
Cdd:cd01942  81 HVRVVDEDSTGVAF-ILTDGDDNQIAYFYPGAMDELEPNDEADPDGLADIV---------HLSSGPGLIELARELaaggi 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 157 --------ELPLFGVCGHLSVIER------NRHllqgftgficsreEAEILSDLS-IVTVEDAIHVanelakkgaPFTVV 221
Cdd:cd01942 151 tvsfdpgqELPRLSGEELEEILERadilfvNDY-------------EAELLKERTgLSEAELASGV---------RVVVV 208

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75426049 222 TMSELGAVYVDRRTATSgHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAST 290
Cdd:cd01942 209 TLGPKGAIVFEDGEEVE-VPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERR 276
bac_FRK cd01167
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ...
 3-288 6.54e-21

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: 90.39  E-value: 6.54e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVDI---KGTSFAPLHKDAknvgditfsnGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGAN 79
Cdd:cd01167   1 KVVCFGEALIDFipeGSGAPETFTKAP----------GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVD 70

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  80 VDHVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSiyALDGVDAV---AIDL--DLSVTVLERLIHLCR 154
Cdd:cd01167  71 TRGIQFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPD--LLSEADILhfgSIALasEPSRSALLELLEAAK 148

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 155 KMELP-LFGVCGHLSVIERNRHLLQGFTGFI-------CSREEAEILSDLSIVTVEDAIhvaneLAKKGAPFTVVTMSEL 226
Cdd:cd01167 149 KAGVLiSFDPNLRPPLWRDEEEARERIAELLeladivkLSDEELELLFGEEDPEEIAAL-----LLLFGLKLVLVTRGAD 223

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 75426049 227 GAVYVDRrtATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQ-------EKSAEEALKLGMKVAAEVIA 288
Cdd:cd01167 224 GALLYTK--GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLSrgllaldEDELAEALRFANAVGALTCT 290
PRK09954 PRK09954
sugar kinase;
6-290 1.45e-18

sugar kinase;


Pssm-ID: 182165 [Multi-domain]  Cd Length: 362  Bit Score: 84.60  E-value: 1.45e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049    6 VIGKVFVDIKGTSFAPLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEM 85
Cdd:PRK09954  62 VVGAINMDIRGMADIRYPQAASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIR 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   86 LEDHGMGMWLAVMDNEGDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSVTVLERLIHLCRkmELPLFGVCG 165
Cdd:PRK09954 142 LHGQSTSTYLAIANRQDETVLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLAD--EIPVFVDTV 219

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  166 HLSVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSElGAVYVDRRTATSGHVGTKK 245
Cdd:PRK09954 220 SEFKAGKIKHWLAHIHTLKPTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPD-ESVFCSEKDGEQFLLTAPA 298

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*
gi 75426049  246 VKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIAST 290
Cdd:PRK09954 299 HTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMACAAISRASG 343
FruK COG1105
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
22-302 3.86e-18

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


Pssm-ID: 440722 [Multi-domain]  Cd Length: 304  Bit Score: 82.88  E-value: 3.86e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  22 LHKDAKN-VGDITFSNGGTGRNVAQNLAVLGNEVR---FISTVTNDQIgvgvLDELKSYGANVDHVEMleDHGMGMWLAV 97
Cdd:COG1105  19 LEPGEVNrASEVRLDPGGKGINVARVLKALGVDVTalgFLGGFTGEFI----EELLDEEGIPTDFVPI--EGETRINIKI 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  98 MDNEGDLQT-------SISKQpDAKLLEEAILRqsiyALDGVDAVAI--DL--DLSVTVLERLIHLCRKMELPLF----- 161
Cdd:COG1105  93 VDPSDGTETeinepgpEISEE-ELEALLERLEE----LLKEGDWVVLsgSLppGVPPDFYAELIRLARARGAKVVldtsg 167

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 162 -----GVCGHLSVIERNRHllqgftgficsreEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTA 236
Cdd:COG1105 168 ealkaALEAGPDLIKPNLE-------------ELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVTEDGV 234

                       250       260       270       280       290       300
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75426049 237 TsgHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVIASTENGLV-PEMLDAL 302
Cdd:COG1105 235 Y--RAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPdREDVEEL 299
adenosine_kinase cd01168
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ...
 37-287 2.09e-15

