|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
3-639 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1112.27 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 3 TQEKQLDVICLGRIAVDFYAQQIGARLEDAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGAD 82
Cdd:COG3892 1 ARMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 83 TRCLITDKRRLTGLVILGIKDQETFPLIFYRENCADMALTPDDIDEAYIASSRALAITGTHLSHPNTRAAVLKALEYARR 162
Cdd:COG3892 81 TSGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 163 HGLRTALDIDYRPVLWGLTSLGDGETRFVESDQVTRELQEVLHHFDLIVGTEEEFHIAGGSTDTLTALKNVRRATAATLV 242
Cdd:COG3892 161 HGGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 243 CKRGAQGCSVFEGEIADDWEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCAPAM 322
Cdd:COG3892 241 CKRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAM 320
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 323 PTKRELDDYLLRERQVTRPDRDARLNHLHRVTTRKQQWPELCVFAFDHRKQLADMAREAGVSEERIPRLKTLLLTAAQQA 402
Cdd:COG3892 321 PTWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQV 400
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 403 AAQAGLNGNSGILADTTYGQAALNEITGQGWWIGRPVELPSSRPLRLEHG-NIGSQLIDWPQEHVVKCLVFYHPHDAAEL 481
Cdd:COG3892 401 AAGAGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAEL 480
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 482 RREQDELIADVYRGCCKSGHELLLEVILPdGNADKDERYYLEMIEHFYRLGIQPDWWKLPPLSAENWQQVGALIDAYDPD 561
Cdd:COG3892 481 RLEQEAQLRRLYDACRRSGHELLLEVIPP-KDGPVDDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPY 559
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310152524 562 CRGVLILGLDSPEAVLKAGFAAAADARWVKGFAVGRTIFGQPSRRWLQGEIDDAALIEQVKQKYLTLIGFWRQYRPQA 639
Cdd:COG3892 560 CRGVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQAA 637
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
327-636 |
2.60e-167 |
|
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: 480.24 E-value: 2.60e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 327 ELDDYLLRERQVTRPDRDARLNHLHRVTTRKQQWPELCVFAFDHRKQLADMAREAGVSEERIPRLKTLLLTAAQQAAAQA 406
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 407 GLNGNSGILADTTYGQAALNEITGQGWWIGRPVELPSSRPLRLEHG-NIGSQLIDWPQEHVVKCLVFYHPHDAAELRREQ 485
Cdd:pfam09863 81 GLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 486 DELIADVYRGCCKSGHELLLEVILPDGNADKDErYYLEMIEHFYRLGIQPDWWKLPPLSAENWQQVGALIDAYDPDCRGV 565
Cdd:pfam09863 161 EAQLRELYDACRKSGHELLLEVIPPKDGPVDDE-TYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRGV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310152524 566 LILGLDSPEAVLKAGFAAAADARWVKGFAVGRTIFGQPSRRWLQGEIDDAALIEQVKQKYLTLIGFWRQYR 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 |
5.65e-164 |
|
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: 471.70 E-value: 5.65e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 7 QLDVICLGRIAVDFYAQQIGARLEDAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCL 86
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 87 ITDKRRLTGLVILGIKDQETFPLIFYRENCADMALTPDDIDEAYIASSRALAITGTHLSHPNTRAAVLKALEYARRHGLR 166
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 167 TALDIDYRPVLWGltslgdgetrfvESDQVTRELQEVLHHFDLIVGTEEEFHIAGGSTDTLTALKNVRRATAATLVCKRG 246
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 247 AQGCSVFEGeiADDWEQVKlhaGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCAPAMPTKR 326
Cdd:TIGR04382 229 PEGSLVYTG--DGEGVEVP---GFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 2310152524 327 ELDDYL 332
Cdd:TIGR04382 304 ELEAFL 309
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
9-328 |
3.96e-84 |
|
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: 266.37 E-value: 3.96e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQ----QIGARLEDAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTR 84
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 85 CLITDKRRLTGLVILGIKDQETFPLIFYRenCADMALTPDDIDEAYIASSRALAITGTHLSHPNTRAAVLKALEYARRHG 164
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 165 LRTALDIDYRPVLWgltslgdgetrfvesDQVTRELQEVLHHFDLIVGTEEEFHIAGGSTDTLTALKNVRRATAATLVCK 244
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 245 RGAQGCSVFEGEiaddweQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCAPAMPT 324
Cdd:COG0524 224 LGAEGALLYTGG------EVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 2310152524 325 KREL 328
