|
Name |
Accession |
Description |
Interval |
E-value |
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
3-317 |
2.02e-137 |
|
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: 391.98 E-value: 2.02e-137
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 3 TFDVLCIGNAIVDILARTDDVFLETNGIIKGAMNLIDAERAELLYSRMgPATEMSGGSAGNTAAGIASLGGRSAYFGKVA 82
Cdd:cd01168 1 RYDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILADMEEQEELLAKL-PVKYIAGGSAANTIRGAAALGGSAAFIGRVG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 83 TDHLGRVFAHDIRAQGVAFDTRPLEKGsPTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKVADARVTYFEGYLWDP 162
Cdd:cd01168 80 DDKLGDFLLKDLRAAGVDTRYQVQPDG-PTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYLLTV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 163 PraKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRsrTVDIVFANEDEAKALYK---TKSLETAIAAMRMDC 239
Cdd:cd01168 159 P--PEAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELLP--YVDILFGNEEEAEALAEaetTDDLEAALKLLALRC 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489055258 240 RLSVITRSEKGAVVVTPDQTLTVPAIEIDDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGPRPQ 317
Cdd:cd01168 235 RIVVITQGAKGAVVVEGGEVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-318 |
8.25e-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: 234.78 E-value: 8.25e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 5 DVLCIGNAIVDILARTDdvfletngiikgamnlIDAERAELLysRMGPATEMSGGSAGNTAAGIASLGGRSAYFGKVATD 84
Cdd:COG0524 1 DVLVIGEALVDLVARVD----------------RLPKGGETV--LAGSFRRSPGGAAANVAVALARLGARVALVGAVGDD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 85 HLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKVADARVTYFEGYLWDPPR 164
Cdd:COG0524 63 PFGDFLLAELRAEGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITLASEP 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 165 AKEAIVMASKIAHESGRQMAMTLSDPFCV-DRYRDEFLQLMRSrtVDIVFANEDEAKALYKTKSLETAIAAMR-MDCRLS 242
Cdd:COG0524 143 PREALLAALEAARAAGVPVSLDPNYRPALwEPARELLRELLAL--VDILFPNEEEAELLTGETDPEEAAAALLaRGVKLV 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055258 243 VITRSEKGAVVVTPDQTLTVPAIEIdDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGPRPQI 318
Cdd:COG0524 221 VVTLGAEGALLYTGGEVVHVPAFPV-EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPAL 295
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
5-323 |
2.48e-58 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 193.87 E-value: 2.48e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 5 DVLCIGNAIVDILARTDDVFLETNGIIKGAMNLID-AERAELLYSRMGPATEMS-GGSAGNTAAGIASLGGRS------- 75
Cdd:PLN02813 71 DVLGLGQAMVDFSGMVDDEFLERLGLEKGTRKVINhEERGKVLRALDGCSYKASaGGSLSNTLVALARLGSQSaagpaln 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 76 -AYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSpTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKVADARVTY 154
Cdd:PLN02813 151 vAMAGSVGSDPLGDFYRTKLRRANVHFLSQPVKDGT-TGTVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVLV 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 155 FEGYLWDPPRAKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMrSRTVDIVFANEDEAKALYK---TKSLETA 231
Cdd:PLN02813 230 VEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVM-GNYADILFANSDEARALCGlgsEESPESA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 232 IAAMRMDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDDlVDTTGAGDLYAAGFLYGYTkdRSLEDCARLGSLA---AGLI 308
Cdd:PLN02813 309 TRYLSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVP-VDTCGAGDAYAAGILYGLL--RGVSDLRGMGELAarvAATV 385
|
330
....*....|....*
gi 489055258 309 IQQMGPRpqISLEAA 323
Cdd:PLN02813 386 VGQQGTR--LRVEDA 398
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
5-315 |
2.23e-45 |
|
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: 155.93 E-value: 2.23e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 5 DVLCIGNAIVDILARTD---DVFLETngiikgamnLIDAERaellysrmgpatEMSGGSAGNTAAGIASLGGRSAYFGKV 81
Cdd:cd01942 1 DVAVVGHLNYDIILKVEsfpGPFESV---------LVKDLR------------REFGGSAGNTAVALAKLGLSPGLVAAV 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 82 ATDHLGRVFAHDIRAQGVafDTRPLEK--GSPTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKvADARVTYFEGYL 159
Cdd:cd01942 60 GEDFHGRLYLEELREEGV--DTSHVRVvdEDSTGVAFILTDGDDNQIAYFYPGAMDELEPNDEADPD-GLADIVHLSSGP 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 160 WDPPRAKEAIVMASKIAHESGRQMAMtlsdpfcvdRYRDEFLQLMRSrtVDIVFANEDEAKALYKTKSLETAIAAMRmdC 239
Cdd:cd01942 137 GLIELARELAAGGITVSFDPGQELPR---------LSGEELEEILER--ADILFVNDYEAELLKERTGLSEAELASG--V 203
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055258 240 RLSVITRSEKGAVVVTPDQTLTVPAIEIDDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGPR 315
Cdd:cd01942 204 RVVVVTLGPKGAIVFEDGEEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
5-315 |
5.85e-44 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 152.50 E-value: 5.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 5 DVLCIGNAIVDILARTDDVFLETNgiikgamnlidaeraellysRMGPATEMSGGSAGNTAAGIASLGGRSAYFGKVATD 84
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELV--------------------RVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDD 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 85 HLGRVFAHDIRAQGVafDTRPLE--KGSPTARSMIFVTPDGERSMNTYLGACVELGPEDVETSK--VADARVTYFEGYLw 160
Cdd:pfam00294 61 NFGEFLLQELKKEGV--DTDYVVidEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEdlLENADLLYISGSL- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 161 DPPRAKEAIVMASKIAHESGRQMaMTLSDPFcvDRYRDEFLQLMRSrtVDIVFANEDEAKALYKTK--SLETAIAA---- 234
Cdd:pfam00294 138 PLGLPEATLEELIEAAKNGGTFD-PNLLDPL--GAAREALLELLPL--ADLLKPNEEELEALTGAKldDIEEALAAlhkl 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 235 MRMDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGP 314
Cdd:pfam00294 213 LAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGA 292
|
.
