|
Name |
Accession |
Description |
Interval |
E-value |
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
5-317 |
3.62e-119 |
|
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: 345.75 E-value: 3.62e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 5 DLFAIGNALIDQEFKVSDDFLSQQGLQKGTMQLSDGETQSALYEKLKQTQdykgqASGGSAANTTVAFSALGGSAFYGCR 84
Cdd:cd01168 3 DVLGLGNALVDILAQVDDAFLEKLGLKKGDMILADMEEQEELLAKLPVKY-----IAGGSAANTIRGAAALGGSAAFIGR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 85 VGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISPDSERTMHTYLGITAELSQDQIDFEPLKTAKWLYIEGYLST 164
Cdd:cd01168 78 VGDDKLGDFLLKDLRAAGVDTRYQVQPDGPTGTCAVLVTPDAERTMCTYLGAANELSPDDLDWSLLAKAKYLYLEGYLLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 165 SETarKAVKQAREIAKAHGVKIALSLSDPAMVQYAREGLEELMdDGVDLLFCNEQEALMYTNTTT---VEDALTQLRFKN 241
Cdd:cd01168 158 VPP--EAILLAAEHAKENGVKIALNLSAPFIVQRFKEALLELL-PYVDILFGNEEEAEALAEAETtddLEAALKLLALRC 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446168811 242 HTVVITQSAKGALVANPTHHFHVAG-RHVEAVDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFGPRL 317
Cdd:cd01168 235 RIVVITQGAKGAVVVEGGEVYPVPAiPVEKIVDTNGAGDAFAGGFLYGLVQGEPLEECIRLGSYAAAEVIQQLGPRL 311
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
5-325 |
1.10e-76 |
|
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: 237.09 E-value: 1.10e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 5 DLFAIGNALIDQEFKVSddflsqqGLQKGTMQLSDGETQSALyeklkqtqdykgqasGGSAANTTVAFSALGGSAFYGCR 84
Cdd:COG0524 1 DVLVIGEALVDLVARVD-------RLPKGGETVLAGSFRRSP---------------GGAAANVAVALARLGARVALVGA 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 85 VGHDELGGIYLQGLNDAGIQTTPKSISEGV-TGTCMVLISPDSERTMHTYLGITAELSQDQIDFEPLKTAKWLYIEGYLS 163
Cdd:COG0524 59 VGDDPFGDFLLAELRAEGVDTSGVRRDPGApTGLAFILVDPDGERTIVFYRGANAELTPEDLDEALLAGADILHLGGITL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 164 TSETARKAVKQAREIAKAHGVKIALSLSD-PAMVQYAREGLEELMDdGVDLLFCNEQEALMYTNTTTVEDALTQLRFKN- 241
Cdd:COG0524 139 ASEPPREALLAALEAARAAGVPVSLDPNYrPALWEPARELLRELLA-LVDILFPNEEEAELLTGETDPEEAAAALLARGv 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 242 HTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFGPRLAIND 321
Cdd:COG0524 218 KLVVVTLGAEGALLYTGGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
....
gi 446168811 322 YAKL 325
Cdd:COG0524 298 REEV 301
|
|
| PLN02813 |
PLN02813 |
pfkB-type carbohydrate kinase family protein |
5-329 |
2.84e-56 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215434 [Multi-domain] Cd Length: 426 Bit Score: 188.48 E-value: 2.84e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 5 DLFAIGNALIDQEFKVSDDFLSQQGLQKGTMQLSDGETQSALYEKLkQTQDYKGQAsGGSAANTTVAFSALGGSAFYGCR 84
Cdd:PLN02813 71 DVLGLGQAMVDFSGMVDDEFLERLGLEKGTRKVINHEERGKVLRAL-DGCSYKASA-GGSLSNTLVALARLGSQSAAGPA 148
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 85 --------VGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISPDSERTMHTYLGITAELSQDQIDFEPLKTAKWL 156
Cdd:PLN02813 149 lnvamagsVGSDPLGDFYRTKLRRANVHFLSQPVKDGTTGTVIVLTTPDAQRTMLSYQGTSSTVNYDSCLASAISKSRVL 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 157 YIEGYLSTSETARKAVKQAREIAKAHGVKIALSLSDPAMVQYAREGLEELMDDGVDLLFCNEQEALMYTNTTTVEDALTQ 236
Cdd:PLN02813 229 VVEGYLWELPQTIEAIAQACEEAHRAGALVAVTASDVSCIERHRDDFWDVMGNYADILFANSDEARALCGLGSEESPESA 308
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 237 LRFKNH---TVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYA-LNHHEDLTAAAQLAILISSEVVSQ 312
Cdd:PLN02813 309 TRYLSHfcpLVSVTDGARGSYIGVKGEAVYIPPSPCVPVDTCGAGDAYAAGILYGlLRGVSDLRGMGELAARVAATVVGQ 388
|
330
....*....|....*..
gi 446168811 313 FGPRLAINDYAKLLENF 329
Cdd:PLN02813 389 QGTRLRVEDAVELAESF 405
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
62-316 |
3.59e-53 |
|
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: 176.61 E-value: 3.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTT-PKSISEGVTGTCMVLISPDSERTMHTYLGITA-- 138
Cdd:cd01166 31 GGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTShVRVDPGRPTGLYFLEIGAGGERRVLYYRAGSAas 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 139 ELSQDQIDFEPLKTAKWLYIEGY-LSTSETARKAVKQAREIAKAHGVKIALSL-SDPAM--VQYAREGLEELMDdGVDLL 214
Cdd:cd01166 111 RLTPEDLDEAALAGADHLHLSGItLALSESAREALLEALEAAKARGVTVSFDLnYRPKLwsAEEAREALEELLP-YVDIV 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 215 FCNEQEALMYTNTTTVEDALTQLRFKNH---TVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNH 291
Cdd:cd01166 190 LPSEEEAEALLGDEDPTDAAERALALALgvkAVVVKLGAEGALVYTGGGRVFVPAYPVEVVDTTGAGDAFAAGFLAGLLE 269
|
250 260
....*....|....*....|....*
gi 446168811 292 HEDLTAAAQLAILISSEVVSQFGPR 316
Cdd:cd01166 270 GWDLEEALRFANAAAALVVTRPGDI 294
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
62-317 |
7.49e-47 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 160.20 E-value: 7.49e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGV-TGTCMVLISPDSERTMHTYLGITAEL 140
Cdd:pfam00294 34 GGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDYVVIDEDTrTGTALIEVDGDGERTIVFNRGAAADL 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 141 SQD--QIDFEPLKTAKWLYIEGYLSTsETARKAVKQAREIAKAHGVKIaLSLSDPAMVqyAREGLEELMDdGVDLLFCNE 218
Cdd:pfam00294 114 TPEelEENEDLLENADLLYISGSLPL-GLPEATLEELIEAAKNGGTFD-PNLLDPLGA--AREALLELLP-LADLLKPNE 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 219 QEALMYTNT--TTVEDALTQLRFKNH----TVVITQSAKGALVANP-THHFHVAGRHVEAVDTNGAGDAFAGAFLYALNH 291
Cdd:pfam00294 189 EELEALTGAklDDIEEALAALHKLLAkgikTVIVTLGADGALVVEGdGEVHVPAVPKVKVVDTTGAGDSFVGGFLAGLLA 268
|
250 260
....*....|....*....|....*.