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: 74.96  E-value: 2.09e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  37 GGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVdHVEMLEDHGMGMWLAVMDNEGD----LQTSISKQP 112
Cdd:cd01168  55 GGSAANTIRGAAALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDT-RYQVQPDGPTGTCAVLVTPDAErtmcTYLGAANEL 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 113 DAKLLEEAILRQS-IYALDGVDavaidLDLSVTVLERLIHLCRKMELPlfgVCGHLS---VIERNR----HLLQGFTGFI 184
Cdd:cd01168 134 SPDDLDWSLLAKAkYLYLEGYL-----LTVPPEAILLAAEHAKENGVK---IALNLSapfIVQRFKeallELLPYVDILF 205

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 185 CSREEAEILSDlsiVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTATsgHVGT-KKVKVVDSTGAGDSFFSAVL 263
Cdd:cd01168 206 GNEEEAEALAE---AETTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGEVY--PVPAiPVEKIVDTNGAGDAFAGGFL 280

                       250       260
                ....*....|....*....|....
gi 75426049 264 SELTQEKSAEEALKLGMKVAAEVI 287
Cdd:cd01168 281 YGLVQGEPLEECIRLGSYAAAEVI 304
RfaE COG2870
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ...
 28-284 4.61e-15

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


Pssm-ID: 442117 [Multi-domain]  Cd Length: 321  Bit Score: 74.08  E-value: 4.61e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  28 NVGDITFSNGGTGrNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDH---------GMGMWLAVM 98
Cdd:COG2870  47 RVEREEERPGGAA-NVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRptttktrviAGGQQLLRL 125

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  99 DNEgdlqtsiSKQPDAKLLEEAILRQSIYALDGVDAVAIdLD-----LSVTVLERLIHLCRKMELPLF----Gvcghlsv 169
Cdd:COG2870 126 DFE-------DRFPLSAELEARLLAALEAALPEVDAVIL-SDygkgvLTPELIQALIALARAAGKPVLvdpkG------- 190

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 170 ieRNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKK-GAPFTVVTMSELGAVYVDRRTATSgHVGTKKVKV 248
Cdd:COG2870 191 --RDFSRYRGATLLTPNLKEAEAAVGIPIADEEELVAAAAELLERlGLEALLVTRGEEGMTLFDADGPPH-HLPAQAREV 267

                       250       260       270
                ....*....|....*....|....*....|....*.
gi 75426049 249 VDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAA 284
Cdd:COG2870 268 FDVTGAGDTVIATLALALAAGASLEEAAELANLAAG 303
ribokinase_group_B cd01945
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ...
 21-284 4.78e-15

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: 73.87  E-value: 4.78e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  21 PLHKDAKNVGDITFSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDhGMGMWLAVMDN 100
Cdd:cd01945  20 PGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPG-ARSPISSITDI 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 101 EGDLQTsisKQPDAKLLEEAILRQSIYALDGVDAVAID---LDLSVTVLERlihlCRKMELPLFGVCGHLSViERNRHLL 177
Cdd:cd01945  99 TGDRAT---ISITAIDTQAAPDSLPDAILGGADAVLVDgrqPEAALHLAQE----ARARGIPIPLDLDGGGL-RVLEELL 170

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 178 QGFTGFICSREEAEILSDLSIVTVEDAihvaneLAKKGAPFTVVTMSELGAVYVDRRTATsGHVGTKKVKVVDSTGAGDS 257
Cdd:cd01945 171 PLADHAICSENFLRPNTGSADDEALEL------LASLGIPFVAVTLGEAGCLWLERDGEL-FHVPAFPVEVVDTTGAGDV 243

                       250       260
                ....*....|....*....|....*..
gi 75426049 258 FFSAVLSELTQEKSAEEALKLGMKVAA 284
Cdd:cd01945 244 FHGAFAHALAEGMPLREALRFASAAAA 270
Fructoselysine_kinase_like cd01940
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ...
 28-287 4.50e-14

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: 70.85  E-value: 4.50e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  28 NVGDITFSN-----GGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVE----------MLEDHGMG 92
Cdd:cd01940   8 NVVDKYLHLgkmypGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRvkegenavadVELVDGDR 87

