|
Name |
Accession |
Description |
Interval |
E-value |
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
4-301 |
1.16e-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: 1.16e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 4 KIAVIGECMIELSQKG-------ADVQRGFGGDTLNTSVYIARQvdsaALAVHYVTALGTDSFSQQMLEAWQHENVDTSL 76
Cdd:cd01166 1 DVVTIGEVMVDLSPPGggrleqaDSFRKFFGGAEANVAVGLARL----GHRVALVTAVGDDPFGRFILAELRREGVDTSH 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 77 TQRMENRLPGLYYIETDDTGERTFYYWRNEAAAKFWLESEQSAAiceALATFDYLYLSGISLAIlSPTSRDKLLSLLREC 156
Cdd:cd01166 77 VRVDPGRPTGLYFLEIGAGGERRVLYYRAGSAASRLTPEDLDEA---ALAGADHLHLSGITLAL-SESAREALLEALEAA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 157 RANGGKVIFDNNYRPRLWtSREETQQVYQKMLECTDIAFLTLDDEDALWGQQPVEKVIART--HAAGVQEVVVKRGADSC 234
Cdd:cd01166 153 KARGVTVSFDLNYRPKLW-SAEEAREALEELLPYVDIVLPSEEEAEALLGDEDPTDAAERAlaLALGVKAVVVKLGAEGA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526017864 235 LVSiQGEALIDVPAvklPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01166 232 LVY-TGGGRVFVPA---YPVEVVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAALVVTRPGDI 294
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
4-308 |
2.73e-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: 232.85 E-value: 2.73e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 4 KIAVIGECMIELSQK------------GADVQRGFGGDTLNTSVYIARqvdsAALAVHYVTALGTDSFSQQMLEAWQHEN 71
Cdd:COG0524 1 DVLVIGEALVDLVARvdrlpkggetvlAGSFRRSPGGAAANVAVALAR----LGARVALVGAVGDDPFGDFLLAELRAEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 72 VDTSLTQRMENRLPGLYYIETDDTGERTFYYWRNeAAAKFWLESEQSAAICEAlatfDYLYLSGISLAilSPTSRDKLLS 151
Cdd:COG0524 77 VDTSGVRRDPGAPTGLAFILVDPDGERTIVFYRG-ANAELTPEDLDEALLAGA----DILHLGGITLA--SEPPREALLA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 152 LLRECRANGGKVIFDNNYRPRLWtsrEETQQVYQKMLECTDIAFLTLDDEDALWGQQPVEKVIARTHAAGVQEVVVKRGA 231
Cdd:COG0524 150 ALEAARAAGVPVSLDPNYRPALW---EPARELLRELLALVDILFPNEEEAELLTGETDPEEAAAALLARGVKLVVVTLGA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 526017864 232 DSCLVSIQGEaLIDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAIiphDAMP 308
Cdd:COG0524 227 EGALLYTGGE-VVHVPAFPV---EVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQ---PALP 296
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
4-302 |
5.92e-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: 226.46 E-value: 5.92e-73
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 4 KIAVIGECMIEL----------SQKGADVQRGFGGDTLNTSVYIARQVDSaalaVHYVTALGTDSFSQQMLEAWQHENVD 73
Cdd:pfam00294 1 KVVVIGEANIDLignveglpgeLVRVSTVEKGPGGKGANVAVALARLGGD----VAFIGAVGDDNFGEFLLQELKKEGVD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 74 TSLTQRMENRLPGLYYIETDDTGERTFYYWRNEAAAKFWLESEQSAAICEAlatFDYLYLSGislaILSPTSRDKLLSLL 153
Cdd:pfam00294 77 TDYVVIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENEDLLEN---ADLLYISG----SLPLGLPEATLEEL 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 154 RECRANGGKviFDNNYRPRLWtsreETQQVYQKMLECTDIAFLTLDDEDALWGQQ--PVEKVIARTH---AAGVQEVVVK 228
Cdd:pfam00294 150 IEAAKNGGT--FDPNLLDPLG----AAREALLELLPLADLLKPNEEELEALTGAKldDIEEALAALHkllAKGIKTVIVT 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526017864 229 RGADSCLVSIQGEALIdVPAVklPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAII 302
