|
Name |
Accession |
Description |
Interval |
E-value |
| IolC |
COG3892 |
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism]; |
1-634 |
0e+00 |
|
Myo-inositol catabolism protein LolC [Carbohydrate transport and metabolism];
Pssm-ID: 443099 [Multi-domain] Cd Length: 640 Bit Score: 1101.10 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 1 MEKQFDVICMGRVAVDLYSQQIGARLEDASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDT 80
Cdd:COG3892 2 RMKTLDVICIGRVSVDLYGQQIGGRLEDMSSFAKYLGGSSGNIAYGTARLGLKSAMLTRVGDEHMGRFLREELEREGVDT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 81 RHLIIDKERLTALVLLGIKDQDTFPLIFYRDNCADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARRH 160
Cdd:COG3892 82 SGVVTDPERLTALVLLGIRDDETFPLIFYRENCADMALTEDDIDEAFIASARALLITGTHLSHPRTRAAVLKALRYARAH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 161 GVRTVLDIDYRPVLWGLTSLGDGETRFIAADRVSRELQEVLHLFDVIVGTEEEFHIAGGSIDTLQALTQVRRVSPATLVC 240
Cdd:COG3892 162 GGKVVLDIDYRPVLWGLTGHGDGETRFVASDAVTAHLQEVLPLFDLIVGTEEEFHIAGGSTDTLAALRAVRRVSTATLVC 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 241 KRGARGCSVYTDAIPPRLDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMP 320
Cdd:COG3892 242 KRGALGCVVFEGAIPDDLDDGITGPGFPVEVFNVLGAGDAFMSGFLRGWLRGESWETACAYANACGALVVSRHGCAPAMP 321
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 321 SKIELDDYLSRERDVPRPDLDPRLNHLHRVTTRRREWSELCVMAFDHRSQLEEMAMQCGASLKRIPVLKTLILQASRAAA 400
Cdd:COG3892 322 TWEELDYFLARGSRVPRPDKDAELNHLHRVTTRRRQWDELCVFAFDHRSQFEDMAREAGADEARIPALKRLLLEAAAQVA 401
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 401 QCAGLAGRAGLLCDGTFGQDALNAITGEGWWIGRPIELPGSRPLEMEHG-NIGTQLISWPQEHVVKCLVLYHPEDVHALR 479
Cdd:COG3892 402 AGAGLRGGIGVLIDDRYGQDALNAATGRGWWIGRPVELPGSRPLRFEHGrDIGSQLVEWPQEHVVKCLVFYHPDDPAELR 481
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 480 LAQERSVAEVYRACCQSGHELLLELILPPDMSHSDDLYLRAVSRFYNLGVYPDCWKLPPLSSAGWSALEAIIERRDPHCR 559
Cdd:COG3892 482 LEQEAQLRRLYDACRRSGHELLLEVIPPKDGPVDDDTVARAIQRFYNLGIKPDWWKLEPMSAAAWQAIDALIAERDPYCR 561
|
570 580 590 600 610 620 630
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1378071945 560 GVLILGLDAPAEELRAGFNAAADHAWVKGFAVGRTLFGDAARAWLRQDIDDAQLVARIRDNYLQLIAWWRERGQA 634
Cdd:COG3892 562 GVVLLGLDAPEEELAAGFAAAAGSPLVKGFAVGRTIFAEPARAWLAGEIDDEEAVAEVADNYARLIDLWRAARQA 636
|
|
| DUF2090 |
pfam09863 |
Uncharacterized protein conserved in bacteria (DUF2090); This domain, found in various ... |
324-632 |
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: 517.99 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 324 ELDDYLSRERDVPRPDLDPRLNHLHRVTTRRREWSELCVMAFDHRSQLEEMAMQCGASLKRIPVLKTLILQASRAAAQCA 403
Cdd:pfam09863 1 ELDYFLSRGERVPRPDKDAELEHLHRVTTRRRQWDELCVLAFDHRSQLEELAREAGADLARIPALKRLLLRAAEEVAQEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 404 GLAGRAGLLCDGTFGQDALNAITGEGWWIGRPIELPGSRPLEMEHG-NIGTQLISWPQEHVVKCLVLYHPEDVHALRLAQ 482
Cdd:pfam09863 81 GLQGGAGVLIDGRYGQDALNAATGRGWWIGRPIELPGSRPLRFEHGrSIGSQLIEWPLEHVVKCLVFYHPDDDAALRAEQ 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 483 ERSVAEVYRACCQSGHELLLELILPPDMSHSDDLYLRAVSRFYNLGVYPDCWKLPPLSSAGWSALEAIIERRDPHCRGVL 562
Cdd:pfam09863 161 EAQLRELYDACRKSGHELLLEVIPPKDGPVDDETYARAIRRFYNLGVKPDWWKLPPLSAAAWEQIDALIEERDPYCRGVV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 563 ILGLDAPAEELRAGFNAAADHAWVKGFAVGRTLFGDAARAWLRQDIDDAQLVARIRDNYLQLIAWWRERG 632
Cdd:pfam09863 241 ILGLDAPEEELAAGFAAAAGFPLVKGFAVGRTIFADPARAWLAGEIDDEELIAEVAANYARLIDLWRQRR 310
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
4-329 |
1.67e-163 |
|
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: 470.16 E-value: 1.67e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 4 QFDVICMGRVAVDLYSQQIGARLEDASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHL 83
Cdd:TIGR04382 1 KLDVITIGRVGVDLYPQQIGVPLEDVTSFAKYLGGSPANIAVGAARLGLKTAFITRVGDDQFGRFVRDYLRREGVDTSHV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 84 IIDKERLTALVLLGIKDQDTFPLIFYRDNCADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARRHGVR 163
Cdd:TIGR04382 81 VTDPGRRTSLVFLEIKPPDEFPLLFYRENAADLALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 164 TVLDIDYRPVLWGltslgdgetrfiAADRVSRELQEVLHLFDVIVGTEEEFHIAGGSIDTLQALTQVRRVSPATLVCKRG 243
Cdd:TIGR04382 161 VVLDIDYRPYLWK------------SPEEAGIYLRLVLPLVDVIIGTREEFDIAGGEGDDEAAARALLDAGVEILVVKRG 228
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 244 ARGCSVYTdaippRLDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPSKI 323
Cdd:TIGR04382 229 PEGSLVYT-----GDGEGVEVPGFPVEVLNVLGAGDAFASGFLYGLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLE 303
|
....*.