gi 489055258 315 R 315
Cdd:pfam00294 293 Q 293
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
1-313 |
1.04e-41 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 147.87 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 1 MATFDVLCIGNAIVDILARTDDVFLETNGIIKGamNLIDAERAEL-LYS---RMGPATEMSGGSAGNTA---AGIASLG- 72
Cdd:PTZ00247 3 SAPKKLLGFGNPLLDISAHVSDEFLEKYGLELG--SAILAEEKQLpIFEeleSIPNVSYVPGGSALNTArvaQWMLQAPk 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 73 GRSAYFGKVATDHLGRVFAHDIRAQGV--AFDtrpLEKGSPTARSMIFVTpDGERSMNTYLGACVELGPEDVETSKVA-- 148
Cdd:PTZ00247 81 GFVCYVGCVGDDRFAEILKEAAEKDGVemLFE---YTTKAPTGTCAVLVC-GKERSLVANLGAANHLSAEHMQSHAVQea 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 149 --DARVTYFEGYLWDPprAKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRSrtVDIVFANEDEAKALYKTK 226
Cdd:PTZ00247 157 ikTAQLYYLEGFFLTV--SPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPY--VDILFGNEEEAKTFAKAM 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 227 SLET---AIAAMRMDC---------RLSVITRSEKGAVVVTPDQTLT--VPAIEIDDLVDTTGAGDLYAAGFLYGYTKDR 292
Cdd:PTZ00247 233 KWDTedlKEIAARIAMlpkysgtrpRLVVFTQGPEPTLIATKDGVTSvpVPPLDQEKIVDTNGAGDAFVGGFLAQYANGK 312
|
330 340
....*....|....*....|.
gi 489055258 293 SLEDCARLGSLAAGLIIQQMG 313
Cdd:PTZ00247 313 DIDRCVEAGHYSAQVIIQHNG 333
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
12-313 |
1.74e-41 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 148.02 E-value: 1.74e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 12 AIVDILARTDDVFLET-NGIIKGAM--------NLIDAERAELLYSR--MGPATEMSGGSAGNTAAGIAS-LGGRSAYFG 79
Cdd:PLN02379 29 ALVDHVARVDWSLLDQiPGDRGGSIrvtieeleHILREVNAHILPSPddLSPIKTMAGGSVANTIRGLSAgFGVSTGIIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 80 KVATDHLGRVFAHDIRAQGVAFdTRPLEKGSPTARSMIFVTPDGERSMNTYLGACV-----ELGPEDVETSKVADARVTY 154
Cdd:PLN02379 109 ACGDDEQGKLFVSNMGFSGVDL-SRLRAKKGPTAQCVCLVDALGNRTMRPCLSSAVklqadELTKEDFKGSKWLVLRYGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 155 FEgylwdppraKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRSRTVDIVFANEDEAKALYK---TKSLETA 231
Cdd:PLN02379 188 YN---------LEVIEAAIRLAKQEGLSVSLDLASFEMVRNFRSPLLQLLESGKIDLCFANEDEARELLRgeqESDPEAA 258
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 232 IAAMRMDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQ 311
Cdd:PLN02379 259 LEFLAKYCNWAVVTLGSKGCIARHGKEVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRA 338
|
..
gi 489055258 312 MG 313
Cdd:PLN02379 339 LG 340
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
5-315 |
4.87e-41 |
|
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: 145.03 E-value: 4.87e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 5 DVLCIGNAIVDILARTDDVFLETNGIikgamnlidaeraellysRMGPatemsGGSAGNTAAGIASLGGRSAYFGKVATD 84
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGGRLEQADSF------------------RKFF-----GGAEANVAVGLARLGHRVALVTAVGDD 57
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 85 HLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTPDGERSMNTYLG--ACVELGPEDVETSKVADARVTYFEGY-LWD 161
Cdd:cd01166 58 PFGRFILAELRREGVDTSHVRVDPGRPTGLYFLEIGAGGERRVLYYRAgsAASRLTPEDLDEAALAGADHLHLSGItLAL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 162 PPRAKEAIVMASKIAHESGRQMAM------TLSDPfcvDRYRDEFLQLMRsrTVDIVFANEDEAKALYKTKSLETAIAAM 235
Cdd:cd01166 138 SESAREALLEALEAAKARGVTVSFdlnyrpKLWSA---EEAREALEELLP--YVDIVLPSEEEAEALLGDEDPTDAAERA 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 236 RM---DCRLSVITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQM 312
Cdd:cd01166 213 LAlalGVKAVVVKLGAEGALVYTGGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRP 291
|
...
