|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
6-637 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1109.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 6 KRLDVICIGRVAVDLYAQQIGARLEDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEY 85
Cdd:COG3892 4 KTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 86 LITDKQRLTALVMLGIKDQETFPLIFYRDNCADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLKALEYARRHGL 165
Cdd:COG3892 84 VVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARAHGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 166 RTALDIDYRPVLWGLTSLGDGETRFIESGQVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKR 245
Cdd:COG3892 164 KVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLVCKR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 246 GPMGCVVLEGAIPDSWDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTK 325
Cdd:COG3892 244 GALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAMPTW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 326 AELDDYLSRAESVPRPDIDARLNHLHRVTSRRQAWPELCIFAFDHRKQLADLALETGRDESCIPQLKLLLLAAAEAAADE 405
Cdd:COG3892 324 EELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQVAAG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 406 AGLDGRSGILADGTYGQRSLNAITGKGWWIGRPIEMPSSRPLRLEHG-NIGSQLIDWPLEHVVKCLVFYHPADPAELRAE 484
Cdd:COG3892 404 AGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAELRLE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 485 QDALLLEVWQACNKSGHELLLEIILPENGPDKDErHYHDMLEHFYQLGIQPDWWKLPPLSSAEWERIGKLIAREDSWCRG 564
Cdd:COG3892 484 QEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDD-TVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPYCRG 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490229945 565 ILILGLDAPSDRLRAGFAEAAKHPMIKGFAVGRTIFGQPSRRWMQGELSDEALINEVKRNYLTLIGYWREARG 637
Cdd:COG3892 563 VVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQ 635
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
327-636 |
2.94e-179 |
|
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various prokaryotic carbohydrate kinases, has no known function.
Pssm-ID: 430888 Cd Length: 310 Bit Score: 510.29 E-value: 2.94e-179
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 327 ELDDYLSRAESVPRPDIDARLNHLHRVTSRRQAWPELCIFAFDHRKQLADLALETGRDESCIPQLKLLLLAAAEAAADEA 406
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 407 GLDGRSGILADGTYGQRSLNAITGKGWWIGRPIEMPSSRPLRLEHG-NIGSQLIDWPLEHVVKCLVFYHPADPAELRAEQ 485
Cdd:pfam09863 81 GLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 486 DALLLEVWQACNKSGHELLLEIILPENGPDKDErHYHDMLEHFYQLGIQPDWWKLPPLSSAEWERIGKLIAREDSWCRGI 565
Cdd:pfam09863 161 EAQLRELYDACRKSGHELLLEVIPPKDGPVDDE-TYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRGV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490229945 566 LILGLDAPSDRLRAGFAEAAKHPMIKGFAVGRTIFGQPSRRWMQGELSDEALINEVKRNYLTLIGYWREAR 636
Cdd:pfam09863 240 VILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
7-332 |
1.08e-161 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 465.53 E-value: 1.08e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 7 RLDVICIGRVAVDLYAQQIGARLEDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYL 86
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 87 ITDKQRLTALVMLGIKDQETFPLIFYRDNCADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLKALEYARRHGLR 166
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 167 TALDIDYRPVLWGltslgdgetrfiESGQVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKRG 246
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 247 PMGCVVLEGAiPDSWdSVPlqqGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTKA 326
Cdd:TIGR04382 229 PEGSLVYTGD-GEGV-EVP---GFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 490229945 327 ELDDYL 332
Cdd:TIGR04382 304 ELEAFL 309
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-328 |
2.37e-82 |
|
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: 261.36 E-value: 2.37e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYAQ----QIGARLEDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTE 84
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 85 YLITDKQRLTALVMLGIKDQETFPLIFYRdnCADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLKALEYARRHG 164
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 165 LRTALDIDYRPVLWGltslgdgetrfiesgQVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCK 244
Cdd:COG0524 159 VPVSLDPNYRPALWE---------------PARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 245 RGPMGCVVLEGaipDSWDSVPlqqGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPT 324
Cdd:COG0524 224 LGAEGALLYTG---GEVVHVP---AFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 490229945 325 KAEL 328
Cdd:COG0524 298 REEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-319 |
3.40e-80 |
|
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: 255.58 E-value: 3.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYAQQIGaRLEDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLIT 88
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 89 DKQRLTALVMLGIKDQETFPLIFYRDNCADMALSPEDIKEEYIASSRALAVTGTHLS-HANTREAVLKALEYARRHGLRT 167
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 168 ALDIDYRPVLWGLtslgdGETRfiesgqvtSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVR--NATKATLVCKR 245
Cdd:cd01166 160 SFDLNYRPKLWSA-----EEAR--------EALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490229945 246 GPMGCVVLEGaipdswDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCA 319
Cdd:cd01166 227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
10-317 |
1.54e-46 |
|
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: 166.27 E-value: 1.54e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVDLYAQQIGarleDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITD 89
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 90 KQRLTALVMLGIKDQ--ETFplIFYRDNCADMALSPEDIKEeyIASSRALAVTGTH-LSHANTREAVLKALEYARRHGLR 166
Cdd:cd01167 78 PAAPTTLAFVTLDADgeRSF--EFYRGPAADLLLDTELNPD--LLSEADILHFGSIaLASEPSRSALLELLEAAKKAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 167 TALDIDYRPVLWgltslGDGETRFiesgqvtSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKRG 246
Cdd:cd01167 154 ISFDPNLRPPLW-----RDEEEAR-------ERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 247 PMGCVVL----EGAIPdswdsvplqqGVRVDVLNVLGAGDAFMSGLLRG-------WLNDEGWEQACRYANACGALVVSR 315
Cdd:cd01167 222 ADGALLYtkggVGEVP----------GIPVEVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTK 291
|
..