gi 1378071945 324 ELDDYL 329
Cdd:TIGR04382 304 ELEAFL 309
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
6-316 |
1.19e-80 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 256.73 E-value: 1.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 6 DVICMGRVAVDLYSQQIGaRLEDASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLII 85
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGG-RLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 86 DKERLTALVLLGIKDQDTFPLIFYRDNCADMAISADDVDEAYIASSRCLAITGTHLS-HPQTREAVLTALGYARRHGVRT 164
Cdd:cd01166 80 DPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAALAGADHLHLSGITLAlSESAREALLEALEAAKARGVTV 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 165 VLDIDYRPVLWGltslgdgetrfiaADRVSRELQEVLHLFDVIVGTEEEFHIAGGSIDTLQALTQVRRVS--PATLVCKR 242
Cdd:cd01166 160 SFDLNYRPKLWS-------------AEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERALALAlgVKAVVVKL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1378071945 243 GARGCSVYTDaipprlDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCS 316
Cdd:cd01166 227 GAEGALVYTG------GGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
6-325 |
1.27e-80 |
|
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: 256.74 E-value: 1.27e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 6 DVICMGRVAVDLYSQ----QIGARLEDASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTR 81
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlPKGGETVLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 82 HLIIDKERLTALVLLGIKDQDTFPLIFYRdnCADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARRHG 161
Cdd:COG0524 81 GVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDEALLAGADILHLGGITLASEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 162 VRTVLDIDYRPVLWgltslgdgetrfiaaDRVSRELQEVLHLFDVIVGTEEEFHIAGGSIDTLQALTQVRRVSPATLVCK 241
Cdd:COG0524 159 VPVSLDPNYRPALW---------------EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVT 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 242 RGARGCSVYTDaipprlDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPS 321
Cdd:COG0524 224 LGAEGALLYTG------GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 1378071945 322 KIEL 325
Cdd:COG0524 298 REEV 301
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
7-314 |
2.95e-50 |
|
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: 176.29 E-value: 2.95e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 7 VICMGRVAVDLYSQQIGARLEdasgFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIID 86
Cdd:cd01167 2 VVCFGEALIDFIPEGSGAPET----FTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAGVDTRGIQFD 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 87 KERLTALVLLGIKDQD--TFplIFYRDNCADM----AISADDVDEAYIassrclAITGTH-LSHPQTREAVLTALGYARR 159
Cdd:cd01167 78 PAAPTTLAFVTLDADGerSF--EFYRGPAADLlldtELNPDLLSEADI------LHFGSIaLASEPSRSALLELLEAAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 160 HGVRTVLDIDYRPVLWgltslgdgETRFIAADRVsrelQEVLHLFDVIVGTEEEFHIAGGSIDTLQALTQVRRVSPATLV 239
Cdd:cd01167 150 AGVLISFDPNLRPPLW--------RDEEEARERI----AELLELADIVKLSDEELELLFGEEDPEEIAALLLLFGLKLVL 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 240 CKRGARGCSVYTDaipprlDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYL-------NDEGWEQSCRYANACGALVVSR 312
Cdd:cd01167 218 VTRGADGALLYTK------GGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLLsrgllalDEDELAEALRFANAVGALTCTK 291
|
..
gi 1378071945 313 HG 314
Cdd:cd01167 292 AG 293
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
6-316 |
9.66e-41 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 150.19 E-value: 9.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 6 DVICMGRVAVDL--YSQQIGARLEDASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHL 83
Cdd:pfam00294 1 KVVVIGEANIDLigNVEGLPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 84 IIDKERLT--ALVLLGiKDQDTFpLIFYRDNCADMAISADDVDEAYIASSRCLAITGTHLSHpqTREAVLTALGYARRHG 161
Cdd:pfam00294 81 VIDEDTRTgtALIEVD-GDGERT-IVFNRGAAADLTPEELEENEDLLENADLLYISGSLPLG--LPEATLEELIEAAKNG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 162 vrTVLDIDYRPVLWGLTSLgdgetrfiaadrvsreLQEVLHLFDVIVGTEEEF----HIAGGSI-DTLQALTQVRRVSPA 236
Cdd:pfam00294 157 --GTFDPNLLDPLGAAREA----------------LLELLPLADLLKPNEEELealtGAKLDDIeEALAALHKLLAKGIK 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 237 TLVCKRGARGCSVYTDaipprlDDGLTVTGVR-VAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGC 315
Cdd:pfam00294 219 TVIVTLGADGALVVEG------DGEVHVPAVPkVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGA 292
|
.