Cdd:pfam00294 224 LGADGALVVEGDGEVH-VPAV--PKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
4-301 |
5.09e-47 |
|
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: 159.72 E-value: 5.09e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 4 KIAVIGECMIELSQKGADVQRGF----GGDTLNTSVYIAR-QVDSAalavhYVTALGTDSFSQQMLEAWQHENVDTSLTQ 78
Cdd:cd01167 1 KVVCFGEALIDFIPEGSGAPETFtkapGGAPANVAVALARlGGKAA-----FIGKVGDDEFGDFLLETLKEAGVDTRGIQ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 79 RMENRLPGLYYIETDDTGERTFYYWRNEAAAKFWLESEQSAAICEAlatfDYLYLSGISLAilSPTSRDKLLSLLRECRA 158
Cdd:cd01167 76 FDPAAPTTLAFVTLDADGERSFEFYRGPAADLLLDTELNPDLLSEA----DILHFGSIALA--SEPSRSALLELLEAAKK 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 159 NGGKVIFDNNYRPRLWTSREETQQVYQKMLECTDIafLTLDDEDALW--GQQPVEKVIARTHAAGVQEVVVKRGADSCLV 236
Cdd:cd01167 150 AGVLISFDPNLRPPLWRDEEEARERIAELLELADI--VKLSDEELELlfGEEDPEEIAALLLLFGLKLVLVTRGADGALL 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 526017864 237 SIQGEALIdVPAvklPKEKVIDTTAAGDSFSAGYLA-------VRLTGGSATDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01167 228 YTKGGVGE-VPG---IPVEVVDTTGAGDAFVAGLLAqllsrglLALDEDELAEALRFANAVGALTCTKAGAI 295
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
20-301 |
2.74e-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: 110.09 E-value: 2.74e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 20 ADVQRGFGGDTLNTSVYIARQVDSAALavhyVTALGTDSFSQQMLEAWQHENVDTSLTQRMENRLPGLYYIETDDTGERT 99
Cdd:cd01942 29 KDLRREFGGSAGNTAVALAKLGLSPGL----VAAVGEDFHGRLYLEELREEGVDTSHVRVVDEDSTGVAFILTDGDDNQI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 100 FY-YWrneAAAKFWLESEqsAAICEALAtfdylylsgislAILSPTSRDKLLSLLRECRANGGKVIFDNNYR-PRLWTSR 177
Cdd:cd01942 105 AYfYP---GAMDELEPND--EADPDGLA------------DIVHLSSGPGLIELARELAAGGITVSFDPGQElPRLSGEE 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 178 EETqqvyqkMLECTDIAF-----LTLDDEDALWGQQPVekviarthAAGVQEVVVKRGADSCLVSIQGEAlIDVPAVklP 252
Cdd:cd01942 168 LEE------ILERADILFvndyeAELLKERTGLSEAEL--------ASGVRVVVVTLGPKGAIVFEDGEE-VEVPAV--P 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 526017864 253 KEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01942 231 AVKVVDTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
4-308 |
3.14e-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: 102.24 E-value: 3.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 4 KIAVIGECMIEL------------SQKGADVQRGFGGDTLNTSVYIARqvdsAALAVHYVTALGTDSFSQQMLEAWQHEN 71
Cdd:cd01174 1 KVVVVGSINVDLvtrvdrlpkpgeTVLGSSFETGPGGKGANQAVAAAR----LGARVAMIGAVGDDAFGDELLENLREEG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 72 VDTSLTQRMENRLPGLYYIETDDTGErtfyywrN------EAAAKFWLESEQSAAicEALATFDYLYLSG-ISLAILspt 144
Cdd:cd01174 77 IDVSYVEVVVGAPTGTAVITVDESGE-------NrivvvpGANGELTPADVDAAL--ELIAAADVLLLQLeIPLETV--- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 145 srdklLSLLRECRANGGKVIFdnNYRPrlwtsreeTQQVYQKMLECTDI--------AFLT----LDDEDAlwgqqpvEK 212
Cdd:cd01174 145 -----LAALRAARRAGVTVIL--NPAP--------ARPLPAELLALVDIlvpneteaALLTgievTDEEDA-------EK 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 213 VIARTHAAGVQEVVVKRGADSCLVSIQGEAlIDVPAvklPKEKVIDTTAAGDSFsAGYLAVRLT-GGSATDAAKRGHLTA 291
Cdd:cd01174 203 AARLLLAKGVKNVIVTLGAKGALLASGGEV-EHVPA---FKVKAVDTTGAGDTF-IGALAAALArGLSLEEAIRFANAAA 277
|
330
....*....|....*..