gi 490229945 316 HG 317
Cdd:cd01167 292 AG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
9-319 |
5.86e-45 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 161.74 E-value: 5.86e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYAQQIGARLED--VASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYL 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELvrVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 87 ITDKQRLT--ALVMLGiKDQETFpLIFYRDNCADMALSPEDIKEEYIASSRALAVTGTHLShaNTREAVLKALEYARRHG 164
Cdd:pfam00294 81 VIDEDTRTgtALIEVD-GDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLPL--GLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 165 lrTALDIDYRPVLWgltslgdgetrfiesgQVTSQLQEVLHLFDLVVGTEEEFHIAGGST-----DTLTALKNVRNATKA 239
Cdd:pfam00294 157 --GTFDPNLLDPLG----------------AAREALLELLPLADLLKPNEEELEALTGAKlddieEALAALHKLLAKGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 240 TLVCKRGPMGCVVLEGAipdswDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCA 319
Cdd:pfam00294 219 TVIVTLGADGALVVEGD-----GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
7-318 |
4.95e-31 |
|
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: 123.49 E-value: 4.95e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 7 RLDVICIGRVAVDLYAQ-----------QIG-------ARLEDVASFSKYL---GGSSGNVAFGTAIQGLKSAMLARVGD 65
Cdd:cd01168 1 RYDVLGLGNALVDILAQvddafleklglKKGdmiladmEEQEELLAKLPVKyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 66 EHNGRFLRETLSRAGVDTEYLITDKQRL-TALVMLGIKDQETfpLIFYRDNCADmaLSPEDIKEEYIASSRALAVTGTHL 144
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQVQPDGPTgTCAVLVTPDAERT--MCTYLGAANE--LSPDDLDWSLLAKAKYLYLEGYLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 145 SHANtrEAVLKALEYARRHGLRTALDIdyrpvlwgltSLGDGETRFIEsgqvtsQLQEVLHLFDLVVGTEEEFHIAGGS- 223
Cdd:cd01168 157 TVPP--EAILLAAEHAKENGVKIALNL----------SAPFIVQRFKE------ALLELLPYVDILFGNEEEAEALAEAe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 224 -TDTLTALKNVRNATKATLVCKRGPMGCVVLEGA----IPdswdsvPLQQGVRVDVLnvlGAGDAFMSGLLRGWLNDEGW 298
Cdd:cd01168 219 tTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGevypVP------AIPVEKIVDTN---GAGDAFAGGFLYGLVQGEPL 289
|
330 340
....*....|....*....|
gi 490229945 299 EQACRYANACGALVVSRHGC 318
Cdd:cd01168 290 EECIRLGSYAAAEVIQQLGP 309
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
10-335 |
3.39e-30 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 121.27 E-value: 3.39e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVDLYAQQIGARLEDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITD 89
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 90 KQRLTALVMLGIKDQETFPLIFYRDNCADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLKALEYARRHGLRTAL 169
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 170 DIDYRPVLW--------GLTSLGDgETRFIEsgqvtsqlqevlhlfdlvVGTEE-EFHIAGGSTDTLTALKNVRNATKAT 240
Cdd:PLN02323 173 DPNLRLPLWpsaeaareGIMSIWD-EADIIK------------------VSDEEvEFLTGGDDPDDDTVVKLWHPNLKLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 241 LVCKrGPMGCVVLegaIPDSWDSVPlqqGVRVDVLNVLGAGDAFMSGLL------RGWLNDEG-WEQACRYANACGALVV 313
Cdd:PLN02323 234 LVTE-GEEGCRYY---TKDFKGRVE---GFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGAITT 306
|
330 340
....*....|....*....|..