gi 1378071945 316 S 316
Cdd:pfam00294 293 Q 293
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
7-331 |
3.65e-30 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 121.27 E-value: 3.65e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 7 VICMGRVAVDLYSQQIGARLEDASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIID 86
Cdd:PLN02323 13 VVCFGEMLIDFVPTVSGVSLAEAPAFKKAPGGAPANVAVGISRLGGSSAFIGKVGDDEFGHMLADILKKNGVNNEGVRFD 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 87 KERLTALVLLGIKDQDTFPLIFYRDNCADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARRHGVRTVL 166
Cdd:PLN02323 93 PGARTALAFVTLRSDGEREFMFYRNPSADMLLRESELDLDLIRKAKIFHYGSISLITEPCRSAHLAAMKIAKEAGALLSY 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 167 DIDYRPVLWGltslgdgetrfiAADRVSRELQEVLHLFDVIVGTEEE--FHIAGGSIDTLQALTQVRRVSPATLVCKrGA 244
Cdd:PLN02323 173 DPNLRLPLWP------------SAEAAREGIMSIWDEADIIKVSDEEveFLTGGDDPDDDTVVKLWHPNLKLLLVTE-GE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 245 RGCSVYTDAIPPRlddgltVTGVRVAILNVLGAGDAFMSGLL------RGYLNDEG-WEQSCRYANACGALVVSRHGCSP 317
Cdd:PLN02323 240 EGCRYYTKDFKGR------VEGFKVKAVDTTGAGDAFVGGLLsqlakdLSLLEDEErLREALRFANACGAITTTERGAIP 313
|
330
....*....|....
gi 1378071945 318 AMPSKIELDDYLSR 331
Cdd:PLN02323 314 ALPTKEAVLKLLKK 327
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
5-317 |
3.58e-27 |
|
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: 112.32 E-value: 3.58e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 5 FDVICMGRVAVDLYSQ-----------QIG-ARLEDASGFAKYL---------GGSSGNVAYGTARQGLRSSMLARVGDE 63
Cdd:cd01168 2 YDVLGLGNALVDILAQvddafleklglKKGdMILADMEEQEELLaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 64 HMGRFLREELRQAGCDTRHLIIDKERL-TALVLLGIKDQDTFplifyrdnCADMAISA----DDVDEAYIASSRCLAITG 138
Cdd:cd01168 82 KLGDFLLKDLRAAGVDTRYQVQPDGPTgTCAVLVTPDAERTM--------CTYLGAANelspDDLDWSLLAKAKYLYLEG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 139 THLSHPQtrEAVLTALGYARRHGVRTVLDidyrpvlwgltsLGDgetRFIAaDRVSRELQEVLHLFDVIVGTEEEFHIAG 218
Cdd:cd01168 154 YLLTVPP--EAILLAAEHAKENGVKIALN------------LSA---PFIV-QRFKEALLELLPYVDILFGNEEEAEALA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 219 GSI--DTLQALTQVRRVSPATLVCKRGARGCSVYTDaipprlDDGLTVTGVRVA-ILNVLGAGDAFMSGLLRGYLNDEGW 295
Cdd:cd01168 216 EAEttDDLEAALKLLALRCRIVVITQGAKGAVVVEG------GEVYPVPAIPVEkIVDTNGAGDAFAGGFLYGLVQGEPL 289
|
330 340
....*....|....*....|..
gi 1378071945 296 EQSCRYANACGALVVSRHGCSP 317
Cdd:cd01168 290 EECIRLGSYAAAEVIQQLGPRL 311
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
6-316 |
8.27e-27 |
|
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: 110.48 E-value: 8.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 6 DVICMGRVAVDLYSQQIGARLEDASGFAK----YLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTR 81
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKdlrrEFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 82 HLIIDKERLTALVLLGIKDQDTFPLIFYRDncaDMAISADDVDEAYIASSRCLAITGthlshpqtrEAVLTALGYARRHG 161
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYFYPG---AMDELEPNDEADPDGLADIVHLSS---------GPGLIELARELAAG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 162 VRTVldidyrpvlwgltSLGDGEtrfIAADRVSRELQEVLHLFDVIVGTEEEF----HIAGGSidtlqalTQVRRVSPAT 237
Cdd:cd01942 149 GITV-------------SFDPGQ---ELPRLSGEELEEILERADILFVNDYEAellkERTGLS-------EAELASGVRV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 238 LVCKRGARGCSVYTD----AIPPRLDdgltvtgvrVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRH 313
Cdd:cd01942 206 VVVTLGPKGAIVFEDgeevEVPAVPA---------VKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERR 276
|
...
