|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-301 |
1.23e-104 |
|
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: 307.20 E-value: 1.23e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 4 KIAVIGECMIELS-------EKGAAVNRGFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQSENVQT 74
Cdd:cd01166 1 DVVTIGEVMVDLSppgggrlEQADSFRKFFGGAEANVAVGLAR------LGhrVALVTAVGDDPFGRFILAELRREGVDT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 75 DLIQRMADRLPGLYYIETDESGERTFYYWRNEAAAKFWLESEQSAticEELATFDYLYLSGISLAIlSPTSREKLLTLLR 154
Cdd:cd01166 75 SHVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDE---AALAGADHLHLSGITLAL-SESAREALLEALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 155 ECRANGGKVIFDNNYRPRLWsSKEETQRVYQQMLACTDIAFLTLDDEDALWGEKPVAEVIART--HAAGVEEVVVKRGAD 232
Cdd:cd01166 151 AAKARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERAlaLALGVKAVVVKLGAE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503993170 233 SCLVAIAGQpLREVPAvklPKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAI 301
Cdd:cd01166 230 GALVYTGGG-RVFVPA---YPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-308 |
1.50e-75 |
|
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: 233.62 E-value: 1.50e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 4 KIAVIGECMIEL------------SEKGAAVNRGFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQS 69
Cdd:COG0524 1 DVLVIGEALVDLvarvdrlpkggeTVLAGSFRRSPGGAAANVAVALAR------LGarVALVGAVGDDPFGDFLLAELRA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 70 ENVQTDLIQRMADRLPGLYYIETDESGERTFYYWRneAAAKFWLESEQSAticEELATFDYLYLSGISLAilSPTSREKL 149
Cdd:COG0524 75 EGVDTSGVRRDPGAPTGLAFILVDPDGERTIVFYR--GANAELTPEDLDE---ALLAGADILHLGGITLA--SEPPREAL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 150 LTLLRECRANGGKVIFDNNYRPRLWsskEETQRVYQQMLACTDIAFLTLDDEDALWGEKPVAEVIARTHAAGVEEVVVKR 229
Cdd:COG0524 148 LAALEAARAAGVPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 503993170 230 GADSCLVAIAGQpLREVPAVKLpkeKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAiipREAMP 308
Cdd:COG0524 225 GAEGALLYTGGE-VVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGA---QPALP 296
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-302 |
6.71e-74 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 229.15 E-value: 6.71e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 4 KIAVIGECMIELSE----------KGAAVNRGFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQSEN 71
Cdd:pfam00294 1 KVVVIGEANIDLIGnveglpgelvRVSTVEKGPGGKGANVAVALAR------LGgdVAFIGAVGDDNFGEFLLQELKKEG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 72 VQTDLIQRMADRLPGLYYIETDESGERTFYYWRNEAAAKFWLESEQSATICEElatFDYLYLSGislaILSPTSREKLLT 151
Cdd:pfam00294 75 VDTDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLEN---ADLLYISG----SLPLGLPEATLE 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 152 LLRECRANGGKviFDNNYRPRLWSSKEetqrVYQQMLACTDIAFLTLDDEDALWGEK--PVAEVIARTH---AAGVEEVV 226
Cdd:pfam00294 148 ELIEAAKNGGT--FDPNLLDPLGAARE----ALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHkllAKGIKTVI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 503993170 227 VKRGADSCLVAIAGQplrEVPAVKLPKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAII 302
Cdd:pfam00294 222 VTLGADGALVVEGDG---EVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
4-301 |
1.52e-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: 150.86 E-value: 1.52e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 4 KIAVIGECMIELSEKGAAVNRGF----GGDTLNTSVYIARqtdasaLGVH--YVTALGTDTFSQQMLESWQSENVQTDLI 77
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFtkapGGAPANVAVALAR------LGGKaaFIGKVGDDEFGDFLLETLKEAGVDTRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 78 QRMADRLPGLYYIETDESGERTFYYWRNEAAAKFWLESEQSATiceeLATFDYLYLSGISLAilSPTSREKLLTLLRECR 157
