|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-301 |
8.11e-102 |
|
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: 300.26 E-value: 8.11e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 4 KIAVIGECMIELSEKNG-------AVNRGFGGDTLNTSVYIARQtdasALSVHYVTALGTDAFSQQMLDSWQQENVNTDL 76
Cdd:cd01166 1 DVVTIGEVMVDLSPPGGgrleqadSFRKFFGGAEANVAVGLARL----GHRVALVTAVGDDPFGRFILAELRREGVDTSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 77 IQRMADRLPGLYYIETDDTGERTFYYWRNEAAAKFWLESDRAAAIceeLATFDYLYLSGISLAIlSPASRDKLFTLLREC 156
Cdd:cd01166 77 VRVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEAA---LAGADHLHLSGITLAL-SESAREALLEALEAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 157 RANGGKVIFDNNYRPRLWaSQAETQQVYQEMLACTDIAFLTLDDEDALWGEKPVAEVIART--HAAGVEEVVVKRGADAC 234
Cdd:cd01166 153 KARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERAlaLALGVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1739856190 235 LVSVSGQpLREVPAVrlaKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAI 301
Cdd:cd01166 232 LVYTGGG-RVFVPAY---PVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-308 |
2.58e-73 |
|
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: 227.85 E-value: 2.58e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 4 KIAVIGECMIEL------------SEKNGAVNRGFGGDTLNTSVYIARQTdasaLSVHYVTALGTDAFSQQMLDSWQQEN 71
Cdd:COG0524 1 DVLVIGEALVDLvarvdrlpkggeTVLAGSFRRSPGGAAANVAVALARLG----ARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 72 VNTDLIQRMADRLPGLYYIETDDTGERTFYYWRNeAAAKFWLESDRAAAIceelATFDYLYLSGISLAilSPASRDKLFT 151
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRG-ANAELTPEDLDEALL----AGADILHLGGITLA--SEPPREALLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 152 LLRECRANGGKVIFDNNYRPRLWasqAETQQVYQEMLACTDIAFLTLDDEDALWGEKPVAEVIARTHAAGVEEVVVKRGA 231
Cdd:COG0524 150 ALEAARAAGVPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1739856190 232 DACLVSVSGQpLREVPAVRLakeKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAiipREAMP 308
Cdd:COG0524 227 EGALLYTGGE-VVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGA---QPALP 296
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-302 |
4.33e-73 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 226.84 E-value: 4.33e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 4 KIAVIGECMIELSE----------KNGAVNRGFGGDTLNTSVYIARQtdasALSVHYVTALGTDAFSQQMLDSWQQENVN 73
Cdd:pfam00294 1 KVVVIGEANIDLIGnveglpgelvRVSTVEKGPGGKGANVAVALARL----GGDVAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 74 TDLIQRMADRLPGLYYIETDDTGERTFYYWRNEAAAKFWLESDRAAAICEElatFDYLYLSGislaILSPASRDKLFTLL 153
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLEN---ADLLYISG----SLPLGLPEATLEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 154 RECRANGGKviFDNNYRPRLWAsqaeTQQVYQEMLACTDIAFLTLDDEDALWGEK--PVAEVIARTH---AAGVEEVVVK 228
Cdd:pfam00294 150 IEAAKNGGT--FDPNLLDPLGA----AREALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHkllAKGIKTVIVT 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1739856190 229 RGADACLVSVSGQplrEVPAVRLAKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAII 302
Cdd:pfam00294 224 LGADGALVVEGDG---EVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
4-301 |
7.00e-43 |
|
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: 148.94 E-value: 7.00e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 4 KIAVIGECMIELSEKNGAVNRGF----GGDTLNTSVYIARQTDASALsvhyVTALGTDAFSQQMLDSWQQENVNTDLIQR 79
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFtkapGGAPANVAVALARLGGKAAF----IGKVGDDEFGDFLLETLKEAGVDTRGIQF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 80 MADRLPGLYYIETDDTGERTFYYWRNEAAAKFWLESDRAAAiceeLATFDYLYLSGISLAilSPASRDKLFTLLRECRAN 159