gi 1378071945 314 GCS 316
Cdd:cd01942 277 GAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
37-326 |
2.86e-24 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 103.48 E-value: 2.86e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 37 GGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLTALVLLGIKDQDTFPLIFYRDNCADM 116
Cdd:PRK09434 28 GGAPANVAVGIARLGGESGFIGRVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHRTSTVVVDLDDQGERSFTFMVRPSADL 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 117 AISADDVDEayIASSRCLAITGTHLSHPQTREAVLTALGYARRHGVRTVLDIDYRPVLWGLTSlgdgetrfiaadrvsrE 196
Cdd:PRK09434 108 FLQPQDLPP--FRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSFDPNLREDLWQDEA----------------E 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 197 LQEVLH----LFDVIVGTEEEFHIAGGSIDTLQALTQVR-RVSPATLVCKRGARGCSVYTDaipprlDDGLTVTGVRVAI 271
Cdd:PRK09434 170 LRECLRqalaLADVVKLSEEELCFLSGTSQLEDAIYALAdRYPIALLLVTLGAEGVLVHTR------GQVQHFPAPSVDP 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1378071945 272 LNVLGAGDAFMSGLLRG------YLNDEGWEQSCRYANACGALVVSRHGCSPAMPSKIELD 326
Cdd:PRK09434 244 VDTTGAGDAFVAGLLAGlsqaglWTDEAELAEIIAQAQACGALATTAKGAMTALPNRQELE 304
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
29-321 |
2.26e-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: 2.26e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 29 ASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLT--ALVLLgikDQDtfpl 106
Cdd:cd01174 28 GSSFETGPGGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGAPTgtAVITV---DES---- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 107 ifyRDNC------ADMAISADDVDEAYIASSRClAITGTHLSHPQtrEAVLTALGYARRHGVRTVLD----IDYRPVLWG 176
Cdd:cd01174 101 ---GENRivvvpgANGELTPADVDAALELIAAA-DVLLLQLEIPL--ETVLAALRAARRAGVTVILNpapaRPLPAELLA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 177 LTSL---GDGETRFIAADRVSRElqevlhlfdvivgtEEEFHIAggsiDTLQALTqvrrvsPATLVCKRGARGCSVYTDa 253
Cdd:cd01174 175 LVDIlvpNETEAALLTGIEVTDE--------------EDAEKAA----RLLLAKG------VKNVIVTLGAKGALLASG- 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1378071945 254 ipprlDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPS 321
Cdd:cd01174 230 -----GEVEHVPAFKVKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAQPSIPT 292
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
29-321 |
3.94e-17 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 81.96 E-value: 3.94e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 29 ASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLTALVLLgikDQDTFPLIF 108
Cdd:cd01945 28 ATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSI---TDITGDRAT 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 109 YRDNCADMAISADDVDEAYIASSRCLAITGtHLshpqtREAVLTALGYARRHGVRTVLDIDyrpvlwgltslgdgetrfI 188
Cdd:cd01945 105 ISITAIDTQAAPDSLPDAILGGADAVLVDG-RQ-----PEAALHLAQEARARGIPIPLDLD------------------G 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 189 AADRVSRELqevLHLFDVIVGTEEEFHIAGGSIDTlQALTQVRRVSPATLVCKRGARGCSVYTDaipprlDDGL-TVTGV 267
Cdd:cd01945 161 GGLRVLEEL---LPLADHAICSENFLRPNTGSADD-EALELLASLGIPFVAVTLGEAGCLWLER------DGELfHVPAF 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1378071945 268 RVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPS 321
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGGRAGLPT 284
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
42-331 |
7.13e-13 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 69.78 E-value: 7.13e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 42 NVAYGTARQGLRSSMLARVGdEHMGRFLREELRQAGCDTRHLIIDKE-RlTALVLLGIKDQDTFPLifyrdNCADMAISA 120
Cdd:COG1105 40 NVARVLKALGVDVTALGFLG-GFTGEFIEELLDEEGIPTDFVPIEGEtR-INIKIVDPSDGTETEI-----NEPGPEISE 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 121 DDVDE------AYIASSRCLAITGthlSHPQ----TREAVLTALgyARRHGVRTVLD---------IDYRPVLwgltslg 181
Cdd:COG1105 113 EELEAllerleELLKEGDWVVLSG---SLPPgvppDFYAELIRL--ARARGAKVVLDtsgealkaaLEAGPDL------- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 182 dgetrfIAADRvsRELQEvlhLFDVIVGTEEEFhiaggsIDTLQAL--TQVRRVspatlVCKRGARGcSVYTDAipprlD 259
Cdd:COG1105 181 ------IKPNL--EELEE---LLGRPLETLEDI------IAAARELleRGAENV-----VVSLGADG-ALLVTE-----D 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1378071945 260 DGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGcsPAMPSKIELDDYLSR 331
Cdd:COG1105 233 GVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPG--TGLPDREDVEELLAQ 302
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
37-330 |
2.02e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 68.36 E-value: 2.02e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 37 GGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLTalvllGIKdqdtfpLIFYRDNC--- 113
