|
Name |
Accession |
Description |
Interval |
E-value |
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
1-312 |
1.68e-110 |
|
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: 323.80 E-value: 1.68e-110
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 1 MDKIIGLGNALVDVLATLkDDTLLDEMGLPKGSMQLIDDAKLQQINERfsqMKTHLATGGAAANTILGLACLGAGTGFIG 80
Cdd:cd01168 1 RYDVLGLGNALVDILAQV-DDAFLEKLGLKKGDMILADMEEQEELLAK---LPVKYIAGGSAANTIRGAAALGGSAAFIG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 81 KIGNDAYGNFFRANLQRNGIEDKLLVS-DLPSGVASTFISPDGERTFGTYLGAASTLKAEDLTLDMFKGYAYLLIEGYLV 159
Cdd:cd01168 77 RVGDDKLGDFLLKDLRAAGVDTRYQVQpDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 160 -QDHDMILHAIELAKEAGLQVCLDMASYNIVAGDLEFFTLLINkYVDIVFANEEEAKAFTG---KEDPKEALELISKKCS 235
Cdd:cd01168 157 tVPPEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLP-YVDILFGNEEEAEALAEaetTDDLEAALKLLALRCR 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492279673 236 IAIVKVGGNGSYIRKGTEEIKVEAIPVKKVIDTTGAGDYFASGFLYGLTCGYSLEKCAKIGSILSGNVIQIVGTTIP 312
Cdd:cd01168 236 IVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
3-319 |
6.09e-76 |
|
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: 235.16 E-value: 6.09e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 3 KIIGLGNALVDVLATLKddtlldemGLPKGSMQLIDDaklqqinerfsqmKTHLATGGAAANTILGLACLGAGTGFIGKI 82
Cdd:COG0524 1 DVLVIGEALVDLVARVD--------RLPKGGETVLAG-------------SFRRSPGGAAANVAVALARLGARVALVGAV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 83 GNDAYGNFFRANLQRNGIEDKLL--VSDLPSGVASTFISPDGERTFGTYLGAASTLKAEDLTLDMFKGYAYLLIEGYLV- 159
Cdd:COG0524 60 GDDPFGDFLLAELRAEGVDTSGVrrDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLa 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 160 --QDHDMILHAIELAKEAGLQVCLDMASY-NIVAGDLEFFTLLInKYVDIVFANEEEAKAFTGKEDPKEALE-LISKKCS 235
Cdd:COG0524 140 sePPREALLAALEAARAAGVPVSLDPNYRpALWEPARELLRELL-ALVDILFPNEEEAELLTGETDPEEAAAaLLARGVK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 236 IAIVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLTCGYSLEKCAKIGSILSGNVIQIVGTTIPGER 315
Cdd:COG0524 219 LVVVTLGAEGALLYTGGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 492279673 316 WDEI 319
Cdd:COG0524 298 REEV 301
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
10-316 |
1.10e-59 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 195.39 E-value: 1.10e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 10 ALVDVLATLkDDTLLDEM-GLPKGSMQL-IDDAK--LQQINERF-------SQMKThLAtGGAAANTILGLAC-LGAGTG 77
Cdd:PLN02379 29 ALVDHVARV-DWSLLDQIpGDRGGSIRVtIEELEhiLREVNAHIlpspddlSPIKT-MA-GGSVANTIRGLSAgFGVSTG 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 78 FIGKIGNDAYGNFFRANLQRNGIE-DKLLVSDLPSGVASTFISPDGERTFGTYLGAASTLKAEDLTLDMFKGYAYLLIEg 156
Cdd:PLN02379 106 IIGACGDDEQGKLFVSNMGFSGVDlSRLRAKKGPTAQCVCLVDALGNRTMRPCLSSAVKLQADELTKEDFKGSKWLVLR- 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 157 YLVQDHDMILHAIELAKEAGLQVCLDMASYNIVAG-DLEFFTLLINKYVDIVFANEEEAKAFTGKE---DPKEALELISK 232
Cdd:PLN02379 185 YGFYNLEVIEAAIRLAKQEGLSVSLDLASFEMVRNfRSPLLQLLESGKIDLCFANEDEARELLRGEqesDPEAALEFLAK 264
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 233 KCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKKVIDTTGAGDYFASGFLYGLTCGYSLEKCAKIGSILSGNVIQIVGTTIP 312
Cdd:PLN02379 265 YCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGEVT 344
|
....
gi 492279673 313 GERW 316
Cdd:PLN02379 345 PENW 348
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
59-308 |
1.16e-51 |
|
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: 172.38 E-value: 1.16e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSD--LPSGVASTFISPDGERTFGTYLG--AAS 134
Cdd:cd01166 31 GGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDpgRPTGLYFLEIGAGGERRVLYYRAgsAAS 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 135 TLKAEDLTLDMFKGYAYLLIEGY---LVQDH-DMILHAIELAKEAGLQVCLD--MASYNIVAGDLEFFTLLINKYVDIVF 208
Cdd:cd01166 111 RLTPEDLDEAALAGADHLHLSGItlaLSESArEALLEALEAAKARGVTVSFDlnYRPKLWSAEEAREALEELLPYVDIVL 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 209 ANEEEAKAFTGKEDPKEALE---LISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLTC 285
Cdd:cd01166 191 PSEEEAEALLGDEDPTDAAEralALALGVKAVVVKLGAEGALVYTGGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLE 269
|
250 260
....*....|....*....|...