Cdd:cd01167 77 DPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDL----LSEADILHFGSIALA--SEPSRSALLELLEAAKKA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 160 GGKVIFDNNYRPRLWASQAETQQVYQEMLACTDIafLTLDDEDALW--GEKPVAEVIARTHAAGVEEVVVKRGADACLVS 237
Cdd:cd01167 151 GVLISFDPNLRPPLWRDEEEARERIAELLELADI--VKLSDEELELlfGEEDPEEIAALLLLFGLKLVLVTRGADGALLY 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1739856190 238 VSGQPLrEVPAVRLakeKVVDTTAAGDSFSAGYLAVRLTGGD-------AESAARRGHLTASTVIQYRGAI 301
Cdd:cd01167 229 TKGGVG-EVPGIPV---EVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-301 |
2.26e-31 |
|
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: 118.57 E-value: 2.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 24 RGFGGDTLNTSVYIARQtdasALSVHYVTALGTDAFSQQMLDSWQQENVNTDLIQRMADRLPGLYYIETDDTGERTFYYW 103
Cdd:cd01942 33 REFGGSAGNTAVALAKL----GLSPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAYFY 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 104 RneAAAKFWLESDRAAAIceelatfdylylsgISLAILSPASRDKLFTLLRECRANGGKVIFDNNYR-PRLWASQAEtqq 182
Cdd:cd01942 109 P--GAMDELEPNDEADPD--------------GLADIVHLSSGPGLIELARELAAGGITVSFDPGQElPRLSGEELE--- 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 183 vyqEMLACTDIAF-----LTLDDEDALWGEKPVAEviarthaaGVEEVVVKRGADACLVsVSGQPLREVPAVrlAKEKVV 257
Cdd:cd01942 170 ---EILERADILFvndyeAELLKERTGLSEAELAS--------GVRVVVVTLGPKGAIV-FEDGEEVEVPAV--PAVKVV 235
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1739856190 258 DTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAI 301
Cdd:cd01942 236 DTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-272 |
2.45e-28 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 110.80 E-value: 2.45e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 1 MSKKIAVIGECMIEL-SEKNGAVNRGFGGDTLNTSVYIARQTDASAlsvhYVTALGTDAFSQQMLDSWQQENVNT----- 74
Cdd:PRK09434 1 MMNKVWVLGDAVVDLiPEGENRYLKCPGGAPANVAVGIARLGGESG----FIGRVGDDPFGRFMQQTLQDEGVDTtylrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 75 DLIQRMADRLPGLyyietDDTGERTFYYWRNEAAAKFwLESDraaaiceELATF---DYLYLSGISLAilSPASRDKLFT 151
Cdd:PRK09434 77 DPAHRTSTVVVDL-----DDQGERSFTFMVRPSADLF-LQPQ-------DLPPFrqgEWLHLCSIALS--AEPSRSTTFE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 152 LLRECRANGGKVIFDNNYRPRLWASQAETQQVYQEMLACTDIAFLTLDDEDALWGEKPVAEVIAR-THAAGVEEVVVKRG 230
Cdd:PRK09434 142 AMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLLVTLG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1739856190 231 ADACLVSVSGQpLREVPAVRLakeKVVDTTAAGDSFSAGYLA 272
Cdd:PRK09434 222 AEGVLVHTRGQ-VQHFPAPSV---DPVDTTGAGDAFVAGLLA 259
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
4-308 |
2.60e-27 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 107.64 E-value: 2.60e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 4 KIAVIGECMIELS------EKNG------AVNRGFGGDTLNTSVYIARqtdASAlSVHYVTALGTDAFSQQMLDSWQQEN 71
Cdd:cd01174 1 KVVVVGSINVDLVtrvdrlPKPGetvlgsSFETGPGGKGANQAVAAAR---LGA-RVAMIGAVGDDAFGDELLENLREEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 72 VNTDLIQRMADRLPGLYYIETDDTGErtfyywrN------EAAAKF-WLESDRAAAIceeLATFDYLYLSG-ISLAILSP 143
Cdd:cd01174 77 IDVSYVEVVVGAPTGTAVITVDESGE-------NrivvvpGANGELtPADVDAALEL---IAAADVLLLQLeIPLETVLA 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 144 AsrdklftlLRECRANGGKVIFDnnyrprlwASQAetQQVYQEMLACTDI--------AFLTLDDEDALWGEKPVAEVIa 215
Cdd:cd01174 147 A--------LRAARRAGVTVILN--------PAPA--RPLPAELLALVDIlvpneteaALLTGIEVTDEEDAEKAARLL- 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 216 rtHAAGVEEVVVKRGADACLVSVSGQPLrEVPAvrlAKEKVVDTTAAGDSFsAGYLAVRLT-GGDAESAARRGHLTASTV 294
Cdd:cd01174 208 --LAKGVKNVIVTLGAKGALLASGGEVE-HVPA---FKVKAVDTTGAGDTF-IGALAAALArGLSLEEAIRFANAAAALS 280
|
330
....*....|....