gi 526017864 292 STVIQYRGAIiphDAMP 308
Cdd:cd01174 278 ALSVTRPGAQ---PSIP 291
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
3-300 |
7.33e-23 |
|
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: 95.11 E-value: 7.33e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 3 KKIAVIGECM-IELSQKGADVqrgfGGDTLNTSVYIARqvdsAALAVHYVTALGTDSFSQQMLEAWQHENVDTSLTqRME 81
Cdd:cd01940 1 RLAAIGDNVVdKYLHLGKMYP----GGNALNVAVYAKR----LGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHC-RVK 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 82 NRLPGLYYIETDDtGERTFyywrneaaakfwLESEQSAAICEALATFDYLYLSGISLAILSPTSR-DKLLSLLRECRANG 160
Cdd:cd01940 72 EGENAVADVELVD-GDRIF------------GLSNKGGVAREHPFEADLEYLSQFDLVHTGIYSHeGHLEKALQALVGAG 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 161 GKVIFDNNYRprlWTSREetqqvYQKMLECTDIAFLTLDDEDAlwgqQPVEKVIARTHAAGVQEVVVKRGADSCLVSiQG 240
Cdd:cd01940 139 ALISFDFSDR---WDDDY-----LQLVCPYVDFAFFSASDLSD----EEVKAKLKEAVSRGAKLVIVTRGEDGAIAY-DG 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526017864 241 EALIDVPAVKlpkEKVIDTTAAGDSFSAGYLAVRLTGGSA-TDAAKRGHLTASTVIQYRGA 300
Cdd:cd01940 206 AVFYSVAPRP---VEVVDTLGAGDSFIAGFLLSLLAGGTAiAEAMRQGAQFAAKTCGHEGA 263
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
1-272 |
1.64e-22 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 95.00 E-value: 1.64e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 1 MPKKIAVIGECMIELSQKGadvQRGF----GGDTLNTSVYIAR-QVDSAalavhYVTALGTDSFSQQMLEAWQHENVDTS 75
Cdd:PRK09434 1 MMNKVWVLGDAVVDLIPEG---ENRYlkcpGGAPANVAVGIARlGGESG-----FIGRVGDDPFGRFMQQTLQDEGVDTT 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 76 L-----TQRMENRLPGLyyietDDTGERTFYYWRNEAAAKFwLESEQsaaiceaLATF---DYLYLSGISLAilSPTSRD 147
Cdd:PRK09434 73 YlrldpAHRTSTVVVDL-----DDQGERSFTFMVRPSADLF-LQPQD-------LPPFrqgEWLHLCSIALS--AEPSRS 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 148 KLLSLLRECRANGGKVIFDNNYRPRLWTSREETQQVYQKMLECTDIAFLTLDDEDALWGQQPVEKVIAR-THAAGVQEVV 226
Cdd:PRK09434 138 TTFEAMRRIKAAGGFVSFDPNLREDLWQDEAELRECLRQALALADVVKLSEEELCFLSGTSQLEDAIYAlADRYPIALLL 217
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 526017864 227 VKRGADSCLVSIQGEALIdVPAVKLpkeKVIDTTAAGDSFSAGYLA 272
Cdd:PRK09434 218 VTLGAEGVLVHTRGQVQH-FPAPSV---DPVDTTGAGDAFVAGLLA 259
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
3-300 |
1.01e-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: 89.97 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 3 KKIAVIGEcmielSQKGADVQRGFGGDTLNTSVYIARqvdsAALAVHYVTALGTDSFSQQMLEAWQHENVDTSLTQRMEN 82
Cdd:TIGR02152 12 DRLPKPGE-----TVHGHSFQIGPGGKGANQAVAAAR----LGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYVGTVKD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 83 RLPGLYYIETDDTGERTFYYWrneAAAKFWLESEQSAAICEALATFDYLYLSgisLAILSPTSrdklLSLLRECRANGGK 162
Cdd:TIGR02152 83 TPTGTAFITVDDTGENRIVVV---AGANAELTPEDIDAAEALIAESDIVLLQ---LEIPLETV----LEAAKIAKKHGVK 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 163 VIFdnNYRPRLWTSREEtqqvyqkMLECTDI--------AFLT---LDDEDAlwgqqpVEKVIARTHAAGVQEVVVKRGA 231
Cdd:TIGR02152 153 VIL--NPAPAIKDLDDE-------LLSLVDIitpneteaEILTgieVTDEED------AEKAAEKLLEKGVKNVIITLGS 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 232 DSCLVSIQGEALIdVPAVKLpkeKVIDTTAAGDSFSAGyLAVRLT-GGSATDAAKRGHLTASTVIQYRGA 300
Cdd:TIGR02152 218 KGALLVSKDESKL-IPAFKV---KAVDTTAAGDTFNGA-FAVALAeGKSLEDAIRFANAAAAISVTRKGA 282
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
27-303 |
3.07e-20 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 89.32 E-value: 3.07e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 27 GGDTLNTSVYIARQVDSAALAVHYVTALGTDSFSQQMLEAWQHENVDTsltqrmenrlpgLYYIETDD-TGERTFYYWRN 105
Cdd:PTZ00247 62 GGSALNTARVAQWMLQAPKGFVCYVGCVGDDRFAEILKEAAEKDGVEM------------LFEYTTKApTGTCAVLVCGK 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 106 E--------AAAKFWLESEQSAAICEALATFDYLYLSGISLAilspTSRDKLLSLLRECRANGGKVIFdNNYRPRLWTSR 177
Cdd:PTZ00247 130 ErslvanlgAANHLSAEHMQSHAVQEAIKTAQLYYLEGFFLT----VSPNNVLQVAKHARESGKLFCL-NLSAPFISQFF 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 178 EETqqvYQKMLECTDIAFLtlDDEDAL-------WGQQPVEKVIART-----HAAGVQEVVV-KRGADSCLVSIQGEaLI 244
