|
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: 1130.38 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 6 KRLDVICIGRVAVDLYAQQIGSRLEDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEY 85
Cdd:COG3892 4 KTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDTSG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 86 LITDKSRLTALVMLGIKDQETFPLIFYRDNCADMALTPDDISEEYIASSRALAVTGTHLSHANTRAAVLKALEYARRHGL 165
Cdd:COG3892 84 VVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARAHGG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 166 RTALDIDYRPVLWGLTSLGDGETRFIESGPVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKR 245
Cdd:COG3892 164 KVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLVCKR 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 246 GPMGCVVLEGDIPDSWDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTK 325
Cdd:COG3892 244 GALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAMPTW 323
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 326 VELDDYLQRAESVPRPDVDERLNHLHRVTSRRQQWPELCIFAFDHRKQLADLARETGRDEACIPQLKLLLLAAAEAAAQE 405
Cdd:COG3892 324 EELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQVAAG 403
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 406 AGLDQRSGILADGTYGQRALNAITGKGWWIGRPIELPSSRPLRLEHG-NIGSQLIDWPLEHVVKCLVFYHPDDPAALRAE 484
Cdd:COG3892 404 AGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAELRLE 483
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 485 QDALLLEVWQACNKSGHELLLEVILPENGPDKDErHYHTMLEHFYQLGIKPDWWKLPPLSSASWQQITALIEREDPWSRG 564
Cdd:COG3892 484 QEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDD-TVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPYCRG 562
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490248684 565 ILILGLDAPSDKLRAGFAEAAAHPMIKGFAVGRTIFGQPSRRWMQGELSDEALIEEVKRNYLTLIGYWREARR 637
Cdd:COG3892 563 VVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQ 635
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
327-636 |
0e+00 |
|
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: 528.78 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 327 ELDDYLQRAESVPRPDVDERLNHLHRVTSRRQQWPELCIFAFDHRKQLADLARETGRDEACIPQLKLLLLAAAEAAAQEA 406
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 407 GLDQRSGILADGTYGQRALNAITGKGWWIGRPIELPSSRPLRLEHG-NIGSQLIDWPLEHVVKCLVFYHPDDPAALRAEQ 485
Cdd:pfam09863 81 GLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 486 DALLLEVWQACNKSGHELLLEVILPENGPDKDErHYHTMLEHFYQLGIKPDWWKLPPLSSASWQQITALIEREDPWSRGI 565
Cdd:pfam09863 161 EAQLRELYDACRKSGHELLLEVIPPKDGPVDDE-TYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRGV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490248684 566 LILGLDAPSDKLRAGFAEAAAHPMIKGFAVGRTIFGQPSRRWMQGELSDEALIEEVKRNYLTLIGYWREAR 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 |
1.37e-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: 465.15 E-value: 1.37e-161
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 7 RLDVICIGRVAVDLYAQQIGSRLEDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYL 86
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 87 ITDKSRLTALVMLGIKDQETFPLIFYRDNCADMALTPDDISEEYIASSRALAVTGTHLSHANTRAAVLKALEYARRHGLR 166
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 167 TALDIDYRPVLWGltslgdgetrfiESGPVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKRG 246
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 247 PMGCVVLEGDipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTKV 326
Cdd:TIGR04382 229 PEGSLVYTGD-----GEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 490248684 327 ELDDYL 332
Cdd:TIGR04382 304 ELEAFL 309
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-328 |
1.10e-81 |
|
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: 259.82 E-value: 1.10e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYAQ----QIGSRLEDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTE 84
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 85 YLITDKSRLTALVMLGIKDQETFPLIFYRdnCADMALTPDDISEEYIASSRALAVTGTHLSHANTRAAVLKALEYARRHG 164
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 165 LRTALDIDYRPVLWGltslgdgetrfiesgPVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCK 244
Cdd:COG0524 159 VPVSLDPNYRPALWE---------------PARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 245 RGPMGCVVLEGDipdSWDQVPlqqGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPT 324
Cdd:COG0524 224 LGAEGALLYTGG---EVVHVP---AFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 490248684 325 KVEL 328
Cdd:COG0524 298 REEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-319 |
1.93e-81 |
|
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: 258.66 E-value: 1.93e-81
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYAQQIGsRLEDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLIT 88
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 89 DKSRLTALVMLGIKDQETFPLIFYRDNCADMALTPDDISEEYIASSRALAVTGTHLS-HANTRAAVLKALEYARRHGLRT 167
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 168 ALDIDYRPVLWGLtslgdGETRfiesgpvtSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVR--NATKATLVCKR 245
Cdd:cd01166 160 SFDLNYRPKLWSA-----EEAR--------EALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALalALGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490248684 246 GPMGCVVLEGdipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCA 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 |
7.50e-48 |
|
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: 169.74 E-value: 7.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYAQQIGsrleDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITD 89
Cdd:cd01167 2 VVCFGEALIDFIPEGSG----APETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 90 KSRLTALVMLGIKDQ--ETFplIFYRDNCADMALTPDDISEeyIASSRALAVTGTH-LSHANTRAAVLKALEYARRHGLR 166
Cdd:cd01167 78 PAAPTTLAFVTLDADgeRSF--EFYRGPAADLLLDTELNPD--LLSEADILHFGSIaLASEPSRSALLELLEAAKKAGVL 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 167 TALDIDYRPVLWgltslGDGETRFiesgpvtSQLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVRNATKATLVCKRG 246
Cdd:cd01167 154 ISFDPNLRPPLW-----RDEEEAR-------ERIAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVLVTRG 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 247 PMGCVVL----EGDIPdswdqvplqqGVRVEVLNVLGAGDAFMSGLLRG-------WLNDEGWEQACRYANACGALVVSR 315
Cdd:cd01167 222 ADGALLYtkggVGEVP----------GIPVEVVDTTGAGDAFVAGLLAQllsrgllALDEDELAEALRFANAVGALTCTK 291
|
..