gi 492279673 286 GYSLEKCAKIGSILSGNVIQIVG 308
Cdd:cd01166 270 GWDLEEALRFANAAAALVVTRPG 292
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
4-288 |
3.55e-49 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 169.60 E-value: 3.55e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 4 IIGLGNALVDVLATLkDDTLLDEMGLPKGSMQLIDdaklqqINERFSQMKT------HLATGGAAANTILGLACLGAGT- 76
Cdd:PLN02813 72 VLGLGQAMVDFSGMV-DDEFLERLGLEKGTRKVIN------HEERGKVLRAldgcsyKASAGGSLSNTLVALARLGSQSa 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 77 -------GFIGKIGNDAYGNFFRANLQRNGIedKLLVSDLPSGVASTFI---SPDGERTFGTYLGAASTLKAEDLTLDMF 146
Cdd:PLN02813 145 agpalnvAMAGSVGSDPLGDFYRTKLRRANV--HFLSQPVKDGTTGTVIvltTPDAQRTMLSYQGTSSTVNYDSCLASAI 222
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 147 KGYAYLLIEGYLVQDHDM---ILHAIELAKEAGLQVCLDMASYNIVAGDLEFFTLLINKYVDIVFANEEEAKAFTG---K 220
Cdd:PLN02813 223 SKSRVLVVEGYLWELPQTieaIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGNYADILFANSDEARALCGlgsE 302
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492279673 221 EDPKEALELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKKViDTTGAGDYFASGFLYGLTCGYS 288
Cdd:PLN02813 303 ESPESATRYLSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVPV-DTCGAGDAYAAGILYGLLRGVS 369
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
51-311 |
6.13e-47 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 160.20 E-value: 6.13e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 51 QMKTHLATGGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIE-DKLLVS-DLPSGVASTFISPDGERTFGT 128
Cdd:pfam00294 26 VSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDtDYVVIDeDTRTGTALIEVDGDGERTIVF 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 129 YLGAASTLKAEDLT--LDMFKGYAYLLIEGYLVQD--HDMILHAIELAKEAGLQVcldmasYNIVAGDLEFFTLL--INK 202
Cdd:pfam00294 106 NRGAAADLTPEELEenEDLLENADLLYISGSLPLGlpEATLEELIEAAKNGGTFD------PNLLDPLGAAREALleLLP 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 203 YVDIVFANEEEAKAFTGKE--DPKEAL----ELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKKVIDTTGAGDYFA 276
Cdd:pfam00294 180 LADLLKPNEEELEALTGAKldDIEEALaalhKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFV 259
|
250 260 270
....*....|....*....|....*....|....*
gi 492279673 277 SGFLYGLTCGYSLEKCAKIGSILSGNVIQIVGTTI 311
Cdd:pfam00294 260 GGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
59-309 |
3.66e-46 |
|
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: 157.86 E-value: 3.66e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSDLPSGVASTFISPDGE--RTFGTYLGAASTL 136
Cdd:cd01942 36 GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDdnQIAYFYPGAMDEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 137 KAEDLtLDMFKGYAYLLIEGYlvqdHDMILHAIELAKEaGLQVCLD---MASYNIVAGDLEFFTLlinkyVDIVFANEEE 213
Cdd:cd01942 116 EPNDE-ADPDGLADIVHLSSG----PGLIELARELAAG-GITVSFDpgqELPRLSGEELEEILER-----ADILFVNDYE 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 214 AKAF---TGKEDPKEAlelisKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKKVIDTTGAGDYFASGFLYGLTCGYSLE 290
Cdd:cd01942 185 AELLkerTGLSEAELA-----SGVRVVVVTLGPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLE 259
|
250
....*....|....*....
gi 492279673 291 KCAKIGSILSGNVIQIVGT 309
Cdd:cd01942 260 ESLRLGNLAASLKVERRGA 278
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
3-313 |
6.35e-44 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 153.64 E-value: 6.35e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 3 KIIGLGNALVDVLATLkDDTLLDEMGLPKGSMQLIDDAKLQQINERFSQMKTHLATGGAAANTILGLA-CLGAGTG---F 78
Cdd:PTZ00247 7 KLLGFGNPLLDISAHV-SDEFLEKYGLELGSAILAEEKQLPIFEELESIPNVSYVPGGSALNTARVAQwMLQAPKGfvcY 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 79 IGKIGNDAYGNFFRANLQRNGIEDKLLV-SDLPSGVASTFISpDGERTFGTYLGAASTLKAEDL-TLDM---FKGYAYLL 153
Cdd:PTZ00247 86 VGCVGDDRFAEILKEAAEKDGVEMLFEYtTKAPTGTCAVLVC-GKERSLVANLGAANHLSAEHMqSHAVqeaIKTAQLYY 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 154 IEGY-LVQDHDMILHAIELAKEAGLQVCLDMASYNIVagdlEFFTLLINK---YVDIVFANEEEAKAFT-----GKEDPK 224
Cdd:PTZ00247 165 LEGFfLTVSPNNVLQVAKHARESGKLFCLNLSAPFIS----QFFFERLLQvlpYVDILFGNEEEAKTFAkamkwDTEDLK 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 225 EALELIS-------KKCSIAIVKVGGNGSYIRKGTEEIKVEAIPV--KKVIDTTGAGDYFASGFLYGLTCGYSLEKCAKI 295
Cdd:PTZ00247 241 EIAARIAmlpkysgTRPRLVVFTQGPEPTLIATKDGVTSVPVPPLdqEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEA 320
|
330
....*....|....*...