gi 490229945 314 SRHGCAPAMPTKAELDDYLSRA 335
Cdd:PLN02323 307 TERGAIPALPTKEAVLKLLKKA 328
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
30-329 |
4.36e-29 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 117.73 E-value: 4.36e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 30 EDVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITDKQRLTALVMLGIKDQETFPL 109
Cdd:PRK09434 18 EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 110 IFYRDNCADMALSPEDI----KEEYiassraLAVTGTHLSHANTREAVLKALEYARRHGLRTALDIDYRPVLWgltslgd 185
Cdd:PRK09434 98 TFMVRPSADLFLQPQDLppfrQGEW------LHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLW------- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 186 getrfiesgQVTSQLQEVLH----LFDLVVGTEEEFHIAGGSTDTLTALKNV--RNATKATLVcKRGPMG-CVVLEGAIp 258
Cdd:PRK09434 165 ---------QDEAELRECLRqalaLADVVKLSEEELCFLSGTSQLEDAIYALadRYPIALLLV-TLGAEGvLVHTRGQV- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490229945 259 dswDSVPlqqGVRVDVLNVLGAGDAFMSGLLRG------WLNDEGWEQACRYANACGALVVSRHGCAPAMPTKAELD 329
Cdd:PRK09434 234 ---QHFP---APSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
9-318 |
1.65e-25 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 106.63 E-value: 1.65e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYAQqiGARLED------VASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVD 82
Cdd:cd01942 1 DVAVVGHLNYDIILK--VESFPGpfesvlVKDLRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVD 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 83 TEYLITdkqrltalvmlgIKDQETfPLIFYRDN-----CADMALSPEDIKEEYIASSRALAVTGTHLShaNTREAVLKAL 157
Cdd:cd01942 79 TSHVRV------------VDEDST-GVAFILTDgddnqIAYFYPGAMDELEPNDEADPDGLADIVHLS--SGPGLIELAR 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 158 EyARRHGLRTALDidyrP--VLWGLTslgdgetrfiesgqvTSQLQEVLHLFDLVVGTEEEFHIAggstDTLTALK-NVR 234
Cdd:cd01942 144 E-LAAGGITVSFD----PgqELPRLS---------------GEELEEILERADILFVNDYEAELL----KERTGLSeAEL 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 235 NATKATLVCKRGPMGCVVLEGAipDSWDSVPLQqgvRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVS 314
Cdd:cd01942 200 ASGVRVVVVTLGPKGAIVFEDG--EEVEVPAVP---AVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVE 274
|
....
gi 490229945 315 RHGC 318
Cdd:cd01942 275 RRGA 278
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
9-324 |
1.85e-24 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 103.78 E-value: 1.85e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYAQ-----QIGARLEdVASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDT 83
Cdd:cd01174 1 KVVVVGSINVDLVTRvdrlpKPGETVL-GSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 84 EYL-ITDKQRL-TALVMLgikDQEtfplifyRDNC------ADMALSPEDIK--EEYIASSRALavtgthLSHANT-REA 152
Cdd:cd01174 80 SYVeVVVGAPTgTAVITV---DES-------GENRivvvpgANGELTPADVDaaLELIAAADVL------LLQLEIpLET 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 153 VLKALEYARRHGLRTALDidyrpvlwgltslgdgetrfieSGQVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTltalkN 232
Cdd:cd01174 144 VLAALRAARRAGVTVILN----------------------PAPARPLPAELLALVDILVPNETEAALLTGIEVT-----D 196
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 233 VRNATKATLVCKRGPMGCVVL----EGAI---PDSWDSVPlqqGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYA 305
Cdd:cd01174 197 EEDAEKAARLLLAKGVKNVIVtlgaKGALlasGGEVEHVP---AFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
330
....*....|....*....