gi 490248684 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 |
4.28e-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: 162.13 E-value: 4.28e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYAQQIGSRLED--VASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYL 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELvrVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 87 ITDKSRLT--ALVMLGiKDQETFpLIFYRDNCADMALTPDDISEEYIASSRALAVTGTHLShaNTRAAVLKALEYARRHG 164
Cdd:pfam00294 81 VIDEDTRTgtALIEVD-GDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLPL--GLPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 165 lrTALDIDYRPVLWgltslgdgetrfiesgPVTSQLQEVLHLFDLVVGTEEEFHIAGGST-----DTLTALKNVRNATKA 239
Cdd:pfam00294 157 --GTFDPNLLDPLG----------------AAREALLELLPLADLLKPNEEELEALTGAKlddieEALAALHKLLAKGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 240 TLVCKRGPMGCVVLEGDipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCA 319
Cdd:pfam00294 219 TVIVTLGADGALVVEGD-----GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
7-318 |
5.68e-30 |
|
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: 120.41 E-value: 5.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 7 RLDVICIGRVAVDLYAQ-----------QIGS-------RLEDVASFAKYL---GGSSGNVAFGTAIQGLKSAMLARVGD 65
Cdd:cd01168 1 RYDVLGLGNALVDILAQvddafleklglKKGDmiladmeEQEELLAKLPVKyiaGGSAANTIRGAAALGGSAAFIGRVGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 66 EHNGRFLRETLNRAGVDTEYLITDKSRL-TALVMLGIKDQETfpLIFYRDNCADmaLTPDDISEEYIASSRALAVTGTHL 144
Cdd:cd01168 81 DKLGDFLLKDLRAAGVDTRYQVQPDGPTgTCAVLVTPDAERT--MCTYLGAANE--LSPDDLDWSLLAKAKYLYLEGYLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 145 SHANtrAAVLKALEYARRHGLRTALDIdyrpvlwgltSLGDGETRFIEsgpvtsQLQEVLHLFDLVVGTEEEFHIAGGS- 223
Cdd:cd01168 157 TVPP--EAILLAAEHAKENGVKIALNL----------SAPFIVQRFKE------ALLELLPYVDILFGNEEEAEALAEAe 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 224 -TDTLTALKNVRNATKATLVCKRGPMGCVVLEGD----IPDSWDqvplqqgvrVEVLNVLGAGDAFMSGLLRGWLNDEGW 298
Cdd:cd01168 219 tTDDLEAALKLLALRCRIVVITQGAKGAVVVEGGevypVPAIPV---------EKIVDTNGAGDAFAGGFLYGLVQGEPL 289
|
330 340
....*....|....*....|
gi 490248684 299 EQACRYANACGALVVSRHGC 318
Cdd:cd01168 290 EECIRLGSYAAAEVIQQLGP 309
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
10-335 |
1.34e-29 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 119.73 E-value: 1.34e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYAQQIGSRLEDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITD 89
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 90 KSRLTALVMLGIKDQETFPLIFYRDNCADMALTPDDISEEYIASSRALAVTGTHLSHANTRAAVLKALEYARRHGLRTAL 169
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 170 DIDYRPVLW--------GLTSLGDgETRFIEsgpvtsqlqevlhlfdlvVGTEE-EFHIAGGSTDTLTALKNVRNATKAT 240
Cdd:PLN02323 173 DPNLRLPLWpsaeaareGIMSIWD-EADIIK------------------VSDEEvEFLTGGDDPDDDTVVKLWHPNLKLL 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 241 LVCKrGPMGCVVLegdIPDSWDQVPlqqGVRVEVLNVLGAGDAFMSGLL------RGWLNDEG-WEQACRYANACGALVV 313
Cdd:PLN02323 234 LVTE-GEEGCRYY---TKDFKGRVE---GFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGAITT 306
|
330 340
....*....|....*....|..