Cdd:COG0524 298 REEV 301
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
9-319 |
1.61e-83 |
|
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: 264.44 E-value: 1.61e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQQIGaRLEDAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLIT 88
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 89 DKRRLTGLVILGIKDQETFPLIFYRENCADMALTPDDIDEAYIASSRALAITGTHLS-HPNTRAAVLKALEYARRHGLRT 167
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 168 ALDIDYRPVLWGLtslgdgetrfvesDQVTRELQEVLHHFDLIVGTEEEFHIAGGSTDTLTALKNVRR--ATAATLVCKR 245
Cdd:cd01166 160 SFDLNYRPKLWSA-------------EEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALAlaLGVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310152524 246 GAQGCSVFEGEiaddwEQVKLhAGVRVEVLNVLGAGDAFMSGLLRGYLndEGWD--QACRYANACGALVVSRHGCA 319
Cdd:cd01166 227 GAEGALVYTGG-----GRVFV-PAYPVEVVDTTGAGDAFAAGFLAGLL--EGWDleEALRFANAAAALVVTRPGDI 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
10-317 |
7.18e-53 |
|
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: 183.61 E-value: 7.18e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 10 VICLGRIAVDFYAQQIGARLedagTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITD 89
Cdd:cd01167 2 VVCFGEALIDFIPEGSGAPE----TFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 90 KRRLTGLVILGIKDQ--ETFplIFYRENCADM----ALTPDDIDEAyiassrALAITGTH-LSHPNTRAAVLKALEYARR 162
Cdd:cd01167 78 PAAPTTLAFVTLDADgeRSF--EFYRGPAADLlldtELNPDLLSEA------DILHFGSIaLASEPSRSALLELLEAAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 163 HGLRTALDIDYRPVLWgltslgdgetrfvESDQVTREL-QEVLHHFDLIVGTEEEFHIAGGSTDTLTALKNVRRATAATL 241
Cdd:cd01167 150 AGVLISFDPNLRPPLW-------------RDEEEARERiAELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLV 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 242 VCKRGAQGCSVFEGeiaddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYL-------NDEGWDQACRYANACGALVVS 314
Cdd:cd01167 217 LVTRGADGALLYTK------GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLsrgllalDEDELAEALRFANAVGALTCT 290
|
...
gi 2310152524 315 RHG 317
Cdd:cd01167 291 KAG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
9-319 |
6.27e-44 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 159.05 E-value: 6.27e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQQIGARLED--AGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCL 86
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELvrVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 87 ITDKRRLTGL-VILGIKDQETFpLIFYRENCADMALTPDDIDEAYIASSRALAITGTHLshPNTRAAVLKALEYARRHGl 165
Cdd:pfam00294 81 VIDEDTRTGTaLIEVDGDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLP--LGLPEATLEELIEAAKNG- 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 166 rTALDIDYRPVLWgltslgdgetrfvesdQVTRELQEVLHHFDLIVGTEEEFHIAGGST-----DTLTALKNVRRATAAT 240
Cdd:pfam00294 157 -GTFDPNLLDPLG----------------AAREALLELLPLADLLKPNEEELEALTGAKlddieEALAALHKLLAKGIKT 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310152524 241 LVCKRGAQGCSVFEGEiaddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCA 319
Cdd:pfam00294 220 VIVTLGADGALVVEGD-----GEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQ 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
1-332 |
8.28e-30 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 120.50 E-value: 8.28e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 1 MATQEKQLdVICLGRIAVDFYAQQIGARLEDAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVG 80
Cdd:PLN02323 5 PSTAESSL-VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 81 ADTRCLITDKRRLTGLVILGIKDQETFPLIFYRENCADMALTPDDIDEAYIASSRALAITGTHLSHPNTRAAVLKALEYA 160
Cdd:PLN02323 84 VNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIA 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 161 RRHGLRTALDIDYRPVLWgltslgdgetrfvESDQVTRE-LQEVLHHFDLIVGTEEE--FHIAGGSTDTLTALKnVRRAT 237
Cdd:PLN02323 164 KEAGALLSYDPNLRLPLW-------------PSAEAAREgIMSIWDEADIIKVSDEEveFLTGGDDPDDDTVVK-LWHPN 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 238 AATLVCKRGAQGC----SVFEGEIaddweqvklhAGVRVEVLNVLGAGDAFMSGLL------RGYLNDEG-WDQACRYAN 306
Cdd:PLN02323 230 LKLLLVTEGEEGCryytKDFKGRV----------EGFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFAN 299
|
330 340
....*....|....*....|....*.