gi 490229945 306 NACGALVVSRHGCAPAMPT 324
Cdd:cd01174 274 NAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-324 |
1.97e-17 |
|
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: 83.11 E-value: 1.97e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYAQQIGARLED----VASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTE 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDgkivATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 85 YLITDKQRLTAlVMLGIKDQETFPLIFYrdNCADMALSPEDIKEEYIASSRALAVTGtHLshantREAVLKALEYARRHG 164
Cdd:cd01945 81 FIVVAPGARSP-ISSITDITGDRATISI--TAIDTQAAPDSLPDAILGGADAVLVDG-RQ-----PEAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 165 LRTALDIDyrpvlwgltslGDGETrfiesgqvtsQLQEVLHLFDLVVGTEEEFHIAGGSTDTLtALKNVRNATKATLVCK 244
Cdd:cd01945 152 IPIPLDLD-----------GGGLR----------VLEELLPLADHAICSENFLRPNTGSADDE-ALELLASLGIPFVAVT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 245 RGPMGCVVLEGAipdswDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPT 324
Cdd:cd01945 210 LGEAGCLWLERD-----GELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
10-317 |
1.82e-15 |
|
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: 76.62 E-value: 1.82e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVDLYAQQIGArledvasfskYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITd 89
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 90 KQRLTALVMLGIKDQETfplIFYRDN---CADMALSPEDIkeEYIASSRaLAVTGTHlSHANTREAVLKALEYArrhGLR 166
Cdd:cd01940 71 KEGENAVADVELVDGDR---IFGLSNkggVAREHPFEADL--EYLSQFD-LVHTGIY-SHEGHLEKALQALVGA---GAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 167 TALDIDYRPVLWGLTSLGDG-ETRFIESGQVTSQLQEVLhlfdlvvgteeefhiaggstdtltaLKNVRNATKATLVCKR 245
Cdd:cd01940 141 ISFDFSDRWDDDYLQLVCPYvDFAFFSASDLSDEEVKAK-------------------------LKEAVSRGAKLVIVTR 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490229945 246 GPMGCVVLEGaipdswDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWL-NDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01940 196 GEDGAIAYDG------AVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
10-317 |
6.38e-15 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 75.16 E-value: 6.38e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVDLYaQQIGarledvasfSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITD 89
Cdd:PRK09813 3 LATIGDNCVDIY-PQLG---------KAFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 90 KQRlTALVMLGIKDQETfplIF--YRDNC-ADMALSPEDIKeeyIASSRALAVTGThLSHAntrEAVLKALeyaRRHGLR 166
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDYA---WLAQYDIVHAAI-WGHA---EDAFPQL---HAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 167 TALDIDYRPvlwgltslgdgetrfiESGQVTSQLQEVLHLFDLvvgteeefhiAGGSTDTLtalknvRNATKAtlVCKRG 246
Cdd:PRK09813 139 TAFDFSDKW----------------DSPLWQTLVPHLDYAFAS----------APQEDEFL------RLKMKA--IVARG 184
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 490229945 247 PmGCVVL----EGAIpdSWDSVPLQQG--VRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:PRK09813 185 A-GVVIVtlgeNGSI--AWDGAQFWRQapEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
10-314 |
4.65e-14 |
|
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: 73.12 E-value: 4.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVDLYAQ-----QIGARLEDVASFSkyLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTE 84
Cdd:cd01941 2 IVVIGAANIDLRGKvsgslVPGTSNPGHVKQS--PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 85 YLITDKQRlTAlvmlgikdqeTFPLIFYRDN-----CADMALSpEDIKEEYIASSR-ALAVTGTHLSHANTREAVLKAL- 157
Cdd:cd01941 80 GIVFEGRS-TA----------SYTAILDKDGdlvvaLADMDIY-ELLTPDFLRKIReALKEAKPIVVDANLPEEALEYLl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 158 EYARRHGLRTALDidyrPVlwgltslgdgetrfieSGQVTSQLQEVLHLFDLVVGTEEEF-HIAGGSTDTLTALKNVRNA 236
Cdd:cd01941 148 ALAAKHGVPVAFE----PT----------------SAPKLKKLFYLLHAIDLLTPNRAELeALAGALIENNEDENKAAKI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 237 TKA----TLVCKRGPMGCVVLEGAIPDSWDSVPlqQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALV 312
Cdd:cd01941 208 LLLpgikNVIVTLGAKGVLLSSREGGVETKLFP--APQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
..