gi 446168811 292 HEDLTAAAQLAILISSEVVSQFGPRL 317
Cdd:pfam00294 269 GKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
1-314 |
1.80e-37 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 137.08 E-value: 1.80e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 1 MATVDLFAIGNALIDQEFKVSDDFLSQQGLQKGTMQLSDgETQSALYEKLKQ--TQDYkgqASGGSAANTT-----VAFS 73
Cdd:PTZ00247 3 SAPKKLLGFGNPLLDISAHVSDEFLEKYGLELGSAILAE-EKQLPIFEELESipNVSY---VPGGSALNTArvaqwMLQA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 74 ALGGSAFYGCrVGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISpDSERTMHTYLGITAELSQDQID----FEP 149
Cdd:PTZ00247 79 PKGFVCYVGC-VGDDRFAEILKEAAEKDGVEMLFEYTTKAPTGTCAVLVC-GKERSLVANLGAANHLSAEHMQshavQEA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 150 LKTAKWLYIEGYLSTseTARKAVKQAREIAKAHGVKIALSLSDPAMVQYAREGLEELMDDgVDLLFCNEQEALMYTN--- 226
Cdd:PTZ00247 157 IKTAQLYYLEGFFLT--VSPNNVLQVAKHARESGKLFCLNLSAPFISQFFFERLLQVLPY-VDILFGNEEEAKTFAKamk 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 227 ---TTTVEDALTQLRFKNHT------VVITQSAKGALVANPTHHFHVAGRHVEA---VDTNGAGDAFAGAFLYALNHHED 294
Cdd:PTZ00247 234 wdtEDLKEIAARIAMLPKYSgtrprlVVFTQGPEPTLIATKDGVTSVPVPPLDQekiVDTNGAGDAFVGGFLAQYANGKD 313
|
330 340
....*....|....*....|
gi 446168811 295 LTAAAQLAILISSEVVSQFG 314
Cdd:PTZ00247 314 IDRCVEAGHYSAQVIIQHNG 333
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
62-314 |
2.20e-37 |
|
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: 135.46 E-value: 2.20e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGG-SAFYGCrVGHDELGGIYLQGLNDAGIQTTP-KSISEGVTGTCMVLISPDSERTMHTYLGITAE 139
Cdd:cd01167 28 GGAPANVAVALARLGGkAAFIGK-VGDDEFGDFLLETLKEAGVDTRGiQFDPAAPTTLAFVTLDADGERSFEFYRGPAAD 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 140 LSQD-QIDFEPLKTAKWLYIeGYLS-TSETARKAVKQAREIAKAHGVKIA------LSLSDPAMVqyAREGLEELMDdGV 211
Cdd:cd01167 107 LLLDtELNPDLLSEADILHF-GSIAlASEPSRSALLELLEAAKKAGVLISfdpnlrPPLWRDEEE--ARERIAELLE-LA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 212 DLLFCNEQEALMYTNTTTVEDALTQLRFKN-HTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYAL- 289
Cdd:cd01167 183 DIVKLSDEELELLFGEEDPEEIAALLLLFGlKLVLVTRGADGALLYTKGGVGEVPGIPVEVVDTTGAGDAFVAGLLAQLl 262
|
250 260 270
....*....|....*....|....*....|.
gi 446168811 290 ------NHHEDLTAAAQLAILISSEVVSQFG 314
Cdd:cd01167 263 srgllaLDEDELAEALRFANAVGALTCTKAG 293
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
62-316 |
4.88e-36 |
|
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: 131.28 E-value: 4.88e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGSA-FYGCrVGHDELGGIYLQGLNDAGIQT-TPKSISEGVTGTCMVLISPDSERTMHTYLGITAE 139
Cdd:cd01942 36 GGSAGNTAVALAKLGLSPgLVAA-VGEDFHGRLYLEELREEGVDTsHVRVVDEDSTGVAFILTDGDDNQIAYFYPGAMDE 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 140 LSQDQIDFEPLKTAkwlyiegYLSTSeTARKAVKQAREIAKAhgvKIALSLsDP--AMVQYAREGLEElMDDGVDLLFCN 217
Cdd:cd01942 115 LEPNDEADPDGLAD-------IVHLS-SGPGLIELARELAAG---GITVSF-DPgqELPRLSGEELEE-ILERADILFVN 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 218 EQEALMY---TNTTTVEDALtqlrfKNHTVVITQSAKGALVANPTHHFHVAGRH-VEAVDTNGAGDAFAGAFLYALNHHE 293
Cdd:cd01942 182 DYEAELLkerTGLSEAELAS-----GVRVVVVTLGPKGAIVFEDGEEVEVPAVPaVKVVDTTGAGDAFRAGFLYGLLRGY 256
|
250 260
....*....|....*....|...