Cdd:cd01167 75 QFDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDL----LSEADILHFGSIALA--SEPSRSALLELLEAAK 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 158 ANGGKVIFDNNYRPRLWSSKEETQRVYQQMLACTDIafLTLDDEDALW--GEKPVAEVIARTHAAGVEEVVVKRGADSCL 235
Cdd:cd01167 149 KAGVLISFDPNLRPPLWRDEEEARERIAELLELADI--VKLSDEELELlfGEEDPEEIAALLLLFGLKLVLVTRGADGAL 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503993170 236 VAIAGQPLrEVPAvklPKEKVVDTTAAGDSFSAGYLAVRLTGGD-------AESAAKRGHLTASTVIQYRGAI 301
Cdd:cd01167 227 LYTKGGVG-EVPG---IPVEVVDTTGAGDAFVAGLLAQLLSRGLlaldedeLAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
24-301 |
1.03e-28 |
|
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: 111.25 E-value: 1.03e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 24 RGFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETDESGERTFY 101
Cdd:cd01942 33 REFGGSAGNTAVALAK------LGlsPGLVAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQIAY 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 102 -YWrneAAAKFWLESEQSaticeelatfDYLYLsgisLAILSPTSREKLLTLLRECRANGGKVIFDNNYRPRLWSSKEet 180
Cdd:cd01942 107 fYP---GAMDELEPNDEA----------DPDGL----ADIVHLSSGPGLIELARELAAGGITVSFDPGQELPRLSGEE-- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 181 qrvYQQMLACTDIAF-----LTLDDEDALWGEKPVAEviarthaaGVEEVVVKRGADSCLVaIAGQPLREVPAVklPKEK 255
Cdd:cd01942 168 ---LEEILERADILFvndyeAELLKERTGLSEAELAS--------GVRVVVVTLGPKGAIV-FEDGEEVEVPAV--PAVK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 503993170 256 VVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAI 301
Cdd:cd01942 234 VVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-272 |
8.68e-27 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 106.56 E-value: 8.68e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 1 MSKKIAVIGECMIEL-SEKGAAVNRGFGGDTLNTSVYIARQTDASAlgvhYVTALGTDTFSQQMLESWQSENVQT----- 74
Cdd:PRK09434 1 MMNKVWVLGDAVVDLiPEGENRYLKCPGGAPANVAVGIARLGGESG----FIGRVGDDPFGRFMQQTLQDEGVDTtylrl 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 75 DLIQRMADRLPGLyyietDESGERTFYYWRNEAAAKFwLESEqsaticeELATF---DYLYLSGISLAilSPTSREKLLT 151
Cdd:PRK09434 77 DPAHRTSTVVVDL-----DDQGERSFTFMVRPSADLF-LQPQ-------DLPPFrqgEWLHLCSIALS--AEPSRSTTFE 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 152 LLRECRANGGKVIFDNNYRPRLWSSKEETQRVYQQMLACTDIAFLTLDDEDALWGEKPVAEVIAR-THAAGVEEVVVKRG 230
Cdd:PRK09434 142 AMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLLVTLG 221
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 503993170 231 ADSCLVAIAGQpLREVPAVKLpkeKVVDTTAAGDSFSAGYLA 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 |
1.75e-25 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 103.01 E-value: 1.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 4 KIAVIGECMIEL------------SEKGAAVNRGFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQS 69
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrlpkpgeTVLGSSFETGPGGKGANQAVAAAR------LGarVAMIGAVGDDAFGDELLENLRE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 70 ENVQTDLIQRMADRLPGLYYIETDESGErtfyywrN------EAAAKFWLESEQSATicEELATFDYLYLSG-ISLails 142
Cdd:cd01174 75 EGIDVSYVEVVVGAPTGTAVITVDESGE-------NrivvvpGANGELTPADVDAAL--ELIAAADVLLLQLeIPL---- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 143 PTSREKLltllRECRANGGKVIFdnN---YRPRLwsskeetqrvyQQMLACTDI--------AFLTLDDEDALWGEKPVA 211
Cdd:cd01174 142 ETVLAAL----RAARRAGVTVIL--NpapARPLP-----------AELLALVDIlvpneteaALLTGIEVTDEEDAEKAA 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 212 EVIartHAAGVEEVVVKRGADSCLVAIAGQPLrEVPAvklPKEKVVDTTAAGDSFsAGYLAVRLT-GGDAESAAKRGHLT 290
Cdd:cd01174 205 RLL---LAKGVKNVIVTLGAKGALLASGGEVE-HVPA---FKVKAVDTTGAGDTF-IGALAAALArGLSLEEAIRFANAA 276
|
330
....*....|....*...