gi 490229945 313 VS 314
Cdd:cd01941 286 LE 287
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
9-328 |
1.17e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 72.46 E-value: 1.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 9 DVICIGRVAVDLYA-----QQIGARLEDvASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDT 83
Cdd:PTZ00292 17 DVVVVGSSNTDLIGyvdrmPQVGETLHG-TSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 84 EYLITDKQRLTALVMLGIKDQETFPLIFYRDNcADMALSPEDI---KEEYIASSRALAVTG-THLshantrEAVLKALEY 159
Cdd:PTZ00292 96 SFVSRTENSSTGLAMIFVDTKTGNNEIVIIPG-ANNALTPQMVdaqTDNIQNICKYLICQNeIPL------ETTLDALKE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 160 ARRHGLRTALDIDYRPvlwgltslgdgetrfieSGQVTSQLQEVLHLFDLVVGTEEEFHIAGGS--TDTLTALK------ 231
Cdd:PTZ00292 169 AKERGCYTVFNPAPAP-----------------KLAEVEIIKPFLKYVSLFCVNEVEAALITGMevTDTESAFKaskelq 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 232 --NVRNATkATLvckrGPMGCVVLEGaipdswDSVPLQ-QGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANAC 308
Cdd:PTZ00292 232 qlGVENVI-ITL----GANGCLIVEK------ENEPVHvPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRI 300
|
330 340
....*....|....*....|
gi 490229945 309 GALVVSRHGCAPAMPTKAEL 328
Cdd:PTZ00292 301 AAISVTRHGTQSSYPHPSEL 320
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
32-334 |
1.77e-13 |
|
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: 71.45 E-value: 1.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 32 VASFSKYLGGSSGNVAFgtaiqglksaMLARVGDE---------HNGRFLRETLSRAGVDTEYL-ITDKQRLTalVMLGI 101
Cdd:TIGR03168 27 VAAVRKDAGGKGINVAR----------VLARLGAEvvatgflggFTGEFIEALLAEEGIKNDFVeVKGETRIN--VKIKE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 102 KDQETFPLifyrdNCADMALSPEDIKE------EYIASSRALAVTGThLSHANTREAVLKALEYARRHGLRTALD----- 170
Cdd:TIGR03168 95 SSGEETEL-----NEPGPEISEEELEQlleklrELLASGDIVVISGS-LPPGVPPDFYAQLIAIARKKGAKVILDtsgea 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 171 ----IDYRPVLwgltslgdgetrfiesgqVTSQLQEVLHLFDLVVGTEEEfhiaggstdtltalknVRNATKATLvcKRG 246
Cdd:TIGR03168 169 lreaLAAKPFL------------------IKPNHEELEELFGRELKTLEE----------------IIEAARELL--DRG 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 247 PmGCVVL----EGAIPDSWDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGcaPAM 322
Cdd:TIGR03168 213 A-ENVLVslgaDGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGL 289
|
330
....*....|..
gi 490229945 323 PTKAELDDYLSR 334
Cdd:TIGR03168 290 PDPEDVEELLDQ 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
40-333 |
5.76e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 67.20 E-value: 5.76e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 40 GGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITDKQRLTALVMlgikdqetfplIFYRDNC--- 116
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVAL-----------IFVNDEGens 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 117 ------ADMALSPEDIKEEY--IASSRALavtgthLSHANT-REAVLKALEYARRHGLRTALDidyrPVlwGLTSLGDge 187
Cdd:PRK11142 108 igihagANAALTPALVEAHRelIANADAL------LMQLETpLETVLAAAKIAKQHGTKVILN----PA--PARELPD-- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 188 trfiesgqvtsqlqEVLHLFDLVVGTEEEfhiaggsTDTLT--ALKNVRNATKATLVCKRGPMGCVVL----EGAipdsW 261
Cdd:PRK11142 174 --------------ELLALVDIITPNETE-------AEKLTgiRVEDDDDAAKAAQVLHQKGIETVLItlgsRGV----W 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490229945 262 DSVPLQQ----GVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTKAELDDYLS 333
Cdd:PRK11142 229 LSENGEGqrvpGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
45-334 |