gi 492279673 296 GSILSGNVIQIVGTTIPG 313
Cdd:PTZ00247 321 GHYSAQVIIQHNGCTYPE 338
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
50-309 |
4.10e-40 |
|
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: 142.30 E-value: 4.10e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 50 SQMKTHLatGGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGI--EDKLLVSDLPSGVASTFISPDGERTFG 127
Cdd:cd01174 29 SSFETGP--GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIdvSYVEVVVGAPTGTAVITVDESGENRIV 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 128 TYLGAASTLKAEDLT--LDMFKGYAYLLIEgyLVQDHDMILHAIELAKEAGLQVCLDMASYNIVAGDLefftLlinKYVD 205
Cdd:cd01174 107 VVPGANGELTPADVDaaLELIAAADVLLLQ--LEIPLETVLAALRAARRAGVTVILNPAPARPLPAEL----L---ALVD 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 206 IVFANEEEAKAFTGKEDP------KEALELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVkKVIDTTGAGDYFASGF 279
Cdd:cd01174 178 ILVPNETEAALLTGIEVTdeedaeKAARLLLAKGVKNVIVTLGAKGALLASGGEVEHVPAFKV-KAVDTTGAGDTFIGAL 256
|
250 260 270
....*....|....*....|....*....|
gi 492279673 280 LYGLTCGYSLEKCAKIGSILSGNVIQIVGT 309
Cdd:cd01174 257 AAALARGLSLEEAIRFANAAAALSVTRPGA 286
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
55-309 |
6.91e-36 |
|
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: 131.18 E-value: 6.91e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 55 HLATGGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLL--VSDLPSGVASTFISPDGERTFGTYLGA 132
Cdd:TIGR02152 27 QIGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVgtVKDTPTGTAFITVDDTGENRIVVVAGA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 133 ASTLKAEDL--TLDMFKGYAYLLIEgyLVQDHDMILHAIELAKEAGLQVCLDMASYNIVAgDLEFFTllinkYVDIVFAN 210
Cdd:TIGR02152 107 NAELTPEDIdaAEALIAESDIVLLQ--LEIPLETVLEAAKIAKKHGVKVILNPAPAIKDL-DDELLS-----LVDIITPN 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 211 EEEAKAFTGK-----EDPKEALE-LISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLT 284
Cdd:TIGR02152 179 ETEAEILTGIevtdeEDAEKAAEkLLEKGVKNVIITLGSKGALLVSKDESKLIPAFKVK-AVDTTAAGDTFNGAFAVALA 257
|
250 260
....*....|....*....|....*
gi 492279673 285 CGYSLEKCAKIGSILSGNVIQIVGT 309
Cdd:TIGR02152 258 EGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
59-284 |
6.46e-34 |
|
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: 126.21 E-value: 6.46e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSD--LPSGVASTFISPDGERTFGTYLG-AAST 135
Cdd:cd01167 28 GGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFDpaAPTTLAFVTLDADGERSFEFYRGpAADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 136 LKAEDLTLDMFKGYAYL------LIEGYLvqdHDMILHAIELAKEAGLQVCLDMasyNI----VAGDLEFFTLLIN--KY 203
Cdd:cd01167 108 LLDTELNPDLLSEADILhfgsiaLASEPS---RSALLELLEAAKKAGVLISFDP---NLrpplWRDEEEARERIAEllEL 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 204 VDIVFANEEEAKAFTGKEDPKEALELISK-KCSIAIVKVGGNGSYIRKGTEEIKVEAIPVkKVIDTTGAGDYFASGFLYG 282
Cdd:cd01167 182 ADIVKLSDEELELLFGEEDPEEIAALLLLfGLKLVLVTRGADGALLYTKGGVGEVPGIPV-EVVDTTGAGDAFVAGLLAQ 260
|
..
gi 492279673 283 LT 284
Cdd:cd01167 261 LL 262
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
4-254 |
1.56e-28 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 114.34 E-value: 1.56e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 4 IIGLGNALVDVLATLkDDTLLDEMGLPKGSMQLIDDAKLQQINERFSQ--MKTHLATGGAAANTILG---LA-----CLG 73
Cdd:PRK15074 36 IVGIDQTLVDIEAKV-DDEFLERYGLSKGHSLVIEDDVAEALYQELKQnnLITHEFAGGTIGNTLHNysvLAddrsvLLG 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 74 AGTGFIgKIGNDAY----GNFFRANLqrngieDKLLVSDLPSGVASTFISPDGERTFGTYLGAASTLKAEDLTLDMFKGY 149
Cdd:PRK15074 115 VMSSNI-EIGSYAYrylcNTSSRTDL------NYLQGVDGPIGRCFTLISEDGERTFAISPGHMNQLRPESIPEDVIAGA 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 150 AYLLIEGYLVQDH------DMILHAIELAKEAGLQVCLDMASYNIVAGDLEFFTLLINKYVDIVFANEEEAKAFTGKEDP 223
Cdd:PRK15074 188 SALVLTAYLVRCKpgepmpEATMKAIEYAKKHNVPVVLTLGTKFVIEDNPQWWQEFLKEHVSILAMNEDEAEALTGESDP 267
|
250 260 270
....*....|....*....|....*....|.