Cdd:PTZ00247 205 FER---LLQVLPYVDILFG--NEEEAKtfakamkWDTEDLKEIAARIamlpkYSGTRPRLVVfTQGPEPTLIATKDG-VT 278
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 526017864 245 DVPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAIIP 303
Cdd:PTZ00247 279 SVPVPPLDQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVIIQHNGCTYP 337
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
27-303 |
7.44e-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: 82.28 E-value: 7.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 27 GGDTLNTSVYIARQVDSAalavHYVTALGTDSFSQQMLEAWQHENVDTSLtQRMENRLPGLYYIETDDTGERTFYywRNE 106
Cdd:cd01168 55 GGSAANTIRGAAALGGSA----AFIGRVGDDKLGDFLLKDLRAAGVDTRY-QVQPDGPTGTCAVLVTPDAERTMC--TYL 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 107 AAAKFwLESEQSAAicEALATFDYLYLSGIslaiLSPTSRDKLLSLLRECRANGGKVIFD-------NNYRPRLWtsree 179
Cdd:cd01168 128 GAANE-LSPDDLDW--SLLAKAKYLYLEGY----LLTVPPEAILLAAEHAKENGVKIALNlsapfivQRFKEALL----- 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 180 tqqvyqKMLECTDIAFLTLDDEDALWGQQPVEKVIA--RTHAAGVQEVVVKRGADSCLVsIQGEALIDVPAVklPKEKVI 257
Cdd:cd01168 196 ------ELLPYVDILFGNEEEAEALAEAETTDDLEAalKLLALRCRIVVITQGAKGAVV-VEGGEVYPVPAI--PVEKIV 266
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 526017864 258 DTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAIIP 303
Cdd:cd01168 267 DTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRLP 312
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
124-272 |
4.14e-16 |
|
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: 75.21 E-value: 4.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 124 ALATFDYLYLSGISLAilsptsRDKLLSLLRECRANGGKVIFDNNYRPRLWTSREetqqvYQKMLECTDIAFLTLDDEDA 203
Cdd:cd00287 54 TLVGADAVVISGLSPA------PEAVLDALEEARRRGVPVVLDPGPRAVRLDGEE-----LEKLLPGVDILTPNEEEAEA 122
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 526017864 204 LWGQQ-PVEKVIART----HAAGVQEVVVKRGADSCLVSIQGEALIDVPAVKlpkEKVIDTTAAGDSFSAGYLA 272
Cdd:cd00287 123 LTGRRdLEVKEAAEAaallLSKGPKVVIVTLGEKGAIVATRGGTEVHVPAFP---VKVVDTTGAGDAFLAALAA 193
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
14-303 |
6.99e-15 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 73.98 E-value: 6.99e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 14 ELSQKGaDVQRGFGGDTLNtSVYIARQVDSAALAVHYVTALGTDSFSQQMLEAWQHENVDtsltqrmenrlpgLYYIETD 93
Cdd:PLN02548 40 ELASKY-NVEYIAGGATQN-SIRVAQWMLQIPGATSYMGCIGKDKFGEEMKKCATAAGVN-------------VHYYEDE 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 94 DT-----------GERTFYywRNEAAAKFW----LESEQSAAICEALatfDYLYLSGISLAIlSPTSrdklLSLLRECRA 158
Cdd:PLN02548 105 STptgtcavlvvgGERSLV--ANLSAANCYkvehLKKPENWALVEKA---KFYYIAGFFLTV-SPES----IMLVAEHAA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 159 NGGKVIFDNNYRPRLWtsrEETQQVYQKMLECTDIAFLTLDDEDAL-----WGQQPVE----KVIARTHAAGVQE--VVV 227
Cdd:PLN02548 175 ANNKTFMMNLSAPFIC---EFFKDQLMEALPYVDFLFGNETEARTFakvqgWETEDVEeialKISALPKASGTHKrtVVI 251
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526017864 228 KRGADSCLVSIQGeALIDVPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAIIP 303
Cdd:PLN02548 252 TQGADPTVVAEDG-KVKEFPVIPLPKEKLVDTNGAGDAFVGGFLSQLVQGKDIEECVRAGNYAANVIIQRSGCTYP 326
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
3-300 |
5.30e-14 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 70.54 E-value: 5.30e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 3 KKIAVIGE-CMIELSQKGadvqRGF-GGDTLNTSVYIARQ-VDSAalavhYVTALGTDSFSQQMLEAWQHENVDTSLTQR 79
Cdd:PRK09813 1 KKLATIGDnCVDIYPQLG----KAFsGGNAVNVAVYCTRYgIQPG-----CITWVGDDDYGTKLKQDLARMGVDISHVHT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 80 MENRlPGLYYIETDDtGERTFYYWRNEAAAKFWLESEQSAAICEalatFDYlylsgISLAILSPTSRDkllslLRECRAN 159
Cdd:PRK09813 72 KHGV-TAQTQVELHD-NDRVFGDYTEGVMADFALSEEDYAWLAQ----YDI-----VHAAIWGHAEDA-----FPQLHAA 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 160 GGKVIFDNNYRPR--LWtsreetqqvyQKMLECTDIAFLTLDDEDAlWGQQPVEKVIARthaaGVQEVVVKRGADSCLvS 237
Cdd:PRK09813 136 GKLTAFDFSDKWDspLW----------QTLVPHLDYAFASAPQEDE-FLRLKMKAIVAR----GAGVVIVTLGENGSI-A 199