gi 503993170 291 ASTVIQYRGAIiprEAMP 308
Cdd:cd01174 277 AALSVTRPGAQ---PSIP 291
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
3-300 |
3.27e-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: 90.88 E-value: 3.27e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 3 KKIAVIGECM-IELSEKGAAVnrgfGGDTLNTSVYIARqtdaSALGVHYVTALGTDTFSQQMLESWQSENVQTDLIqRMA 81
Cdd:cd01940 1 RLAAIGDNVVdKYLHLGKMYP----GGNALNVAVYAKR----LGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 82 DRLPGLYYIETDEsGERTFyywrneaaakfwLESEQSATICEELATFDYLYLSGISLAILSPTSREK-LLTLLRECRANG 160
Cdd:cd01940 72 EGENAVADVELVD-GDRIF------------GLSNKGGVAREHPFEADLEYLSQFDLVHTGIYSHEGhLEKALQALVGAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 161 GKVIFDNNYRprlWSSKEetqrvYQQMLACTDIAFLTLDDEDalwgEKPVAEVIARTHAAGVEEVVVKRGADSCLvAIAG 240
Cdd:cd01940 139 ALISFDFSDR---WDDDY-----LQLVCPYVDFAFFSASDLS----DEEVKAKLKEAVSRGAKLVIVTRGEDGAI-AYDG 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503993170 241 QPLREVPAVKlpkEKVVDTTAAGDSFSAGYLAVRLTGGDA-ESAAKRGHLTASTVIQYRGA 300
Cdd:cd01940 206 AVFYSVAPRP---VEVVDTLGAGDSFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTCGHEGA 263
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
27-303 |
3.52e-20 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 89.32 E-value: 3.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 27 GGDTLNTSVYIARQTDASALGVHYVTALGTDTFSQQMLESWQSENVQTdliqrmadrlpgLYYIETDE-SGERTFYYWRN 105
Cdd:PTZ00247 62 GGSALNTARVAQWMLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEM------------LFEYTTKApTGTCAVLVCGK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 106 E--------AAAKFWLESEQSATICEELATFDYLYLSGISLAilspTSREKLLTLLRECRANGGKVIFDNNyRPRLWSSK 177
Cdd:PTZ00247 130 ErslvanlgAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFLT----VSPNNVLQVAKHARESGKLFCLNLS-APFISQFF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 178 EETQRvyqQMLACTDIAFLtlDDEDAL-------WGEKPVAEVIARthAAGVEEVVVKR--------GADSCLVAIAGQp 242
Cdd:PTZ00247 205 FERLL---QVLPYVDILFG--NEEEAKtfakamkWDTEDLKEIAAR--IAMLPKYSGTRprlvvftqGPEPTLIATKDG- 276
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503993170 243 LREVPAVKLPKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAIIP 303
Cdd:PTZ00247 277 VTSVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| KDG_KDGal_kin_Halo |
NF041332 |
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase; |
68-292 |
8.08e-20 |
|
bifunctional 2-dehydro-3-deoxygluconokinase/2-dehydro-3-deoxygalactonokinase;
Pssm-ID: 469229 [Multi-domain] Cd Length: 318 Bit Score: 87.66 E-value: 8.08e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 68 QSENVQTDLIQRMADRLpGLYYIET-DESGERTFYYWRNEAAAkfwleseQSATIcEELAT-----FDYLYLSGISLAiL 141
Cdd:NF041332 70 RSHGVDTDVVWDDEGRQ-GTYYLEHgGEPRGTNVIYDRADAAV-------TTATP-EELPLdrirdAEVFYTSGITPA-L 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 142 SPTSREKLLTLLRECRANGGKVIFDNNYRPRLWSSkEETQRVYQQMLACTDIAFLTLDDEDALWGEKPVAEVIARTHAA- 220
Cdd:NF041332 140 SETLAETTAALLEAAQEAGTTTAFDLNYRSKLWSP-EEARETLESLFPAVDVLVVAERDARTVLGRDGDAEEIAHGLASe 218
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503993170 221 -GVEEVVVKRGADSCLvAIAGQPLREVPAVklpKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTAS 292
Cdd:NF041332 219 yDFETVVVTRGEEGAL-ALHDGEVHEQPAY---EADTVDPIGTGDAFVGGFLARRLAGGDVPTALEYGAATAA 287
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
27-303 |
1.46e-18 |
|