gi 2310152524 307 ACGALVVSRHGCAPAMPTKRELDDYL 332
Cdd:PLN02323 300 ACGAITTTERGAIPALPTKEAVLKLL 325
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
9-318 |
4.30e-29 |
|
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: 117.72 E-value: 4.30e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQ-----------QIG-ARLEDAGTF--------AKYL-GGSSGNVAYGTAIQGLKSGMLARVGDEH 67
Cdd:cd01168 3 DVLGLGNALVDILAQvddafleklglKKGdMILADMEEQeellaklpVKYIaGGSAANTIRGAAALGGSAAFIGRVGDDK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 68 MGRFLREELQRVGADTRcLITDKRRLTG--LVILGIKDQETfpLIFYRENCADmaLTPDDIDEAYIASSRALAITGTHLS 145
Cdd:cd01168 83 LGDFLLKDLRAAGVDTR-YQVQPDGPTGtcAVLVTPDAERT--MCTYLGAANE--LSPDDLDWSLLAKAKYLYLEGYLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 146 HPNtrAAVLKALEYARRHGLRTALDIdyrpvlwgltSLGDGETRFVEsdqvtrELQEVLHHFDLIVGTEEEFHIAGGS-- 223
Cdd:cd01168 158 VPP--EAILLAAEHAKENGVKIALNL----------SAPFIVQRFKE------ALLELLPYVDILFGNEEEAEALAEAet 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 224 TDTLTALKNVRRATAATLVCKRGAQGCSVFEGEiaddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACR 303
Cdd:cd01168 220 TDDLEAALKLLALRCRIVVITQGAKGAVVVEGG-----EVYPVPAIPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIR 294
|
330
....*....|....*
gi 2310152524 304 YANACGALVVSRHGC 318
Cdd:cd01168 295 LGSYAAAEVIQQLGP 309
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
30-329 |
2.52e-27 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 112.34 E-value: 2.52e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 30 EDAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITDKRRLTGLVILGIKDQETFPL 109
Cdd:PRK09434 18 EGENRYLKCPGGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSF 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 110 IFYRENCADMALTPDDI-----DEAYIASSRALAitgthlSHPnTRAAVLKALEYARRHGLRTALDIDYRPVLWGltslg 184
Cdd:PRK09434 98 TFMVRPSADLFLQPQDLppfrqGEWLHLCSIALS------AEP-SRSTTFEAMRRIKAAGGFVSFDPNLREDLWQ----- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 185 dgetrfveSDQVTRE-LQEVLHHFDLIVGTEEEFHIAGGSTDTLTALKNVR-RATAATLVCKRGAqgcsvfEGEIADDWE 262
Cdd:PRK09434 166 --------DEAELREcLRQALALADVVKLSEEELCFLSGTSQLEDAIYALAdRYPIALLLVTLGA------EGVLVHTRG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310152524 263 QVKLHAGVRVEVLNVLGAGDAFMSGLLRG------YLNDEGWDQACRYANACGALVVSRHGCAPAMPTKRELD 329
Cdd:PRK09434 232 QVQHFPAPSVDPVDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
9-318 |
1.87e-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: 109.32 E-value: 1.87e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQQIGARLEDAGTFAK----YLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTR 84
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 85 CLITDKRRLTGL-VILGIKDQETfplIFYRENCADMALTPDDIDEaYIASSRALaitgthlsHPNTRAAVLKALEYARRH 163
Cdd:cd01942 81 HVRVVDEDSTGVaFILTDGDDNQ---IAYFYPGAMDELEPNDEAD-PDGLADIV--------HLSSGPGLIELARELAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 164 GLRTALDidyrP--VLWGLTslgdgetrfvesdqvTRELQEVLHHFDLIVGTEEEFHIAggstDTLTALK-NVRRATAAT 240
Cdd:cd01942 149 GITVSFD----PgqELPRLS---------------GEELEEILERADILFVNDYEAELL----KERTGLSeAELASGVRV 205
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310152524 241 LVCKRGAQGCSVFEGEiaddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGC 318
Cdd:cd01942 206 VVVTLGPKGAIVFEDG-----EEVEVPAVPAVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGA 278
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
9-324 |
2.17e-22 |
|
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: 97.62 E-value: 2.17e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQ-----QIGARLEdAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADT 83
Cdd:cd01174 1 KVVVVGSINVDLVTRvdrlpKPGETVL-GSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 84 RCLITDKRRLTGLVIlgIKDQETfplifyRENC------ADMALTPDDIDEAyiassRALAITGTHLSHPN--TRAAVLK 155
Cdd:cd01174 80 SYVEVVVGAPTGTAV--ITVDES------GENRivvvpgANGELTPADVDAA-----LELIAAADVLLLQLeiPLETVLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 156 ALEYARRHGLRTALD----IDYRPVLWGLTslgdgetrfvesdqvtrelqevlhhfDLIVGTEEEFHIAGGSTDT----- 226
Cdd:cd01174 147 ALRAARRAGVTVILNpapaRPLPAELLALV--------------------------DILVPNETEAALLTGIEVTdeeda 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 227 LTALKNVRRATAATLVCKRGAQGCSVFEGeiaddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYAN 306
Cdd:cd01174 201 EKAARLLLAKGVKNVIVTLGAKGALLASG------GEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFAN 274
|
330
....*....|....*...