gi 489055258 313 GPR 315
Cdd:cd01166 292 GDI 294
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
9-313 |
3.63e-34 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 127.52 E-value: 3.63e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 9 IGNAIVDILARTDDVFLETNGIIKGamNLIDAERAEL-LYSRMG--PATE-MSGGSAGNT---AAGIASLGGRSAYFGKV 81
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLN--NAILAEEKHLpMYDELAskYNVEyIAGGATQNSirvAQWMLQIPGATSYMGCI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 82 ATDHLGRVFAHDIRAQGVAFDTRPLEKgSPTARSMIFVTpDGERSMNTYLGACVELGPEDVETSK----VADARVTYFEG 157
Cdd:PLN02548 79 GKDKFGEEMKKCATAAGVNVHYYEDES-TPTGTCAVLVV-GGERSLVANLSAANCYKVEHLKKPEnwalVEKAKFYYIAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 158 Y-LWDPPrakEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRsrTVDIVFANEDEAKALYKTKSLET------ 230
Cdd:PLN02548 157 FfLTVSP---ESIMLVAEHAAANNKTFMMNLSAPFICEFFKDQLMEALP--YVDFLFGNETEARTFAKVQGWETedveei 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 231 --AIAAMRMDC----RLSVITRSEKGAVVVTPDQTLTVPAIEI--DDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGS 302
Cdd:PLN02548 232 alKISALPKASgthkRTVVITQGADPTVVAEDGKVKEFPVIPLpkEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGN 311
|
330
....*....|.
gi 489055258 303 LAAGLIIQQMG 313
Cdd:PLN02548 312 YAANVIIQRSG 322
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
58-313 |
1.70e-27 |
|
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: 108.79 E-value: 1.70e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTPDGERSMNTYLGACVEL 137
Cdd:cd01174 36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVVPGANGEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 138 GPEDVETSKV----ADARVTYFEgylwDPPrakEAIVMASKIAHESGrqmAMTLSDPFCVDRYRDEFLQLmrsrtVDIVF 213
Cdd:cd01174 116 TPADVDAALEliaaADVLLLQLE----IPL---ETVLAALRAARRAG---VTVILNPAPARPLPAELLAL-----VDILV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 214 ANEDEAKALY--KTKSLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTLTVPAIEIdDLVDTTGAGDLYAAGFLYG 287
Cdd:cd01174 181 PNETEAALLTgiEVTDEEDAEKAARlllaKGVKNVIVTLGAKGALLASGGEVEHVPAFKV-KAVDTTGAGDTFIGALAAA 259
|
250 260
....*....|....*....|....*.
gi 489055258 288 YTKDRSLEDCARLGSLAAGLIIQQMG 313
Cdd:cd01174 260 LARGLSLEEAIRFANAAAALSVTRPG 285
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
6-307 |
4.63e-27 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 107.72 E-value: 4.63e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 6 VLCIGNAIVDILARTDDVfletngiikgamnlidaeraellysrMGPATEMSGGSAGNTAAGIASLGGRSAYFGKVATDH 85
Cdd:cd01167 2 VVCFGEALIDFIPEGSGA--------------------------PETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDE 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 86 LGRVFAHDIRAQGVafDTRPL--EKGSPTARSMIFVTPDGERSMNTYLGACVELGPEDVET-SKVADARVTYFeG--YLW 160
Cdd:cd01167 56 FGDFLLETLKEAGV--DTRGIqfDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNpDLLSEADILHF-GsiALA 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 161 DPPrAKEAIVMASKIAHESGrqmAMTLSDP-----FCVDRYRD-----EFLQLmrsrtVDIVFANEDEAKALYKTKSLET 230
Cdd:cd01167 133 SEP-SRSALLELLEAAKKAG---VLISFDPnlrppLWRDEEEAreriaELLEL-----ADIVKLSDEELELLFGEEDPEE 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 231 AIAAMR-MDCRLSVITRSEKGAVVVTPDQTLTVPAIEIdDLVDTTGAGDLYAAGFLYGYTKD-------RSLEDCARLGS 302
Cdd:cd01167 204 IAALLLlFGLKLVLVTRGADGALLYTKGGVGEVPGIPV-EVVDTTGAGDAFVAGLLAQLLSRgllaldeDELAEALRFAN 282
|
....*
gi 489055258 303 LAAGL 307
Cdd:cd01167 283 AVGAL 287
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
58-318 |
8.38e-25 |
|
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: 101.52 E-value: 8.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTPDGERSMNTYLGACVEL 137
Cdd:TIGR02152 31 GGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVVVAGANAEL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 138 GPEDVETSKVADARVTYFEGYLWDPPrakEAIVMASKIAHESGRQmamTLSDPFCVDRYRD-EFLQLmrsrtVDIVFANE 216
Cdd:TIGR02152 111 TPEDIDAAEALIAESDIVLLQLEIPL---ETVLEAAKIAKKHGVK---VILNPAPAIKDLDdELLSL-----VDIITPNE 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 217 DEAKALY--KTKSLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDLYAAGFLYGYTK 290
Cdd:TIGR02152 180 TEAEILTgiEVTDEEDAEKAAEklleKGVKNVIITLGSKGALLVSKDESKLIPAFKVK-AVDTTAAGDTFNGAFAVALAE 258
|
250 260
....*....|....*....|....*...