gi 446168811 294 DLTAAAQLAILISSEVVSQFGPR 316
Cdd:cd01942 257 DLEESLRLGNLAASLKVERRGAQ 279
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
62-314 |
5.23e-36 |
|
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: 131.52 E-value: 5.23e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGV-TGTCMVLISPDSERTMHTYLGITAEL 140
Cdd:cd01174 36 GGKGANQAVAAARLGARVAMIGAVGDDAFGDELLENLREEGIDVSYVEVVVGApTGTAVITVDESGENRIVVVPGANGEL 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 141 SQDQID--FEPLKTAKWLYIEGylstsETARKAVKQAREIAKAHGVKIALslsDPAMvqyAREGLEELMDDgVDLLFCNE 218
Cdd:cd01174 116 TPADVDaaLELIAAADVLLLQL-----EIPLETVLAALRAARRAGVTVIL---NPAP---ARPLPAELLAL-VDILVPNE 183
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 219 QEALMYTNTTTVE--------DALTQLRFKNhtVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALN 290
Cdd:cd01174 184 TEAALLTGIEVTDeedaekaaRLLLAKGVKN--VIVTLGAKGALLASGGEVEHVPAFKVKAVDTTGAGDTFIGALAAALA 261
|
250 260
....*....|....*....|....
gi 446168811 291 HHEDLTAAAQLAILISSEVVSQFG 314
Cdd:cd01174 262 RGLSLEEAIRFANAAAALSVTRPG 285
|
|
| D_ribokin_bact |
TIGR02152 |
ribokinase; This model describes ribokinase, an enzyme catalyzing the first step in ribose ... |
40-314 |
4.88e-34 |
|
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: 126.56 E-value: 4.88e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 40 GETQSAlyeklkqtQDYKgQASGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTP-KSISEGVTGTC 118
Cdd:TIGR02152 18 GETVHG--------HSFQ-IGPGGKGANQAVAAARLGAEVSMIGKVGDDAFGDELLENLKSNGIDTEYvGTVKDTPTGTA 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 119 MVLISPDSERTMHTYLGITAELSQDQID--FEPLKTAKWLYIEGylstsETARKAVKQAREIAKAHGVKIALslsDPAMv 196
Cdd:TIGR02152 89 FITVDDTGENRIVVVAGANAELTPEDIDaaEALIAESDIVLLQL-----EIPLETVLEAAKIAKKHGVKVIL---NPAP- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 197 qyAREGLEELMDDGVDLLFCNEQEALMYTNTT-----TVEDALTQLRFKN-HTVVITQSAKGALVANPTHHFHVAGRHVE 270
Cdd:TIGR02152 160 --AIKDLDDELLSLVDIITPNETEAEILTGIEvtdeeDAEKAAEKLLEKGvKNVIITLGSKGALLVSKDESKLIPAFKVK 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 446168811 271 AVDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFG 314
Cdd:TIGR02152 238 AVDTTAAGDTFNGAFAVALAEGKSLEDAIRFANAAAAISVTRKG 281
|
|
| myo_inos_iolC_N |
TIGR04382 |
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are ... |
62-327 |
6.71e-27 |
|
5-dehydro-2-deoxygluconokinase; All members of the seed alignment for this model are translated from the iolC gene of known or putative inositol catabolism operons. Members with characterized function are 5-dehydro-2-deoxygluconokinase, the enzyme catalyzing the fifth step in degradation from myo-inositol or closely related compounds. Note that many members of this family are fusion proteins with an additional C-terminal domain, of unknown function, described by pfam09863. [Energy metabolism, Sugars]
Pssm-ID: 275175 [Multi-domain] Cd Length: 309 Bit Score: 107.68 E-value: 6.71e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGG-SAFYGCrVGHDELGGIYLQGLNDAGIQTTP-KSISEGVTGTCMVLISPDSERTMHTYLGITA- 138
Cdd:TIGR04382 34 GGSPANIAVGAARLGLkTAFITR-VGDDQFGRFVRDYLRREGVDTSHvVTDPGRRTSLVFLEIKPPDEFPLLFYRENAAd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 139 -ELSQDQIDFEPLKTAKWLYIEGYLSTSETARKAVKQAREIAKAHGVKIALSL--------SDPAMVQYAREGLEElmdd 209
Cdd:TIGR04382 113 lALTPDDVDEDYIASARALLVSGTALSQEPSREAVLKALEYARAAGVRVVLDIdyrpylwkSPEEAGIYLRLVLPL---- 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 210 gVDLLFCNEQEALMYTNTTTVEDALTQLR-FKNHTVVITQSAKGALV-ANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLY 287
Cdd:TIGR04382 189 -VDVIIGTREEFDIAGGEGDDEAAARALLdAGVEILVVKRGPEGSLVyTGDGEGVEVPGFPVEVLNVLGAGDAFASGFLY 267
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 446168811 288 ALNHHEDLTAAAQLAILISSEVVSQFGPRLAINDYAKLLE 327
Cdd:TIGR04382 268 GLLAGWDLEKALRYGNACGAIVVSRHSCSPAMPTLEELEA 307
|
|
| PRK09434 |
PRK09434 |
aminoimidazole riboside kinase; Provisional |
59-306 |
1.47e-25 |
|
aminoimidazole riboside kinase; Provisional
Pssm-ID: 236514 [Multi-domain] Cd Length: 304 Bit Score: 103.86 E-value: 1.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 59 QASGGSAANTTVAFSALGG-SAFYGcRVGHDELGGIYLQGLNDAGIQTTPKSISEGV-TGTCMVLISPDSERTMhTYLgi 136
Cdd:PRK09434 25 KCPGGAPANVAVGIARLGGeSGFIG-RVGDDPFGRFMQQTLQDEGVDTTYLRLDPAHrTSTVVVDLDDQGERSF-TFM-- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 137 tAELSQDQI----DFEPLKTAKWLYIEGYLSTSETARKAVKQAREIAKAHGVKIALslsDPAMvqyaREGL---EELMDD 209
Cdd:PRK09434 101 -VRPSADLFlqpqDLPPFRQGEWLHLCSIALSAEPSRSTTFEAMRRIKAAGGFVSF---DPNL----REDLwqdEAELRE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 210 GV-------DLLFCNEQEALMYTNTTTVEDALTQL--RFKNHTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDA 280
Cdd:PRK09434 173 CLrqalalaDVVKLSEEELCFLSGTSQLEDAIYALadRYPIALLLVTLGAEGVLVHTRGQVQHFPAPSVDPVDTTGAGDA 252
|
250 260
....*....|....*....|....*.