gi 1739856190 295 IQYRGAIiprEAMP 308
Cdd:cd01174 281 VTRPGAQ---PSIP 291
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
27-300 |
4.67e-21 |
|
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: 90.11 E-value: 4.67e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 27 GGDTLNTSVYIARQTDASAlsvhYVTALGTDAFSQQMLDSWQQENVNTDLIqRMADRLPGLYYIETDDtGERTFYYWRNE 106
Cdd:cd01940 22 GGNALNVAVYAKRLGHESA----YIGAVGNDDAGAHVRSTLKRLGVDISHC-RVKEGENAVADVELVD-GDRIFGLSNKG 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 107 AAAKFWLESDRAAAiceeLATFDYLYLSGISLAILSPAsrdklftLLRECRANGGKVIFDNNYRprlWasqaetqQVYQE 186
Cdd:cd01940 96 GVAREHPFEADLEY----LSQFDLVHTGIYSHEGHLEK-------ALQALVGAGALISFDFSDR---W-------DDDYL 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 187 MLAC--TDIAFLTLDDEDalwgEKPVAEVIARTHAAGVEEVVVKRGADACLVSvSGQPLREVPAVRlakEKVVDTTAAGD 264
Cdd:cd01940 155 QLVCpyVDFAFFSASDLS----DEEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DGAVFYSVAPRP---VEVVDTLGAGD 226
|
250 260 270
....*....|....*....|....*....|....*..
gi 1739856190 265 SFSAGYLAVRLTGGDA-ESAARRGHLTASTVIQYRGA 300
Cdd:cd01940 227 SFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTCGHEGA 263
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
25-300 |
1.91e-20 |
|
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose catabolism. The rbsK gene encoding ribokinase typically is found with ribose transport genes. Ribokinase belongs to the carbohydrate kinase pfkB family (pfam00294). In the wide gulf between the current trusted (360 bit) and noise (100 bit) cutoffs are a number of sequences, few of which are clustered with predicted ribose transport genes but many of which are currently annotated as if having ribokinase activity. Most likely some have this function and others do not. [Energy metabolism, Sugars]
Pssm-ID: 274000 [Multi-domain] Cd Length: 293 Bit Score: 89.20 E-value: 1.91e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 25 GFGGDTLNTSVYIARqtdaSALSVHYVTALGTDAFSQQMLDSWQQENVNTDLIQRMADRLPGLYYIETDDTGERTFYYwr 104
Cdd:TIGR02152 29 GPGGKGANQAVAAAR----LGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVV-- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 105 NEAAAKFWLESDRAAAIcEELATFDYLYLSG-ISLAILSPAsrdklftlLRECRANGGKVIFdnNYRPrlwasqaETQQV 183
Cdd:TIGR02152 103 VAGANAELTPEDIDAAE-ALIAESDIVLLQLeIPLETVLEA--------AKIAKKHGVKVIL--NPAP-------AIKDL 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 184 YQEMLACTDI--------AFLT---LDDEDAlwgekpvAEVIART-HAAGVEEVVVKRGADACLVSVSGQPlREVPAvrl 251
Cdd:TIGR02152 165 DDELLSLVDIitpneteaEILTgieVTDEED-------AEKAAEKlLEKGVKNVIITLGSKGALLVSKDES-KLIPA--- 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1739856190 252 AKEKVVDTTAAGDSFSAGyLAVRLT-GGDAESAARRGHLTASTVIQYRGA 300
Cdd:TIGR02152 234 FKVKAVDTTAAGDTFNGA-FAVALAeGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
17-303 |
4.97e-20 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 88.93 E-value: 4.97e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 17 EKNGAVNRGFGGDTLNTSVYIARQTDASALSVHYVTALGTDAFSQQMLDSWQQENVNTdliqrmadrlpgLYYIETDD-T 95
Cdd:PTZ00247 52 ESIPNVSYVPGGSALNTARVAQWMLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEM------------LFEYTTKApT 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 96 GERTFYYWRNE--------AAAKFWLESDRAAAICEELATFDYLYLSGISLAIlSPASRDKLFtllRECRANGGKVIFdN 167