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGEST-----GVA------LIFVNDEGens 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 114 ------ADMAISADDVD--EAYIASSRCLAItgtHLSHPQtrEAVLTALGYARRHGVRTVLDidyrPVlwGLTSLGDget 185
Cdd:PRK11142 108 igihagANAALTPALVEahRELIANADALLM---QLETPL--ETVLAAAKIAKQHGTKVILN----PA--PARELPD--- 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 186 rfiaadrvsrelqEVLHLFDVIVGTEEEFHIAGG----SIDTLQALTQV-RRVSPATLVCKRGARG--CSVYtdaipprl 258
Cdd:PRK11142 174 -------------ELLALVDIITPNETEAEKLTGirveDDDDAAKAAQVlHQKGIETVLITLGSRGvwLSEN-------- 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1378071945 259 DDGLTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPSKIELDDYLS 330
Cdd:PRK11142 233 GEGQRVPGFRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGAQPSIPWREEIDAFLQ 304
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
7-314 |
1.85e-11 |
|
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: 65.07 E-value: 1.85e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 7 VICMGRVAVDLYSQQIGArledasgfakYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIId 86
Cdd:cd01940 2 LAAIGDNVVDKYLHLGKM----------YPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRV- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 87 KERLTALVLLGIKDQDTfplIFYRDN---CADMAISADDVdeAYIASSRcLAITGTHlSHPQTREAVLTALGYArrhGVR 163
Cdd:cd01940 71 KEGENAVADVELVDGDR---IFGLSNkggVAREHPFEADL--EYLSQFD-LVHTGIY-SHEGHLEKALQALVGA---GAL 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 164 TVLDIDYRPVLWGLTSLGDG-ETRFIAADRVSRELQEVLhlfdvivgteeefhiaggsidtlqaLTQVRRVSPATLVCKR 242
Cdd:cd01940 141 ISFDFSDRWDDDYLQLVCPYvDFAFFSASDLSDEEVKAK-------------------------LKEAVSRGAKLVIVTR 195
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378071945 243 GARGCSVYTDaipprlDDGLTVTGVRVAILNVLGAGDAFMSGLLRGYL-NDEGWEQSCRYANACGALVVSRHG 314
Cdd:cd01940 196 GEDGAIAYDG------AVFYSVAPRPVEVVDTLGAGDSFIAGFLLSLLaGGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
2-307 |
5.05e-11 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 65.24 E-value: 5.05e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 2 EKQFDVICMGRVAVDL-----------------YSQQIGARLEDASGFAkyLGGSSgNVAYGTARQGLRSSMLARVGDEH 64
Cdd:PLN02341 70 GKEIDVATLGNLCVDIvlpvpelpppsreerkaYMEELAASPPDKKSWE--AGGNC-NFAIAAARLGLRCSTIGHVGDEI 146
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 65 MGRFLREELRQAGCDTRHLIID----------KERLTALVLLG------------IKDQDTFPLIFYRDNCADMAISadd 122
Cdd:PLN02341 147 YGKFLLDVLAEEGISVVGLIEGtdagdsssasYETLLCWVLVDplqrhgfcsradFGPEPAFSWISKLSAEAKMAIR--- 223
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 123 vdeayiaSSRCLAITGTHLSHPQTrEAVLTALGYARRHGVRTVLDIDYRpvlwgltslgdGETRFIAADRVSRELQEVLH 202
Cdd:PLN02341 224 -------QSKALFCNGYVFDELSP-SAIASAVDYAIDVGTAVFFDPGPR-----------GKSLLVGTPDERRALEHLLR 284
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 203 LFDVIVGTEEEFHIAGGSIDTLQALTQVRRVSPAT--LVCKRGARGCSVYTdaipprLDDGLTVTGVRVAILNVLGAGDA 280
Cdd:PLN02341 285 MSDVLLLTSEEAEALTGIRNPILAGQELLRPGIRTkwVVVKMGSKGSILVT------RSSVSCAPAFKVNVVDTVGCGDS 358
|
330 340
....*....|....*....|....*..
gi 1378071945 281 FMSGLLRGYLNDEGWEQSCRYANACGA 307
Cdd:PLN02341 359 FAAAIALGYIHNLPLVNTLTLANAVGA 385
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
54-324 |
8.39e-11 |
|
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: 63.36 E-value: 8.39e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 54 SSMLARVGDE---------HMGRFLREELRQAGCDTRHLIIDKE-RLTalVLLGIKDQDTFPLifyrdNCADMAISADDV 123
Cdd:TIGR03168 42 ARVLARLGAEvvatgflggFTGEFIEALLAEEGIKNDFVEVKGEtRIN--VKIKESSGEETEL-----NEPGPEISEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 124 DE------AYIASSRCLAITGthlSHPQTRE----AVLTALgyARRHGVRTVLD---------IDYRPVLwgltslgdge 184
Cdd:TIGR03168 115 EQlleklrELLASGDIVVISG---SLPPGVPpdfyAQLIAI--ARKKGAKVILDtsgealreaLAAKPFL---------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 185 trfIAADRvsRELQEvlhLFDVIVGTEEEFhiaggsidtLQALTQVRRVSPATLVCKRGARGcSVYTDAipprlDDGLTV 264
Cdd:TIGR03168 180 ---IKPNH--EELEE---LFGRELKTLEEI---------IEAARELLDRGAENVLVSLGADG-ALLVTK-----EGALKA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 265 TGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPSKIE 324
Cdd:TIGR03168 237 TPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDVE 296
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
37-311 |
4.24e-10 |
|
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: 61.18 E-value: 4.24e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 37 GGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERlTALVLLgikdqdtfplIFYRDN---- 112
Cdd:cd01941 35 GGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRS-TASYTA----------ILDKDGdlvv 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 113 -CADMAISaDDVDEAYIASSR-------CLAITGtHLShpqtREAVLTALGYARRHGVRTVLDidyrPVlwgltslgdge 184
Cdd:cd01941 104 aLADMDIY-ELLTPDFLRKIRealkeakPIVVDA-NLP----EEALEYLLALAAKHGVPVAFE----PT----------- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 185 trfiAADRVSReLQEVLHLFDVIVGTEEEF-----HIAGGSIDTLQALTQVRRVSPATLVCKRGARG-------CSVYTD 252