gi 446168811 281 FAGAFLYALNHHEDLTAAAQLAILIS 306
Cdd:PRK09434 253 FVAGLLAGLSQAGLWTDEAELAEIIA 278
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
12-289 |
5.83e-24 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 100.64 E-value: 5.83e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 12 ALIDQEFKVSDDFLSQ-QGLQKGTMQLSDGETQSALYEKLKQTQDYKGQAS------GGSAANTTVAFSA-LGGS-AFYG 82
Cdd:PLN02379 29 ALVDHVARVDWSLLDQiPGDRGGSIRVTIEELEHILREVNAHILPSPDDLSpiktmaGGSVANTIRGLSAgFGVStGIIG 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 83 CRvGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISPDSERTMHTYLGITAELSQDQIDFEPLKTAKWLYIEGYL 162
Cdd:PLN02379 109 AC-GDDEQGKLFVSNMGFSGVDLSRLRAKKGPTAQCVCLVDALGNRTMRPCLSSAVKLQADELTKEDFKGSKWLVLRYGF 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 163 STSETARKAVKqareIAKAHGVKIALSLSDPAMVQYAREGLEELMDDG-VDLLFCNEQEA---LMYTNTTTVEDALTQLR 238
Cdd:PLN02379 188 YNLEVIEAAIR----LAKQEGLSVSLDLASFEMVRNFRSPLLQLLESGkIDLCFANEDEArelLRGEQESDPEAALEFLA 263
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 446168811 239 FKNHTVVITQSAKGALVANPTHHFHV-AGRHVEAVDTNGAGDAFAGAFLYAL 289
Cdd:PLN02379 264 KYCNWAVVTLGSKGCIARHGKEVVRVpAIGETNAVDATGAGDLFASGFLYGL 315
|
|
| YegV_kinase_like |
cd01944 |
YegV-like sugar kinase. Found only in bacteria, YegV-like kinase is part of the ribokinase ... |
63-314 |
7.36e-22 |
|
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: 93.64 E-value: 7.36e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 63 GSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISPDSERTMHTYLGITAELSQ 142
Cdd:cd01944 36 GGGFNVMVAASRLGIPTVNAGPLGNGNWADQIRQAMRDEGIEILLPPRGGDDGGCLVALVEPDGERSFISISGAEQDWST 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 143 DQIDFEPLKTAKWLYIEGYLSTSETARKAVKQAREIAKAHGVKIALSLSdPAMVQYAREGLEELMDDGVdLLFCNEQEAL 222
Cdd:cd01944 116 EWFATLTVAPYDYVYLSGYTLASENASKVILLEWLEALPAGTTLVFDPG-PRISDIPDTILQALMAKRP-IWSCNREEAA 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 223 MYTNTTTVEDALTQLRF---KNHTVVITQSAKGALVANP---THHfhVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLT 296
Cdd:cd01944 194 IFAERGDPAAEASALRIyakTAAPVVVRLGSNGAWIRLPdgnTHI--IPGFKVKAVDTIGAGDTHAGGMLAGLAKGMSLA 271
|
250
....*....|....*...
gi 446168811 297 AAAQLAILISSEVVSQFG 314
Cdd:cd01944 272 DAVLLANAAAAIVVTRSG 289
|
|
| PLN02548 |
PLN02548 |
adenosine kinase |
9-295 |
4.25e-21 |
|
adenosine kinase
Pssm-ID: 178163 [Multi-domain] Cd Length: 332 Bit Score: 92.09 E-value: 4.25e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 9 IGNALIDQEFKVSDDFLSQQGLQKGTMQLSDgETQSALYEKLKQTQDYKGQAsGGSAANTT-VA---FSALGGSAFYGCr 84
Cdd:PLN02548 1 MGNPLLDISAVVDQDFLDKYDVKLNNAILAE-EKHLPMYDELASKYNVEYIA-GGATQNSIrVAqwmLQIPGATSYMGC- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 85 VGHDELGGIYLQGLNDAGI-------QTTPksisegvTGTCMVLISpDSERTMHTYLGITAELSQDQID----FEPLKTA 153
Cdd:PLN02548 78 IGKDKFGEEMKKCATAAGVnvhyyedESTP-------TGTCAVLVV-GGERSLVANLSAANCYKVEHLKkpenWALVEKA 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 154 KWLYIEGYLST--SETARKAVKQAREIAKAHgvkiALSLSDPAMVQYAREGLEELMDdGVDLLFCNEQEALMY------- 224
Cdd:PLN02548 150 KFYYIAGFFLTvsPESIMLVAEHAAANNKTF----MMNLSAPFICEFFKDQLMEALP-YVDFLFGNETEARTFakvqgwe 224
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 225 -TNTTTVEDALTQLRFKN----HTVVITQSAKGALVAnpthhfhVAGRHVE----------AVDTNGAGDAFAGAFLYAL 289
Cdd:PLN02548 225 tEDVEEIALKISALPKASgthkRTVVITQGADPTVVA-------EDGKVKEfpviplpkekLVDTNGAGDAFVGGFLSQL 297
|
....*.
gi 446168811 290 NHHEDL 295
Cdd:PLN02548 298 VQGKDI 303
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
55-302 |
4.63e-21 |
|
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: 91.20 E-value: 4.63e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 55 DYKGQAsGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISPDSERTMHTYL 134
Cdd:cd01945 30 DYAVIG-GGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIVVAPGARSPISSITDITGDRATISIT 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 135 GITAELSQDQIDFEPLKTAKWLYIEGYLStsETARKAVKQAReiakAHGVKIALSLsDPAMVqyarEGLEELMDdGVDLL 214
Cdd:cd01945 109 AIDTQAAPDSLPDAILGGADAVLVDGRQP--EAALHLAQEAR----ARGIPIPLDL-DGGGL----RVLEELLP-LADHA 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 215 FCNEQEALmyTNTTTVEDALTQL--RFKNHTVVITQSAKGALVANPT-HHFHVAGRHVEAVDTNGAGDAFAGAFLYALNH 291
Cdd:cd01945 177 ICSENFLR--PNTGSADDEALELlaSLGIPFVAVTLGEAGCLWLERDgELFHVPAFPVEVVDTTGAGDVFHGAFAHALAE 254
|
250
....*....|.