gi 492279673 224 KEALELISKKCSIAIVKVGGNGSYIRKGTEE 254
Cdd:PRK15074 268 LLASDKALDWVDLVLCTAGPIGLYMAGYTED 298
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
7-313 |
3.07e-27 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 109.03 E-value: 3.07e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 7 LGNALVDVLATLkDDTLLDEMGLPKGSMQLIDDAKLQQINERFSQMKTHLATGGAAANTI----LGLACLGAgTGFIGKI 82
Cdd:PLN02548 1 MGNPLLDISAVV-DQDFLDKYDVKLNNAILAEEKHLPMYDELASKYNVEYIAGGATQNSIrvaqWMLQIPGA-TSYMGCI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 83 GNDAYGNFFRANLQRNGIEDKLLVSD-LPSGVASTFISpDGERTFGTYLGAASTLKAEDL----TLDMFKGYAYLLIEGY 157
Cdd:PLN02548 79 GKDKFGEEMKKCATAAGVNVHYYEDEsTPTGTCAVLVV-GGERSLVANLSAANCYKVEHLkkpeNWALVEKAKFYYIAGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 158 -LVQDHDMILHAIELAKEAGLQVCLDMASYNIVagdlEFFTLLINK---YVDIVFANEEEAKAFT-----GKEDPKE-AL 227
Cdd:PLN02548 158 fLTVSPESIMLVAEHAAANNKTFMMNLSAPFIC----EFFKDQLMEalpYVDFLFGNETEARTFAkvqgwETEDVEEiAL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 228 EL---------------ISKKCSIAIVKVGGNgsyirkgTEEIKVEAIPVKKVIDTTGAGDYFASGFLYGLTCGYSLEKC 292
Cdd:PLN02548 234 KIsalpkasgthkrtvvITQGADPTVVAEDGK-------VKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEEC 306
|
330 340
....*....|....*....|.
gi 492279673 293 AKIGSILSGNVIQIVGTTIPG 313
Cdd:PLN02548 307 VRAGNYAANVIIQRSGCTYPE 327
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
59-310 |
3.57e-27 |
|
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: 107.50 E-value: 3.57e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSDLPSGVASTFISPDGERTFgTYLGAAstlKA 138
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFIDPNGERTI-TVPGER---LE 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 139 EDLTLDMFKGYAYLLIEGYLVQDHdmILHAIELAKEAGLQVCLDMASYNIVAgdlefftllINKYVDIVFANEEEAkaft 218
Cdd:cd01947 112 DDLKWPILDEGDGVFITAAAVDKE--AIRKCRETKLVILQVTPRVRVDELNQ---------ALIPLDILIGSRLDP---- 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 219 GKEDPKEALELISKKCSIaiVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLTCGYSLEKCAKIGSI 298
Cdd:cd01947 177 GELVVAEKIAGPFPRYLI--VTEGELGAILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQ 253
|
250
....*....|..
gi 492279673 299 LSGNVIQIVGTT 310
Cdd:cd01947 254 CGAICVSHFGPY 265
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
60-305 |
3.63e-27 |
|
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: 107.89 E-value: 3.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 60 GAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVS-DLPSGVASTFISPDGERTFGTYLGAASTLKA 138
Cdd:cd01944 36 GGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRgGDDGGCLVALVEPDGERSFISISGAEQDWST 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 139 EDLTLDMFKGYAYLLIEGYLVQDH---DMILHAIELAKEAGLQVCLDmASYNIVAGDLEFFTLLINKYVdIVFANEEEAK 215
Cdd:cd01944 116 EWFATLTVAPYDYVYLSGYTLASEnasKVILLEWLEALPAGTTLVFD-PGPRISDIPDTILQALMAKRP-IWSCNREEAA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 216 AFTGKEDP---KEALELISKKCSIAIVKVGGNGSYIR-KGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLTCGYSLEK 291
Cdd:cd01944 194 IFAERGDPaaeASALRIYAKTAAPVVVRLGSNGAWIRlPDGNTHIIPGFKVK-AVDTIGAGDTHAGGMLAGLAKGMSLAD 272
|
250
....*....|....