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: 84.20 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 27 GGDTLNTSVYIArqtdasALG--VHYVTALGTDTFSQQMLESWQSENVQTDLiQRMADRLPGLYYIETDESGERTFYywR 104
Cdd:cd01168 55 GGSAANTIRGAA------ALGgsAAFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAERTMC--T 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 105 NEAAAKFwLESEQSATicEELATFDYLYLSGIslaiLSPTSREKLLTLLRECRANGGKVIFDnnyrprlWSSKEETQRVY 184
Cdd:cd01168 126 YLGAANE-LSPDDLDW--SLLAKAKYLYLEGY----LLTVPPEAILLAAEHAKENGVKIALN-------LSAPFIVQRFK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 185 QQMLAC---TDIAFLTLDDEDALWGEKP--VAEVIARTHAAGVEEVVVKRGADSCLVAIAGQplrEVPAVKLPKEKVVDT 259
Cdd:cd01168 192 EALLELlpyVDILFGNEEEAEALAEAETtdDLEAALKLLALRCRIVVITQGAKGAVVVEGGE---VYPVPAIPVEKIVDT 268
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 503993170 260 TAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAIIP 303
Cdd:cd01168 269 NGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
25-300 |
3.36e-18 |
|
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: 83.03 E-value: 3.36e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 25 GFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETDESGERTFYY 102
Cdd:TIGR02152 29 GPGGKGANQAVAAAR------LGaeVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKDTPTGTAFITVDDTGENRIVV 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 103 WrneAAAKFWLESEQSATICEELATFDYLYLSgisLAILSPTSREklltLLRECRANGGKVIFdnNYRPRLWSSKEEtqr 182
Cdd:TIGR02152 103 V---AGANAELTPEDIDAAEALIAESDIVLLQ---LEIPLETVLE----AAKIAKKHGVKVIL--NPAPAIKDLDDE--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 183 vyqqMLACTDI--------AFLT---LDDEDAlwgekpvAEVIART-HAAGVEEVVVKRGADSCLVAIAGQPlREVPAVK 250
Cdd:TIGR02152 168 ----LLSLVDIitpneteaEILTgieVTDEED-------AEKAAEKlLEKGVKNVIITLGSKGALLVSKDES-KLIPAFK 235
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 503993170 251 LpkeKVVDTTAAGDSFSAGyLAVRLT-GGDAESAAKRGHLTASTVIQYRGA 300
Cdd:TIGR02152 236 V---KAVDTTAAGDTFNGA-FAVALAeGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
125-272 |
1.28e-15 |
|
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: 73.67 E-value: 1.28e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 125 LATFDYLYLSGISLAilsptsREKLLTLLRECRANGGKVIFDNNYRPRLWSSKEetqrvYQQMLACTDIAFLTLDDEDAL 204
Cdd:cd00287 55 LVGADAVVISGLSPA------PEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVDILTPNEEEAEAL 123
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503993170 205 -----WGEKPVAEVIARTHAAGVEEVVVKRGADSCLVAIAGQPLREVPAVKlpkEKVVDTTAAGDSFSAGYLA 272
Cdd:cd00287 124 tgrrdLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFP---VKVVDTTGAGDAFLAALAA 193
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
7.23e-15 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 74.00 E-value: 7.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 1 MSKKIAVIGECMIEL------------SEKGAAVNRGFGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLES 66
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLigyvdrmpqvgeTLHGTSFHKGFGGKGANQAVMASK------LGakVAMVGMVGTDGFGSDTIKN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 67 WQSENVQTDLIQRMADRLPGLYYIETDESgertfyywrneaaakfwlESEQSATIC---EELATFDYL------YLSGIS 137
Cdd:PTZ00292 88 FKRNGVNTSFVSRTENSSTGLAMIFVDTK------------------TGNNEIVIIpgaNNALTPQMVdaqtdnIQNICK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 138 LAIL-SPTSREKLLTLLRECRANGGKVIFdnNYRPrlwSSKEETQRVYQQMLACTDIaFLTLDDEDALWGEKPVA--EVI 214