gi 446168811 292 HEDLTAAAQLA 302
Cdd:cd01945 255 GMPLREALRFA 265
|
|
| PRK15074 |
PRK15074 |
inosine/guanosine kinase; Provisional |
9-225 |
9.92e-21 |
|
inosine/guanosine kinase; Provisional
Pssm-ID: 185033 Cd Length: 434 Bit Score: 92.38 E-value: 9.92e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 9 IGNALIDQEFKVSDDFLSQQGLQKGTMQLSDGETQSALYEKLKQTQDYKGQASGGSAANTTVAFSAL------------- 75
Cdd:PRK15074 39 IDQTLVDIEAKVDDEFLERYGLSKGHSLVIEDDVAEALYQELKQNNLITHEFAGGTIGNTLHNYSVLaddrsvllgvmss 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 76 ----GGSAF-YGC----RVGHDelggiYLQGLNdagiqttpksiseGVTGTCMVLISPDSERTMHTYLGITAELSQDQID 146
Cdd:PRK15074 119 nieiGSYAYrYLCntssRTDLN-----YLQGVD-------------GPIGRCFTLISEDGERTFAISPGHMNQLRPESIP 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 147 FEPLKTAKWLYIEGYL---STSETARKAVKQAREIAKAHGVKIALSLSDPAMVQYAREGLEELMDDGVDLLFCNEQEALM 223
Cdd:PRK15074 181 EDVIAGASALVLTAYLvrcKPGEPMPEATMKAIEYAKKHNVPVVLTLGTKFVIEDNPQWWQEFLKEHVSILAMNEDEAEA 260
|
..
gi 446168811 224 YT 225
Cdd:PRK15074 261 LT 262
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
152-289 |
2.45e-20 |
|
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: 87.15 E-value: 2.45e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 152 TAKWLYIEGYLSTSETARKAVKQAREiakaHGVKIALslsDPAMVQY--AREGLEELMDdGVDLLFCNEQEALMYTNTT- 228
Cdd:cd00287 57 GADAVVISGLSPAPEAVLDALEEARR----RGVPVVL---DPGPRAVrlDGEELEKLLP-GVDILTPNEEEAEALTGRRd 128
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446168811 229 -TVEDALTQLR----FKNHTVVITQSAKGALVANPT-HHFHVAGRHVEAVDTNGAGDAFAGAFLYAL 289
Cdd:cd00287 129 lEVKEAAEAAAlllsKGPKVVIVTLGEKGAIVATRGgTEVHVPAFPVKVVDTTGAGDAFLAALAAGL 195
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
62-314 |
4.33e-20 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 89.03 E-value: 4.33e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKS-ISEGVTGTCMVLIspDSERTMHTYL---GIT 137
Cdd:PTZ00292 52 GGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGVNTSFVSrTENSSTGLAMIFV--DTKTGNNEIViipGAN 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 138 AELSQDQIDfeplktAKWLYIEGYLS----TSETARKAVKQAREIAKAHGVKIALSLSdPAMVQYAREGLEELMDdGVDL 213
Cdd:PTZ00292 130 NALTPQMVD------AQTDNIQNICKylicQNEIPLETTLDALKEAKERGCYTVFNPA-PAPKLAEVEIIKPFLK-YVSL 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 214 LFCNEQEALMYT----NTTTVED----ALTQLRFKNhtVVITQSAKG-ALVANPTHHFHVAGRHVEAVDTNGAGDAFAGA 284
Cdd:PTZ00292 202 FCVNEVEAALITgmevTDTESAFkaskELQQLGVEN--VIITLGANGcLIVEKENEPVHVPGKRVKAVDTTGAGDCFVGS 279
|
250 260 270
....*....|....*....|....*....|
gi 446168811 285 FLYALNHHEDLTAAAQLAILISSEVVSQFG 314
Cdd:PTZ00292 280 MAYFMSRGKDLKESCKRANRIAAISVTRHG 309
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
91-327 |
1.00e-19 |
|
hexose kinase, 1-phosphofructokinase family; This family consists largely of 1-phosphofructokinases, but also includes tagatose-6-kinases and 6-phosphofructokinases.
Pssm-ID: 274464 [Multi-domain] Cd Length: 303 Bit Score: 87.63 E-value: 1.00e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 91 GGIYLQGLNDAGIQTTPKSIsEGVTGTCMVLISPDSERTMHTYLGitAELSQDQID------FEPLKTAKWLYIEGYLST 164
Cdd:TIGR03168 63 GEFIEALLAEEGIKNDFVEV-KGETRINVKIKESSGEETELNEPG--PEISEEELEqlleklRELLASGDIVVISGSLPP 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 165 SETARkAVKQAREIAKAHGVKIALSLSDPAMvqyaREGLEElmddGVDLLFCNEQEALMYTNT--TTVED---ALTQLRF 239
Cdd:TIGR03168 140 GVPPD-FYAQLIAIARKKGAKVILDTSGEAL----REALAA----KPFLIKPNHEELEELFGRelKTLEEiieAARELLD 210
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 240 K-NHTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFGPRLA 318
Cdd:TIGR03168 211 RgAENVLVSLGADGALLVTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLP 290
|
250
....*....|
gi 446168811 319 -INDYAKLLE 327
Cdd:TIGR03168 291 dPEDVEELLD 300
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
69-327 |
4.99e-19 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 85.96 E-value: 4.99e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 69 TVAFSALGGSAfygcrvghdelGGIYLQGLNDAGIQTTPKSIsEGVTGTCMVLISPDSERTMHtYLGITAELSQDQID-- 146
Cdd:COG1105 52 VTALGFLGGFT-----------GEFIEELLDEEGIPTDFVPI-EGETRINIKIVDPSDGTETE-INEPGPEISEEELEal 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 147 ----FEPLKTAKWLYIEGYLSTSETArKAVKQAREIAKAHGVKIALSLSDPAMvqyaREGLEElmddGVDLLFCNEQEAL 222
Cdd:COG1105 119 lerlEELLKEGDWVVLSGSLPPGVPP-DFYAELIRLARARGAKVVLDTSGEAL----KAALEA----GPDLIKPNLEELE 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 223 MYTNT--TTVED---ALTQLRFKN-HTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLT 296
Cdd:COG1105 190 ELLGRplETLEDiiaAARELLERGaENVVVSLGADGALLVTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLE 269
|
250 260 270
....*....|....*....|....*....|..