gi 492279673 292 CAKIGSILSGNVIQ 305
Cdd:cd01944 273 AVLLANAAAAIVVT 286
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
59-309 |
4.16e-26 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 105.59 E-value: 4.16e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGI--EDKLLVSDLPSGVASTFI-SPDGERTFGTYLGAAST 135
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVntSFVSRTENSSTGLAMIFVdTKTGNNEIVIIPGANNA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 136 LKAEDL---TLDMFKGYAYLLiegylVQDH---DMILHAIELAKEAGLQVCLDMA---SYNIVAGDLEFFtllinKYVDI 206
Cdd:PTZ00292 132 LTPQMVdaqTDNIQNICKYLI-----CQNEiplETTLDALKEAKERGCYTVFNPApapKLAEVEIIKPFL-----KYVSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 207 VFANEEEAKAFTGKE--DPKEAL----ELISKKCSIAIVKVGGNG-SYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGF 279
Cdd:PTZ00292 202 FCVNEVEAALITGMEvtDTESAFkaskELQQLGVENVIITLGANGcLIVEKENEPVHVPGKRVK-AVDTTGAGDCFVGSM 280
|
250 260 270
....*....|....*....|....*....|
gi 492279673 280 LYGLTCGYSLEKCAKIGSILSGNVIQIVGT 309
Cdd:PTZ00292 281 AYFMSRGKDLKESCKRANRIAAISVTRHGT 310
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
59-291 |
4.62e-24 |
|
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: 99.29 E-value: 4.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIE--DKLLVSDLPSGVAS-TFISPDGERTfgTYLGAAST 135
Cdd:cd01945 36 GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDtsFIVVAPGARSPISSiTDITGDRATI--SITAIDTQ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 136 LKAEDLTLDMFKGYAYLLIEGYLvqdHDMILHAIELAKEAGLQVCLDmasynIVAGDLEFFTLLInKYVDIVFANEEEAK 215
Cdd:cd01945 114 AAPDSLPDAILGGADAVLVDGRQ---PEAALHLAQEARARGIPIPLD-----LDGGGLRVLEELL-PLADHAICSENFLR 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 492279673 216 AFTGKEDPKEALELISKKCSIAIVKVGGNGSYIRKGTEE-IKVEAIPVKkVIDTTGAGDYFASGFLYGLTCGYSLEK 291
Cdd:cd01945 185 PNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGElFHVPAFPVE-VVDTTGAGDVFHGAFAHALAEGMPLRE 260
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
59-308 |
6.74e-22 |
|
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: 92.80 E-value: 6.74e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDK-LLVSDLPSGVASTFIsPDGERTFGTY-LGAASTL 136
Cdd:cd01940 22 GGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIShCRVKEGENAVADVEL-VDGDRIFGLSnKGGVARE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 137 KAEDLTLDMFKGYAYLLIEGYLVQDHdmILHAIELAKEAGLQVCLDMaSYNivaGDLEFFTLLInKYVDIVFANEEEaka 216
Cdd:cd01940 101 HPFEADLEYLSQFDLVHTGIYSHEGH--LEKALQALVGAGALISFDF-SDR---WDDDYLQLVC-PYVDFAFFSASD--- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 217 FTGKEDPKEALELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVkKVIDTTGAGDYFASGFLYG-LTCGYSLEKCAKI 295
Cdd:cd01940 171 LSDEEVKAKLKEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPV-EVVDTLGAGDSFIAGFLLSlLAGGTAIAEAMRQ 249
|
250
....*....|...
gi 492279673 296 GSILSGNVIQIVG 308
Cdd:cd01940 250 GAQFAAKTCGHEG 262
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
55-290 |
7.86e-22 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 93.40 E-value: 7.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 55 HLATGGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGI--EDKLLVSDLPSGVASTFISPDGERTFGTYLGA 132
Cdd:PRK11142 35 QVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIdtAPVSVIKGESTGVALIFVNDEGENSIGIHAGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 133 ASTLKAEDLT--LDMFKGYAYLLIEgyLVQDHDMILHAIELAKEAGLQVCLDMASYNIVAGDLEfftllinKYVDIVFAN 210
Cdd:PRK11142 115 NAALTPALVEahRELIANADALLMQ--LETPLETVLAAAKIAKQHGTKVILNPAPARELPDELL-------ALVDIITPN 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 211 EEEAKAFTG-----KEDPKEALELISKK-CSIAIVKVGGNGSYI-RKGTEEIkVEAIPVkKVIDTTGAGDYFASGFLYGL 283
Cdd:PRK11142 186 ETEAEKLTGirvedDDDAAKAAQVLHQKgIETVLITLGSRGVWLsENGEGQR-VPGFRV-QAVDTIAAGDTFNGALVTAL 263
|
....*..
gi 492279673 284 TCGYSLE 290
Cdd:PRK11142 264 LEGKPLP 270
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
59-283 |
9.44e-22 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 93.46 E-value: 9.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSDlPSGVASTFI---SPDGERTFgTYL---GA 132
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLD-PAHRTSTVVvdlDDQGERSF-TFMvrpSA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 133 ASTLKAEDLTldMFKGYAYLLIEGY-LVQD--HDMILHAIELAKEAGLQVCLDMasyNI---VAGDLEFFTLLINKYV-- 204
Cdd:PRK09434 106 DLFLQPQDLP--PFRQGEWLHLCSIaLSAEpsRSTTFEAMRRIKAAGGFVSFDP---NLredLWQDEAELRECLRQALal 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 205 -DIVFANEEEAKAFTGKEDPKEALELISKKCSIA--IVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLY 281
Cdd:PRK09434 181 aDVVKLSEEELCFLSGTSQLEDAIYALADRYPIAllLVTLGAEGVLVHTRGQVQHFPAPSVD-PVDTTGAGDAFVAGLLA 259
|
..