Cdd:PTZ00292 150 YLICqNEIPLETTLDALKEAKERGCYTVF--NPAP---APKLAEVEIIKPFLKYVSL-FCVNEVEAALITGMEVTdtESA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 215 ARTHAA----GVEEVVVKRGADSCLVAIAGQPLREVPAVKLpkeKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLT 290
Cdd:PTZ00292 224 FKASKElqqlGVENVIITLGANGCLIVEKENEPVHVPGKRV---KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRI 300
|
330
....*....|
gi 503993170 291 ASTVIQYRGA 300
Cdd:PTZ00292 301 AAISVTRHGT 310
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
50-303 |
1.58e-13 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 70.13 E-value: 1.58e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 50 YVTALGTDTFSQQMLESWQSENVQTDliqrmadrlpglYYIetDES------------GERTFYywRNEAAAKFW----L 113
Cdd:PLN02548 74 YMGCIGKDKFGEEMKKCATAAGVNVH------------YYE--DEStptgtcavlvvgGERSLV--ANLSAANCYkvehL 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 114 ESEQSATICEELatfDYLYLSGISLAIlSPtsrEKLLTLLRECRANGgKVIFDNNYRPRLwsskeeTQRVYQQMLACTDI 193
Cdd:PLN02548 138 KKPENWALVEKA---KFYYIAGFFLTV-SP---ESIMLVAEHAAANN-KTFMMNLSAPFI------CEFFKDQLMEALPY 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 194 AfltlddeDALWGEKPVAEVIARTHAAG---VEEVVVK------------------RGADSCLVAIAGQpLREVPAVKLP 252
Cdd:PLN02548 204 V-------DFLFGNETEARTFAKVQGWEtedVEEIALKisalpkasgthkrtvvitQGADPTVVAEDGK-VKEFPVIPLP 275
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 503993170 253 KEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAIIP 303
Cdd:PLN02548 276 KEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYP 326
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-300 |
4.44e-13 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 67.84 E-value: 4.44e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 3 KKIAVIGECMIELSEKgaaVNRGF-GGDTLNTSVYIARqtdasaLGVH--YVTALGTDTFSQQMLESWQSENVQTDLIqR 79
Cdd:PRK09813 1 KKLATIGDNCVDIYPQ---LGKAFsGGNAVNVAVYCTR------YGIQpgCITWVGDDDYGTKLKQDLARMGVDISHV-H 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 80 MADRLPGLYYIETDeSGERTFYYWRNEAAAKFWLESEQSATICEelatFDYlylsgISLAILSPTSREklltlLRECRAN 159
Cdd:PRK09813 71 TKHGVTAQTQVELH-DNDRVFGDYTEGVMADFALSEEDYAWLAQ----YDI-----VHAAIWGHAEDA-----FPQLHAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 160 GGKVIFDNNYRPR--LWsskeetqrvyQQMLACTDIAFLTLDDEDAlWGEKPVAEVIARthAAGVeeVVVKRGADSCLvA 237
Cdd:PRK09813 136 GKLTAFDFSDKWDspLW----------QTLVPHLDYAFASAPQEDE-FLRLKMKAIVAR--GAGV--VIVTLGENGSI-A 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 503993170 238 IAGQPLREVPAVKLpkeKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGA 300
Cdd:PRK09813 200 WDGAQFWRQAPEPV---TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
27-271 |
2.30e-10 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 60.41 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 27 GGDTLNTSVYIARQTDASAlgvhYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETDESGERTFYYWRNE 106
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSA----FIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 107 AAAKFWLESEQSATICEELATFDYlylSGISLaILSPtSREKLLTLLRECRANGGKVIFDNNYRPRLWSSKEETQRvyqQ 186
Cdd:PLN02323 119 SADMLLRESELDLDLIRKAKIFHY---GSISL-ITEP-CRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSAEAARE---G 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 187 MLACTDIA-FLTLDDEDALW---GEKPVAEVIARTHAAGVEEVVVKRGADSCLV---AIAGQplreVPAVKLpkeKVVDT 259
Cdd:PLN02323 191 IMSIWDEAdIIKVSDEEVEFltgGDDPDDDTVVKLWHPNLKLLLVTEGEEGCRYytkDFKGR----VEGFKV---KAVDT 263
|
250
....*....|..