gi 2310152524 307 ACGALVVSRHGCAPAMPT 324
Cdd:cd01174 275 AAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
9-324 |
1.11e-16 |
|
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: 80.80 E-value: 1.11e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 9 DVICLGRIAVDFYAQQIGARLED----AGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTR 84
Cdd:cd01945 1 RVLGVGLAVLDLIYLVASFPGGDgkivATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 85 CLITdKRRLTGLVILGIKDQETFPLIFYreNCADMALTPDDIDEAYIASSRALAITGtHLshpntRAAVLKALEYARRHG 164
Cdd:cd01945 81 FIVV-APGARSPISSITDITGDRATISI--TAIDTQAAPDSLPDAILGGADAVLVDG-RQ-----PEAALHLAQEARARG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 165 LRTALDIDyrpvlwgltslgdgetrfVESDQVTRELqevLHHFDLIVGTEEEFHIAGGSTDTLtALKNVRRATAATLVCK 244
Cdd:cd01945 152 IPIPLDLD------------------GGGLRVLEEL---LPLADHAICSENFLRPNTGSADDE-ALELLASLGIPFVAVT 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 245 RGAQGCSVFEgeiaDDWEQVKLHAgVRVEVLNVLGAGDAFMSGLLRGYLndEGWD--QACRYANACGALVVSRHGCAPAM 322
Cdd:cd01945 210 LGEAGCLWLE----RDGELFHVPA-FPVEVVDTTGAGDVFHGAFAHALA--EGMPlrEALRFASAAAALKCRGLGGRAGL 282
|
..
gi 2310152524 323 PT 324
Cdd:cd01945 283 PT 284
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
40-332 |
1.35e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 69.13 E-value: 1.35e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 40 GGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITDKRRLTGLVILGIKDQEtfplifyrENC--- 116
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEG--------ENSigi 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 117 ---ADMALTPDDID--EAYIASSRALAItgtHLSHPntRAAVLKALEYARRHGLRTALDidyrPVlwGLTSLGDgetrfv 191
Cdd:PRK11142 111 hagANAALTPALVEahRELIANADALLM---QLETP--LETVLAAAKIAKQHGTKVILN----PA--PARELPD------ 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 192 esdqvtrelqEVLHHFDLIVGTEEEfhiaggsTDTLTALKNVRRATAA------------TLVCKRGAQGCSVFEGEiad 259
Cdd:PRK11142 174 ----------ELLALVDIITPNETE-------AEKLTGIRVEDDDDAAkaaqvlhqkgieTVLITLGSRGVWLSENG--- 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310152524 260 dweQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCAPAMPTKRELDDYL 332
Cdd:PRK11142 234 ---EGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFL 303
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
10-317 |
3.97e-12 |
|
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: 66.99 E-value: 3.97e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 10 VICLGRIAVDFYAQQIGArledagtfakYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTR-CLIt 88
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDIShCRV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 89 dKRRLTGLVILGIKDQETfplIFYRENCADMA-LTPDDIDEAYIASSRaLAITGTHlSHPNTRAAVLKALEYArrhGLRT 167
Cdd:cd01940 71 -KEGENAVADVELVDGDR---IFGLSNKGGVArEHPFEADLEYLSQFD-LVHTGIY-SHEGHLEKALQALVGA---GALI 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 168 ALDIDYRpvlwgltslgdgetrfVESDqvtrELQEVLHHFDLIVGTEEEFhiagGSTDTLTALKNVRRATAATLVCKRGA 247
Cdd:cd01940 142 SFDFSDR----------------WDDD----YLQLVCPYVDFAFFSASDL----SDEEVKAKLKEAVSRGAKLVIVTRGE 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310152524 248 QGCSVFEGeiADDWEQvklhAGVRVEVLNVLGAGDAFMSGLLRGYLnDEGWD--QACRYANACGALVVSRHG 317
Cdd:cd01940 198 DGAIAYDG--AVFYSV----APRPVEVVDTLGAGDSFIAGFLLSLL-AGGTAiaEAMRQGAQFAAKTCGHEG 262
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
126-293 |
8.22e-12 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 64.81 E-value: 8.22e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 126 IDEAYIASSRALAITGTHLShpntRAAVLKALEYARRHGLRTALDidyrpvlwgltsLGDGETRFVEsdqvtRELQEVLH 205
Cdd:cd00287 50 GVSVTLVGADAVVISGLSPA----PEAVLDALEEARRRGVPVVLD------------PGPRAVRLDG-----EELEKLLP 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 206 HFDLIVGTEEEFHIAGG-----STDTLTALKNVRRATAATLVCKRGAQGCSVFEGeiaDDWEqvkLHAG-VRVEVLNVLG 279
Cdd:cd00287 109 GVDILTPNEEEAEALTGrrdleVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATR---GGTE---VHVPaFPVKVVDTTG 182
|
170
....*....|....