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  93 MWLA----VMDNEGDLQTSISKQPDAKLLEEAILRQSIYALD-----GVDAVAIDLDLSVTVLERLIHLcrkmelplfgV 163
Cdd:cd01940  88 IFGLsnkgGVAREHPFEADLEYLSQFDLVHTGIYSHEGHLEKalqalVGAGALISFDFSDRWDDDYLQL----------V 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 164 CGHLSViernrhllqGFtgFICSREEAEILSDLsivtvedaihvANELAKKGAPFTVVTMSELGAVYVDrrTATSGHVGT 243
Cdd:cd01940 158 CPYVDF---------AF--FSASDLSDEEVKAK-----------LKEAVSRGAKLVIVTRGEDGAIAYD--GAVFYSVAP 213

                       250       260       270       280
                ....*....|....*....|....*....|....*....|....*
gi 75426049 244 KKVKVVDSTGAGDSFFSAVLSELTQEKSA-EEALKLGMKVAAEVI 287
Cdd:cd01940 214 RPVEVVDTLGAGDSFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTC 258
FruK_PfkB_like cd01164
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ...
 187-293 1.35e-13

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: 69.48  E-value: 1.35e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 187 REEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGAVYVDRRTATsgHVGTKKVKVVDSTGAGDSFFSAVLSEL 266
Cdd:cd01164 185 REELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDGVY--RASPPKVKVVSTVGAGDSMVAGFVAGL 262

                        90       100
                ....*....|....*....|....*..
gi 75426049 267 TQEKSAEEALKLGMKVAAEVIASTENG 293
Cdd:cd01164 263 AQGLSLEEALRLAVAAGSATAFSPGTG 289
PTZ00292 PTZ00292
ribokinase; Provisional
 1-284 4.96e-13

ribokinase; Provisional


Pssm-ID: 185541 [Multi-domain]  Cd Length: 326  Bit Score: 68.23  E-value: 4.96e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049    1 MNKIAVIGKVFVD--------------IKGTSFaplHKdaknvgditfSNGGTGRNVAQNLAVLGNEVRFISTVTNDQIG 66
Cdd:PTZ00292  15 EPDVVVVGSSNTDligyvdrmpqvgetLHGTSF---HK----------GFGGKGANQAVMASKLGAKVAMVGMVGTDGFG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   67 VGVLDELKSYGANVDHVEMLEDHGMGMWLAVMDNE-GDLQTSISKQPDAKLLEEAILRQSIYALDGVDAVAIDLDLSV-T 144
Cdd:PTZ00292  82 SDTIKNFKRNGVNTSFVSRTENSSTGLAMIFVDTKtGNNEIVIIPGANNALTPQMVDAQTDNIQNICKYLICQNEIPLeT 161

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  145 VLERLIHLCRKMELPLFGVC--GHLSVIERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANELAKKGAPFTVVT 222
Cdd:PTZ00292 162 TLDALKEAKERGCYTVFNPApaPKLAEVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIIT 241

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 75426049  223 MSELGAVYVDRRTATSgHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAA 284
Cdd:PTZ00292 242 LGANGCLIVEKENEPV-HVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAA 302
ribokinase_pfkB_like cd00287
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ...
 131-263 4.35e-12

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: 64.04  E-value: 4.35e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 131 GVDAVAI-DLDLSVTVLERLIHLCRKMELPLFgVCGHLSVIERNR----HLLQGFTGFICSREEAEILSDLSIVTVEDAI 205
Cdd:cd00287  57 GADAVVIsGLSPAPEAVLDALEEARRRGVPVV-LDPGPRAVRLDGeeleKLLPGVDILTPNEEEAEALTGRRDLEVKEAA 135

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 75426049 206 HVANELAKKGAPFTVVTMSELGAVYVDRRtATSGHVGTKKVKVVDSTGAGDSFFSAVL 263
Cdd:cd00287 136 EAAALLLSKGPKVVIVTLGEKGAIVATRG-GTEVHVPAFPVKVVDTTGAGDAFLAALA 192
RfaE_like cd01172
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ...
 3-261 8.79e-12