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 526017864 238 IQGEALIDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGA 300
Cdd:PRK09813 200 WDGAQFWRQAPEPV---TVVDTMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQYHGA 259
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
1-300 |
2.23e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 69.38 E-value: 2.23e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 1 MPKKIAVIGECMIEL------------SQKGADVQRGFGGDTLNTSVYIARQVDSAALavhyVTALGTDSFSQQMLEAWQ 68
Cdd:PTZ00292 14 AEPDVVVVGSSNTDLigyvdrmpqvgeTLHGTSFHKGFGGKGANQAVMASKLGAKVAM----VGMVGTDGFGSDTIKNFK 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 69 HENVDTSLTQRMENRLPGLYYIETDDTgertfyywrneaaakfwlESEQSAAIC----EALaTFDYL------YLSGISL 138
Cdd:PTZ00292 90 RNGVNTSFVSRTENSSTGLAMIFVDTK------------------TGNNEIVIIpganNAL-TPQMVdaqtdnIQNICKY 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 139 AIL-SPTSRDKLLSLLRECRANGGKVIFDNNYRPRLWTSREETQQ-VYQKML-----ECTDIAFLTLDDEdalwgqQPVE 211
Cdd:PTZ00292 151 LICqNEIPLETTLDALKEAKERGCYTVFNPAPAPKLAEVEIIKPFlKYVSLFcvnevEAALITGMEVTDT------ESAF 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 212 KVIARTHAAGVQEVVVKRGADSCLVSIQGEALIDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTA 291
Cdd:PTZ00292 225 KASKELQQLGVENVIITLGANGCLIVEKENEPVHVPGKRV---KAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIA 301
|
....*....
gi 526017864 292 STVIQYRGA 300
Cdd:PTZ00292 302 AISVTRHGT 310
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
119-287 |
4.41e-11 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 62.46 E-value: 4.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 119 AAICEALATFDYLYLSGiSLAilSPTSRDKLLSLLRECRANGGKVIFDnnyrprlwTSREETQQVYQ------KM----L 188
Cdd:COG1105 120 ERLEELLKEGDWVVLSG-SLP--PGVPPDFYAELIRLARARGAKVVLD--------TSGEALKAALEagpdliKPnleeL 188
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 189 EctDIAFLTLDDEDAlwgqqpVEKVIARTHAAGVQEVVVKRGADSCLVSIQGEALIdvpaVKLPKEKVIDTTAAGDSFSA 268
Cdd:COG1105 189 E--ELLGRPLETLED------IIAAARELLERGAENVVVSLGADGALLVTEDGVYR----AKPPKVEVVSTVGAGDSMVA 256
|
170
....*....|....*....
gi 526017864 269 GYLAVRLTGGSATDAAKRG 287
Cdd:COG1105 257 GFLAGLARGLDLEEALRLA 275
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
27-271 |
8.15e-11 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 61.95 E-value: 8.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 27 GGDTLNTSVYIARQVDSAAlavhYVTALGTDSFSQQMLEAWQHENVDTSLTQRMENRLPGLYYIETDDTGERTFYYWRNE 106
Cdd:PLN02323 43 GGAPANVAVGISRLGGSSA----FIGKVGDDEFGHMLADILKKNGVNNEGVRFDPGARTALAFVTLRSDGEREFMFYRNP 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 107 AAAKFWLESEQSAAICEALATFDYlylSGISLaILSPtSRDKLLSLLRECRANGGKVIFDNNYRPRLWTSREETQQVYQK 186
Cdd:PLN02323 119 SADMLLRESELDLDLIRKAKIFHY---GSISL-ITEP-CRSAHLAAMKIAKEAGALLSYDPNLRLPLWPSAEAAREGIMS 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 187 MLECTDI--------AFLT-LDDEDAlwgqqpvEKVIARTHAaGVQEVVVKRGADSCLV---SIQGEalidVPAVKLpke 254
Cdd:PLN02323 194 IWDEADIikvsdeevEFLTgGDDPDD-------DTVVKLWHP-NLKLLLVTEGEEGCRYytkDFKGR----VEGFKV--- 258
|
250
....*....|....*..
gi 526017864 255 KVIDTTAAGDSFSAGYL 271
Cdd:PLN02323 259 KAVDTTGAGDAFVGGLL 275
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
54-299 |
2.25e-10 |
|
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: 60.13 E-value: 2.25e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 54 LGTDSFSQQMLEAWQHENVDTSLTQRM-ENRLPGLYYIETDdtGERTFYYWrneAAAKFWLESEQSAAIceALATFDYLY 132
Cdd:cd01944 58 LGNGNWADQIRQAMRDEGIEILLPPRGgDDGGCLVALVEPD--GERSFISI---SGAEQDWSTEWFATL--TVAPYDYVY 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 133 LSGISLAilSPTSRDKLLSLLRECRANGGKVIFDnnYRPRLwtsREETQQVYQKMLECTDIafLTLDDEDALW----GQQ 208
Cdd:cd01944 131 LSGYTLA--SENASKVILLEWLEALPAGTTLVFD--PGPRI---SDIPDTILQALMAKRPI--WSCNREEAAIfaerGDP 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 209 PVEKVIARTHAAGVQEVVVKRGADSCLVSIQGEALIDVPAVKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGH 288
Cdd:cd01944 202 AAEASALRIYAKTAAPVVVRLGSNGAWIRLPDGNTHIIPGFKV---KAVDTIGAGDTHAGGMLAGLAKGMSLADAVLLAN 278
|
250
....*....|.