Cdd:PTZ00247 120 GTCAVLVCGKErslvanlgAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFLTV-SPNNVLQVA---KHARESGKLFCL-N 194
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 168 NYRPrlWASQAETQQVYQeMLACTDIAFLtlDDEDAL-------WGEKPVAEVIARthAAGVEEVVVKR--------GAD 232
Cdd:PTZ00247 195 LSAP--FISQFFFERLLQ-VLPYVDILFG--NEEEAKtfakamkWDTEDLKEIAAR--IAMLPKYSGTRprlvvftqGPE 267
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1739856190 233 ACLVSVSGQpLREVPAVRLAKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAIIP 303
Cdd:PTZ00247 268 PTLIATKDG-VTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
27-303 |
1.69e-16 |
|
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: 78.42 E-value: 1.69e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 27 GGDTLNTSVYIArqtdASALSVHYVTALGTDAFSQQMLDSWQQENVNTDLiQRMADRLPGLYYIETDDTGERTFYywRNE 106
Cdd:cd01168 55 GGSAANTIRGAA----ALGGSAAFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAERTMC--TYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 107 AAAKFWLESDRAAAIceeLATFDYLYLSGISLAILSPAsrdkLFTLLRECRANGGKVIFD-------NNYRPRLWasqae 179
Cdd:cd01168 128 GAANELSPDDLDWSL---LAKAKYLYLEGYLLTVPPEA----ILLAAEHAKENGVKIALNlsapfivQRFKEALL----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 180 tqqvyqEMLACTDIAFLTLDDEDALWGEKP--VAEVIARTHAAGVEEVVVKRGADACLVSVSGQplrEVPAVRLAKEKVV 257
Cdd:cd01168 196 ------ELLPYVDILFGNEEEAEALAEAETtdDLEAALKLLALRCRIVVITQGAKGAVVVEGGE---VYPVPAIPVEKIV 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1739856190 258 DTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAIIP 303
Cdd:cd01168 267 DTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
125-272 |
1.07e-14 |
|
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: 71.36 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 125 LATFDYLYLSGISLAilspasRDKLFTLLRECRANGGKVIFDNNYRPRLWASQAetqqvYQEMLACTDIAFLTLDDEDAL 204
Cdd:cd00287 55 LVGADAVVISGLSPA------PEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVDILTPNEEEAEAL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1739856190 205 -----WGEKPVAEVIARTHAAGVEEVVVKRGADACLVSVSGQPLREVPAVrlaKEKVVDTTAAGDSFSAGYLA 272
Cdd:cd00287 124 tgrrdLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAF---PVKVVDTTGAGDAFLAALAA 193
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
27-303 |
6.71e-14 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 70.90 E-value: 6.71e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 27 GGDTLNtSVYIARQTDASALSVHYVTALGTDAFSQQMLDSWQQENVNtdlIQRMADrlpglyyiETDDTG---------E 97
Cdd:PLN02548 52 GGATQN-SIRVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVN---VHYYED--------ESTPTGtcavlvvggE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 98 RTFYywRNEAAAKFW----LESDRAAAICEELatfDYLYLSGISLAIlSPASrdkLFTLLRECRANGgKVIFDNNYRP-- 171
Cdd:PLN02548 120 RSLV--ANLSAANCYkvehLKKPENWALVEKA---KFYYIAGFFLTV-SPES---IMLVAEHAAANN-KTFMMNLSAPfi 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 172 -RLWASQAETQQVYQEMLACTDIAFLTLDDEDAlWGEKPVAEV---IART-HAAGVEE--VVVKRGADACLVSVSGQpLR 244
Cdd:PLN02548 190 cEFFKDQLMEALPYVDFLFGNETEARTFAKVQG-WETEDVEEIalkISALpKASGTHKrtVVITQGADPTVVAEDGK-VK 267
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1739856190 245 EVPAVRLAKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAIIP 303
Cdd:PLN02548 268 EFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYP 326