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


Pssm-ID: 238577 [Multi-domain]  Cd Length: 304  Bit Score: 64.50  E-value: 8.79e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   3 KIAVIGKVFVD-------IKGTSFAPLhkDAKNVGDITFSNGGTGrNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKS 75
Cdd:cd01172   1 KVLVVGDVILDeylygdvERISPEAPV--PVVKVEREEIRLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEK 77

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  76 YGANVDHVE-----------MLEDHGMgmwLAVMDNEGDlqTSISKQPDAKLLEeaILRQSiyaLDGVDAVAI-DLD--- 140
Cdd:cd01172  78 EGIDTDGIVdegrptttktrVIARNQQ---LLRVDREDD--SPLSAEEEQRLIE--RIAER---LPEADVVILsDYGkgv 147

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 141 LSVTVLERLIHLCRKMELPLFGVCGhlsviERNRHLLQGFTGFICSREEAEILSDLSIVTVEDAIHVANEL-AKKGAPFT 219
Cdd:cd01172 148 LTPRVIEALIAAARELGIPVLVDPK-----GRDYSKYRGATLLTPNEKEAREALGDEINDDDELEAAGEKLlELLNLEAL 222

                       250       260       270       280
                ....*....|....*....|....*....|....*....|..
gi 75426049 220 VVTMSELGAVYVDRRTATSgHVGTKKVKVVDSTGAGDSFFSA 261
Cdd:cd01172 223 LVTLGEEGMTLFERDGEVQ-HIPALAKEVYDVTGAGDTVIAT 263
PRK11142 PRK11142
ribokinase; Provisional
 37-293 3.54e-11

ribokinase; Provisional


Pssm-ID: 236858 [Multi-domain]  Cd Length: 306  Bit Score: 62.58  E-value: 3.54e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   37 GGTGRNVAQNLAVLGNEVRFISTVTNDQIGVGVLDELKSYGANVDHVEMLEDHGMGMWLAVMDNEGDLQTSISKQPDAKL 116
Cdd:PRK11142  39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHAGANAAL 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  117 LEEAILR-QSIYAldgvDAVAIdldlsvtvlerLIHLcrkmELPLFGVCGHLSVIERNR---------------HLLQgF 180
Cdd:PRK11142 119 TPALVEAhRELIA----NADAL-----------LMQL----ETPLETVLAAAKIAKQHGtkvilnpaparelpdELLA-L 178

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  181 TGFICSRE-EAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELGaVYVDRRtATSGHVGTKKVKVVDSTGAGDSFF 259
Cdd:PRK11142 179 VDIITPNEtEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRG-VWLSEN-GEGQRVPGFRVQAVDTIAAGDTFN 256

                        250       260       270
                 ....*....|....*....|....*....|....
gi 75426049  260 SAVLSELTQEKSAEEALKLGMKVAAevIASTENG 293
Cdd:PRK11142 257 GALVTALLEGKPLPEAIRFAHAAAA--IAVTRKG 288
PdxK COG2240
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ...
 189-290 2.43e-09

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: 57.08  E-value: 2.43e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 189 EAEILSDLSIVTVEDAIHVANELAKKGAPFTVVT--------MSELGAVYVDRRTATsgHVGTKKVKvVDSTGAGDSFFS 260
Cdd:COG2240 148 ELALLTGRPYETLEEALAAARALLALGPKIVVVTsvplddtpADKIGNLAVTADGAW--LVETPLLP-FSPNGTGDLFAA 224

                        90       100       110
                ....*....|....*....|....*....|
gi 75426049 261 AVLSELTQEKSAEEALKLGMKVAAEVIAST 290
Cdd:COG2240 225 LLLAHLLRGKSLEEALERAAAFVYEVLERT 254
PLN02323 PLN02323
probable fructokinase
 220-298 2.27e-08

probable fructokinase


Pssm-ID: 215183 [Multi-domain]  Cd Length: 330  Bit Score: 54.63  E-value: 2.27e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  220 VVTMSELGAVYVDRrtATSGHVGTKKVKVVDSTGAGDSFFSAVLSELTQEKSA---EEALKLGMKVAAE--VIASTENGL 294
Cdd:PLN02323 234 LVTEGEEGCRYYTK--DFKGRVEGFKVKAVDTTGAGDAFVGGLLSQLAKDLSLledEERLREALRFANAcgAITTTERGA 311