gi 446168811 297 AAAQLAILISSEVVSQFGPRLA-INDYAKLLE 327
Cdd:COG1105 270 EALRLAVAAGAAAALSPGTGLPdREDVEELLA 301
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
60-302 |
1.84e-18 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 84.15 E-value: 1.84e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 60 ASGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGV-TGTCMVLISPDSERTMHTYLGITA 138
Cdd:PRK11142 37 AFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGIDTAPVSVIKGEsTGVALIFVNDEGENSIGIHAGANA 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 139 ELSQDQID--FEPLKTAKWLyiegyLSTSETARKAVKQAREIAKAHGVKIALslsDPAMvqyAREGLEELMDdGVDLLFC 216
Cdd:PRK11142 117 ALTPALVEahRELIANADAL-----LMQLETPLETVLAAAKIAKQHGTKVIL---NPAP---ARELPDELLA-LVDIITP 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 217 NEQEALMYTNTTtVEDALTQLRFKN-------HTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYAL 289
Cdd:PRK11142 185 NETEAEKLTGIR-VEDDDDAAKAAQvlhqkgiETVLITLGSRGVWLSENGEGQRVPGFRVQAVDTIAAGDTFNGALVTAL 263
|
250
....*....|...
gi 446168811 290 NHHEDLTAAAQLA 302
Cdd:PRK11142 264 LEGKPLPEAIRFA 276
|
|
| PLN02323 |
PLN02323 |
probable fructokinase |
59-286 |
6.15e-17 |
|
probable fructokinase
Pssm-ID: 215183 [Multi-domain] Cd Length: 330 Bit Score: 80.05 E-value: 6.15e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 59 QASGGSAANTTVAFSALGG-SAFYGcRVGHDELG----GIYLQ-GLNDAGIQTTPksisEGVTGTCMVLISPDSERTMHT 132
Cdd:PLN02323 40 KAPGGAPANVAVGISRLGGsSAFIG-KVGDDEFGhmlaDILKKnGVNNEGVRFDP----GARTALAFVTLRSDGEREFMF 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 133 YLGITAE--LSQDQIDFEPLKTAKWLYiegYLSTS---ETARKAVKQAREIAKAHGvkiALSLSDPAM-------VQYAR 200
Cdd:PLN02323 115 YRNPSADmlLRESELDLDLIRKAKIFH---YGSISlitEPCRSAHLAAMKIAKEAG---ALLSYDPNLrlplwpsAEAAR 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 201 EGLEELMDDGvDLLFCNEQEALMYTNTTTVED--ALTQLRFKNHTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAG 278
Cdd:PLN02323 189 EGIMSIWDEA-DIIKVSDEEVEFLTGGDDPDDdtVVKLWHPNLKLLLVTEGEEGCRYYTKDFKGRVEGFKVKAVDTTGAG 267
|
....*...
gi 446168811 279 DAFAGAFL 286
Cdd:PLN02323 268 DAFVGGLL 275
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
62-316 |
3.15e-16 |
|
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: 77.07 E-value: 3.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTpKSISEGVTGTCMVLISPDSERTmhtylgITAELS 141
Cdd:cd01947 36 GGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKHT-VAWRDKPTRKTLSFIDPNGERT------ITVPGE 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 142 QDQIDFEPLKTAKW--LYIEGYLSTSETARKAVKQAREIAKAHGvkialslsdpamvqyaREGLEELMD--DGVDLLFCN 217
Cdd:cd01947 109 RLEDDLKWPILDEGdgVFITAAAVDKEAIRKCRETKLVILQVTP----------------RVRVDELNQalIPLDILIGS 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 218 EQEALMYTNTTtvEDALTQLRfknhTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLTA 297
Cdd:cd01947 173 RLDPGELVVAE--KIAGPFPR----YLIVTEGELGAILYPGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEE 246
|
250
....*....|....*....
gi 446168811 298 AAQLAILISSEVVSQFGPR 316
Cdd:cd01947 247 ALELGAQCGAICVSHFGPY 265
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
91-314 |
1.50e-15 |
|
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: 75.65 E-value: 1.50e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 91 GGIYLQGLNDAGIQTTPKSIsEGVTGTCMVLISPDSERTMhtYLGITAELSQDQID------FEPLKTAKWLYIEGYLST 164
Cdd:cd01164 64 GDFFEALLKEEGIPDDFVEV-AGETRINVKIKEEDGTETE--INEPGPEISEEELEalleklKALLKKGDIVVLSGSLPP 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 165 SETARKAVKQAReIAKAHGVKIALSLSDPAMvqyaREGLEElmddGVDLLFCNEQE--ALMYTNTTTVED---ALTQLRF 239
Cdd:cd01164 141 GVPADFYAELVR-LAREKGARVILDTSGEAL----LAALAA----KPFLIKPNREEleELFGRPLGDEEDviaAARKLIE 211
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446168811 240 K-NHTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFG 314
Cdd:cd01164 212 RgAENVLVSLGADGALLVTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPG 287
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
54-314 |
1.87e-15 |
|
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: 75.08 E-value: 1.87e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 54 QDYKGQASGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGVTG-TCMVLISPDSERTMHT 132
Cdd:cd01940 14 LHLGKMYPGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRSTLKRLGVDISHCRVKEGENAvADVELVDGDRIFGLSN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 133 YLGITAELSQDQiDFEPLKTAKWLYIeGYLSTSETARKAVKQAreiaKAHGVKIALSLSDPAMVQYARegleeLMDDGVD 212
Cdd:cd01940 94 KGGVAREHPFEA-DLEYLSQFDLVHT-GIYSHEGHLEKALQAL----VGAGALISFDFSDRWDDDYLQ-----LVCPYVD 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 213 LLFCNEQEAlmytNTTTVEDAL-TQLRFKNHTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYA-LN 290
Cdd:cd01940 163 FAFFSASDL----SDEEVKAKLkEAVSRGAKLVIVTRGEDGAIAYDGAVFYSVAPRPVEVVDTLGAGDSFIAGFLLSlLA 238
|
250 260
....*....|....*....|....