gi 490248684 314 SRHGCAPAMPTKVELDDYLQRA 335
Cdd:PLN02323 307 TERGAIPALPTKEAVLKLLKKA 328
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
30-329 |
6.21e-28 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 114.26 E-value: 6.21e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 30 EDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITDKSRLTALVMLGIKDQETFPL 109
Cdd:PRK09434 18 EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 110 IFYRDNCADMALTPDDISEeyIASSRALAVTGTHLSHANTRAAVLKALEYARRHGLRTALDIDYRPVLWGLTSlgdgetr 189
Cdd:PRK09434 98 TFMVRPSADLFLQPQDLPP--FRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEA------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 190 fiESGPVtsqLQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNV--RNATKATLVcKRGPMG-CVVLEGdipdswdQVPL 266
Cdd:PRK09434 169 --ELREC---LRQALALADVVKLSEEELCFLSGTSQLEDAIYALadRYPIALLLV-TLGAEGvLVHTRG-------QVQH 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490248684 267 QQGVRVEVLNVLGAGDAFMSGLLRG------WLNDEGWEQACRYANACGALVVSRHGCAPAMPTKVELD 329
Cdd:PRK09434 236 FPAPSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
9-324 |
4.88e-26 |
|
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: 108.41 E-value: 4.88e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYAQ-----QIGsrlEDVA--SFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGV 81
Cdd:cd01174 1 KVVVVGSINVDLVTRvdrlpKPG---ETVLgsSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGI 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 82 DTEY--LITDKSRLTALVMLgikDQEtfplifyRDNC------ADMALTPDDIS--EEYIASSRALavtgthLSHANT-R 150
Cdd:cd01174 78 DVSYveVVVGAPTGTAVITV---DES-------GENRivvvpgANGELTPADVDaaLELIAAADVL------LLQLEIpL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 151 AAVLKALEYARRHGLRTALDidyrpvlwgltslgdgetrfieSGPVTSQLQEVLHLFDLVVGTEEEFHIAGGSTDT---- 226
Cdd:cd01174 142 ETVLAALRAARRAGVTVILN----------------------PAPARPLPAELLALVDILVPNETEAALLTGIEVTdeed 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 227 -LTALKNVRNATKATLVCKRGPMGCVVLEGDipdSWDQVPlqqGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYA 305
Cdd:cd01174 200 aEKAARLLLAKGVKNVIVTLGAKGALLASGG---EVEHVP---AFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFA 273
|
330
....*....|....*....
gi 490248684 306 NACGALVVSRHGCAPAMPT 324
Cdd:cd01174 274 NAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
9-318 |
8.39e-26 |
|
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: 107.40 E-value: 8.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYAQQIGSRLEDVASFAK----YLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTE 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 85 YLITdksrltalvmlgIKDQETfPLIFYRDN-----CADMALTPDDISEEYIASSRALAVTGTHLShaNTRAAVLKALEy 159
Cdd:cd01942 81 HVRV------------VDEDST-GVAFILTDgddnqIAYFYPGAMDELEPNDEADPDGLADIVHLS--SGPGLIELARE- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 160 ARRHGLRTALDidyrP--VLWGLTslgdgetrfiesgpvTSQLQEVLHLFDLVVGTEEEFHIAggstDTLTALK-NVRNA 236
Cdd:cd01942 145 LAAGGITVSFD----PgqELPRLS---------------GEELEEILERADILFVNDYEAELL----KERTGLSeAELAS 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 237 TKATLVCKRGPMGCVVLEGDipDSWDQVPLQqgvRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRH 316
Cdd:cd01942 202 GVRVVVVTLGPKGAIVFEDG--EEVEVPAVP---AVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERR 276
|
..