gi 489055258 291 DRSLEDCARLGSLAAGLIIQQMGPRPQI 318
Cdd:TIGR02152 259 GKSLEDAIRFANAAAAISVTRKGAQSSI 286
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
5-315 |
2.17e-20 |
|
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: 89.28 E-value: 2.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 5 DVLCIGNAIVDILARTDDVFLETNGIIkgAMNLidaeraellysrmgpaTEMSGGSAGNTAAGIASLGGRSAYFGKVATD 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDGKIV--ATDY----------------AVIGGGNAANAAVAVARLGGQARLIGVVGDD 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 85 HLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIfVTPDGERSMNTYLGACVELGPEDVETSKVADARVTYFEGYLWDppr 164
Cdd:cd01945 63 AIGRLILAELAAEGVDTSFIVVAPGARSPISSI-TDITGDRATISITAIDTQAAPDSLPDAILGGADAVLVDGRQPE--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 165 akeAIVMASKIAHESGRQmAMTLSDPfCVDRYRDEFLQLmrsrtVDIVFANEDEAKALYKTKSLETAIAAMRMDCRLSVI 244
Cdd:cd01945 139 ---AALHLAQEARARGIP-IPLDLDG-GGLRVLEELLPL-----ADHAICSENFLRPNTGSADDEALELLASLGIPFVAV 208
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489055258 245 TRSEKGAVVVTPD-QTLTVPAIEIdDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGPR 315
Cdd:cd01945 209 TLGEAGCLWLERDgELFHVPAFPV-EVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGR 279
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
58-315 |
3.94e-18 |
|
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: 82.47 E-value: 3.94e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRaQGVAFDTRPLEKGsPTARSMIFVTPDGERSmntylgACVEL 137
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELE-SGGDKHTVAWRDK-PTRKTLSFIDPNGERT------ITVPG 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 138 GP--EDVETSKVADARVTYFEGYLWDPPRAKEAIVMASKIahesgrqMAMTLSDPFcvdryrDEFLQLmrSRTVDIVFAN 215
Cdd:cd01947 108 ERleDDLKWPILDEGDGVFITAAAVDKEAIRKCRETKLVI-------LQVTPRVRV------DELNQA--LIPLDILIGS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 216 EDEAKALyktkSLETAIAAMRMDCRlsVITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDLYAAGFLYGYTKDRSLE 295
Cdd:cd01947 173 RLDPGEL----VVAEKIAGPFPRYL--IVTEGELGAILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIE 245
|
250 260
....*....|....*....|
gi 489055258 296 DCARLGSLAAGLIIQQMGPR 315
Cdd:cd01947 246 EALELGAQCGAICVSHFGPY 265
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
58-287 |
1.08e-17 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 81.91 E-value: 1.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVafDTRPLEKgSPTARSMIFV---TPDGERSMnTYL--- 131
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGV--DTTYLRL-DPAHRTSTVVvdlDDQGERSF-TFMvrp 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 132 GACVELGPEDVETSKVAD-------------ARVTYFEGylwdpprakeaivmASKIAHESGRqmamtlsdpFCVD-RYR 197
Cdd:PRK09434 104 SADLFLQPQDLPPFRQGEwlhlcsialsaepSRSTTFEA--------------MRRIKAAGGF---------VSFDpNLR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 198 DEFLQ--------LMRS-RTVDIVFANEDEAKALYKTKSLETAIAAM--RMDCRLSVITRSEKGAVVVTPDQTLTVPAIE 266
Cdd:PRK09434 161 EDLWQdeaelrecLRQAlALADVVKLSEEELCFLSGTSQLEDAIYALadRYPIALLLVTLGAEGVLVHTRGQVQHFPAPS 240
|
250 260
....*....|....*....|.
gi 489055258 267 IDdLVDTTGAGDLYAAGFLYG 287
Cdd:PRK09434 241 VD-PVDTTGAGDAFVAGLLAG 260
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
58-300 |
1.52e-17 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 81.98 E-value: 1.52e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFA-----HDIRAQGVAFDtrplekgsPTARS-MIFVT--PDGERSMNT 129
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLAdilkkNGVNNEGVRFD--------PGARTaLAFVTlrSDGEREFMF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 130 YL--GACVELGPEDVETSKVADARVTYFEGY-LWDPPrAKEAIVMASKIAHESGrqmAMTLSDPF-------CVDRYRDE 199
Cdd:PLN02323 115 YRnpSADMLLRESELDLDLIRKAKIFHYGSIsLITEP-CRSAHLAAMKIAKEAG---ALLSYDPNlrlplwpSAEAAREG 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 200 FLQLMrsRTVDIVFANEDEAKALYK--TKSLETAIAAMRMDCRLSVITRSEKGAVVVTPDQTLTVPAIEIdDLVDTTGAG 277
Cdd:PLN02323 191 IMSIW--DEADIIKVSDEEVEFLTGgdDPDDDTVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKV-KAVDTTGAG 267
|
250 260
....*....|....*....|....