Cdd:cd01941 163 ----SAPKLKK-LFYLLHAIDLLTPNRAELealagALIENNEDENKAAKILLLPGIKNVIVTLGAKGvllssreGGVETK 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1378071945 253 AIPPRLDDgltvtgvrvAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVS 311
Cdd:cd01941 238 LFPAPQPE---------TVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
54-314 |
2.80e-09 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 58.70 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 54 SSMLARVGDE---------HMGRFLREELRQAGCDTRHLIIDKERLTALVLLGIKDQDTfplifyRDNCADMAISADDVD 124
Cdd:cd01164 43 ARVLKDLGVEvtalgflggFTGDFFEALLKEEGIPDDFVEVAGETRINVKIKEEDGTET------EINEPGPEISEEELE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 125 ------EAYIASSRCLAITGthlSHPQ--TREAVLTALGYARRHGVRTVLDIDYRPVLWGLTSLGDgetrFIAADRvsRE 196
Cdd:cd01164 117 alleklKALLKKGDIVVLSG---SLPPgvPADFYAELVRLAREKGARVILDTSGEALLAALAAKPF----LIKPNR--EE 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 197 LQEvlhLFDVIVGTEEefhiaggsiDTLQALTQVRRVSPATLVCKRGARGcSVYTDAipprlDDGLTVTGVRVAILNVLG 276
Cdd:cd01164 188 LEE---LFGRPLGDEE---------DVIAAARKLIERGAENVLVSLGADG-ALLVTK-----DGVYRASPPKVKVVSTVG 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 1378071945 277 AGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHG 314
Cdd:cd01164 250 AGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
34-325 |
2.93e-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: 58.73 E-value: 2.93e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 34 KYLGGSsGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTrHLIIDKERLTALVLLGIKDQDTFPLIFYRDnc 113
Cdd:cd01172 37 IRLGGA-ANVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDT-DGIVDEGRPTTTKTRVIARNQQLLRVDRED-- 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 114 aDMAISADDVDE--AYIAS--SRCLAITGTHLSH----PQTREAVLTAlgyARRHGVRTVLDidyrpvlwgltSLGDGET 185
Cdd:cd01172 113 -DSPLSAEEEQRliERIAErlPEADVVILSDYGKgvltPRVIEALIAA---ARELGIPVLVD-----------PKGRDYS 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 186 RFIAADRVSRELQEVLHLFDVIVGTEEEFHIAGgsiDTLQALTQVRrvspaTLVCKRGARGCSVYTD-----AIPprldd 260
Cdd:cd01172 178 KYRGATLLTPNEKEAREALGDEINDDDELEAAG---EKLLELLNLE-----ALLVTLGEEGMTLFERdgevqHIP----- 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1378071945 261 glTVTgvrVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPSKIEL 325
Cdd:cd01172 245 --ALA---KEVYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVGTAPVTPKELLL 304
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
21-325 |
3.74e-09 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 58.60 E-value: 3.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 21 QIGARLEDASgFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLT--ALVLLGI 98
Cdd:PTZ00292 37 QVGETLHGTS-FHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSRTENSSTglAMIFVDT 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 99 KDQDTFPLIfyrdnC--ADMAISADDVDEAYIASSRCLAITGTHLSHPQtrEAVLTALGYARRHGVRTVLDIDYRPVLwg 176
Cdd:PTZ00292 116 KTGNNEIVI-----IpgANNALTPQMVDAQTDNIQNICKYLICQNEIPL--ETTLDALKEAKERGCYTVFNPAPAPKL-- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 177 ltslgdgetrfiAADRVSRELQEVLHLFdvIVGTEEEFHIAGGSIDT----LQALTQVRRVSPATLVCKRGARGCSVYTD 252
Cdd:PTZ00292 187 ------------AEVEIIKPFLKYVSLF--CVNEVEAALITGMEVTDtesaFKASKELQQLGVENVIITLGANGCLIVEK 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378071945 253 AIPPRlddglTVTGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAMPSKIEL 325
Cdd:PTZ00292 253 ENEPV-----HVPGKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYPHPSEL 320
|
|
| PLN02967 |
PLN02967 |
kinase |
4-308 |
6.68e-09 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 58.90 E-value: 6.68e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 4 QFDVICMGRVAVDLYSQQIGARLEDA----SGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCD 79
Cdd:PLN02967 206 QHAFVPSGRPANRLLDYEIHERMKDAfwapEKFVRAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQ 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 80 TRHLIIDKERLTALVLLGIKDQDTFPLIFYRDnCADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARR 159
Cdd:PLN02967 286 TRSVCIDGKRATAVSTMKIAKRGRLKTTCVKP-CAEDSLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKK 364
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 160 HGVRTVLDIDYRPVLWGLTSlgdgETRFIaadrvsreLQEVLHLFDVIVGTEEEFHIAGG-----SIDTL-QALTQVRRV 233
Cdd:PLN02967 365 LGGVIFYDLNLPLPLWSSSE----ETKSF--------IQEAWNLADIIEVTKQELEFLCGiepteEFDTKdNDKSKFVHY 432
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 234 SPAT-----------LVCKRGARGCSVYTdaippRLDDGlTVTGVRVAIL-----NVLGAGDAFMSGLLR------GYLN 291
Cdd:PLN02967 433 SPEVvaplwhenlkvLFVTNGTSKIHYYT-----KEHNG-AVHGMEDAPItpftsDMSASGDGIVAGLMRmltvqpHLIT 506
|
330
....*....|....*...