gi 490248684 317 GC 318
Cdd:cd01942 277 GA 278
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-324 |
1.61e-18 |
|
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: 86.19 E-value: 1.61e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYAQQIGSRLED----VASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTE 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDgkivATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 85 YLITDK---SRLTALVMLGIKDQETFPlifyrdNCADMALTPDDISEEYIASSRALAVTGtHLshantRAAVLKALEYAR 161
Cdd:cd01945 81 FIVVAPgarSPISSITDITGDRATISI------TAIDTQAAPDSLPDAILGGADAVLVDG-RQ-----PEAALHLAQEAR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 162 RHGLRTALDIDyrpvlwgltslGDGETrfiesgpvtsQLQEVLHLFDLVVGTEEEFHIAGGSTDTLtALKNVRNATKATL 241
Cdd:cd01945 149 ARGIPIPLDLD-----------GGGLR----------VLEELLPLADHAICSENFLRPNTGSADDE-ALELLASLGIPFV 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 242 VCKRGPMGCVVLEGDipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPA 321
Cdd:cd01945 207 AVTLGEAGCLWLERD-----GELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAG 281
|
...
gi 490248684 322 MPT 324
Cdd:cd01945 282 LPT 284
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
10-317 |
2.75e-14 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 73.16 E-value: 2.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYAQQIGSrledvasfakYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITd 89
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 90 KSRLTALVMLGIKDQETfplIFYRDN---CADMALTPDDIseEYIASSRaLAVTGTHlSHANTRAAVLKALEYArrhGLR 166
Cdd:cd01940 71 KEGENAVADVELVDGDR---IFGLSNkggVAREHPFEADL--EYLSQFD-LVHTGIY-SHEGHLEKALQALVGA---GAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 167 TALDIDYRpvlwgltslGDGEtrfiesgpvtsqlqevlhLFDLVV-GTEEEFHIAGGSTDTL--TALKNVRNATKATLVC 243
Cdd:cd01940 141 ISFDFSDR---------WDDD------------------YLQLVCpYVDFAFFSASDLSDEEvkAKLKEAVSRGAKLVIV 193
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490248684 244 KRGPMGCVVLEGdipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWL-NDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01940 194 TRGEDGAIAYDG------AVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
10-314 |
1.16e-13 |
|
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: 71.96 E-value: 1.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYAQ-----QIGSRLEDVASFAkyLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTE 84
Cdd:cd01941 2 IVVIGAANIDLRGKvsgslVPGTSNPGHVKQS--PGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVR 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 85 yLITDKSRLTAlvmlgikdqeTFPLIFYRDN-----CADMALTpDDISEEYIASSR-ALAVTGTHLSHANTRAAVLKAL- 157
Cdd:cd01941 80 -GIVFEGRSTA----------SYTAILDKDGdlvvaLADMDIY-ELLTPDFLRKIReALKEAKPIVVDANLPEEALEYLl 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 158 EYARRHGLRTALDidyrPVlwgltslgdgetrfieSGPVTSQLQEVLHLFDLVVGTEEEF-HIAGGSTDTLTALKNVRNA 236
Cdd:cd01941 148 ALAAKHGVPVAFE----PT----------------SAPKLKKLFYLLHAIDLLTPNRAELeALAGALIENNEDENKAAKI 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 237 TKA----TLVCKRGPMGCVVLEGDIPDSWDQVPlqQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALV 312
Cdd:cd01941 208 LLLpgikNVIVTLGAKGVLLSSREGGVETKLFP--APQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALT 285
|
..
gi 490248684 313 VS 314
Cdd:cd01941 286 LE 287
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
10-317 |
2.23e-13 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 70.54 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYaQQIGSrledvasfaKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITD 89
Cdd:PRK09813 3 LATIGDNCVDIY-PQLGK---------AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 90 KSRlTALVMLGIKDQETfplIF--YRDNC-ADMALTPDDISeeyIASSRALAVTGThLSHAntrAAVLKALeyaRRHGLR 166
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDYA---WLAQYDIVHAAI-WGHA---EDAFPQL---HAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 167 TALDIDYRPvlwgltslgdgetrfiESGPVTSQLQEVLHLFDLvvgteeefhiAGGSTDTL-TALKNVRNATKATLVCKR 245
Cdd:PRK09813 139 TAFDFSDKW----------------DSPLWQTLVPHLDYAFAS----------APQEDEFLrLKMKAIVARGAGVVIVTL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 490248684 246 GPMGCVVLEGDipDSWDQVPLQqgvrVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:PRK09813 193 GENGSIAWDGA--QFWRQAPEP----VTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
9-328 |
3.48e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 70.92 E-value: 3.48e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 9 DVICIGRVAVDLYA-----QQIGSRLEDvASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDT 83
Cdd:PTZ00292 17 DVVVVGSSNTDLIGyvdrmPQVGETLHG-TSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNT 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 84 EYLITDKSRLTALVMLGIKDQETFPLIFYRDNcADMALTPDDISEEY--IASSRALAVTGTHLSHANTraavLKALEYAR 161
Cdd:PTZ00292 96 SFVSRTENSSTGLAMIFVDTKTGNNEIVIIPG-ANNALTPQMVDAQTdnIQNICKYLICQNEIPLETT----LDALKEAK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 162 RHGLRTALDIDYRPvlwgltslgdgetrfieSGPVTSQLQEVLHLFDLVVGTEEEFHIAGGS--TDTLTALK-------- 231
Cdd:PTZ00292 171 ERGCYTVFNPAPAP-----------------KLAEVEIIKPFLKYVSLFCVNEVEAALITGMevTDTESAFKaskelqql 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 232 NVRNATkATLvckrGPMGCVVLEGDIPDSwdQVPlqqGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGAL 311
Cdd:PTZ00292 234 GVENVI-ITL----GANGCLIVEKENEPV--HVP---GKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAI 303
|
330
....*....|....*..