gi 489055258 278 DLYAAGFLYGYTKDRS-LEDCARL 300
Cdd:PLN02323 268 DAFVGGLLSQLAKDLSlLEDEERL 291
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
58-313 |
1.03e-15 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 76.39 E-value: 1.03e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGsAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTP-------DGERSmnTY 130
Cdd:COG2870 56 GG-AANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTKTRVIAGgqqllrlDFEDR--FP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 131 LGACVELGPEDVETSKVADARVT----YFEGYLwDPPRAKEAIVMASKiahesgrqmamtLSDPFCVDRYRDEFLqlmRS 206
Cdd:COG2870 133 LSAELEARLLAALEAALPEVDAVilsdYGKGVL-TPELIQALIALARA------------AGKPVLVDPKGRDFS---RY 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 207 RTVDIVFANEDEAKAL--YKTKSLETAIAA-----MRMDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDDLVDTTGAGDL 279
Cdd:COG2870 197 RGATLLTPNLKEAEAAvgIPIADEEELVAAaaellERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDT 276
|
250 260 270
....*....|....*....|....*....|....
gi 489055258 280 YAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMG 313
Cdd:COG2870 277 VIATLALALAAGASLEEAAELANLAAGIVVGKLG 310
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
6-313 |
1.50e-15 |
|
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: 75.52 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 6 VLCIGNAIVDILArTDDVFLETNGIIKgamnlidaeraellysrmgpATEMS---GGSAGNTAAGIASLGGRSAYFGKVA 82
Cdd:cd01939 2 VLCVGLTVLDFIT-TVDKYPFEDSDQR--------------------TTNGRwqrGGNASNSCTVLRLLGLSCEFLGVLS 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 83 TDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKVADARVTYFEGYlwdp 162
Cdd:cd01939 61 RGPVFESLLDDFQSRGIDISHCYRKDIDEPASSYIIRSRAGGRTTIVNDNNLPEVTYDDFSKIDLTQYGWIHFEGR---- 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 163 pRAKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRSrtVDIVFANEDEAKALYKtKSLETAIAAMRMDCRLS 242
Cdd:cd01939 137 -NPDETLRMMQHIEEHNNRRPEIRITISVEVEKPREELLELAAY--CDVVFVSKDWAQSRGY-KSPEECLRGEGPRAKKA 212
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 489055258 243 VI---TRSEKGAVVVTPDQTLT-VPAIEIDDLVDTTGAGDLYAAGFLYGYTK-DRSLEDCARLGSLAAGLIIQQMG 313
Cdd:cd01939 213 ALlvcTWGDQGAGALGPDGEYVhSPAHKPIRVVDTLGAGDTFNAAVIYALNKgPDDLSEALDFGNRVASQKCTGVG 288
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
6-310 |
2.64e-15 |
|
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: 75.04 E-value: 2.64e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 6 VLCIGNAIVDILARTDDVfletngIIKGAmnlidaeraellySRMGPATEMSGGSAGNTAAGIASLGGRSAYFGKVATDH 85
Cdd:cd01941 2 IVVIGAANIDLRGKVSGS------LVPGT-------------SNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDS 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 86 LGRVFAHDIRAQGVafDTRPLEK-GSPTARSMIFVTPDGErsmnTYLGAC-----VELGPEDVE--TSKVADARVTYFEG 157
Cdd:cd01941 63 EGESILEESEKAGL--NVRGIVFeGRSTASYTAILDKDGD----LVVALAdmdiyELLTPDFLRkiREALKEAKPIVVDA 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 158 YLwdPPRAKEAIVmasKIAHESGRQMAMtlsDPFCVDRYRDEFLQLmrsRTVDIVFANEDEAKALYK----TKSLETAIA 233
Cdd:cd01941 137 NL--PEEALEYLL---ALAAKHGVPVAF---EPTSAPKLKKLFYLL---HAIDLLTPNRAELEALAGalieNNEDENKAA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 234 AMRMDCRLS--VITRSEKGAVVV---TPDQTLTVPAIEIDDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLI 308
Cdd:cd01941 206 KILLLPGIKnvIVTLGAKGVLLSsreGGVETKLFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
..
gi 489055258 309 IQ 310
Cdd:cd01941 286 LE 287
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
58-318 |
7.69e-15 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 73.75 E-value: 7.69e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGrvfaHDIRAQ----GVAFDTRPLEKGSPTARSMIFVTPDGERSMNTYLGA 133
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIG----ESMRQQlakdGIDTAPVSVIKGESTGVALIFVNDEGENSIGIHAGA 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 134 CVELGPEDVET--SKVADARvtYFEGYLWDPpraKEAIVMASKIAHESGRQM------AMTLSDpfcvdryrdEFLQLmr 205
Cdd:PRK11142 115 NAALTPALVEAhrELIANAD--ALLMQLETP---LETVLAAAKIAKQHGTKVilnpapARELPD---------ELLAL-- 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 206 srtVDIVFANEDEAKAL--YKTKSLETAIAAMRM----DCRLSVITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDL 279
Cdd:PRK11142 179 ---VDIITPNETEAEKLtgIRVEDDDDAAKAAQVlhqkGIETVLITLGSRGVWLSENGEGQRVPGFRVQ-AVDTIAAGDT 254
|
250 260 270
....*....|....*....|....*....|....*....