5.98e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 64.00 E-value: 5.98e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 45 NVAFGTAIQGLKSAMLARVGdEHNGRFLRETLSRAGVDTEYL-ITDKQRlTALVMLGIKDQETFPLifyrdNCADMALSP 123
Cdd:COG1105 40 NVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVpIEGETR-INIKIVDPSDGTETEI-----NEPGPEISE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 124 EDIKE------EYIASSRALAVTGThLSHANTREAVLKALEYARRHGLRTALDIdyrpvlwgltslgdgetrfieSGQVt 197
Cdd:COG1105 113 EELEAllerleELLKEGDWVVLSGS-LPPGVPPDFYAELIRLARARGAKVVLDT---------------------SGEA- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 198 sqLQEVL-HLFDLVVGTEEEF-HIAGGSTDTLTALKNVrnatkATLVCKRGPmGCVVL----EGAIPDSWDSVPLQQGVR 271
Cdd:COG1105 170 --LKAALeAGPDLIKPNLEELeELLGRPLETLEDIIAA-----ARELLERGA-ENVVVslgaDGALLVTEDGVYRAKPPK 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490229945 272 VDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGcaPAMPTKAELDDYLSR 334
Cdd:COG1105 242 VEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
3-310 |
1.48e-10 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 63.70 E-value: 1.48e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 3 AAVKRLDVICIGRVAVDL-----------------YAQQIGARLEDVASFSkyLGGSSgNVAFGTAIQGLKSAMLARVGD 65
Cdd:PLN02341 68 AAGKEIDVATLGNLCVDIvlpvpelpppsreerkaYMEELAASPPDKKSWE--AGGNC-NFAIAAARLGLRCSTIGHVGD 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 66 EHNGRFLRETLSRAGVDTEYLITDkqrlTALVMLGIKDQET---FPLI--FYR-------DNCADMALS-----PEDIKE 128
Cdd:PLN02341 145 EIYGKFLLDVLAEEGISVVGLIEG----TDAGDSSSASYETllcWVLVdpLQRhgfcsraDFGPEPAFSwisklSAEAKM 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 129 EyIASSRALAVTGTHLSHANTrEAVLKALEYARRHGlrTALDIDYRPVLWGLtSLGDGETRfiesgqvtSQLQEVLHLFD 208
Cdd:PLN02341 221 A-IRQSKALFCNGYVFDELSP-SAIASAVDYAIDVG--TAVFFDPGPRGKSL-LVGTPDER--------RALEHLLRMSD 287
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 209 LVVGTEEEFHiaggstdtltALKNVRNATKAT------------LVCKRGPmgcvvlEGAIPDSWDSVPLQQGVRVDVLN 276
Cdd:PLN02341 288 VLLLTSEEAE----------ALTGIRNPILAGqellrpgirtkwVVVKMGS------KGSILVTRSSVSCAPAFKVNVVD 351
|
330 340 350
....*....|....*....|....*....|....
gi 490229945 277 VLGAGDAFMSGLLRGWLNDEGWEQACRYANACGA 310
Cdd:PLN02341 352 TVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
131-293 |
1.60e-10 |
|
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: 60.96 E-value: 1.60e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 131 IASSRALAVTGTHLSHAN-TREAVLKALEYARRHGLRTALDIDYRPVLWGLTslgdgetrfiesgqvtsQLQEVLHLFDL 209
Cdd:cd00287 50 GVSVTLVGADAVVISGLSpAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGE-----------------ELEKLLPGVDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 210 VVGTEEEFHIAGGSTDTLTALKNVRNATKA-----TLVCKRGPMGCVVLEGaiPDSWDSVPLqqgVRVDVLNVLGAGDAF 284
Cdd:cd00287 113 LTPNEEEAEALTGRRDLEVKEAAEAAALLLskgpkVVIVTLGEKGAIVATR--GGTEVHVPA---FPVKVVDTTGAGDAF 187
|
....*....
gi 490229945 285 MSGLLRGWL 293
Cdd:cd00287 188 LAALAAGLA 196
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
45-317 |
3.87e-09 |
|
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: 58.31 E-value: 3.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 45 NVAFGTAIQGLKSAMLARVGDEhNGRFLRETLSRAGVDTEYL-ITDKQRlTALVMLGIKDQETfplifyRDNCADMALSP 123
Cdd:cd01164 41 NVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVeVAGETR-INVKIKEEDGTET------EINEPGPEISE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 124 EDIkEEYIASSRALAVTGTHL-------SHANTrEAVLKALEYARRHGLRTALDIDYRPvlwgltslgdgetrfiesgqv 196
Cdd:cd01164 113 EEL-EALLEKLKALLKKGDIVvlsgslpPGVPA-DFYAELVRLAREKGARVILDTSGEA--------------------- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 197 tsqLQEVLHLF-DLVVGTEEEFH-IAGGSTDTLTALKNVrnatkATLVCKRGPmGCVVL----EGAI----PDSWDSVPL 266