gi 526017864 289 LTASTVIQYRG 299
Cdd:cd01944 279 AAAAIVVTRSG 289
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
4-301 |
1.38e-09 |
|
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: 57.81 E-value: 1.38e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 4 KIAVIG--ECMIELS-----QKGA-----DVQRGFGGDTLNTSVYIARQVDSaalaVHYVTALGTDSFSQQMLEAWQHEN 71
Cdd:cd01947 1 KIAVVGhvEWDIFLSldappQPGGishssDSRESPGGGGANVAVQLAKLGND----VRFFSNLGRDEIGIQSLEELESGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 72 VdtSLTQRMENRLPGLYYIETDDTGERTFYY-WRNEAAAKFWLEseqsaaiceaLATFDYLYLSgiSLAILSPTsrdkll 150
Cdd:cd01947 77 D--KHTVAWRDKPTRKTLSFIDPNGERTITVpGERLEDDLKWPI----------LDEGDGVFIT--AAAVDKEA------ 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 151 slLRECRaNGGKVIFDNNYRPRLWTSREETQQVyqKMLECTDIAFLTLDDEDALWGQQPvekviaRThaagvqeVVVKRG 230
Cdd:cd01947 137 --IRKCR-ETKLVILQVTPRVRVDELNQALIPL--DILIGSRLDPGELVVAEKIAGPFP------RY-------LIVTEG 198
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526017864 231 ADSCLVSIQGEALidvpAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGAI 301
Cdd:cd01947 199 ELGAILYPGGRYN----HVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSHFGPY 265
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
123-287 |
1.60e-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: 54.85 E-value: 1.60e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 123 EALATFDYLYLSGiSL-AILSPtsrDKLLSLLRECRANGGKVIFDnnyrprlwTSREETQQVYQ------KM--LECTDI 193
Cdd:cd01164 124 ALLKKGDIVVLSG-SLpPGVPA---DFYAELVRLAREKGARVILD--------TSGEALLAALAakpfliKPnrEELEEL 191
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 194 AFLTLDDEDAlwgqqpVEKVIARTHAAGVQEVVVKRGADSCLVSIQGEALIdvpaVKLPKEKVIDTTAAGDSFSAGYLAV 273
Cdd:cd01164 192 FGRPLGDEED------VIAAARKLIERGAENVLVSLGADGALLVTKDGVYR----ASPPKVKVVSTVGAGDSMVAGFVAG 261
|
170
....*....|....
gi 526017864 274 RLTGGSATDAAKRG 287
Cdd:cd01164 262 LAQGLSLEEALRLA 275
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
26-300 |
2.05e-08 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 54.49 E-value: 2.05e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 26 FGGDTLNTSVYIARqvdSAAlAVHYVTALGTDSFSQQMLEAWQHENVDTSLTQRMENRLPGLYYIETDDTGErtfyywrN 105
Cdd:PRK11142 38 FGGKGANQAVAAAR---LGA-DIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGESTGVALIFVNDEGE-------N 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 106 ----EAAAKFWLESEQSAAICEALATFDYLylsgisLAIL-SPTsrDKLLSLLRECRANGGKVIFdnNYRPrlwtsreeT 180
Cdd:PRK11142 107 sigiHAGANAALTPALVEAHRELIANADAL------LMQLeTPL--ETVLAAAKIAKQHGTKVIL--NPAP--------A 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 181 QQVYQKMLECTDI--------AFLT----LDDEDAlwgqqpvEKVIARTHAAGVQEVVVKRGADSCLVSIQGEALIdVPA 248
Cdd:PRK11142 169 RELPDELLALVDIitpneteaEKLTgirvEDDDDA-------AKAAQVLHQKGIETVLITLGSRGVWLSENGEGQR-VPG 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 526017864 249 VKLpkeKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGA 300
Cdd:PRK11142 241 FRV---QAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAAIAVTRKGA 289
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
17-286 |
3.69e-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: 53.45 E-value: 3.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 17 QKGADVQRGFGGDTLNTSVYIARQVDSAALavhyVTALGTDSFSQQMLEAWQHENVDTSLTQRMENRLPGLYYIeTDDTG 96
Cdd:cd01945 26 IVATDYAVIGGGNAANAAVAVARLGGQARL----IGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSI-TDITG 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 97 ER--TFYYWRNEAAAKFWLESeqsaaicEALATFDYLYLSGislailspTSRDKLLSLLRECRANGGKVIFDNNyRPRLW 174
Cdd:cd01945 101 DRatISITAIDTQAAPDSLPD-------AILGGADAVLVDG--------RQPEAALHLAQEARARGIPIPLDLD-GGGLR 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 175 TSREetqqvyqkMLECTDIAFLTlddEDAL--WGQQPVEKVIARTHAAGVQEVVVKRGADSCLVSIQGEALIDVPAvklP 252
Cdd:cd01945 165 VLEE--------LLPLADHAICS---ENFLrpNTGSADDEALELLASLGIPFVAVTLGEAGCLWLERDGELFHVPA---F 230
|
250 260 270
....*....|....*....|....*....|....