gi 446168811 291 HHEDLTAAAQLAILISSEVVSQFG 314
Cdd:cd01940 239 GGTAIAEAMRQGAQFAAKTCGHEG 262
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
59-304 |
1.28e-14 |
|
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: 73.12 E-value: 1.28e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 59 QASGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISPDSERT-----MHTY 133
Cdd:cd01941 32 QSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRGIVFEGRSTASYTAILDKDGDLVvaladMDIY 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 134 LGITAELSQDQIDFepLKTAKWLYIEGYLStSETARKAVKQAREiakaHGVKIALSlsdPAMVQYAREGLEELmdDGVDL 213
Cdd:cd01941 112 ELLTPDFLRKIREA--LKEAKPIVVDANLP-EEALEYLLALAAK----HGVPVAFE---PTSAPKLKKLFYLL--HAIDL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 214 LFCNEQEALMYTNTTTVED--------ALTQLRFKNhtVVITQSAKGALVANP-----THHFHVAGRHvEAVDTNGAGDA 280
Cdd:cd01941 180 LTPNRAELEALAGALIENNedenkaakILLLPGIKN--VIVTLGAKGVLLSSReggveTKLFPAPQPE-TVVNVTGAGDA 256
|
250 260
....*....|....*....|....
gi 446168811 281 FAGAFLYALNHHEDLTAAAQLAIL 304
Cdd:cd01941 257 FVAGLVAGLLEGMSLDDSLRFAQA 280
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
61-315 |
3.45e-11 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 62.45 E-value: 3.45e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 61 SGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSISEGVTGTCMVLISpDSERTMHTYL-GITAE 139
Cdd:PRK09813 22 SGGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDISHVHTKHGVTAQTQVELH-DNDRVFGDYTeGVMAD 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 140 --LSQDQIDF----EPLKTAKWLYIEGYLSTsetarkavkqareiAKAHGVKIALSLSDPAMVQYAREGLEElmddgVDL 213
Cdd:PRK09813 101 faLSEEDYAWlaqyDIVHAAIWGHAEDAFPQ--------------LHAAGKLTAFDFSDKWDSPLWQTLVPH-----LDY 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 214 LFcneqeALMYTNTTTVEDALTQLRFKNHTVVI-TQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHH 292
Cdd:PRK09813 162 AF-----ASAPQEDEFLRLKMKAIVARGAGVVIvTLGENGSIAWDGAQFWRQAPEPVTVVDTMGAGDSFIAGFLCGWLAG 236
|
250 260
....*....|....*....|...
gi 446168811 293 EDLTAAAQLAILISSEVVSQFGP 315
Cdd:PRK09813 237 MTLPQAMAQGTACAAKTIQYHGA 259
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
63-314 |
4.78e-10 |
|
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: 59.50 E-value: 4.78e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 63 GSAANTTVAFSALGGSAFYGCRVGHDELG----------GIYLQGLNDAGIQTTPKS--ISEGVTgtcmvLISPDSERTm 130
Cdd:cd01172 40 GGAANVANNLASLGAKVTLLGVVGDDEAGdllrkllekeGIDTDGIVDEGRPTTTKTrvIARNQQ-----LLRVDREDD- 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 131 hTYLGITAELSQDQIDFEPLKTAKWL----YIEGYLSTSetarkAVKQAREIAKAHGVKIalsLSDPAMVQYAREgleel 206
Cdd:cd01172 114 -SPLSAEEEQRLIERIAERLPEADVVilsdYGKGVLTPR-----VIEALIAAARELGIPV---LVDPKGRDYSKY----- 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 207 mdDGVDLLFCNEQEAL----MYTNT-----TTVEDALTQLRFKNhtVVITQSAKGALVANPT-HHFHVAGRHVEAVDTNG 276
Cdd:cd01172 180 --RGATLLTPNEKEARealgDEINDddeleAAGEKLLELLNLEA--LLVTLGEEGMTLFERDgEVQHIPALAKEVYDVTG 255
|
250 260 270
....*....|....*....|....*....|....*...
gi 446168811 277 AGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFG 314
Cdd:cd01172 256 AGDTVIATLALALAAGADLEEAAFLANAAAGVVVGKVG 293
|
|
| PLN02543 |
PLN02543 |
pfkB-type carbohydrate kinase family protein |
34-207 |
4.20e-06 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215299 Cd Length: 496 Bit Score: 48.37 E-value: 4.20e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 34 TMQLSDGETQSALYEKLKQTQ---DYKGQASGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTTPKSI 110
Cdd:PLN02543 141 TVRVHDNQMHPDMYSQWKMLQwdpPEFARAPGGPPSNVAISHVRLGGRAAFMGKVGDDDFGEELVLMMNKERVQTRAVKF 220
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 111 SEGVTGTC--MVLISPDSERTMHTYLGITAE--LSQDQIDFEPLKTAKWLYIEGYLSTSETARKAVKQAREIAKAHGVKI 186
Cdd:PLN02543 221 DENAKTACsrMKIKFRDGGKMVAETVKEAAEdsLLASELNLAVLKEARMFHFNSEVLTSPSMQSTLFRAIELSKKFGGLI 300
|
170 180
....*....|....*....|.