gi 503993170 260 TAAGDSFSAGYL 271
Cdd:PLN02323 264 TGAGDAFVGGLL 275
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
119-287 |
4.66e-10 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 59.38 E-value: 4.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 119 ATICEELATFDYLYLSGiSLAilSPTSREKLLTLLRECRANGGKVIFDnnyrprlwSSKEETQRV----------YQQML 188
Cdd:COG1105 120 ERLEELLKEGDWVVLSG-SLP--PGVPPDFYAELIRLARARGAKVVLD--------TSGEALKAAleagpdlikpNLEEL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 189 ActDIAFLTLDDEDAlwgekpVAEVIARTHAAGVEEVVVKRGADSCLVAIAGQPLRevpaVKLPKEKVVDTTAAGDSFSA 268
Cdd:COG1105 189 E--ELLGRPLETLED------IIAAARELLERGAENVVVSLGADGALLVTEDGVYR----AKPPKVEVVSTVGAGDSMVA 256
|
170
....*....|....*....
gi 503993170 269 GYLAVRLTGGDAESAAKRG 287
Cdd:COG1105 257 GFLAGLARGLDLEEALRLA 275
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
26-309 |
2.80e-09 |
|
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: 56.92 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 26 FGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETDESGERT-FYY 102
Cdd:cd01945 35 GGGNAANAAVAVAR------LGgqARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATiSIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 103 WRNEAAAKFWLESEqsaticeELATFDYLYLSGislailspTSREKLLTLLRECRANGGKVIFDNNyrprlWSSKEETQR 182
Cdd:cd01945 109 AIDTQAAPDSLPDA-------ILGGADAVLVDG--------RQPEAALHLAQEARARGIPIPLDLD-----GGGLRVLEE 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 183 VYQqmlACTDIAFltldDEDAL--WGEKPVAEVIARTHAAGVEEVVVKRGADSCLVAIAGQPLREVPAvklPKEKVVDTT 260
Cdd:cd01945 169 LLP---LADHAIC----SENFLrpNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPA---FPVEVVDTT 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 503993170 261 AAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAiipREAMPQ 309
Cdd:cd01945 239 GAGDVFHGAFAHALAEGMPLREALRFASAAAALKCRGLGG---RAGLPT 284
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
4-301 |
1.68e-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: 54.35 E-value: 1.68e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 4 KIAVIG--ECMIELS-----EKGAAVN-----RGFGGDTLNTSVYIARQTDAsalgVHYVTALGTDTFSQQMLESWQSEN 71
Cdd:cd01947 1 KIAVVGhvEWDIFLSldappQPGGISHssdsrESPGGGGANVAVQLAKLGND----VRFFSNLGRDEIGIQSLEELESGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 72 VqTDLIQrMADRLPGLYYIETDESGERTFYY-WRNEAAAKFWleseqsaticEELATFDYLYLsgislailspTSREKLL 150
Cdd:cd01947 77 D-KHTVA-WRDKPTRKTLSFIDPNGERTITVpGERLEDDLKW----------PILDEGDGVFI----------TAAAVDK 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 151 TLLRECRaNGGKVIFDNNYRPRLWSSKEETQRVyqQMLACTDIAFLTLDDEDALWGEKPvaeviaRThaagveeVVVKRG 230
Cdd:cd01947 135 EAIRKCR-ETKLVILQVTPRVRVDELNQALIPL--DILIGSRLDPGELVVAEKIAGPFP------RY-------LIVTEG 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 503993170 231 AdscLVAIAGqPLREVPAVKLPKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGAI 301
Cdd:cd01947 199 E---LGAILY-PGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
43-299 |
2.02e-08 |
|
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238919 [Multi-domain] Cd Length: 289 Bit Score: 54.35 E-value: 2.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 43 ASALGVHYVTA--LGTDTFSQQMLESWQSENVQTDLIQRMADRlPGLYYIETDESGERTFYYWrneAAAKFWLESEQSAT 120
Cdd:cd01944 45 ASRLGIPTVNAgpLGNGNWADQIRQAMRDEGIEILLPPRGGDD-GGCLVALVEPDGERSFISI---SGAEQDWSTEWFAT 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 121 IceELATFDYLYLSGISLAilSPTSREKLLTLLRECRANGGKVIFDnnYRPRLWS-SKEETQRVyqqmLACTDIafLTLD 199
Cdd:cd01944 121 L--TVAPYDYVYLSGYTLA--SENASKVILLEWLEALPAGTTLVFD--PGPRISDiPDTILQAL----MAKRPI--WSCN 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 200 DEDALW----GEKPVAEVIARTHAAGVEEVVVKRGADSCLVAIAGQPLREVPAVKLpkeKVVDTTAAGDSFSAGYLAVRL 275
Cdd:cd01944 189 REEAAIfaerGDPAAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFKV---KAVDTIGAGDTHAGGMLAGLA 265
|
250 260
....*....|....*....|....