gi 526017864 253 KEKVIDTTAAGDSFSAGYlAVRLTGGSATDAAKR 286
Cdd:cd01945 231 PVEVVDTTGAGDVFHGAF-AHALAEGMPLREALR 263
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
115-309 |
5.92e-08 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 53.68 E-value: 5.92e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 115 SEQSAAICEALATFDYLYLSGISLAILSPtsrDKLLSLLRECRANGGKVIFDNNYRPR-LWTSREETQQVYQKMLECTDI 193
Cdd:PLN02341 212 SKLSAEAKMAIRQSKALFCNGYVFDELSP---SAIASAVDYAIDVGTAVFFDPGPRGKsLLVGTPDERRALEHLLRMSDV 288
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 194 AFLTLDDEDALWG-QQPVE--KVIARThAAGVQEVVVKRGAD-SCLVSIQGEALidVPAvklPKEKVIDTTAAGDSFSA- 268
Cdd:PLN02341 289 LLLTSEEAEALTGiRNPILagQELLRP-GIRTKWVVVKMGSKgSILVTRSSVSC--APA---FKVNVVDTVGCGDSFAAa 362
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 526017864 269 ---GYL-------------AVrltgGSATD---AAKRGHLTASTVIQ-YRGAIIPHDAMPQ 309
Cdd:PLN02341 363 ialGYIhnlplvntltlanAV----GAATAmgcGAGRNVATLEKVLElLRASNLNEDDTFW 419
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
192-296 |
3.10e-07 |
|
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: 50.78 E-value: 3.10e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 192 DIAFLTLDDEDALWGQ-----QPVEKVIARTHAAGVQEVVVKRGADSCLVSIQGEALI--DVPAVKlpKEKVIDTTAAGD 264
Cdd:cd01941 178 DLLTPNRAELEALAGAliennEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVEtkLFPAPQ--PETVVNVTGAGD 255
|
90 100 110
....*....|....*....|....*....|..
gi 526017864 265 SFSAGYLAVRLTGGSATDAAKRGHLTASTVIQ 296
Cdd:cd01941 256 AFVAGLVAGLLEGMSLDDSLRFAQAAAALTLE 287
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
225-299 |
2.45e-05 |
|
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: 45.41 E-value: 2.45e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 526017864 225 VVVKRGADSCLV-SIQGEALIDVPAVKLPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRG 299
Cdd:cd01943 228 VVLRCGKLGCYVgSADSGPELWLPAYHTKSTKVVDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVG 303
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
24-193 |
3.92e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 44.90 E-value: 3.92e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 24 RGFGGDTLNTSVYIARQVDSAAlavhYVTALGTDSFSQQMLEAWQHENVDTSLTQRMENRLPGLYYIETD-DTGERTFYY 102
Cdd:PLN02543 169 RAPGGPPSNVAISHVRLGGRAA----FMGKVGDDDFGEELVLMMNKERVQTRAVKFDENAKTACSRMKIKfRDGGKMVAE 244
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 103 WRNEAAAKFWLESEQSAAICEALATFDYlylsgISLAILSPTSRDKLLSLLRECRANGGKVIFDNNYRPRLWTSREETQQ 182
Cdd:PLN02543 245 TVKEAAEDSLLASELNLAVLKEARMFHF-----NSEVLTSPSMQSTLFRAIELSKKFGGLIFFDLNLPLPLWRSRDETRE 319
|
170
....*....|.
gi 526017864 183 VYQKMLECTDI 193
Cdd:PLN02543 320 LIKKAWNEADI 330
|
|
| PLN02967 |
PLN02967 |
kinase |
24-212 |
6.11e-05 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 44.27 E-value: 6.11e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 24 RGFGGDTLNTSVYIArqvdSAALAVHYVTALGTDSFSQQMLEAWQHENVDTSLTQRMENRLPGLYYIETDDTGERTFYYW 103
Cdd:PLN02967 240 RAPGGSAGGVAIALA----SLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQTRSVCIDGKRATAVSTMKIAKRGRLKTTCV 315
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 104 RNEAAAKFwLESEQSAAICEALATFdylYLSgiSLAILSPTSRDKLLSLLRECRANGGKVIFDNNYRPRLWTSREETQQV 183
Cdd:PLN02967 316 KPCAEDSL-SKSEINIDVLKEAKMF---YFN--THSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLPLPLWSSSEETKSF 389
|
170 180
....*....|....*....|....*....