gi 490248684 312 VVSRHGCAPAMPTKVEL 328
Cdd:PTZ00292 304 SVTRHGTQSSYPHPSEL 320
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
32-334 |
1.34e-12 |
|
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: 68.76 E-value: 1.34e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 32 VASFAKYLGGSSGNVAFgtaiqglksaMLARVGDE---------HNGRFLRETLNRAGVDTEYL-----------ITDKS 91
Cdd:TIGR03168 27 VAAVRKDAGGKGINVAR----------VLARLGAEvvatgflggFTGEFIEALLAEEGIKNDFVevkgetrinvkIKESS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 92 -RLTALVMLGikdqetfPLIfyRDNCADMALTpddISEEYIASSRALAVTGThLShANTRAAVLKAL-EYARRHGLRTAL 169
Cdd:TIGR03168 97 gEETELNEPG-------PEI--SEEELEQLLE---KLRELLASGDIVVISGS-LP-PGVPPDFYAQLiAIARKKGAKVIL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 170 DIDYRPVLWGLtslgdgetrfiESGP--VTSQLQEVLHLFDLVVGTEEEfhiaggstdtltalknVRNATKATLvcKRGP 247
Cdd:TIGR03168 163 DTSGEALREAL-----------AAKPflIKPNHEELEELFGRELKTLEE----------------IIEAARELL--DRGA 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 248 mGCVVL----EGDIPDSWDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGcaPAMP 323
Cdd:TIGR03168 214 -ENVLVslgaDGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLP 290
|
330
....*....|.
gi 490248684 324 TKVELDDYLQR 334
Cdd:TIGR03168 291 DPEDVEELLDQ 301
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
32-334 |
4.34e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 64.39 E-value: 4.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 32 VASFAKYLGGSSgnVAFGTaiqglksamlarVGdEHNGRFLRETLNRAGVDTEYL-ITDKSRlTALVMLGIKDQETFPLi 110
Cdd:COG1105 41 VARVLKALGVDV--TALGF------------LG-GFTGEFIEELLDEEGIPTDFVpIEGETR-INIKIVDPSDGTETEI- 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 111 fyrdNCADMALTPDDIsEEYIASSRALAVTGTHLshantraaVL--------------KALEYARRHGLRTALDIDyrpv 176
Cdd:COG1105 104 ----NEPGPEISEEEL-EALLERLEELLKEGDWV--------VLsgslppgvppdfyaELIRLARARGAKVVLDTS---- 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 177 lwgltslGDGETRFIESGPvtsqlqevlhlfDLVVGTEEEF-HIAGGSTDTLTALKNVrnatkATLVCKRGPmGCVVL-- 253
Cdd:COG1105 167 -------GEALKAALEAGP------------DLIKPNLEELeELLGRPLETLEDIIAA-----ARELLERGA-ENVVVsl 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 254 --EGDI---PDSWDQVPlqqGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGcaPAMPTKVEL 328
Cdd:COG1105 222 gaDGALlvtEDGVYRAK---PPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDV 296
|
....*.