gi 492279673 282 GL 283
Cdd:PRK09434 260 GL 261
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
59-296 |
5.43e-19 |
|
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: 85.44 E-value: 5.43e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIED-KLLVSDLPSGVASTFISPDGErtfgTYLGAASTLK 137
Cdd:cd01941 35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVrGIVFEGRSTASYTAILDKDGD----LVVALADMDI 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 138 AEDLTLDMFKGYAYLLIE-GYLVQD----HDMILHAIELAKEAGLQVCLDMASYNIVAgdlefFTLLINKYVDIVFANEE 212
Cdd:cd01941 111 YELLTPDFLRKIREALKEaKPIVVDanlpEEALEYLLALAAKHGVPVAFEPTSAPKLK-----KLFYLLHAIDLLTPNRA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 213 EAKAFTG------KEDPKEALELISKKCSIAIVKVGGNGSYIR-KGTEEIKVEAIP--VKKVIDTTGAGDYFASGFLYGL 283
Cdd:cd01941 186 ELEALAGaliennEDENKAAKILLLPGIKNVIVTLGAKGVLLSsREGGVETKLFPApqPETVVNVTGAGDAFVAGLVAGL 265
|
250
....*....|...
gi 492279673 284 TCGYSLEKCAKIG 296
Cdd:cd01941 266 LEGMSLDDSLRFA 278
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
57-280 |
8.29e-19 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 85.44 E-value: 8.29e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 57 ATGGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSDLPSGVASTFIS--PDGERTFGTYL--GA 132
Cdd:PLN02323 41 APGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTlrSDGEREFMFYRnpSA 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 133 ASTLKAEDLTLDMFKGYAYL------LIEGYLVQDHdmiLHAIELAKEAG--------LQVCL----DMASYNIvagdle 194
Cdd:PLN02323 121 DMLLRESELDLDLIRKAKIFhygsisLITEPCRSAH---LAAMKIAKEAGallsydpnLRLPLwpsaEAAREGI------ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 195 fftLLINKYVDIVFANEEEAKAFTGKEDPKE--ALELISKKCSIAIVKVGGNGSyiRKGTEEIK--VEAIPVkKVIDTTG 270
Cdd:PLN02323 192 ---MSIWDEADIIKVSDEEVEFLTGGDDPDDdtVVKLWHPNLKLLLVTEGEEGC--RYYTKDFKgrVEGFKV-KAVDTTG 265
|
250
....*....|
gi 492279673 271 AGDYFASGFL 280
Cdd:PLN02323 266 AGDAFVGGLL 275
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
60-310 |
3.80e-17 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 80.63 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 60 GAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSDlpsGVAST-----FISP-------DGERTFg 127
Cdd:COG2870 56 GGAANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVD---PRRPTttktrVIAGgqqllrlDFEDRF- 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 128 tYLGAASTLKAEDLTLDMFKGYAYLLIEGY----LVQDHdmILHAIELAKEAGLQVCLDMASYNivagdlefftLLINKY 203
Cdd:COG2870 132 -PLSAELEARLLAALEAALPEVDAVILSDYgkgvLTPEL--IQALIALARAAGKPVLVDPKGRD----------FSRYRG 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 204 VDIVFANEEEAKAFTGKEDPKE------ALELISK-KCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKKVIDTTGAGDYFA 276
Cdd:COG2870 199 ATLLTPNLKEAEAAVGIPIADEeelvaaAAELLERlGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVI 278
|
250 260 270
....*....|....*....|....*....|....
gi 492279673 277 SGFLYGLTCGYSLEKCAKIGSILSGNVIQIVGTT 310
Cdd:COG2870 279 ATLALALAAGASLEEAAELANLAAGIVVGKLGTA 312
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
60-309 |
2.32e-15 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 75.29 E-value: 2.32e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 60 GAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDKLLVS-DLPSGVASTFISP-------DGERTfgTYLG 131
Cdd:cd01172 40 GGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTDGIVDeGRPTTTKTRVIARnqqllrvDREDD--SPLS 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 132 AASTLKAEDLTLDMFKGYAYLLIE--GYLVQDHDMILHAIELAKEAGLQVCLDmasynivAGDLEFFtllinKY--VDIV 207
Cdd:cd01172 118 AEEEQRLIERIAERLPEADVVILSdyGKGVLTPRVIEALIAAARELGIPVLVD-------PKGRDYS-----KYrgATLL 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 208 FANEEEAKAFTGKEDPKE------ALELISKK-CSIAIVKVGGNGSYIRKGTEEIkvEAIPV--KKVIDTTGAGDYFASG 278
Cdd:cd01172 186 TPNEKEAREALGDEINDDdeleaaGEKLLELLnLEALLVTLGEEGMTLFERDGEV--QHIPAlaKEVYDVTGAGDTVIAT 263
|
250 260 270
....*....|....*....|....*....|.