gi 1378071945 292 DEGW-EQSCRYANACGAL 308
Cdd:PLN02967 507 DKGYlEKTIKYAIDCGVI 524
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
7-314 |
8.86e-09 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 56.67 E-value: 8.86e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 7 VICMGRVAVDLYsQQIGArledasgfaKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIID 86
Cdd:PRK09813 3 LATIGDNCVDIY-PQLGK---------AFSGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 87 KERlTALVLLGIKDQDTFPLIFYRDNCADMAISADDVDeaYIASSRCL--AITG-THLSHPQTREA-VLTALGYARRHG- 161
Cdd:PRK09813 73 HGV-TAQTQVELHDNDRVFGDYTEGVMADFALSEEDYA--WLAQYDIVhaAIWGhAEDAFPQLHAAgKLTAFDFSDKWDs 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 162 ---VRTVLDIDYrpvlwgLTSLGDGETRFIaADRVSRELQEVLHLFDVIVGTEeefhiagGSIdtlqaltqvrrvspatl 238
Cdd:PRK09813 150 plwQTLVPHLDY------AFASAPQEDEFL-RLKMKAIVARGAGVVIVTLGEN-------GSI----------------- 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1378071945 239 vCKRGARgcsVYTDAIPPrlddgltvtgvrVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHG 314
Cdd:PRK09813 199 -AWDGAQ---FWRQAPEP------------VTVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHG 258
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
124-290 |
1.29e-08 |
|
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: 55.18 E-value: 1.29e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 124 DEAYIASSRCLAITGTHLShpqtREAVLTALGYARRHGVRTVLDIDYRpvlwgltslgdgetrfiAADRVSRELQEVLHL 203
Cdd:cd00287 51 VSVTLVGADAVVISGLSPA----PEAVLDALEEARRRGVPVVLDPGPR-----------------AVRLDGEELEKLLPG 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 204 FDVIVGTEEEF-HIAGGSIDTLQALTQVRRVS----PATLVCKRGARGCSVYTDaipprlDDGLTVTG-VRVAILNVLGA 277
Cdd:cd00287 110 VDILTPNEEEAeALTGRRDLEVKEAAEAAALLlskgPKVVIVTLGEKGAIVATR------GGTEVHVPaFPVKVVDTTGA 183
|
170
....*....|...
gi 1378071945 278 GDAFMSGLLRGYL 290
Cdd:cd00287 184 GDAFLAALAAGLA 196
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
35-325 |
2.57e-08 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 55.97 E-value: 2.57e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 35 YLGGSsGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLTAL---------VLLGIKDQDTFP 105
Cdd:COG2870 54 RPGGA-ANVAANLAALGAQVTLVGVVGDDEAGRELRRLLEEAGIDTDGLVVDPRRPTTTktrviaggqQLLRLDFEDRFP 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 106 lifyrdncadmaISADDVD------EAYIASSRCLAIT----GThLSHPQTREAVLTalgyARRHGVRTVLD---IDYrp 172
Cdd:COG2870 133 ------------LSAELEArllaalEAALPEVDAVILSdygkGV-LTPELIQALIAL----ARAAGKPVLVDpkgRDF-- 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 173 vlwgltslgdgeTRFIAADRVS---RELQEVLHLFDVivgTEEEFHIAGGsidTLQALTQVRRVspatLVCkRGARGCSV 249
Cdd:COG2870 194 ------------SRYRGATLLTpnlKEAEAAVGIPIA---DEEELVAAAA---ELLERLGLEAL----LVT-RGEEGMTL 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1378071945 250 YTDAIPPrLDDGLTVTGVrvaiLNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGCSPAmpSKIEL 325
Cdd:COG2870 251 FDADGPP-HHLPAQAREV----FDVTGAGDTVIATLALALAAGASLEEAAELANLAAGIVVGKLGTATV--SPEEL 319
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
33-314 |
3.89e-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: 55.12 E-value: 3.89e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 33 AKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDtrHLIIDKER-----LTALVLLGIKDqdTFpLI 107
Cdd:cd01944 31 KSYVIGGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIE--ILLPPRGGddggcLVALVEPDGER--SF-IS 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 108 FYRdncADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARRHGVRTVLDIDYRpvlwgLTSLGDGETRF 187
Cdd:cd01944 106 ISG---AEQDWSTEWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPGPR-----ISDIPDTILQA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 188 IAADRVsrelqevlhlfdVIVGTEEEFHIAGGSIDTLQALTQVRRVSP--ATLVCKRGARGCSVYTDAIPPRlddglTVT 265
Cdd:cd01944 178 LMAKRP------------IWSCNREEAAIFAERGDPAAEASALRIYAKtaAPVVVRLGSNGAWIRLPDGNTH-----IIP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1378071945 266 GVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHG 314
Cdd:cd01944 241 GFKVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
54-331 |
5.31e-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: 54.90 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 54 SSMLARVGDE---------HMGRFLREELRQAGCDTRHLIIDKE-RLTalVLLGIKDQDTFPLifyrdNCADMAISADDV 123
Cdd:TIGR03828 42 SRVLKNLGVDvvalgflggFTGDFIEALLREEGIKTDFVRVPGEtRIN--VKIKEPSGTETKL-----NGPGPEISEEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 124 DE------AYIASSRCLAITGthlSHPQTRE----AVLTALgyARRHGVRTVLD---------IDYRPVLwgltslgdge 184