gi 526017864 184 YQKMLECTDIAFLTLDDEDALWGQQPVEK 212
Cdd:PLN02967 390 IQEAWNLADIIEVTKQELEFLCGIEPTEE 418
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
147-299 |
7.88e-05 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 43.63 E-value: 7.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 147 DKLLSLLRECRANGGKVIFD-------NNYRPRLwtsreetqqvyQKMLECTDIAFLTLDDEDA---LWGQQPVEKVIAR 216
Cdd:PLN02379 191 EVIEAAIRLAKQEGLSVSLDlasfemvRNFRSPL-----------LQLLESGKIDLCFANEDEArelLRGEQESDPEAAL 259
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 217 THAAG-VQEVVVKRGADSCLVSiQGEALIDVPAVKlpKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVI 295
Cdd:PLN02379 260 EFLAKyCNWAVVTLGSKGCIAR-HGKEVVRVPAIG--ETNAVDATGAGDLFASGFLYGLIKGLSLEECCKVGACSGGSVV 336
|
....
gi 526017864 296 QYRG 299
Cdd:PLN02379 337 RALG 340
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
181-306 |
3.49e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 41.72 E-value: 3.49e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 181 QQVYQKMLECTDIAFLTLDDEDALWGQQPVEKVI--ARTHAAGVQEVVVKRGADSCLVSIQGEALIDVPAVKLPkekvID 258
Cdd:PLN02813 273 DDFWDVMGNYADILFANSDEARALCGLGSEESPEsaTRYLSHFCPLVSVTDGARGSYIGVKGEAVYIPPSPCVP----VD 348
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 526017864 259 TTAAGDSFSAGYLAVRLTGgsATDAAKRGHLT---ASTVIQYRGAIIPHDA 306
Cdd:PLN02813 349 TCGAGDAYAAGILYGLLRG--VSDLRGMGELAarvAATVVGQQGTRLRVED 397
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
218-306 |
9.58e-04 |
|
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: 40.24 E-value: 9.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 218 HAAGVQEVVVKRGADSCLVSIQGEALIDVPAVKLPkekVIDTTAAGDSFSAGYLAVRLTGGSATDAAKRGHLTASTVIQY 297
Cdd:cd01172 215 ELLNLEALLVTLGEEGMTLFERDGEVQHIPALAKE---VYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGVVVGK 291
|
....*....
gi 526017864 298 RGAIIPHDA 306
Cdd:cd01172 292 VGTAPVTPK 300
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
192-295 |
1.06e-03 |
|
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: 40.08 E-value: 1.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 192 DIAFLTLDDEDALWGQQPVEkvIARTHAA-GVQEVVVKRGADSCLVsIQGEALIDVPAvklPKEKVIDTTAAGDSFSAGY 270
Cdd:cd01937 155 LHDVLKLSRVEAEVISTPTE--LARLIKEtGVKEIIVTDGEEGGYI-FDGNGKYTIPA---SKKDVVDPTGAGDVFLAAF 228
|
90 100
....*....|....*....|....*
gi 526017864 271 LAVRLTGGSATDAAKRGHLTASTVI 295
Cdd:cd01937 229 LYSRLSGKDIKEAAEFAAAAAAKFI 253
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
173-296 |
1.40e-03 |
|
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: 39.76 E-value: 1.40e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 173 LW--TSREETQQVYQKMlectDIafLTLDDEDA--LWGQQPVEKVIARTHAAGVQEVVVKRGADSCLVSIQgEALIDVPA 248
Cdd:cd01946 148 FWisIKPEKLKKVLAKV----DV--VIINDGEArqLTGAANLVKAARLILAMGPKALIIKRGEYGALLFTD-DGYFAAPA 220
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 526017864 249 vkLPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAKR-----GHLTASTVIQ 296
Cdd:cd01946 221 --YPLESVFDPTGAGDTFAGGFIGYLASQKDTSEANMRraiiyGSAMASFCVE 271
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
172-285 |
4.17e-03 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 38.37 E-value: 4.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 172 RLWTSREETQQVYQKMLECtdiafltlddedaLWGQqPVEKVIART------HAAGVQEVVVKRGADSCLVSIQ-GEALI 244
Cdd:PRK09954 228 KHWLAHIHTLKPTQPELEI-------------LWGQ-AITSDADRNaavnalHQQGVQQIFVYLPDESVFCSEKdGEQFL 293
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 526017864 245 DVPavklPKEKVIDTTAAGDSFSAGYLAVRLTGGSATDAAK 285
Cdd:PRK09954 294 LTA----PAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSAR 330
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
187-304 |
7.56e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 37.48 E-value: 7.56e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 526017864 187 MLEctDIAFLTLDDEDALWgqQPVEKVIARTHaagvqeVVVKRGADSCLVSIQ-GEALID-VPAVKlpkekvIDTTAAGD 264
Cdd:PLN02630 178 MLP--RIGFLKASSEEALF--IDVEEVRQKCC------VIVTNGKKGCRIYWKdGEMRVPpFPAIQ------VDPTGAGD 241
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 526017864 265 SFSAGYLAVRLTGGSATDAAKRGHLTASTVIQYRGaiIPH 304
Cdd:PLN02630 242 SFLGGFVAGLVQGLAVPDAALLGNYFGSLAVEQVG--IPK 279
|
|
| |