gi 2310152524 280 AGDAFMSGLLRGYL 293
Cdd:cd00287 183 AGDAFLAALAAGLA 196
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
37-323 |
9.67e-12 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 66.43 E-value: 9.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 37 KYLGGSsGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRcLITDKRRLTGLVILGIKDQETFPLIfYRENc 116
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTD-GIVDEGRPTTTKTRVIARNQQLLRV-DRED- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 117 admaltPDDIDEAyiASSRALAITGTHLSHPN------------TRAAVLKALEYARRHGLRTALDidyrpvlwgltSLG 184
Cdd:cd01172 113 ------DSPLSAE--EEQRLIERIAERLPEADvvilsdygkgvlTPRVIEALIAAARELGIPVLVD-----------PKG 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 185 DGETRFvesdqvtrelqevlHHFDLIVGTEEEFHIAGGSTDT-----LTALKNVRRATAATLVC-KRGAQGCSVFEGEia 258
Cdd:cd01172 174 RDYSKY--------------RGATLLTPNEKEAREALGDEINdddelEAAGEKLLELLNLEALLvTLGEEGMTLFERD-- 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310152524 259 ddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCAPAMP 323
Cdd:cd01172 238 ---GEVQHIPALAKEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTP 299
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-328 |
2.09e-11 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 65.53 E-value: 2.09e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 1 MATQEKqlDVICLGRIAVDFYA-----QQIGARLEdAGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREE 75
Cdd:PTZ00292 11 GGEAEP--DVVVVGSSNTDLIGyvdrmPQVGETLH-GTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 76 LQRVGADTRCLITDKRRLTGLVILGIKDQETFPLIFYRENcADMALTPDDIDEAY--IASSRALAITGTHLSHPNTraav 153
Cdd:PTZ00292 88 FKRNGVNTSFVSRTENSSTGLAMIFVDTKTGNNEIVIIPG-ANNALTPQMVDAQTdnIQNICKYLICQNEIPLETT---- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 154 LKALEYARRHGLRTALDIDYRPvlwgltslgdgetrfveSDQVTRELQEVLHHFDLIVGTEEEFHIAGGS--TDTLTALK 231
Cdd:PTZ00292 163 LDALKEAKERGCYTVFNPAPAP-----------------KLAEVEIIKPFLKYVSLFCVNEVEAALITGMevTDTESAFK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 232 NVR---RATAATLVCKRGAQGCSVFEgeiaDDWEQVKLhAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANAC 308
Cdd:PTZ00292 226 ASKelqQLGVENVIITLGANGCLIVE----KENEPVHV-PGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRI 300
|
330 340
....*....|....*....|
gi 2310152524 309 GALVVSRHGCAPAMPTKREL 328
Cdd:PTZ00292 301 AAISVTRHGTQSSYPHPSEL 320
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
40-314 |
3.82e-11 |
|
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: 64.26 E-value: 3.82e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 40 GGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITDKRRlTGlvilgikdqeTFPLIFYREN---- 115
Cdd:cd01941 35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRS-TA----------SYTAILDKDGdlvv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 116 -CADMA----LTPDDIDEAYIASSRALAItgthLSHPNTRAAVLKAL-EYARRHGLRTALDidyrPVlwgltslgdgetr 189
Cdd:cd01941 104 aLADMDiyelLTPDFLRKIREALKEAKPI----VVDANLPEEALEYLlALAAKHGVPVAFE----PT------------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 190 fveSDQVTRELQEVLHHFDLIVGTEEEF-----HIAGGSTDTLTALKNVRRATAATLVCKRGAQGCSVFEGEIADdwEQV 264
Cdd:cd01941 163 ---SAPKLKKLFYLLHAIDLLTPNRAELealagALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGV--ETK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 2310152524 265 KLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVS 314
Cdd:cd01941 238 LFPAPQPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
67-332 |
9.38e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 63.23 E-value: 9.38e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 67 HMGRFLREELQRVGADTRCLITDKR-RlTGLVILGIKDQETfplifYRENCADMALTPDDIDE------AYIASSRALAI 139
Cdd:COG1105 61 FTGEFIEELLDEEGIPTDFVPIEGEtR-INIKIVDPSDGTE-----TEINEPGPEISEEELEAllerleELLKEGDWVVL 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 140 TGthlSHP-NTRAAVLKAL-EYARRHGLRTALDIDyrpvlwgltslgdGETrfvesdqvtreLQEVL-HHFDLIVGTEEE 216
Cdd:COG1105 135 SG---SLPpGVPPDFYAELiRLARARGAKVVLDTS-------------GEA-----------LKAALeAGPDLIKPNLEE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 217 F-HIAGGS----TDTLTALKNVRRATAATLVCKRGAQGCSVFEGEIAddweqvkLHAGV-RVEVLNVLGAGDAFMSGLLR 290
Cdd:COG1105 188 LeELLGRPletlEDIIAAARELLERGAENVVVSLGADGALLVTEDGV-------YRAKPpKVEVVSTVGAGDSMVAGFLA 260
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 2310152524 291 GYLNDEGWDQACRYANACGALVVSRHGcaPAMPTKRELDDYL 332