gi 492279673 279 FLYGLTCGYSLEKCAKIGSILSGNVIQIVGT 309
Cdd:cd01172 264 LALALAAGADLEEAAFLANAAAGVVVGKVGT 294
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
148-284 |
5.30e-15 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 72.51 E-value: 5.30e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 148 GYAYLLIEGYLVQDHDMILhAIELAKEAGLQVCLDMASyniVAGDLEFFTLL-INKYVDIVFANEEEAKAFTGKEDPKE- 225
Cdd:cd00287 57 GADAVVISGLSPAPEAVLD-ALEEARRRGVPVVLDPGP---RAVRLDGEELEkLLPGVDILTPNEEEAEALTGRRDLEVk 132
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 492279673 226 -----ALELISKKCSIAIVKVGGNGSYI--RKGTEeIKVEAIPVKkVIDTTGAGDYFASGFLYGLT 284
Cdd:cd00287 133 eaaeaAALLLSKGPKVVIVTLGEKGAIVatRGGTE-VHVPAFPVK-VVDTTGAGDAFLAALAAGLA 196
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
59-308 |
1.15e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 67.07 E-value: 1.15e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIE-DKLLVSDLPSGVASTFISpDGERTFGTY---LGAAS 134
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDiSHVHTKHGVTAQTQVELH-DNDRVFGDYtegVMADF 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 135 TLKAEDLTLDMfkgyaylliegylvqDHDMILHAI------ELAK--EAGLQVCLDMASynivAGDLEFFTLLInKYVDI 206
Cdd:PRK09813 102 ALSEEDYAWLA---------------QYDIVHAAIwghaedAFPQlhAAGKLTAFDFSD----KWDSPLWQTLV-PHLDY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 207 VFANEEeakaftgKEDP---KEALELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGL 283
Cdd:PRK09813 162 AFASAP-------QEDEflrLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVT-VVDTMGAGDSFIAGFLCGW 233
|
250 260
....*....|....*....|....*
gi 492279673 284 TCGYSLEKCAKIGSILSGNVIQIVG 308
Cdd:PRK09813 234 LAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
69-312 |
4.65e-12 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 65.54 E-value: 4.65e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 69 LACLGA---GTGFIGkiGNDayGNFFRANLQRNGIEDKLLVSDLPSGVASTFISPDGERTF-----GTYLGAASTLKAED 140
Cdd:COG1105 45 LKALGVdvtALGFLG--GFT--GEFIEELLDEEGIPTDFVPIEGETRINIKIVDPSDGTETeinepGPEISEEELEALLE 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 141 LTLDMFKGYAYLLIEGYLVQ--DHDMILHAIELAKEAGLQVCLDmASynivaGDLefFTLLINKYVDIVFANEEEAKAFT 218
Cdd:COG1105 121 RLEELLKEGDWVVLSGSLPPgvPPDFYAELIRLARARGAKVVLD-TS-----GEA--LKAALEAGPDLIKPNLEELEELL 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 219 GKEDP------KEALELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLTCGYSLEKC 292
Cdd:COG1105 193 GRPLEtlediiAAARELLERGAENVVVSLGADGALLVTEDGVYRAKPPKVE-VVSTVGAGDSMVAGFLAGLARGLDLEEA 271
|
250 260
....*....|....*....|
gi 492279673 293 AKIGSILSGNVIQIVGTTIP 312
Cdd:COG1105 272 LRLAVAAGAAAALSPGTGLP 291
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
61-283 |
5.41e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 63.31 E-value: 5.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 61 AAANtiLGLAClgagtGFIGKIGNDAYGNFFRANLQRNGIEDKLLVSDLPSGVAST--------FISPDGERT------- 125
Cdd:PLN02341 128 AAAR--LGLRC-----STIGHVGDEIYGKFLLDVLAEEGISVVGLIEGTDAGDSSSasyetllcWVLVDPLQRhgfcsra 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 126 -FGTY--LGAASTLKAEDLTldMFKGYAYLLIEGYLVQDH--DMILHAIELAKEAGLQVCLD---MASYNIVAGDLEFFT 197
Cdd:PLN02341 201 dFGPEpaFSWISKLSAEAKM--AIRQSKALFCNGYVFDELspSAIASAVDYAIDVGTAVFFDpgpRGKSLLVGTPDERRA 278
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 198 L-LINKYVDIVFANEEEAKAFTGKEDPKEALELISKKCSIA---IVKVGGNGS-YIRKGTeeIKVEAIPVKKVIDTTGAG 272
Cdd:PLN02341 279 LeHLLRMSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwvVVKMGSKGSiLVTRSS--VSCAPAFKVNVVDTVGCG 356
|
250
....*....|....*
gi 492279673 273 DYFAS----GFLYGL 283
Cdd:PLN02341 357 DSFAAaialGYIHNL 371
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
59-286 |
2.36e-10 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 60.50 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 59 GGAAANTILGLACLGAGTGFIGKIGNDAYGNFFRANLQRNGIEDkllvSDLP----SGVASTFI--SPDGERTFGTYLGA 132
Cdd:cd01939 36 GGNASNSCTVLRLLGLSCEFLGVLSRGPVFESLLDDFQSRGIDI----SHCYrkdiDEPASSYIirSRAGGRTTIVNDNN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 133 ASTLKAEDLTLDMFKGYAYLLIEG-YLVQDHDMILHAIELAKEAGLQvcldmaSYNIvagDLEFF-----TLLINKYVDI 206
Cdd:cd01939 112 LPEVTYDDFSKIDLTQYGWIHFEGrNPDETLRMMQHIEEHNNRRPEI------RITI---SVEVEkpreeLLELAAYCDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 207 VFANEEEAKAFtGKEDPKEALELIS---KKCSIAIVKVGGNGSYIRKGTEEI-KVEAIPVKKVIDTTGAGDYFASGFLYG 282
Cdd:cd01939 183 VFVSKDWAQSR-GYKSPEECLRGEGpraKKAALLVCTWGDQGAGALGPDGEYvHSPAHKPIRVVDTLGAGDTFNAAVIYA 261
|
....