gi 503993170 276 TGGDAESAAKRGHLTASTVIQYRG 299
Cdd:cd01944 266 KGMSLADAVLLANAAAAIVVTRSG 289
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
225-304 |
3.48e-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: 53.88 E-value: 3.48e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 225 VVVKRGADSCLVAIA-GQPLREVPAVKLPKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGaiIP 303
Cdd:cd01943 228 VVLRCGKLGCYVGSAdSGPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG--LP 305
|
.
gi 503993170 304 R 304
Cdd:cd01943 306 R 306
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
26-300 |
5.18e-08 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 53.33 E-value: 5.18e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 26 FGGDTLNTSVYIARqtdasaLG--VHYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETDESGErtfyyw 103
Cdd:PRK11142 38 FGGKGANQAVAAAR------LGadIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGE------ 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 104 rN----EAAAKFWLESEQSATICEELATFDYLylsgisLAIL-SPTsrEKLLTLLRECRANGGKVIFdnNYRPrlwsske 178
Cdd:PRK11142 106 -NsigiHAGANAALTPALVEAHRELIANADAL------LMQLeTPL--ETVLAAAKIAKQHGTKVIL--NPAP------- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 179 eTQRVYQQMLACTDI--------AFLT----LDDEDAlwgekpvAEVIARTHAAGVEEVVVKRGADSCLVAIAGQPlREV 246
Cdd:PRK11142 168 -ARELPDELLALVDIitpneteaEKLTgirvEDDDDA-------AKAAQVLHQKGIETVLITLGSRGVWLSENGEG-QRV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 503993170 247 PAVKLpkeKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQYRGA 300
Cdd:PRK11142 239 PGFRV---QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
125-287 |
8.61e-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: 52.53 E-value: 8.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 125 LATFDYLYLSGiSL-AILSPtsrEKLLTLLRECRANGGKVIFDnnyrprlwSSKEETQRVYQQM----------LActDI 193
Cdd:cd01164 126 LKKGDIVVLSG-SLpPGVPA---DFYAELVRLAREKGARVILD--------TSGEALLAALAAKpflikpnreeLE--EL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 194 AFLTLDDEDALWgekpvaEVIARTHAAGVEEVVVKRGADSCLVAIAGQPLRevpaVKLPKEKVVDTTAAGDSFSAGYLAV 273
Cdd:cd01164 192 FGRPLGDEEDVI------AAARKLIERGAENVLVSLGADGALLVTKDGVYR----ASPPKVKVVSTVGAGDSMVAGFVAG 261
|
170
....*....|....
gi 503993170 274 RLTGGDAESAAKRG 287
Cdd:cd01164 262 LAQGLSLEEALRLA 275
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
192-296 |
9.17e-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: 52.32 E-value: 9.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 192 DIAFLTLDDEDALWG-----EKPVAEVIARTHAAGVEEVVVKRGADSCLVA--IAGQPLREVPAVKlpKEKVVDTTAAGD 264
Cdd:cd01941 178 DLLTPNRAELEALAGalienNEDENKAAKILLLPGIKNVIVTLGAKGVLLSsrEGGVETKLFPAPQ--PETVVNVTGAGD 255
|
90 100 110
....*....|....*....|....*....|..
gi 503993170 265 SFSAGYLAVRLTGGDAESAAKRGHLTASTVIQ 296
Cdd:cd01941 256 AFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
128-271 |
5.91e-07 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 50.60 E-value: 5.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 128 FDYLYLSGISLAILSPTSreklltllrecraNGGKVIFDNNyrPRLWSSKEET---QRVYQQMLACTDIAFLTLDDEDAL 204
Cdd:PLN02341 235 FDELSPSAIASAVDYAID-------------VGTAVFFDPG--PRGKSLLVGTpdeRRALEHLLRMSDVLLLTSEEAEAL 299
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 503993170 205 WGEKP---VAEVIARThAAGVEEVVVKRGAD-SCLVAIAGQPLreVPAvklPKEKVVDTTAAGDSFSA----GYL 271
Cdd:PLN02341 300 TGIRNpilAGQELLRP-GIRTKWVVVKMGSKgSILVTRSSVSC--APA---FKVNVVDTVGCGDSFAAaialGYI 368
|
|
| PLN02967 |
PLN02967 |
kinase |
24-212 |
4.57e-06 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 48.12 E-value: 4.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 24 RGFGGDTLNTSVYIArqtdasALG--VHYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETDESGERTFY 101
Cdd:PLN02967 240 RAPGGSAGGVAIALA------SLGgkVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTT 313
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 102 YWRNEAAAKFwLESEQSATICEELATFdylYLSgiSLAILSPTSREKLLTLLRECRANGGKVIFDNNYRPRLWSSKEETQ 181
Cdd:PLN02967 314 CVKPCAEDSL-SKSEINIDVLKEAKMF---YFN--THSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETK 387
|
170 180 190
....*....|....*....|....*....|.