gi 489055258 280 YAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGPRPQI 318
Cdd:PRK11142 255 FNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSI 293
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
80-313 |
2.78e-14 |
|
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: 72.07 E-value: 2.78e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 80 KVATDHLGRV----FAHDIRA----QGVAFDTRPLEkGSPTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKVADAR 151
Cdd:cd01944 49 GIPTVNAGPLgngnWADQIRQamrdEGIEILLPPRG-GDDGGCLVALVEPDGERSFISISGAEQDWSTEWFATLTVAPYD 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 152 VTYFEGYLWDPPRAKEAIVMASKIAHESGRQMAMTLSdPFCVDRYRDEFLQLMRSRTvdIVFANEDEAKALYKTKSLETA 231
Cdd:cd01944 128 YVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPG-PRISDIPDTILQALMAKRP--IWSCNREEAAIFAERGDPAAE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 232 IAAMRMDCRLS---VITRSEKGAVVVTPD-QTLTVPAIEIDdLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGL 307
Cdd:cd01944 205 ASALRIYAKTAapvVVRLGSNGAWIRLPDgNTHIIPGFKVK-AVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAI 283
|
....*.
gi 489055258 308 IIQQMG 313
Cdd:cd01944 284 VVTRSG 289
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
215-306 |
3.21e-14 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 72.09 E-value: 3.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 215 NEDEAKALYKTK--SLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDLYAAGFLYGY 288
Cdd:COG1105 184 NLEELEELLGRPleTLEDIIAAARelleRGAENVVVSLGADGALLVTEDGVYRAKPPKVE-VVSTVGAGDSMVAGFLAGL 262
|
90
....*....|....*...
gi 489055258 289 TKDRSLEDCARLGSlAAG 306
Cdd:COG1105 263 ARGLDLEEALRLAV-AAG 279
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
9-222 |
6.35e-14 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 71.96 E-value: 6.35e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 9 IGNAIVDILARTDDVFLETNGIIKGAMNLIDAERAELLYSRMGP----ATEMSGGSAGNTAAGIASLG-GRSAYFGkvat 83
Cdd:PRK15074 39 IDQTLVDIEAKVDDEFLERYGLSKGHSLVIEDDVAEALYQELKQnnliTHEFAGGTIGNTLHNYSVLAdDRSVLLG---- 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 84 dhlgrVFAHDIRAQGVAFdtRPLEKGS-------------PTARSMIFVTPDGERSMNTYLGACVELGPEDVETSKVADA 150
Cdd:PRK15074 115 -----VMSSNIEIGSYAY--RYLCNTSsrtdlnylqgvdgPIGRCFTLISEDGERTFAISPGHMNQLRPESIPEDVIAGA 187
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489055258 151 RVTYFEGYLW-----DPprAKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRSRtVDIVFANEDEAKAL 222
Cdd:PRK15074 188 SALVLTAYLVrckpgEP--MPEATMKAIEYAKKHNVPVVLTLGTKFVIEDNPQWWQEFLKEH-VSILAMNEDEAEAL 261
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
71-314 |
1.52e-13 |
|
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: 69.80 E-value: 1.52e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 71 LGGRSAYFGKVATdhlgrvFAHDIRAQGVAFDTRPlEKGSPTARSMIFVTPDGERSMN--TYLGACVELGpeDVETSKVA 148
Cdd:cd01946 24 LGGSATYFSLSAS------YFTDVRLVGVVGEDFP-EEDYKLLNSHNIVTLGLLSKEDgkTFHWAGRYHY--DLNEADTL 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 149 DARVTYFEGYlwDP--PRAKE--AIVMASKIAHESGRQMAMTLSDP---------FCVDRYRDEFLQLMRSrtVDIVFAN 215
Cdd:cd01946 95 DTDLNVFADF--DPqlPEHYKdsEFVFLGNIAPELQREVLEQVKDPklvvmdtmnFWISIKPEKLKKVLAK--VDVVIIN 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 216 EDEAKALYKTKSL-ETAIAAMRMDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDDLVDTTGAGDLYAAGFLyGY---TKD 291
Cdd:cd01946 171 DGEARQLTGAANLvKAARLILAMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVFDPTGAGDTFAGGFI-GYlasQKD 249
|
250 260
....*....|....*....|....*.