gi 492279673 283 LTCG 286
Cdd:cd01939 262 LNKG 265
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
76-296 |
3.57e-10 |
|
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: 59.85 E-value: 3.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 76 TGFIGKigndAYGNFFRANLQRNGIEDKLLVSDLPSGVASTFISPDGERTfgTYLGAASTLKAEDLT------LDMFKGY 149
Cdd:cd01164 56 LGFLGG----FTGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGTET--EINEPGPEISEEELEalleklKALLKKG 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 150 AYLLIEGYLVQD--HDMILHAIELAKEAGLQVCLDmasyniVAGDLefFTLLINKYVDIVFANEEEAKAFTGK-----ED 222
Cdd:cd01164 130 DIVVLSGSLPPGvpADFYAELVRLAREKGARVILD------TSGEA--LLAALAAKPFLIKPNREELEELFGRplgdeED 201
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 492279673 223 PKEAL-ELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKkVIDTTGAGDYFASGFLYGLTCGYSLEKCAKIG 296
Cdd:cd01164 202 VIAAArKLIERGAENVLVSLGADGALLVTKDGVYRASPPKVK-VVSTVGAGDSMVAGFVAGLAQGLSLEEALRLA 275
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
57-304 |
1.96e-08 |
|
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: 54.33 E-value: 1.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 57 ATGGAAANTILGLACLGAGTGFIGKIGNDAYGNFfrANLQRNGIEdkllVSDLPSGVASTF---ISPDGERTFGTYLGAA 133
Cdd:cd01937 22 KPGGPATYASLTLSRLGLTVKLVTKVGRDYPDKW--SDLFDNGIE----VISLLSTETTTFelnYTNEGRTRTLLAKCAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 134 STLKAEDLtldmfkgyAYLLIEGYLVQD--HDMIlhaIELAKEAGLqVCLDMASYNIVAGDLEFFTLLINKYVDIVFANE 211
Cdd:cd01937 96 IPDTESPL--------STITAEIVILGPvpEEIS---PSLFRKFAF-ISLDAQGFLRRANQEKLIKCVILKLHDVLKLSR 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 212 EEAKAFTgkeDPKEALELI-SKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPvKKVIDTTGAGDYFASGFLYGLTCGYSLE 290
Cdd:cd01937 164 VEAEVIS---TPTELARLIkETGVKEIIVTDGEEGGYIFDGNGKYTIPASK-KDVVDPTGAGDVFLAAFLYSRLSGKDIK 239
|
250
....*....|....
gi 492279673 291 KCAKIGSILSGNVI 304
Cdd:cd01937 240 EAAEFAAAAAAKFI 253
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
192-312 |
3.68e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 50.96 E-value: 3.68e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 192 DLEFFTLLinKYVDIVFANEEEAKAFTgkedpkeaLELISKKCSIaIVKVGGNGSYIRKGTEEIKVEAIPVKKViDTTGA 271
Cdd:PLN02630 172 ETGFYDML--PRIGFLKASSEEALFID--------VEEVRQKCCV-IVTNGKKGCRIYWKDGEMRVPPFPAIQV-DPTGA 239
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 492279673 272 GDYFASGFLYGLTCGYSLEKCAKIGSILSGNVIQIVGttIP 312
Cdd:PLN02630 240 GDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG--IP 278
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
189-316 |
1.05e-06 |
|
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: 49.65 E-value: 1.05e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 492279673 189 VAGDLEFFtLLINKYVDIVFANEEEAKAFTGKEDPKEALELISKKC--------------SIAIVKVGGNGSYIR--KGT 252
Cdd:cd01943 167 DPENLEDL-LQALPRVDVFSPNLEEAARLLGLPTSEPSSDEEKEAVlqallfsgilqdpgGGVVLRCGKLGCYVGsaDSG 245
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 492279673 253 EEIKVEAI--PVKKVIDTTGAGDYFASGFLYGLTCGYSLEKCAKIGSILSGNVIQIVG----TTIPG-ERW 316
Cdd:cd01943 246 PELWLPAYhtKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGlprlTKVEGeELW 316
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
204-280 |
1.18e-06 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 49.00 E-value: 1.18e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 492279673 204 VDIVFANEEEAKAFTGKEDP-KEALELISKKCSIAIVKVGGNGSYIRKGTEEIKVEAIPVKKVIDTTGAGDYFASGFL 280
Cdd:cd01946 164 VDVVIINDGEARQLTGAANLvKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGFI 241
|
|
| |