gi 446168811 187 ALSLSDPAMVQYAREGLEELM 207
Cdd:PLN02543 301 FFDLNLPLPLWRSRDETRELI 321
|
|
| PLN02967 |
PLN02967 |
kinase |
59-193 |
4.97e-06 |
|
kinase
Pssm-ID: 215521 [Multi-domain] Cd Length: 581 Bit Score: 48.12 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 59 QASGGSAANTTVAFSALGGSAFYGCRVGHDELGGIYLQGLNDAGIQTtpKSIsegvtgtCMVLISPDSERTMH----TYL 134
Cdd:PLN02967 240 RAPGGSAGGVAIALASLGGKVAFMGKLGDDDYGQAMLYYLNVNKVQT--RSV-------CIDGKRATAVSTMKiakrGRL 310
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446168811 135 GIT-----AE--LSQDQIDFEPLKTAKWLYIEGYLSTSETARKAVKQAREIAKAHGVKIALSLSDP 193
Cdd:PLN02967 311 KTTcvkpcAEdsLSKSEINIDVLKEAKMFYFNTHSLLDPTMRSTTLRAIKISKKLGGVIFYDLNLP 376
|
|
| ribokinase_group_C |
cd01946 |
Ribokinase-like subgroup C. Found only in bacteria, this subgroup is part of the ribokinase ... |
204-315 |
1.66e-05 |
|
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: 45.53 E-value: 1.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 204 EELMD--DGVDLLFCNEQEALMYTNTTTVEDALTQLR-FKNHTVVITQSAKGALVANPTHHFHVAGRHVEAV-DTNGAGD 279
Cdd:cd01946 155 EKLKKvlAKVDVVIINDGEARQLTGAANLVKAARLILaMGPKALIIKRGEYGALLFTDDGYFAAPAYPLESVfDPTGAGD 234
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 446168811 280 AFAGAFLYALNHHEDLT-AAAQLAILISSEVVS----QFGP 315
Cdd:cd01946 235 TFAGGFIGYLASQKDTSeANMRRAIIYGSAMASfcveDFGT 275
|
|
| Ketohexokinase |
cd01939 |
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to ... |
62-314 |
1.86e-05 |
|
Ketohexokinase (fructokinase, KHK) catalyzes the phosphorylation of fructose to fructose-1-phosphate (F1P), the first step in the metabolism of dietary fructose. KHK can also phosphorylate several other furanose sugars. It is found in higher eukaryotes where it is believed to function as a dimer and requires K(+) and ATP to be active. In humans, hepatic KHK deficiency causes fructosuria, a benign inborn error of metabolism.
Pssm-ID: 238914 [Multi-domain] Cd Length: 290 Bit Score: 45.48 E-value: 1.86e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 62 GGSAANTTVAFSALGGS-AFYG--CRVGHDElggIYLQGLNDAGIQT---TPKSISEGVTgTCMVLISPDSERTMHTYLG 135
Cdd:cd01939 36 GGNASNSCTVLRLLGLScEFLGvlSRGPVFE---SLLDDFQSRGIDIshcYRKDIDEPAS-SYIIRSRAGGRTTIVNDNN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 136 ItAELSQDQIDFEPLKTAKWLYIEGyLSTSETAR--KAVKQAREiaKAHGVKIALSLSdpamVQYAREGLEELMDDgVDL 213
Cdd:cd01939 112 L-PEVTYDDFSKIDLTQYGWIHFEG-RNPDETLRmmQHIEEHNN--RRPEIRITISVE----VEKPREELLELAAY-CDV 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 214 LFCNEQ--EALMYTNTTTVEDALTQLRFKNHTVVITQSAKGA--LVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYAL 289
Cdd:cd01939 183 VFVSKDwaQSRGYKSPEECLRGEGPRAKKAALLVCTWGDQGAgaLGPDGEYVHSPAHKPIRVVDTLGAGDTFNAAVIYAL 262
|
250 260
....*....|....*....|....*.
gi 446168811 290 NHHED-LTAAAQLAILISSEVVSQFG 314
Cdd:cd01939 263 NKGPDdLSEALDFGNRVASQKCTGVG 288
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
212-310 |
3.15e-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: 3.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 212 DLLFCNEQEalMYTNTTTVEDALTQLRFKNHTVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNH 291
Cdd:cd01937 157 DVLKLSRVE--AEVISTPTELARLIKETGVKEIIVTDGEEGGYIFDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLS 234
|
90
....*....|....*....
gi 446168811 292 HEDLTAAAQLAILISSEVV 310
Cdd:cd01937 235 GKDIKEAAEFAAAAAAKFI 253
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
211-317 |
4.49e-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: 44.64 E-value: 4.49e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 211 VDLLFCNEQEALM----YTNTTTVEDALTQLRFKNH----------TVVITQSAKGALVANPTH--HFHVAGRHVEA--- 271
Cdd:cd01943 181 VDVFSPNLEEAARllglPTSEPSSDEEKEAVLQALLfsgilqdpggGVVLRCGKLGCYVGSADSgpELWLPAYHTKStkv 260
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 446168811 272 VDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISSEVVSQFG-PRL 317
Cdd:cd01943 261 VDPTGGGNSFLGGFAAGLALTKSIDEACIYGSVAASFAIEQVGlPRL 307
|
|
| PdxK |
COG2240 |
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal ... |
224-302 |
6.64e-05 |
|
Pyridoxal/pyridoxine/pyridoxamine kinase [Coenzyme transport and metabolism]; Pyridoxal/pyridoxine/pyridoxamine kinase is part of the Pathway/BioSystem: Pyridoxal phosphate biosynthesis
Pssm-ID: 441841 [Multi-domain] Cd Length: 272 Bit Score: 43.98 E-value: 6.64e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 224 YTNTTTVEDALTQLR-FKNHTVVITqSAK---------GALVANPTHHFHVAGRHVEaVDTNGAGDAFAGAFLYALNHHE 293
Cdd:COG2240 157 YETLEEALAAARALLaLGPKIVVVT-SVPlddtpadkiGNLAVTADGAWLVETPLLP-FSPNGTGDLFAALLLAHLLRGK 234
|
....*....
gi 446168811 294 DLTAAAQLA 302
Cdd:COG2240 235 SLEEALERA 243
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
230-325 |
4.42e-04 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 41.60 E-value: 4.42e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446168811 230 VEDALTQLRFKN--HtVVITQSAKGALVANPTHHFHVAGRHVEAVDTNGAGDAFAGAFLYALNHHEDLTAAAQLAILISS 307
Cdd:PRK09513 205 VIEAAHALREQGiaH-VVISLGAEGALWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSA 283
|
90
....*....|....*...
gi 446168811 308 EVVSQfgPRLAINDYAKL 325
Cdd:PRK09513 284 LAVSQ--SNVGITDRPQL 299
|
|
| |