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
9.70e-14 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 9.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 1 MSKKIAVIGECMIELSeknGAVNR---------------GFGGDTLNTSVYIARQtdasALSVHYVTALGTDAFSQQMLD 65
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLI---GYVDRmpqvgetlhgtsfhkGFGGKGANQAVMASKL----GAKVAMVGMVGTDGFGSDTIK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 66 SWQQENVNTDLIQRMADRLPGLYYIETDDT---GERTFYYWRNEAAAKFWLesDRAAAICEELAtfDYLYLSG-ISLAIl 141
Cdd:PTZ00292 87 NFKRNGVNTSFVSRTENSSTGLAMIFVDTKtgnNEIVIIPGANNALTPQMV--DAQTDNIQNIC--KYLICQNeIPLET- 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 142 spasrdklfTL--LRECRANGGKVIFdnNYRPrlwASQAETQQVYQEMLACTDIaFLTLDDEDALWGEKPVA--EVIART 217
Cdd:PTZ00292 162 ---------TLdaLKEAKERGCYTVF--NPAP---APKLAEVEIIKPFLKYVSL-FCVNEVEAALITGMEVTdtESAFKA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 218 HAA----GVEEVVVKRGADACLVSVSGQPLREVPAVRLakeKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTAST 293
Cdd:PTZ00292 227 SKElqqlGVENVIITLGANGCLIVEKENEPVHVPGKRV---KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAI 303
|
....*..
gi 1739856190 294 VIQYRGA 300
Cdd:PTZ00292 304 SVTRHGT 310
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
26-300 |
1.17e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 67.20 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 26 FGGDTLNTSVYIARqtdaSALSVHYVTALGTDAFSQQMLDSWQQENVNTDLIQRMADRLPGLYYIETDDTGErtfyywrN 105
Cdd:PRK11142 38 FGGKGANQAVAAAR----LGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGE-------N 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 106 ----EAAAKFWLESDRAAAICEELATFDYLY------LSGISLAilspasrdklftlLRECRANGGKVIFDnnyrPrlwa 175
Cdd:PRK11142 107 sigiHAGANAALTPALVEAHRELIANADALLmqletpLETVLAA-------------AKIAKQHGTKVILN----P---- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 176 sqAETQQVYQEMLACTDI--------AFLT----LDDEDAlwgekpvAEVIARTHAAGVEEVVVKRGADACLVSVSGQPl 243
Cdd:PRK11142 166 --APARELPDELLALVDIitpneteaEKLTgirvEDDDDA-------AKAAQVLHQKGIETVLITLGSRGVWLSENGEG- 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1739856190 244 REVPAVRLakeKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGA 300
Cdd:PRK11142 236 QRVPGFRV---QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-300 |
1.72e-12 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 66.30 E-value: 1.72e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 3 KKIAVIGECMIELSEKNGavnRGF-GGDTLNTSVYIARQtdasALSVHYVTALGTDAFSQQMLDSWQQENVNTDLIqRMA 81
Cdd:PRK09813 1 KKLATIGDNCVDIYPQLG---KAFsGGNAVNVAVYCTRY----GIQPGCITWVGDDDYGTKLKQDLARMGVDISHV-HTK 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 82 DRLPGLYYIETDDtGERTFYYWRNEAAAKFWLESDRAAAICEelatFDYlylsgISLAILSPASRDklftlLRECRANGG 161
Cdd:PRK09813 73 HGVTAQTQVELHD-NDRVFGDYTEGVMADFALSEEDYAWLAQ----YDI-----VHAAIWGHAEDA-----FPQLHAAGK 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 162 KVIFDNNYRPR--LWasqaetqqvyQEMLACTDIAFLTLDDEDAlWGEKPVAEVIARthAAGVeeVVVKRGADACLvSVS 239
Cdd:PRK09813 138 LTAFDFSDKWDspLW----------QTLVPHLDYAFASAPQEDE-FLRLKMKAIVAR--GAGV--VIVTLGENGSI-AWD 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1739856190 240 GQPLREVPAVRLakeKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGA 300