gi 489055258 292 RSLEDCAR---LGSLAAGLIIQQMGP 314
Cdd:cd01946 250 TSEANMRRaiiYGSAMASFCVEDFGT 275
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
57-313 |
7.83e-13 |
|
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: 67.38 E-value: 7.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 57 SGGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGsPTARSMIfVTPDGERSMNTY-LGACV 135
Cdd:cd01940 21 PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEG-ENAVADV-ELVDGDRIFGLSnKGGVA 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 136 ELGPEDVETSKVADARVTY-----FEGYLwdpPRAKEAIVMAS-KIAHEsgrqmamtlsdpfCVDRYRDEFLQLMRSRtV 209
Cdd:cd01940 99 REHPFEADLEYLSQFDLVHtgiysHEGHL---EKALQALVGAGaLISFD-------------FSDRWDDDYLQLVCPY-V 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 210 DIVFAN-----EDEAKALYKTksletaiaAMRMDCRLSVITRSEKGAVVVTPDQTLTVpAIEIDDLVDTTGAGDLYAAGF 284
Cdd:cd01940 162 DFAFFSasdlsDEEVKAKLKE--------AVSRGAKLVIVTRGEDGAIAYDGAVFYSV-APRPVEVVDTLGAGDSFIAGF 232
|
250 260 270
....*....|....*....|....*....|
gi 489055258 285 LYGY-TKDRSLEDCARLGSLAAGLIIQQMG 313
Cdd:cd01940 233 LLSLlAGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
58-313 |
1.09e-12 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 67.84 E-value: 1.09e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVtpDGERSMNTYL---GAC 134
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTGLAMIFV--DTKTGNNEIViipGAN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 135 VELGPEDVETS-----KVADARVTYFEGYLwdpprakEAIVMASKIAHESGrqmAMTLSDP-----FCVDRYRDEFLQLm 204
Cdd:PTZ00292 130 NALTPQMVDAQtdniqNICKYLICQNEIPL-------ETTLDALKEAKERG---CYTVFNPapapkLAEVEIIKPFLKY- 198
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 205 rsrtVDIVFANEDEAKALY--KTKSLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTLT-VPAIEIDdLVDTTGAG 277
Cdd:PTZ00292 199 ----VSLFCVNEVEAALITgmEVTDTESAFKASKelqqLGVENVIITLGANGCLIVEKENEPVhVPGKRVK-AVDTTGAG 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 489055258 278 DLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMG 313
Cdd:PTZ00292 274 DCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
46-314 |
1.83e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 66.30 E-value: 1.83e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 46 LYSRMGPAteMSGGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVafDTRPLEKG-SPTARSMIFVTpDGE 124
Cdd:PRK09813 13 IYPQLGKA--FSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGV--DISHVHTKhGVTAQTQVELH-DND 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 125 RSMNTYLGACVE---LGPEDVETSKVADARVTYfegyLWDppRAKEAIvmaSKIaHESGRQMAMTLSDpfcvdRYRDEFL 201
Cdd:PRK09813 88 RVFGDYTEGVMAdfaLSEEDYAWLAQYDIVHAA----IWG--HAEDAF---PQL-HAAGKLTAFDFSD-----KWDSPLW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 202 QLMRSrTVDIVFANEDEakalyKTKSLETAIAAMR-MDCRLSVITRSEKGAVVVTPDQTLTVPaIEIDDLVDTTGAGDLY 280
Cdd:PRK09813 153 QTLVP-HLDYAFASAPQ-----EDEFLRLKMKAIVaRGAGVVIVTLGENGSIAWDGAQFWRQA-PEPVTVVDTMGAGDSF 225
|
250 260 270
....*....|....*....|....*....|....
gi 489055258 281 AAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGP 314
Cdd:PRK09813 226 IAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
189-289 |
2.22e-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: 64.81 E-value: 2.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 189 DPFCVDRYRDEFLQLMRSRTVDIVFANEDEAKALYKTKSLETAIAAMRMDCRLS------VITRSEKGAVVVTPD-QTLT 261
Cdd:cd00287 90 DPGPRAVRLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSkgpkvvIVTLGEKGAIVATRGgTEVH 169
|
90 100
....*....|....*....|....*...
gi 489055258 262 VPAIEIDdLVDTTGAGDLYAAGFLYGYT 289
Cdd:cd00287 170 VPAFPVK-VVDTTGAGDAFLAALAAGLA 196
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
215-306 |
5.91e-11 |
|
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: 62.16 E-value: 5.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 215 NEDEAKALYKTK--SLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDLYAAGFLYGY 288
Cdd:cd01164 184 NREELEELFGRPlgDEEDVIAAARklieRGAENVLVSLGADGALLVTKDGVYRASPPKVK-VVSTVGAGDSMVAGFVAGL 262
|
90
....*....|....*...
gi 489055258 289 TKDRSLEDCARLGsLAAG 306
Cdd:cd01164 263 AQGLSLEEALRLA-VAAG 279
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
55-316 |
1.55e-10 |
|
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: 61.04 E-value: 1.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 55 EMSGGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVafDTRPL-EKGSPTARSMIFVTP-------DGERs 126
Cdd:cd01172 36 EIRLGGAANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI--DTDGIvDEGRPTTTKTRVIARnqqllrvDRED- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 127 mNTYLGACVELGPEDVETSKVADARVTYFEGY---LWDPPRAKEAIVMAskiahesgRQMAM-TLSDPFCVD--RYRDef 200
Cdd:cd01172 113 -DSPLSAEEEQRLIERIAERLPEADVVILSDYgkgVLTPRVIEALIAAA--------RELGIpVLVDPKGRDysKYRG-- 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 201 lqlmrsrtVDIVFANEDEAKA-----LYKTKSLETAIAAMRMDCRLS--VITRSEKGAVVVTPDQTLT-VPAIEiDDLVD 272
Cdd:cd01172 182 --------ATLLTPNEKEAREalgdeINDDDELEAAGEKLLELLNLEalLVTLGEEGMTLFERDGEVQhIPALA-KEVYD 252
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 489055258 273 TTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMGPRP 316
Cdd:cd01172 253 VTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAP 296
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
215-315 |
2.59e-10 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 60.30 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 215 NEDEAKALYKT--KSLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTL--TVPAIEiddLVDTTGAGDLYAAGFLY 286
Cdd:TIGR03828 183 NDEELEELFGRelKTLEEIIEAARelldLGAENVLISLGADGALLVTKEGALfaQPPKGE---VVSTVGAGDSMVAGFLA 259
|
90 100
....*....|....*....|....*....