Cdd:COG1105 261 GLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELL 300
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
59-339 |
2.55e-10 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 61.82 E-value: 2.55e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 59 MLARVGDE---------HMGRFLREELQ---------RVGADTRCLITdkrrltglvilgIKD---QETfplifyRENCA 117
Cdd:TIGR03168 44 VLARLGAEvvatgflggFTGEFIEALLAeegikndfvEVKGETRINVK------------IKEssgEET------ELNEP 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 118 DMALTPDDIDE------AYIASSRALAITGThLShPNTRAAVLKAL-EYARRHGLRTALD---------IDYRPVLwglt 181
Cdd:TIGR03168 106 GPEISEEELEQlleklrELLASGDIVVISGS-LP-PGVPPDFYAQLiAIARKKGAKVILDtsgealreaLAAKPFL---- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 182 slgdgetrfVESDQvtRELQEvlhHFDLIVGTEEEFhiaggstdtLTALKNVRRATAATLVCKRGAqgcsvfEGEIADDW 261
Cdd:TIGR03168 180 ---------IKPNH--EELEE---LFGRELKTLEEI---------IEAARELLDRGAENVLVSLGA------DGALLVTK 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310152524 262 EQVkLHAGV-RVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGcaPAMPTKRELDDYLlreRQVT 339
Cdd:TIGR03168 231 EGA-LKATPpKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPG--TGLPDPEDVEELL---DQVT 303
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
32-317 |
5.85e-10 |
|
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: 60.51 E-value: 5.85e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 32 AGTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITDKRRLTGLVILGIKDQETFpLIF 111
Cdd:cd01947 28 SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHTVAWRDKPTRKTLSFIDPNGERTI-TVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 112 YRENCADMAL-TPDDIDEAYIASSRALAitgthlshpntraavlKALEYARRHGLrtaldidyrpVLWGLTslgdGETRF 190
Cdd:cd01947 107 GERLEDDLKWpILDEGDGVFITAAAVDK----------------EAIRKCRETKL----------VILQVT----PRVRV 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 191 VESDQVTRelqevlhHFDLIVGTEEEFhiaGGSTDTLTALKNVRRataaTLVCKRGAQGCSVFEGEiadDWEQVKLhagV 270
Cdd:cd01947 157 DELNQALI-------PLDILIGSRLDP---GELVVAEKIAGPFPR----YLIVTEGELGAILYPGG---RYNHVPA---K 216
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2310152524 271 RVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHG 317
Cdd:cd01947 217 KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
33-317 |
4.62e-09 |
|
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: 58.20 E-value: 4.62e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 33 GTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTrcLITDKRRLTG--LVILGIKDQE-TFPL 109
Cdd:cd01944 28 AKSKSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEI--LLPPRGGDDGgcLVALVEPDGErSFIS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 110 IFYRENcadmALTPDDIDEAYIASSRALAITGTHLSHPNTRAAVLkaLEYARRHGLRTALDIDYRPVLwgltslgdgetr 189
Cdd:cd01944 106 ISGAEQ----DWSTEWFATLTVAPYDYVYLSGYTLASENASKVIL--LEWLEALPAGTTLVFDPGPRI------------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 190 fveSDQVTRELQEVLHHFDLIVGTEEEFHIAGGsTDTLTALKNVRRATA---ATLVCKRGAQGCSVFEgeiADDweQVKL 266
Cdd:cd01944 168 ---SDIPDTILQALMAKRPIWSCNREEAAIFAE-RGDPAAEASALRIYAktaAPVVVRLGSNGAWIRL---PDG--NTHI 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 2310152524 267 HAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHG 317
Cdd:cd01944 239 IPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
5-310 |
5.68e-09 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 58.69 E-value: 5.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 5 EKQLDVICLGRIAVDF-----------------YAQQIGARLEDAgtfaKYL-GGSSGNVAYGTAIQGLKSGMLARVGDE 66
Cdd:PLN02341 70 GKEIDVATLGNLCVDIvlpvpelpppsreerkaYMEELAASPPDK----KSWeAGGNCNFAIAAARLGLRCSTIGHVGDE 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 67 HMGRFLREELQRVGADTRCLITDkrrlTGLVILGIKDQET---FPLI--FYREN-CA-----------DMALTPDDIDEA 129
Cdd:PLN02341 146 IYGKFLLDVLAEEGISVVGLIEG----TDAGDSSSASYETllcWVLVdpLQRHGfCSradfgpepafsWISKLSAEAKMA 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 130 yIASSRALAITGTHLSHPNTrAAVLKALEYARRHGlrTALDIDYRPvlwgltslgDGETRFVESDQVTRELQEVLHHFDL 209
Cdd:PLN02341 222 -IRQSKALFCNGYVFDELSP-SAIASAVDYAIDVG--TAVFFDPGP---------RGKSLLVGTPDERRALEHLLRMSDV 288
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 210 IVGTEEEFHIAGGSTDTLTALKNVRRATAAT--LVCKRGAQGCSVFEGEiaddweQVKLHAGVRVEVLNVLGAGDAFMSG 287
Cdd:PLN02341 289 LLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVTRS------SVSCAPAFKVNVVDTVGCGDSFAAA 362
|
330 340
....*....|....*....|...