Cdd:TIGR03828 115 EAlleklrAQLAEGDWLVLSG---SLPPGVPpdfyAELIAL--AREKGAKVILDtsgealrdgLKAKPFL---------- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 185 trfIAADRvsRELQEvlhLFDVIVGTEEEFHIAGgsiDTLQALtQVRRVspatlVCKRGARGcSVYTDAipprlDDGLTV 264
Cdd:TIGR03828 180 ---IKPND--EELEE---LFGRELKTLEEIIEAA---RELLDL-GAENV-----LISLGADG-ALLVTK-----EGALFA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1378071945 265 TGVRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGcsPAMPSKIELDDYLSR 331
Cdd:TIGR03828 237 QPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEG--TGLPDPEDIEELLPQ 301
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
29-314 |
1.23e-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: 53.58 E-value: 1.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 29 ASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGcDTRHLII-DKERLTALVLLGIKDQDTFPLI 107
Cdd:cd01947 28 SSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGG-DKHTVAWrDKPTRKTLSFIDPNGERTITVP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 108 FYRDNcADMAISA-DDVDEAYIASSRCLAitgTHLSHPQTREAVLTALGyarrhgvrtvldidyrpvlwgltslgdGETR 186
Cdd:cd01947 107 GERLE-DDLKWPIlDEGDGVFITAAAVDK---EAIRKCRETKLVILQVT---------------------------PRVR 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 187 FIaadrvsrELQEVLHLFDVIVGTEEEFhiAGGSIDTLQALTQVRrvspaTLVCKRGARGCSVYT----DAIPPRlddgl 262
Cdd:cd01947 156 VD-------ELNQALIPLDILIGSRLDP--GELVVAEKIAGPFPR-----YLIVTEGELGAILYPggryNHVPAK----- 216
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1378071945 263 tvtgvRVAILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHG 314
Cdd:cd01947 217 -----KAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFG 263
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
60-323 |
4.54e-07 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 52.34 E-value: 4.54e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 60 VGDEHMGRFLREELRQAGCDTrHLIIDKERLTAL--VLLGIKDQDTFPLIFYRDNCADMAISADDVDEAyIASSRCLAIT 137
Cdd:PTZ00247 89 VGDDRFAEILKEAAEKDGVEM-LFEYTTKAPTGTcaVLVCGKERSLVANLGAANHLSAEHMQSHAVQEA-IKTAQLYYLE 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 138 GTHLShpqTR-EAVLTALGYARRHGVRTVLdidyrpvlwGLTSLgdgetrFIAADRVSReLQEVLHLFDVIVGTEEEFHI 216
Cdd:PTZ00247 167 GFFLT---VSpNNVLQVAKHARESGKLFCL---------NLSAP------FISQFFFER-LLQVLPYVDILFGNEEEAKT 227
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 217 AGGSID-TLQALTQV-RRVspATLVCKRGARG-CSVYTDAIPPRL---DDGLTVTGVR-VA---ILNVLGAGDAFMSGLL 286
Cdd:PTZ00247 228 FAKAMKwDTEDLKEIaARI--AMLPKYSGTRPrLVVFTQGPEPTLiatKDGVTSVPVPpLDqekIVDTNGAGDAFVGGFL 305
|
250 260 270
....*....|....*....|....*....|....*...
gi 1378071945 287 RGYLNDEGWEQSCRYANACGALVVSRHGCS-PAMPSKI 323
Cdd:PTZ00247 306 AQYANGKDIDRCVEAGHYSAQVIIQHNGCTyPEKPPFL 343
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
16-175 |
1.61e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 44.51 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 16 DLYSQQigARLE-DASGFAKYLGGSSGNVAYGTARQGLRSSMLARVGDEHMGRFLREELRQAGCDTRHLIIDKERLTALV 94
Cdd:PLN02543 152 DMYSQW--KMLQwDPPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACS 229
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 95 LLGIKDQDTFPLIFYR-DNCADMAISADDVDEAYIASSRCLAITGTHLSHPQTREAVLTALGYARRHGVRTVLDIDYRPV 173
Cdd:PLN02543 230 RMKIKFRDGGKMVAETvKEAAEDSLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLP 309
|
..
gi 1378071945 174 LW 175
Cdd:PLN02543 310 LW 311
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
196-314 |
4.70e-04 |
|
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238921 [Multi-domain] Cd Length: 277 Bit Score: 42.45 E-value: 4.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1378071945 196 ELQEVLHLFDVIVGTEEEFHIAGGSIDTLQALTQVRRVSPATLVCKRGARGCSVYTD----AIPPR-LDDgltvtgvrva 270
Cdd:cd01946 156 KLKKVLAKVDVVIINDGEARQLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTDdgyfAAPAYpLES---------- 225
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1378071945 271 ILNVLGAGDAFMSGLLrGYL------NDEGWEQSCRYANACGALVVSRHG 314
Cdd:cd01946 226 VFDPTGAGDTFAGGFI-GYLasqkdtSEANMRRAIIYGSAMASFCVEDFG 274
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
271-333 |
2.48e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 40.40 E-value: 2.48e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1378071945 271 ILNVLGAGDAFMSGLLRGYLNDEGWEQSCRYANACGALVVSRHGcspaMPskiELDDYLSRER 333
Cdd:cd01943 260 VVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG----LP---RLTKVEGEEL 315
|
|
| |