gi 503993170 182 RVYQQMLACTDIAFLTLDDEDALWGEKPVAE 212
Cdd:PLN02967 388 SFIQEAWNLADIIEVTKQELEFLCGIEPTEE 418
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
218-301 |
2.01e-05 |
|
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: 45.24 E-value: 2.01e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 218 HAAGVEEVVVKRGADSCLVAIAGQPLREVPAVKLPkekVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVIQY 297
Cdd:cd01172 215 ELLNLEALLVTLGEEGMTLFERDGEVQHIPALAKE---VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGK 291
|
....
gi 503993170 298 RGAI 301
Cdd:cd01172 292 VGTA 295
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
172-295 |
3.19e-05 |
|
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: 44.70 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 172 RLWSSKEETQRVYQQmlactDIAFLTLDDEDALWGEKPvAEVIARTHAAGVEEVVVKRGADSCLVAIAGQPLRevpaVKL 251
Cdd:cd01937 140 RRANQEKLIKCVILK-----LHDVLKLSRVEAEVISTP-TELARLIKETGVKEIIVTDGEEGGYIFDGNGKYT----IPA 209
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 503993170 252 PKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVI 295
Cdd:cd01937 210 SKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
147-305 |
1.50e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 42.86 E-value: 1.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 147 EKLLTLLRECRANGGKVIFD-------NNYRPRLwsskeetqrvyQQMLACTDIAFLTLDDEDA---LWGE-KPVAEVIA 215
Cdd:PLN02379 191 EVIEAAIRLAKQEGLSVSLDlasfemvRNFRSPL-----------LQLLESGKIDLCFANEDEArelLRGEqESDPEAAL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 216 RTHAAGVEEVVVKRGADSCLvAIAGQPLREVPAVKlpKEKVVDTTAAGDSFSAGYLAVRLTGGDAESAAKRGHLTASTVI 295
Cdd:PLN02379 260 EFLAKYCNWAVVTLGSKGCI-ARHGKEVVRVPAIG--ETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVV 336
|
170
....*....|
gi 503993170 296 QYRGAIIPRE 305
Cdd:PLN02379 337 RALGGEVTPE 346
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
182-300 |
5.89e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 41.33 E-value: 5.89e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 182 RVYQQML----ACTDIAFLTLDDEDAL--WGEKPVAEVIARTHAAGVEEVVVKRGADSCLVAIAGqplrEVPAVKLPKEK 255
Cdd:PLN02813 270 RHRDDFWdvmgNYADILFANSDEARALcgLGSEESPESATRYLSHFCPLVSVTDGARGSYIGVKG----EAVYIPPSPCV 345
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 503993170 256 VVDTTAAGDSFSAGYLAVRLTG-GDAESAAKRGHLTASTVIQYRGA 300
Cdd:PLN02813 346 PVDTCGAGDAYAAGILYGLLRGvSDLRGMGELAARVAATVVGQQGT 391
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
24-193 |
1.55e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 39.89 E-value: 1.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 24 RGFGGDTLNTSVYIARQTDASAlgvhYVTALGTDTFSQQMLESWQSENVQTDLIQRMADRLPGLYYIETD-ESGERTFYY 102
Cdd:PLN02543 169 RAPGGPPSNVAISHVRLGGRAA----FMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfRDGGKMVAE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 503993170 103 WRNEAAAKFWLESEQSATICEELATFDYlylsgISLAILSPTSREKLLTLLRECRANGGKVIFDNNYRPRLWSSKEETQR 182
Cdd:PLN02543 245 TVKEAAEDSLLASELNLAVLKEARMFHF-----NSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRE 319
|
170
....*....|.
gi 503993170 183 VYQQMLACTDI 193
Cdd:PLN02543 320 LIKKAWNEADI 330
|
|
| |