gi 2310152524 288 LLRGYLNDEGWDQACRYANACGA 310
Cdd:PLN02341 363 IALGYIHNLPLVNTLTLANAVGA 385
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
10-317 |
9.36e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.67 E-value: 9.36e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 10 VICLGRIAVDFYaQQIGArledagtfaKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITD 89
Cdd:PRK09813 3 LATIGDNCVDIY-PQLGK---------AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 90 KRRlTGLVILGIKDQETfplIF--YRENC-ADMALTPDDIDeayiassralAITGTHLSHPNTRAAVLKALEYARRHGLR 166
Cdd:PRK09813 73 HGV-TAQTQVELHDNDR---VFgdYTEGVmADFALSEEDYA----------WLAQYDIVHAAIWGHAEDAFPQLHAAGKL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 167 TALDIDYRPvlwgltslgdgETRFVESdqvtrelqeVLHHFDLIvgteeeFHIAGGSTDTL-TALKNVRRATAATLVCKR 245
Cdd:PRK09813 139 TAFDFSDKW-----------DSPLWQT---------LVPHLDYA------FASAPQEDEFLrLKMKAIVARGAGVVIVTL 192
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310152524 246 GAqgcsvfEGEIADDWEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHG 317
Cdd:PRK09813 193 GE------NGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| PLN02967 |
PLN02967 |
kinase |
14-216 |
3.95e-08 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 56.21 E-value: 3.95e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 14 GRIAVDFYAQQIGARLEDA----GTFAKYLGGSSGNVAYGTAIQGLKSGMLARVGDEHMGRFLREELQRVGADTRCLITD 89
Cdd:PLN02967 213 GRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCID 292
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 90 KRRLTGLVILGIKDQETFPLIFYREnCADMALTPDDIDEAYIASSRALAITGTHLSHPNTRAAVLKALEYARRHGLRTAL 169
Cdd:PLN02967 293 GKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFY 371
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 2310152524 170 DIDYRPVLWgltslgdgetrfvESDQVTREL-QEVLHHFDLIVGTEEE 216
Cdd:PLN02967 372 DLNLPLPLW-------------SSSEETKSFiQEAWNLADIIEVTKQE 406
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
68-317 |
1.02e-07 |
|
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: 54.08 E-value: 1.02e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 68 MGRFLREELQRVGADTRCL-ITDKRRlTGLVILGIKDQETfplifyRENCADMALTPDDID------EAYIASSRALAIT 140
Cdd:cd01164 63 TGDFFEALLKEEGIPDDFVeVAGETR-INVKIKEEDGTET------EINEPGPEISEEELEalleklKALLKKGDIVVLS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 141 GTHLSHPNTRAAVlKALEYARRHGLRTALDIDYRPvlwgltslgdgetrfvesdqvtreLQEVL-HHFDLIVGTEEEFH- 218
Cdd:cd01164 136 GSLPPGVPADFYA-ELVRLAREKGARVILDTSGEA------------------------LLAALaAKPFLIKPNREELEe 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 219 IAGGSTDTLTALKnvrraTAATLVCKRGAQgCSVF----EGEIADDWEQVkLHAGV-RVEVLNVLGAGDAFMSGLLRGYL 293
Cdd:cd01164 191 LFGRPLGDEEDVI-----AAARKLIERGAE-NVLVslgaDGALLVTKDGV-YRASPpKVKVVSTVGAGDSMVAGFVAGLA 263
|
250 260
....*....|....*....|....