gi 490248684 329 DDYLQR 334
Cdd:COG1105 297 EELLAQ 302
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
17-317 |
9.07e-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: 63.32 E-value: 9.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 17 AVDLYAQ----QIGS--RLEDVASFAkylGGSSGNVAFGTAIQGLKSAMLARVGDEhNGRFLRETLNRAGVDTEYL-ITD 89
Cdd:cd01164 10 AIDLTIEldqlQPGEvnRVSSTRKDA---GGKGINVARVLKDLGVEVTALGFLGGF-TGDFFEALLKEEGIPDDFVeVAG 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 90 KSRlTALVMLGIKDQETfplifyRDNCADMALTPDDIsEEYIASSRALAVTGTHL-------SHANTRAAVlKALEYARR 162
Cdd:cd01164 86 ETR-INVKIKEEDGTET------EINEPGPEISEEEL-EALLEKLKALLKKGDIVvlsgslpPGVPADFYA-ELVRLARE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 163 HGLRTALDIDYRPVLWGLtslgdgetrfiESGPvtsqlqevlhlfDLVVGTEEEFH-IAGGSTDTLTALKNVrnatkATL 241
Cdd:cd01164 157 KGARVILDTSGEALLAAL-----------AAKP------------FLIKPNREELEeLFGRPLGDEEDVIAA-----ARK 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 242 VCKRGPmGCVVL----EGDIPDSWDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01164 209 LIERGA-ENVLVslgaDGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
40-333 |
6.41e-10 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 60.65 E-value: 6.41e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 40 GGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITDKSRLTALVMlgikdqetfplIFYRDNC--- 116
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVAL-----------IFVNDEGens 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 117 ------ADMALTPDDI--SEEYIASSRALavtgthLSHANT-RAAVLKALEYARRHGLRTALDidyrPvlwgltslgdge 187
Cdd:PRK11142 108 igihagANAALTPALVeaHRELIANADAL------LMQLETpLETVLAAAKIAKQHGTKVILN----P------------ 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 188 trfiesGPVTSQLQEVLHLFDLVVGTEEEfhiaggsTDTLT--ALKNVRNATKATLVCKRGPMGCVVL------------ 253
Cdd:PRK11142 166 ------APARELPDELLALVDIITPNETE-------AEKLTgiRVEDDDDAAKAAQVLHQKGIETVLItlgsrgvwlsen 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 254 -EGDIpdswdqVPlqqGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCAPAMPTKVELDDYL 332
Cdd:PRK11142 233 gEGQR------VP---GFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
.
gi 490248684 333 Q 333
Cdd:PRK11142 304 Q 304
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
131-293 |
9.14e-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: 58.65 E-value: 9.14e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 131 IASSRALAVTGTHLSHAN-TRAAVLKALEYARRHGLRTALDIDYRPVLWGLTslgdgetrfiesgpvtsQLQEVLHLFDL 209
Cdd:cd00287 50 GVSVTLVGADAVVISGLSpAPEAVLDALEEARRRGVPVVLDPGPRAVRLDGE-----------------ELEKLLPGVDI 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 210 VVGTEEEFHIAGGSTDTLTALKNVRNATKA-----TLVCKRGPMGCVVLEGDipDSWDQVPLqqgVRVEVLNVLGAGDAF 284
Cdd:cd00287 113 LTPNEEEAEALTGRRDLEVKEAAEAAALLLskgpkVVIVTLGEKGAIVATRG--GTEVHVPA---FPVKVVDTTGAGDAF 187
|
....*....
gi 490248684 285 MSGLLRGWL 293
Cdd:cd00287 188 LAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
10-328 |
1.19e-09 |
|
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: 59.88 E-value: 1.19e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVD--LYAQQIGSRLE------DVASFAKYLGGSsGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGV 81
Cdd:cd01172 2 VLVVGDVILDeyLYGDVERISPEapvpvvKVEREEIRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 82 DTeYLITDKSRLTAlvmlgIK------DQETFPLIFYRDncadmalTPDDISEEyiasSRALAVTGTHLSHAN------- 148
Cdd:cd01172 81 DT-DGIVDEGRPTT-----TKtrviarNQQLLRVDREDD-------SPLSAEEE----QRLIERIAERLPEADvvilsdy 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 149 -----TRAAVLKALEYARRHGLRTALDidyrpvlwgltSLGDGETRFieSGpvtsqlqevlhlFDLVVGTEEEFHIAGGS 223
Cdd:cd01172 144 gkgvlTPRVIEALIAAARELGIPVLVD-----------PKGRDYSKY--RG------------ATLLTPNEKEAREALGD 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 224 TDT-----LTALKNVRNATKATLVC-KRGPMGCVVLEGDipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEG 297
Cdd:cd01172 199 EINdddelEAAGEKLLELLNLEALLvTLGEEGMTLFERD-----GEVQHIPALAKEVYDVTGAGDTVIATLALALAAGAD 273
|
330 340 350
....*....|....*....|....*....|.