Cdd:PRK09813 202 GAQFWRQAPEPV---TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
119-287 |
6.28e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 58.99 E-value: 6.28e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 119 AAICEELATFDYLYLSGiSLAilSPASRDKLFTLLRECRANGGKVIFDnnyrprlwASQAETQQVYQ-----------EM 187
Cdd:COG1105 120 ERLEELLKEGDWVVLSG-SLP--PGVPPDFYAELIRLARARGAKVVLD--------TSGEALKAALEagpdlikpnleEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 188 LACTDIAFLTLDDedalwgekpVAEVIARTHAAGVEEVVVKRGAD-ACLVSVSGQPLREVPAVrlakeKVVDTTAAGDSF 266
Cdd:COG1105 189 EELLGRPLETLED---------IIAAARELLERGAENVVVSLGADgALLVTEDGVYRAKPPKV-----EVVSTVGAGDSM 254
|
170 180
....*....|....*....|.
gi 1739856190 267 SAGYLAVRLTGGDAESAARRG 287
Cdd:COG1105 255 VAGFLAGLARGLDLEEALRLA 275
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
27-271 |
4.87e-09 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 56.55 E-value: 4.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 27 GGDTLNTSVYIARQTDASAlsvhYVTALGTDAFSQQMLDSWQQENVNTDLIQRMADRLPGLYYIETDDTGERTFYYWRNE 106
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSA----FIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 107 AAAKFWLESDRAAAICEELATFDYlylSGISLaILSPaSRDKLFTLLRECRANGGKVIFDNNYRPRLWAS---------- 176
Cdd:PLN02323 119 SADMLLRESELDLDLIRKAKIFHY---GSISL-ITEP-CRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSaeaaregims 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 177 ---QAETQQVYQEmlactDIAFLTlddedalWGEKPVAEVIARTHAAGVEEVVVKRGADACLV---SVSGQplreVPAVr 250
Cdd:PLN02323 194 iwdEADIIKVSDE-----EVEFLT-------GGDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYytkDFKGR----VEGF- 256
|
250 260
....*....|....*....|.
gi 1739856190 251 laKEKVVDTTAAGDSFSAGYL 271
Cdd:PLN02323 257 --KVKAVDTTGAGDAFVGGLL 275
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
26-309 |
1.39e-08 |
|
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: 54.99 E-value: 1.39e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 26 FGGDTLNTSVYIARQtdasALSVHYVTALGTDAFSQQMLDSWQQENVNTDLIQRMADRLPGLYYIeTDDTGER--TFYYW 103
Cdd:cd01945 35 GGGNAANAAVAVARL----GGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSI-TDITGDRatISITA 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 104 RNEAAAKFWLESDraaaiceELATFDYLYLSGIslaiLSPASRDklftLLRECRANGGKVIFDnnyrprlwaSQAETQQV 183
Cdd:cd01945 110 IDTQAAPDSLPDA-------ILGGADAVLVDGR----QPEAALH----LAQEARARGIPIPLD---------LDGGGLRV 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 184 YQEMLACTDIAFLTlddEDAL--WGEKPVAEVIARTHAAGVEEVVVKRGADACLVSVSGQPLREVPAvrlAKEKVVDTTA 261
Cdd:cd01945 166 LEELLPLADHAICS---ENFLrpNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPA---FPVEVVDTTG 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1739856190 262 AGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAiipREAMPQ 309
Cdd:cd01945 240 AGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG---RAGLPT 284
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
192-296 |
1.61e-08 |
|
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: 54.63 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 192 DIAFLTLDDEDALWG-----EKPVAEVIARTHAAGVEEVVVKRGADACLVSVSGQPL--REVPAVrlAKEKVVDTTAAGD 264
Cdd:cd01941 178 DLLTPNRAELEALAGalienNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVetKLFPAP--QPETVVNVTGAGD 255
|
90 100 110
....*....|....*....|....*....|..