                 ....
gi 75426049  295 VPEM 298
Cdd:PLN02323 312 IPAL 315
PRK09434 PRK09434
aminoimidazole riboside kinase; Provisional
 186-288 6.28e-08

aminoimidazole riboside kinase; Provisional


Pssm-ID: 236514 [Multi-domain]  Cd Length: 304  Bit Score: 53.02  E-value: 6.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  186 SREEAEILSDLSivTVEDAIHvanELAKK-GAPFTVVTMSELGAVYVDRRTATsgHVGTKKVKVVDSTGAGDSFFSAVLS 264
Cdd:PRK09434 187 SEEELCFLSGTS--QLEDAIY---ALADRyPIALLLVTLGAEGVLVHTRGQVQ--HFPAPSVDPVDTTGAGDAFVAGLLA 259

                         90       100
                 ....*....|....*....|....
gi 75426049  265 ELTQEKSAEEALKLgmkvaAEVIA 288
Cdd:PRK09434 260 GLSQAGLWTDEAEL-----AEIIA 278
pyridoxal_pyridoxamine_kinase cd01173
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ...
 189-290 8.54e-08

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: 52.20  E-value: 8.54e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 189 EAEILSDLSIVTVEDAIHVANELAKKGAPFTVVT------MSELGAVYVDRRTAtsGHVGTKKVKVVDS-TGAGDSFFSA 261
Cdd:cd01173 146 ELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEA--WLVQRPKIPFPAYfNGTGDLFAAL 223

                        90       100
                ....*....|....*....|....*....
gi 75426049 262 VLSELTQEKSAEEALKLGMKVAAEVIAST 290
Cdd:cd01173 224 LLARLLKGKSLAEALEKALNFVHEVLEAT 252
YegV_kinase_like cd01944
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ...
 185-287 1.64e-07

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


Pssm-ID: 238919 [Multi-domain]  Cd Length: 289  Bit Score: 51.65  E-value: 1.64e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 185 CSREEAEILSDLSivTVEDAIHVANELAKKGAPFtVVTMSELGAVYVDRrTATSGHVGTKKVKVVDSTGAGDSFFSAVLS 264
Cdd:cd01944 187 CNREEAAIFAERG--DPAAEASALRIYAKTAAPV-VVRLGSNGAWIRLP-DGNTHIIPGFKVKAVDTIGAGDTHAGGMLA 262

                        90       100
                ....*....|....*....|...
gi 75426049 265 ELTQEKSAEEALKLGMKVAAEVI 287
Cdd:cd01944 263 GLAKGMSLADAVLLANAAAAIVV 285
PLN02341 PLN02341
pfkB-type carbohydrate kinase family protein
 188-262 4.23e-06

pfkB-type carbohydrate kinase family protein


Pssm-ID: 215195 [Multi-domain]  Cd Length: 470  Bit Score: 47.90  E-value: 4.23e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 75426049  188 EEAEILSDLSivtveDAIHVANELAKKG--APFTVVTMSELGAVYVDRRTATSghVGTKKVKVVDSTGAGDSFFSAV 262
Cdd:PLN02341 294 EEAEALTGIR-----NPILAGQELLRPGirTKWVVVKMGSKGSILVTRSSVSC--APAFKVNVVDTVGCGDSFAAAI 363
PRK12413 PRK12413
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
189-278 7.29e-06

bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;


Pssm-ID: 183513 [Multi-domain]  Cd Length: 253  Bit Score: 46.59  E-value: 7.29e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  189 EAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTmselGAVYVDRRTATSGHVGTKKVKVVDS-------TGAGDSFFSA 261
Cdd:PRK12413 139 EAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIK----GGNRLSQKKAIDLFYDGKEFVILESpvleknnIGAGCTFASS 214