gi 490248684 298 WEQACRYANACGALVVSRHGCAPAMPTKVEL 328
Cdd:cd01172 274 LEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
3-310 |
6.55e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 58.69 E-value: 6.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 3 AAVKRLDVICIGRVAVD-------------LYAQQIGSRLEDVASFAKYL-GGSSGNVAFGTAIQGLKSAMLARVGDEHN 68
Cdd:PLN02341 68 AAGKEIDVATLGNLCVDivlpvpelpppsrEERKAYMEELAASPPDKKSWeAGGNCNFAIAAARLGLRCSTIGHVGDEIY 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 69 GRFLRETLNRAGVDTEYLITDksrlTALVMLGIKDQET---FPLI--FYRDN-CADMALTPD-------DISEEY---IA 132
Cdd:PLN02341 148 GKFLLDVLAEEGISVVGLIEG----TDAGDSSSASYETllcWVLVdpLQRHGfCSRADFGPEpafswisKLSAEAkmaIR 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 133 SSRALAVTGTHLSHANTrAAVLKALEYARRHGlrTALDIDYRPvlwgltslgDGETRFIESGPVTSQLQEVLHLFDLVVG 212
Cdd:PLN02341 224 QSKALFCNGYVFDELSP-SAIASAVDYAIDVG--TAVFFDPGP---------RGKSLLVGTPDERRALEHLLRMSDVLLL 291
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 213 TEEEFHiaggstdtltALKNVRNATKAT------------LVCKRGPMGCVVLegdipdSWDQVPLQQGVRVEVLNVLGA 280
Cdd:PLN02341 292 TSEEAE----------ALTGIRNPILAGqellrpgirtkwVVVKMGSKGSILV------TRSSVSCAPAFKVNVVDTVGC 355
|
330 340 350
....*....|....*....|....*....|
gi 490248684 281 GDAFMSGLLRGWLNDEGWEQACRYANACGA 310
Cdd:PLN02341 356 GDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| PLN02967 |
PLN02967 |
kinase |
14-216 |
1.21e-08 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 58.13 E-value: 1.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 14 GRVAVDLYAQQIGSRLEDV----ASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEYLITD 89
Cdd:PLN02967 213 GRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCID 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 90 KSRLTALVMLGIKDQETFPLIFYRDnCADMALTPDDISEEYIASSRALAVTGTHLSHANTRAAVLKALEYARRHGLRTAL 169
Cdd:PLN02967 293 GKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFY 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 490248684 170 DIDYRPVLWGLTSlgdgETRfiesgpvtSQLQEVLHLFDLVVGTEEE 216
Cdd:PLN02967 372 DLNLPLPLWSSSE----ETK--------SFIQEAWNLADIIEVTKQE 406
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
10-317 |
5.28e-08 |
|
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: 54.74 E-value: 5.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYAQQigSRL-----EDVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVdtE 84
Cdd:cd01944 2 VLVIGAAVVDIVLDV--DKLpasggDIEAKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGI--E 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 85 YLITDKSR-----LTALVMLGIKdqETFpLIFYRdncADMALTPDDISEEYIASSRALAVTGTHLSHANTRAAVLKALey 159
Cdd:cd01944 78 ILLPPRGGddggcLVALVEPDGE--RSF-ISISG---AEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEW-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 160 arrhglrtaldidyrpvlwgLTSLGDGETRFIESGPVTSQ-----LQEVLHLFDLVVGTEEEFHIAGGSTDTLTALKNVR 234
Cdd:cd01944 150 --------------------LEALPAGTTLVFDPGPRISDipdtiLQALMAKRPIWSCNREEAAIFAERGDPAAEASALR 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 235 NA--TKATLVCKRGPMGCVVLEGDipdswDQVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALV 312
Cdd:cd01944 210 IYakTAAPVVVRLGSNGAWIRLPD-----GNTHIIPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIV 284
|
....*
gi 490248684 313 VSRHG 317
Cdd:cd01944 285 VTRSG 289
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
32-334 |
7.39e-08 |
|
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: 54.52 E-value: 7.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 32 VASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGdEHNGRFLRETLNRAGVDTEYL-ITDKSRLTalVMLGIKDQETFPLi 110
Cdd:TIGR03828 27 VESTRIDAGGKGINVSRVLKNLGVDVVALGFLG-GFTGDFIEALLREEGIKTDFVrVPGETRIN--VKIKEPSGTETKL- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 111 fyrdNCADMALTPDDIsEEYIASSRALAVTGTHLSHANTRAAVLKA------LEYARRHGLRTALD---------IDYRP 175
Cdd:TIGR03828 103 ----NGPGPEISEEEL-EALLEKLRAQLAEGDWLVLSGSLPPGVPPdfyaelIALAREKGAKVILDtsgealrdgLKAKP 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 176 VLwgltslgdgetrfiesgpVTSQLQEVLHLFDLVVGTEEEFHIAGgstDTLTALKnVRNAtkatlVCKRGPMGCVVLEG 255