Cdd:cd01164 170 ---LLAALAAKpFLIKPNREELEeLFGRPLGDEEDVIAA-----ARKLIERGA-ENVLVslgaDGALlvtkDGVYRASPP 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490229945 267 QqgvrVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01164 241 K----VKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
32-334 |
8.48e-09 |
|
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: 57.21 E-value: 8.48e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 32 VASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGdEHNGRFLRETLSRAGVDTEYL-ITDKQRLTalVMLGIKDQETFPLi 110
Cdd:TIGR03828 27 VESTRIDAGGKGINVSRVLKNLGVDVVALGFLG-GFTGDFIEALLREEGIKTDFVrVPGETRIN--VKIKEPSGTETKL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 111 fyrdNCADMALSPEDIkEEYIASSRALAVTGTHLSHA-----NTREAVLKAL-EYARRHGLRTALD---------IDYRP 175
Cdd:TIGR03828 103 ----NGPGPEISEEEL-EALLEKLRAQLAEGDWLVLSgslppGVPPDFYAELiALAREKGAKVILDtsgealrdgLKAKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 176 VLwgltslgdgetrfiesgqVTSQLQEVLHLFDLVVGTEEEfhiaggstdtltalknVRNATKATLVckrgpMGC--VVL 253
Cdd:TIGR03828 178 FL------------------IKPNDEELEELFGRELKTLEE----------------IIEAARELLD-----LGAenVLI 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 254 ----EGAIPDSWDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGcaPAMPTKAELD 329
Cdd:TIGR03828 219 slgaDGALLVTKEGALFAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIE 296
|
....*
gi 490229945 330 DYLSR 334
Cdd:TIGR03828 297 ELLPQ 301
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
10-323 |
1.19e-08 |
|
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: 56.80 E-value: 1.19e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVD--LYAQQIGARLE------DVASFSKYLGGSsGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGV 81
Cdd:cd01172 2 VLVVGDVILDeyLYGDVERISPEapvpvvKVEREEIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 82 DTeYLITDKQRLTAlvmlgIK------DQETFPLIFYRDncadmalSPEDIKEEyiasSRALAVTGTHLSHAN------- 148
Cdd:cd01172 81 DT-DGIVDEGRPTT-----TKtrviarNQQLLRVDREDD-------SPLSAEEE----QRLIERIAERLPEADvvilsdy 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 149 -----TREAVLKALEYARRHGLRTALDidyrpvlwgltSLGDGETRFIESGQVTSQLQEVLHLFDLVVGTEEEFhiaggs 223
Cdd:cd01172 144 gkgvlTPRVIEALIAAARELGIPVLVD-----------PKGRDYSKYRGATLLTPNEKEAREALGDEINDDDEL------ 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 224 tdtLTALKNVRNATKATLVC-KRGPMGCVVLEGaiPDSWDSVPlqqGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQAC 302
Cdd:cd01172 207 ---EAAGEKLLELLNLEALLvTLGEEGMTLFER--DGEVQHIP---ALAKEVYDVTGAGDTVIATLALALAAGADLEEAA 278
|
330 340
....*....|....*....|.
gi 490229945 303 RYANACGALVVSRHGCAPAMP 323
Cdd:cd01172 279 FLANAAAGVVVGKVGTAPVTP 299
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
63-323 |
3.48e-08 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 55.80 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 63 VGDEHNGRFLRETLSRAGVDTEYLITDKQRL-TALVMLGIKDQETFPLIfyrdnCADMALSPEDIK----EEYIASSRAL 137
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEMLFEYTTKAPTgTCAVLVCGKERSLVANL-----GAANHLSAEHMQshavQEAIKTAQLY 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 138 AVTGTHLshaNTR-EAVLKALEYARRHGlrtaldidyRPVLWGLTSLgdgetrFIeSGQVTSQLQEVLHLFDLVVGTEEE 216
Cdd:PTZ00247 164 YLEGFFL---TVSpNNVLQVAKHARESG---------KLFCLNLSAP------FI-SQFFFERLLQVLPYVDILFGNEEE 224
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 217 FHIAG-----GSTDTLTALKNV-----RNATKATL-VCKRGPMGCVVlegAIPDSWDSVPLQQGVRVDVLNVLGAGDAFM 285
Cdd:PTZ00247 225 AKTFAkamkwDTEDLKEIAARIamlpkYSGTRPRLvVFTQGPEPTLI---ATKDGVTSVPVPPLDQEKIVDTNGAGDAFV 301
|
250 260 270
....*....|....*....|....*....|....*....