gi 489055258 287 GYTKDRSLEDCARLGSLAAGLIIQQMGPR 315
Cdd:TIGR03828 260 GLESGLSLEEALRLAVAAGSAAAFSEGTG 288
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
215-329 |
3.56e-10 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 59.90 E-value: 3.56e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 215 NEDEAKALYKT--KSLETAIAAMR----MDCRLSVITRSEKGAVVVTPDQTL--TVPAIEiddLVDTTGAGDLYAAGFLY 286
Cdd:TIGR03168 183 NHEELEELFGRelKTLEEIIEAARelldRGAENVLVSLGADGALLVTKEGALkaTPPKVE---VVNTVGAGDSMVAGFLA 259
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 489055258 287 GYTKDRSLEDCARLGsLAAGLiiqqmgprpqisleAAASQAGL 329
Cdd:TIGR03168 260 GLARGLSLEEALRFA-VAAGS--------------AAAFSPGT 287
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
205-315 |
6.40e-07 |
|
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: 50.42 E-value: 6.40e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 205 RSRTVDIVFANEDEAKALY-----KTKSLETAIAAMRMDCRL--------SVITRS-EKGAVVVTPDQ--TLTVPAI--E 266
Cdd:cd01943 177 ALPRVDVFSPNLEEAARLLglptsEPSSDEEKEAVLQALLFSgilqdpggGVVLRCgKLGCYVGSADSgpELWLPAYhtK 256
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 489055258 267 IDDLVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMG-PR 315
Cdd:cd01943 257 STKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGlPR 306
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
243-313 |
1.42e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 49.42 E-value: 1.42e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 489055258 243 VITRSEKGAVVVTPDQTLTVPAIEIDDlVDTTGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLIIQQMG 313
Cdd:PLN02630 207 IVTNGKKGCRIYWKDGEMRVPPFPAIQ-VDPTGAGDSFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG 276
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
210-300 |
4.20e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 48.29 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 210 DIVFANEDEAKALYKTKS-LETAIAAMRMDCRLS--VITRSEKGAVVVTPDQTLTVPAIEIDdLVDTTGAGDLYAAGFLY 286
Cdd:PLN02341 287 DVLLLTSEEAEALTGIRNpILAGQELLRPGIRTKwvVVKMGSKGSILVTRSSVSCAPAFKVN-VVDTVGCGDSFAAAIAL 365
|
90
....*....|....
gi 489055258 287 GYTKDRSLEDCARL 300
Cdd:PLN02341 366 GYIHNLPLVNTLTL 379
|
|
| PLN02967 |
PLN02967 |
kinase |
58-180 |
1.06e-05 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 46.96 E-value: 1.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVTPDGERSMnTYLGACVE- 136
Cdd:PLN02967 243 GGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKT-TCVKPCAEd 321
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 489055258 137 -LGPEDVETSKVADARVTYFEGYLWDPPRAKEAIVMASKIAHESG 180
Cdd:PLN02967 322 sLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLG 366
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
58-222 |
1.13e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 46.82 E-value: 1.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 58 GGSAGNTAAGIASLGGRSAYFGKVATDHLGRVFAHDIRAQGVAFDTRPLEKGSPTARSMIFVT--PDGERSMNTylgacV 135
Cdd:PLN02543 172 GGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfrDGGKMVAET-----V 246
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 136 ELGPED------VETSKVADARVTYFEGYLWDPPRAKEAIVMASKIAHESGRQMAMTLSDPFCVDRYRDEFLQLMRS--R 207
Cdd:PLN02543 247 KEAAEDsllaseLNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKawN 326
|
170
....*....|....*
gi 489055258 208 TVDIVFANEDEAKAL 222
Cdd:PLN02543 327 EADIIEVSRQELEFL 341
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
195-309 |
2.82e-05 |
|
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: 44.70 E-value: 2.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489055258 195 RYRDEFLQLmrsrtVDIVFANEDEAKalyKTKSLETAIAAMRM-DCRLSVITRSEKGAVVVTPDQTLTVPAIEIDdLVDT 273
Cdd:cd01937 147 LIKCVILKL-----HDVLKLSRVEAE---VISTPTELARLIKEtGVKEIIVTDGEEGGYIFDGNGKYTIPASKKD-VVDP 217
|
90 100 110
....*....|....*....|....*....|....*.
gi 489055258 274 TGAGDLYAAGFLYGYTKDRSLEDCARLGSLAAGLII 309
Cdd:cd01937 218 TGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| |