Cdd:TIGR03828 178 FL------------------IKPNDEELEELFGRELKTLEEIIEAA---RELLDLG-AENV-----LISLGADGALLVTK 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490248684 256 DipDSWdqvpLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGcaPAMPTKVELDDYLQR 334
Cdd:TIGR03828 231 E--GAL----FAQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELLPQ 301
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
10-317 |
6.13e-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: 6.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 10 VICIGRVAVDLYAQ-----QIGSRLEdVASFAKYLGGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLnRAGVDTE 84
Cdd:cd01947 2 IAVVGHVEWDIFLSldappQPGGISH-SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEEL-ESGGDKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 85 YLitdksrltalvmlGIKDQETFPLIFYRDNCADMALTpdDISEEYIASSRALAVTGTHLSHANTRAAVLKALEYARRHG 164
Cdd:cd01947 80 TV-------------AWRDKPTRKTLSFIDPNGERTIT--VPGERLEDDLKWPILDEGDGVFITAAAVDKEAIRKCRETK 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 165 LrtaldidyrpVLWGLTslgdGETRFIEsgpvtsqLQEVLHLFDLVVGTEEEFhiAGGSTDTLTALKNVRnatkaTLVCK 244
Cdd:cd01947 145 L----------VILQVT----PRVRVDE-------LNQALIPLDILIGSRLDP--GELVVAEKIAGPFPR-----YLIVT 196
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490248684 245 RGPMGCVVLEGDipdSWDQVPLQQgvrVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01947 197 EGELGAILYPGG---RYNHVPAKK---AKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
63-323 |
1.50e-06 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 50.80 E-value: 1.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 63 VGDEHNGRFLRETLNRAGVDTEY-------------LITDKSRlTALVMLGIKdqetfplifyrdNCADMALTPDDISEE 129
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEMLFeyttkaptgtcavLVCGKER-SLVANLGAA------------NHLSAEHMQSHAVQE 155
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 130 YIASSRALAVTGTHLshaNTRAA-VLKALEYARRHGlrtaldidyRPVLWGLTSLgdgetrFIeSGPVTSQLQEVLHLFD 208
Cdd:PTZ00247 156 AIKTAQLYYLEGFFL---TVSPNnVLQVAKHARESG---------KLFCLNLSAP------FI-SQFFFERLLQVLPYVD 216
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 209 LVVGTEEEFHIAG-----GSTDTLTALKNV-----RNATKATL-VCKRGPMGCVVLEGDIPDSwdqVPLQQGVRVEVLNV 277
Cdd:PTZ00247 217 ILFGNEEEAKTFAkamkwDTEDLKEIAARIamlpkYSGTRPRLvVFTQGPEPTLIATKDGVTS---VPVPPLDQEKIVDT 293
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 490248684 278 LGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHGCA-PAMP 323
Cdd:PTZ00247 294 NGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKP 340
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
40-314 |
2.75e-04 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 43.44 E-value: 2.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 40 GGSSGNVAFGTAIQGLKSAMLARVGDEHNGRFLRETLNRAGVDTEY-LITDKSRLTALVMLGIKDQETFPLIfyrdncAD 118
Cdd:PRK09850 40 GGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQSGVYVDKcLIVPGENTSSYLSLLDNTGEMLVAI------ND 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 119 MALTpDDISEEYIASSRalavtgthlshantraavlkalEYARRHGLRTA-LDIDYRPVLWGLTSLGDGETrFIEsgPVT 197
Cdd:PRK09850 114 MNIS-NAITAEYLAQHR----------------------EFIQRAKVIVAdCNISEEALAWILDNAANVPV-FVD--PVS 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490248684 198 S----QLQEVLHLFDLVVGTEEEFHIAGGstdtlTALKNVRNATKAT----------LVCKRGPMGCVVLEGDIPDSWdQ 263
Cdd:PRK09850 168 AwkcvKVRDRLNQIHTLKPNRLEAETLSG-----IALSGREDVAKVAawfhqhglnrLVLSMGGDGVYYSDISGESGW-S 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 490248684 264 VPlqqgVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVS 314
Cdd:PRK09850 242 AP----IKTNVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALS 288
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
246-317 |
5.09e-04 |
|
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: 42.71 E-value: 5.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490248684 246 GPMGCVVL-EGDIPDSWdqVPLQQGVRVEVLNVLGAGDAFMSGLLRGWLNDEGWEQACRYANACGALVVSRHG 317
Cdd:cd01943 233 GKLGCYVGsADSGPELW--LPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| |