gi 490229945 286 SGLLRGWLNDEGWEQACRYANACGALVVSRHGCA-PAMP 323
Cdd:PTZ00247 302 GGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKP 340
|
|
| PLN02967 |
PLN02967 |
kinase |
14-216 |
5.59e-08 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 55.82 E-value: 5.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 14 GRVAVDLYAQQIGARLEDV----ASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITD 89
Cdd:PLN02967 213 GRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCID 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 90 KQRLTALVMLGIKDQETFPLIFYRDnCADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLKALEYARRHGLRTAL 169
Cdd:PLN02967 293 GKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFY 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 490229945 170 DIDYRPVLWgltslgdgetrfiESGQVTSQL-QEVLHLFDLVVGTEEE 216
Cdd:PLN02967 372 DLNLPLPLW-------------SSSEETKSFiQEAWNLADIIEVTKQE 406
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
34-317 |
7.15e-07 |
|
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: 51.26 E-value: 7.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 34 SFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVDTEYLITDKQ-RLTALVMlgikDQETFPLIFY 112
Cdd:cd01947 30 DSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPtRKTLSFI----DPNGERTITV 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 113 RDNcADMALSPEDIKEEYiassRALAVTGThlshantreAVLK-ALEYARRHGLrtaldidyrpVLWGLTslgdGETRFI 191
Cdd:cd01947 106 PGE-RLEDDLKWPILDEG----DGVFITAA---------AVDKeAIRKCRETKL----------VILQVT----PRVRVD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 192 EsgqvtsqLQEVLHLFDLVVGTEEEFhiAGGSTDTLTALKNVRnatkaTLVCKRGPMGCVVlegaipdsWDSVPLQQ--G 269
Cdd:cd01947 158 E-------LNQALIPLDILIGSRLDP--GELVVAEKIAGPFPR-----YLIVTEGELGAIL--------YPGGRYNHvpA 215
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490229945 270 VRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01947 216 KKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
10-317 |
6.31e-06 |
|
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: 48.57 E-value: 6.31e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 10 VICIGRVAVDLYAQ--QIGARLEDV-ASFSKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLSRAGVdtEYL 86
Cdd:cd01944 2 VLVIGAAVVDIVLDvdKLPASGGDIeAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGI--EIL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 87 ITDKQR-----LTALVMLGIKdqETFpLIFYRdncADMALSPEDIKEEYIASSRALAVTGTHLSHANTREAVLkaLEYAR 161
Cdd:cd01944 80 LPPRGGddggcLVALVEPDGE--RSF-ISISG---AEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVIL--LEWLE 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 162 RHGLRTALDIDYRPVLwglTSLGDGEtrfiesgqvtsqLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNA--TKA 239
Cdd:cd01944 152 ALPAGTTLVFDPGPRI---SDIPDTI------------LQALMAKRPIWSCNREEAAIFAERGDPAAEASALRIYakTAA 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 240 TLVCKRGPMGCVVLEGA-----IPdswdsvplqqGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVS 314
Cdd:cd01944 217 PVVVRLGSNGAWIRLPDgnthiIP----------GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVT 286
|
...
gi 490229945 315 RHG 317
Cdd:cd01944 287 RSG 289
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
121-316 |
6.20e-05 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 45.77 E-value: 6.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 121 LSPEDIKEEYIASSRALAVTgTHLSHAN----TREAVLKALEYARRHGLrtaldidyrPVLwgLTsLGdgeTRF-IESGQ 195
Cdd:PRK15074 174 LRPESIPEDVIAGASALVLT-AYLVRCKpgepMPEATMKAIEYAKKHNV---------PVV--LT-LG---TKFvIEDNP 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 196 vtSQLQEVL--HLfDLVVGTEEEFHIAGGSTDTLTAlknvrnATKA----TLV-CKRGPMGCV----------------V 252
Cdd:PRK15074 238 --QWWQEFLkeHV-SILAMNEDEAEALTGESDPLLA------SDKAldwvDLVlCTAGPIGLYmagytedeakretqhpL 308
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490229945 253 LEGAIPD--SWD-SVPL-----QQGVRV------------DVLNVLGAGDAFMSGLL--------------------RGW 292
Cdd:PRK15074 309 LPGAIAEfnRYEfSRAMrkkdcQNPLRVyshiapymggpeKIMNTNGAGDGALSALLhditansyhrsnvpnsskhkRTY 388
|
250 260
....*....|....*....|....
gi 490229945 293 LNDEGWEQACRYANACGALVVSRH 316
Cdd:PRK15074 389 LTYSSLAQVCKYANRVSYEVLNQH 412
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
270-314 |
5.14e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 42.67 E-value: 5.14e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490229945 270 VRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVS 314
Cdd:PRK09850 244 IKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
254-314 |
1.35e-03 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 41.22 E-value: 1.35e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490229945 254 EGAIPDSWDSVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVS 314
Cdd:PRK09513 227 EGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVS 287
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
246-317 |
2.50e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 40.40 E-value: 2.50e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490229945 246 GPMGCVVL-EGAIPDSWdsVPLQQGVRVDVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01943 233 GKLGCYVGsADSGPELW--LPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| |