                         90
                 ....*....|....*..
gi 75426049  262 VLSELTQEKSAEEALKL 278
Cdd:PRK12413 215 IASQLVKGKSPLEAVKN 231
PRK09813 PRK09813
fructoselysine 6-kinase; Provisional
 210-287 8.88e-05

fructoselysine 6-kinase; Provisional


Pssm-ID: 182090 [Multi-domain]  Cd Length: 260  Bit Score: 43.19  E-value: 8.88e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 75426049  210 ELAKKGAPFTVVTMSELGAVYVDRRTATSGhvGTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVI 287
Cdd:PRK09813 179 AIVARGAGVVIVTLGENGSIAWDGAQFWRQ--APEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTI 254
ribokinase_group_D cd01937
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ...
 186-287 1.38e-04

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: 42.39  E-value: 1.38e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 186 SREEAEILSDLSivtvedaihvanELAKK----GAPFTVVTMSELGAvYVDRRTAtSGHVGTKKVKVVDSTGAGDSFFSA 261
Cdd:cd01937 162 SRVEAEVISTPT------------ELARLiketGVKEIIVTDGEEGG-YIFDGNG-KYTIPASKKDVVDPTGAGDVFLAA 227

                        90       100
                ....*....|....*....|....*.
gi 75426049 262 VLSELTQEKSAEEALKLGMKVAAEVI 287
Cdd:cd01937 228 FLYSRLSGKDIKEAAEFAAAAAAKFI 253
PTZ00344 PTZ00344
pyridoxal kinase; Provisional
 189-293 1.41e-04

pyridoxal kinase; Provisional


Pssm-ID: 240372 [Multi-domain]  Cd Length: 296  Bit Score: 42.76  E-value: 1.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049  189 EAEILSDLSIVTVEDAIHVANELAKKGAPFTVVTMSELG---------AVYVDRRTAtSGHVGTKKVKVVDS--TGAGDS 257
Cdd:PTZ00344 149 EASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSFREDedpthlrflLSCRDKDTK-NNKRFTGKVPYIEGryTGTGDL 227

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 75426049  258 FFSAVLSELTQEKSaEEALKLGMKVAAEVIASTENG 293
Cdd:PTZ00344 228 FAALLLAFSHQHPM-DLAVGKAMGVLQDIIKATRES 262
Phos_pyr_kin pfam08543
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ...
 189-279 3.21e-04

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: 41.31  E-value: 3.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049   189 EAEILSDLSIVTVEDAIHVANELAKKGAPFTVVT---MSELGAVYVDRrTATSGHVGTKKVKVVDST---GAGDSFFSAV 262
Cdd:pfam08543 129 EAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKgghLEGEEAVVTDV-LYDGGGFYTLEAPRIPTKnthGTGCTLSAAI 207

                          90
                  ....*....|....*..
gi 75426049   263 LSELTQEKSAEEALKLG 279
Cdd:pfam08543 208 AANLAKGLSLPEAVREA 224
PLN02548 PLN02548
adenosine kinase
 244-287 4.28e-04

adenosine kinase


Pssm-ID: 178163 [Multi-domain]  Cd Length: 332  Bit Score: 41.24  E-value: 4.28e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 75426049  244 KKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGmKVAAEVI 287
Cdd:PLN02548 275 PKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAG-NYAANVI 317
MAK32 cd01943
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ...
 163-284 2.33e-03

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


Pssm-ID: 238918 [Multi-domain]  Cd Length: 328  Bit Score: 39.25  E-value: 2.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 75426049 163 VCGHLSVIERNRHLLQGFTGFICSREEAEILSDlsivTVEDAIHVANELAKKGaPFTVVTMSELGAVYvdrRTATSG--- 239
Cdd:cd01943 177 ALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKE----AVLQALLFSGILQDPG-GGVVLRCGKLGCYV---GSADSGpel 248

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 75426049 240 -----HvgTKKVKVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGmKVAA 284
Cdd:cd01943 249 wlpayH--TKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYG-SVAA 295
PTZ00247 PTZ00247
adenosine kinase; Provisional
 236-287 5.44e-03

adenosine kinase; Provisional


Pssm-ID: 240328 [Multi-domain]  Cd Length: 345  Bit Score: 38.08  E-value: 5.44e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 75426049  236 ATSGHVGTKKV------KVVDSTGAGDSFFSAVLSELTQEKSAEEALKLGMKVAAEVI 287
Cdd:PTZ00247 272 ATKDGVTSVPVppldqeKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVII 329
 
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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