gi 1739856190 265 SFSAGYLAVRLTGGDAESAARRGHLTASTVIQ 296
Cdd:cd01941 256 AFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
225-304 |
2.98e-08 |
|
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: 54.27 E-value: 2.98e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 225 VVVKRGADACLV-SVSGQPLREVPAVRLAKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGaiIP 303
Cdd:cd01943 228 VVLRCGKLGCYVgSADSGPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG--LP 305
|
.
gi 1739856190 304 R 304
Cdd:cd01943 306 R 306
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
125-287 |
3.28e-08 |
|
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: 53.69 E-value: 3.28e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 125 LATFDYLYLSGiSLAilSPASRDKLFTLLRECRANGGKVIFDNNYRPRLWASQAetqQVY------QEMLACTDIAFLTL 198
Cdd:cd01164 126 LKKGDIVVLSG-SLP--PGVPADFYAELVRLAREKGARVILDTSGEALLAALAA---KPFlikpnrEELEELFGRPLGDE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 199 DDedalwgekpVAEVIARTHAAGVEEVVVKRGADACLVSVSGQPLRevpaVRLAKEKVVDTTAAGDSFSAGYLAVRLTGG 278
Cdd:cd01164 200 ED---------VIAAARKLIERGAENVLVSLGADGALLVTKDGVYR----ASPPKVKVVSTVGAGDSMVAGFVAGLAQGL 266
|
....*....
gi 1739856190 279 DAESAARRG 287
Cdd:cd01164 267 SLEEALRLA 275
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
27-301 |
7.46e-08 |
|
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: 52.42 E-value: 7.46e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 27 GGDTLNTSVYIARQTDasalSVHYVTALGTDAFSQQMLDSWQQENVnTDLIQrMADRLPGLYYIETDDTGERTFYYWRNE 106
Cdd:cd01947 36 GGGGANVAVQLAKLGN----DVRFFSNLGRDEIGIQSLEELESGGD-KHTVA-WRDKPTRKTLSFIDPNGERTITVPGER 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 107 aaakfwLESDRAAAIceeLATFDYLYLSGISLailspasrdkLFTLLRECRaNGGKVIFDNNYRPRLWASQAETQQVyqE 186
Cdd:cd01947 110 ------LEDDLKWPI---LDEGDGVFITAAAV----------DKEAIRKCR-ETKLVILQVTPRVRVDELNQALIPL--D 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 187 MLACTDIAFLTLDDEDALWGEKPvaeviaRThaagveeVVVKRGADACLVsVSGQPLREVPAVrlaKEKVVDTTAAGDSF 266
Cdd:cd01947 168 ILIGSRLDPGELVVAEKIAGPFP------RY-------LIVTEGELGAIL-YPGGRYNHVPAK---KAKVPDSTGAGDSF 230
|
250 260 270
....*....|....*....|....*....|....*
gi 1739856190 267 SAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAI 301
Cdd:cd01947 231 AAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
218-301 |
3.20e-06 |
|
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: 47.94 E-value: 3.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 218 HAAGVEEVVVKRGADACLVSVSGQPLREVPAvrLAKEkVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQY 297
Cdd:cd01172 215 ELLNLEALLVTLGEEGMTLFERDGEVQHIPA--LAKE-VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGK 291
|
....