gi 2310152524 294 NDEGWDQACRYANACGALVVSRHG 317
Cdd:cd01164 264 QGLSLEEALRLAVAAGSATAFSPG 287
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
57-339 |
3.69e-06 |
|
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: 49.12 E-value: 3.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 57 SGMLARVGDE---------HMGRFLREELQRVGADTRCLITDKRRLTGLVILGIKDQETfplifyRENCADMALTPDDID 127
Cdd:TIGR03828 42 SRVLKNLGVDvvalgflggFTGDFIEALLREEGIKTDFVRVPGETRINVKIKEPSGTET------KLNGPGPEISEEELE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 128 E------AYIASSRALAITGThLShPNTRAAVLKAL-EYARRHGLRTALD---------IDYRPVLwgltslgdgetrfv 191
Cdd:TIGR03828 116 AlleklrAQLAEGDWLVLSGS-LP-PGVPPDFYAELiALAREKGAKVILDtsgealrdgLKAKPFL-------------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 192 esdqVTRELQEVLHHFDLIVGTEEEFhiaggstdtLTALKNVRRATAATLVCKRGAQGCSVFEGEIAddweqvkLHA-GV 270
Cdd:TIGR03828 180 ----IKPNDEELEELFGRELKTLEEI---------IEAARELLDLGAENVLISLGADGALLVTKEGA-------LFAqPP 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310152524 271 RVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGcaPAMPTKRELDDYLlreRQVT 339
Cdd:TIGR03828 240 KGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELL---PQVT 303
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
199-326 |
1.67e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 47.33 E-value: 1.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 199 ELQEVLHHFDLIVGTEEEFHIAGGSTD-TLTALKNVRRATAA----------TLVCKRGAQGCSVFEGeiaDDWEQVKLH 267
Cdd:PTZ00247 207 RLLQVLPYVDILFGNEEEAKTFAKAMKwDTEDLKEIAARIAMlpkysgtrprLVVFTQGPEPTLIATK---DGVTSVPVP 283
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 268 AGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHGCA-PAMPTKR 326
Cdd:PTZ00247 284 PLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKPPFL 343
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
274-317 |
4.32e-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: 4.32e-04
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2310152524 274 VLNVLGAGDAFMSGLLRGYLNDEGWDQACRYANACGALVVSRHG 317
Cdd:cd01943 260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
76-316 |
5.35e-04 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 42.69 E-value: 5.35e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 76 LQRV-GADTRC--LITDKRRLTGLVILGIKDQetfplifyrencadmaLTPDDIDEAYIASSRALAITG----THLSHPN 148
Cdd:PRK15074 142 LQGVdGPIGRCftLISEDGERTFAISPGHMNQ----------------LRPESIPEDVIAGASALVLTAylvrCKPGEPM 205
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 149 TRAAvLKALEYARRHGLrtaldidyrPVLwgLTsLGdgeTRFVESDQVTRELQEVLHHFDLIVGTEEEFHIAGGSTDTLT 228
Cdd:PRK15074 206 PEAT-MKAIEYAKKHNV---------PVV--LT-LG---TKFVIEDNPQWWQEFLKEHVSILAMNEDEAEALTGESDPLL 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 229 AlknvrrATAA----TLV-CKRGAQGC----------------SVFEGEIAD----DWEQVKLHAG----VRV------- 272
Cdd:PRK15074 270 A------SDKAldwvDLVlCTAGPIGLymagytedeakretqhPLLPGAIAEfnryEFSRAMRKKDcqnpLRVyshiapy 343
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2310152524 273 -----EVLNVLGAGDAFMSGLL--------------------RGYLNDEGWDQACRYANACGALVVSRH 316
Cdd:PRK15074 344 mggpeKIMNTNGAGDGALSALLhditansyhrsnvpnsskhkRTYLTYSSLAQVCKYANRVSYEVLNQH 412
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
153-313 |
7.39e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 39.00 E-value: 7.39e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 153 VLKALEYARRHGLRTALDI-------DYRPVLWGLTSLGDGETRFVESDQvTRELqevlhhfdliVGTEEEFhiaggstD 225
Cdd:PLN02379 193 IEAAIRLAKQEGLSVSLDLasfemvrNFRSPLLQLLESGKIDLCFANEDE-AREL----------LRGEQES-------D 254
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310152524 226 TLTAL----KNVRRAtaatlVCKRGAQGCSVFEGEiaddwEQVKLHAGVRVEVLNVLGAGDAFMSGLLRGYLNDEGWDQA 301
Cdd:PLN02379 255 PEAALeflaKYCNWA-----VVTLGSKGCIARHGK-----EVVRVPAIGETNAVDATGAGDLFASGFLYGLIKGLSLEEC 324
|
170
....*....|..
gi 2310152524 302 CRYANACGALVV 313
Cdd:PLN02379 325 CKVGACSGGSVV 336
|
|
| |