gi 1739856190 298 RGAI 301
Cdd:cd01172 292 VGTA 295
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
90-299 |
1.05e-05 |
|
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: 46.26 E-value: 1.05e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 90 IETDdtGERTFYYWrneAAAKFWLESDRAAAIceELATFDYLYLSGISLAIlSPASRDKLFTLLRECRAnGGKVIFDnnY 169
Cdd:cd01944 95 VEPD--GERSFISI---SGAEQDWSTEWFATL--TVAPYDYVYLSGYTLAS-ENASKVILLEWLEALPA-GTTLVFD--P 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 170 RPRLwasqaetQQVYQEMLA--CTDIAFLTLDDEDALW----GEKPVAEVIARTHAAGVEEVVVKRGADACLVSVSGQPL 243
Cdd:cd01944 164 GPRI-------SDIPDTILQalMAKRPIWSCNREEAAIfaerGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNT 236
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 1739856190 244 REVPAVrlaKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRG 299
Cdd:cd01944 237 HIIPGF---KVKAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLANAAAAIVVTRSG 289
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
128-271 |
1.76e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 45.98 E-value: 1.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 128 FDYLYLSGISLAILSPASrdklftllrecraNGGKVIFDNNYRPR-LWASQAETQQVYQEMLACTDIAFLTLDDEDALWG 206
Cdd:PLN02341 235 FDELSPSAIASAVDYAID-------------VGTAVFFDPGPRGKsLLVGTPDERRALEHLLRMSDVLLLTSEEAEALTG 301
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1739856190 207 EKP---VAEVIARThAAGVEEVVVKRGAD-ACLVSVSGQPLREVPAVrlakeKVVDTTAAGDSFSA----GYL 271
Cdd:PLN02341 302 IRNpilAGQELLRP-GIRTKWVVVKMGSKgSILVTRSSVSCAPAFKV-----NVVDTVGCGDSFAAaialGYI 368
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
214-295 |
2.17e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 42.00 E-value: 2.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 214 IARTHAA-GVEEVVVKRGADACLVsVSGQPLREVPAvrlAKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTAS 292
Cdd:cd01937 175 LARLIKEtGVKEIIVTDGEEGGYI-FDGNGKYTIPA---SKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAA 250
|
...
gi 1739856190 293 TVI 295
Cdd:cd01937 251 KFI 253
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
27-300 |
1.58e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 39.79 E-value: 1.58e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 27 GGDTLNTSVYIAR----QTDASALSVHYVTALGTDAFSQQMLDSWQQENVNTdLIQRMADRLPGLYYIETDDTGERTFYY 102
Cdd:PLN02813 126 GGSLSNTLVALARlgsqSAAGPALNVAMAGSVGSDPLGDFYRTKLRRANVHF-LSQPVKDGTTGTVIVLTTPDAQRTMLS 204
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 103 WRNeAAAKFWLESDRAAAI--CEELATFDYLYLSGISLAILSPAsrdklftlLRECRANGGKVIfdnnyrprLWASQAET 180
Cdd:PLN02813 205 YQG-TSSTVNYDSCLASAIskSRVLVVEGYLWELPQTIEAIAQA--------CEEAHRAGALVA--------VTASDVSC 267
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 181 -----QQVYQEMLACTDIAFLTLDDEDAL--WGEKPVAEVIARTHAAGVEEVVVKRGADACLVSVSGqplrEVPAVRLAK 253
Cdd:PLN02813 268 ierhrDDFWDVMGNYADILFANSDEARALcgLGSEESPESATRYLSHFCPLVSVTDGARGSYIGVKG----EAVYIPPSP 343
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1739856190 254 EKVVDTTAAGDSFSAGYLAVRLTG-----GDAESAARrghlTASTVIQYRGA 300
Cdd:PLN02813 344 CVPVDTCGAGDAYAAGILYGLLRGvsdlrGMGELAAR----VAATVVGQQGT 391
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
226-305 |
2.72e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 39.00 E-value: 2.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1739856190 226 VVKRGADACLVSvSGQPLREVPAVrlAKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAARRGHLTASTVIQYRGAIIPRE 305
Cdd:PLN02379 270 VVTLGSKGCIAR-HGKEVVRVPAI--GETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVVRALGGEVTPE 346
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
137-193 |
4.02e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 38.74 E-value: 4.02e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1739856190 137 SLAILSPASRDKLFTLLRECRANGGKVIFDNNYRPRLWASQAETQQVYQEMLACTDI 193
Cdd:PLN02543 274 SEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRELIKKAWNEADI 330
|
|
| |
