|
Name |
Accession |
Description |
Interval |
E-value |
| glk |
PRK00292 |
glucokinase; Provisional |
12-326 |
9.91e-157 |
|
glucokinase; Provisional
Pssm-ID: 234716 Cd Length: 316 Bit Score: 441.14 E-value: 9.91e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 12 LGLVGDIGGTNARFAL--WRGQRLESIEVLACADYPRPELAVRDYLARigESVANIDSVCLACAGPVGAADFRFTNNHWV 89
Cdd:PRK00292 3 PALVGDIGGTNARFALcdWANGEIEQIKTYATADYPSLEDAIRAYLAD--EHGVQVRSACFAIAGPVDGDEVRMTNHHWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 90 INRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLgGGRWEVLPCEGG 169
Cdd:PRK00292 81 FSIAAMKQELGLDHLLLINDFTAQALAIPRLGEEDLVQIGGGEPVPGAPIAVIGPGTGLGVAGLVPV-DGRWIVLPGEGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 170 HVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVLEHFFL 248
Cdd:PRK00292 160 HVDFAPRSEEEAQILQYLRAEFGHVSAERVLSGPGLVNLYRAICKADGREPELLTPADITERALAGsCPLCRRTLSLFCV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489205800 249 WLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVALQQA 326
Cdd:PRK00292 240 ILGRVAGNLALTLGARGGVYIAGGIVPRFLEFFKASGFRAAFEDKGRFS-AYLADIPVYVITHPQPGLLGAGAYLRQA 316
|
|
| Glucokinase |
pfam02685 |
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes ... |
14-325 |
2.49e-139 |
|
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes phosphorylate glucose using ATP as a donor to give glucose-6-phosphate and ADP.
Pssm-ID: 397005 Cd Length: 314 Bit Score: 396.93 E-value: 2.49e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWRGQRLE----SIEVLACADYPRPELAVRDYLARiGESVANIDSVCLACAGPVGAADFRFTNNHWV 89
Cdd:pfam02685 1 LAGDIGGTNARFALVTASGGEpqplSIRTYASADYPSLEEAIQDYLAE-DAGVTQPRHACFAVAGPVDGDRVRLTNLPWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 90 INRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLGGGRWeVLPCEGG 169
Cdd:pfam02685 80 ISIEELRATLGLDAVLLINDFEAVAYAIPRLGADDLVQLGGGKPDPGAPRAVLGPGTGLGVAGLIPRGGRWI-VLPGEGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 170 HVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVLEHFFL 248
Cdd:pfam02685 159 HVDFAPRSEREIELLRYLRRRFGHVSAERVLSGPGLVNLYRALCALDGITPELLTPADITAAALAGdDPLAREALELFCA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489205800 249 WLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVALQQ 325
Cdd:pfam02685 239 ILGSVAGNLALTLGARGGVYIAGGIAPRILEFLKASGFRAAFEDKGRFS-ALLRDIPVYVITHPQPGLLGAAAAARQ 314
|
|
| Glk |
COG0837 |
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway ... |
8-326 |
2.16e-130 |
|
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440599 Cd Length: 320 Bit Score: 374.45 E-value: 2.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 8 SAGGLGLVGDIGGTNARFALWR---GQRLESIEVLACADYPRPELAVRDYLARIGesVANIDSVCLACAGPVGAADFRFT 84
Cdd:COG0837 2 TAPTPILVADIGGTNARLALAEgggGLELLEIRRYPSADYASLEDALRAYLAELG--LPRPRAACLAVAGPVDGDRVKLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 85 NNHWVINRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPlGGGRWEVL 164
Cdd:COG0837 80 NLPWSISAAALRAALGLERVLLINDFEALAYALPALSPDDLVQLGGGEPDPGGPRAVIGPGTGLGVAGLVP-DGGGWIVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 165 PCEGGHVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVL 243
Cdd:COG0837 159 PSEGGHVDFAPRDERELELLRYLRRRYGHVSAERVLSGPGLVNLYRALAALDGAPPAPLSPAEITAAALAGsDPLAVEAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 244 EHFFLWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVAL 323
Cdd:COG0837 239 ELFCRILGRVAGNLALTLGARGGVYLAGGIAPRILPLLDRSGFREAFEDKGRFS-ALLADIPVYVITHPQPGLLGAAAYA 317
|
...
gi 489205800 324 QQA 326
Cdd:COG0837 318 AQL 320
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
14-319 |
1.18e-101 |
|
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. Glucokinases are mainly found in invertebrates and microorganisms and highly specific for glucose. Glucokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466858 [Multi-domain] Cd Length: 313 Bit Score: 301.45 E-value: 1.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWR----GQRLESIEVLACADYPRPELAVRDYLARIGESVanIDSVCLACAGPVGAADFRFTNNHWV 89
Cdd:cd24008 2 LVGDIGGTNARLALADagdgSGDLLFVRKYPSADFASLEDALAAFLAELGAPR--PKAACIAVAGPVDGGRVRLTNLDWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 90 INRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQV-RAGSAQADRARLIIGPGTGLGVGSLLPLGGGRWEVLPCEG 168
Cdd:cd24008 80 IDAAELRKALGIGRVRLLNDFEAAAYGLPALGPEDLLVLyGGGGPLPGGPRAVLGPGTGLGVALLVPDGDGGYVVLPSEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 169 GHVDLPVTSPRDFALWQGLQARYGH-VSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAGDAQADAVLEHFF 247
Cdd:cd24008 160 GHADFAPVTEEEAELLEFLRKRFGRsVSYEDVLSGPGLENIYEFLAKLDGAEPPDLTAEEIAEAALAGDPLAREALDLFA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489205800 248 LWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGA 319
Cdd:cd24008 240 RILGRFAGNLALSFLATGGVYLAGGIAPKNLDLLDSSAFREAFLDKGRMS-DLLEDIPVYLVTNEDLGLLGA 310
|
|
| glk |
TIGR00749 |
glucokinase, proteobacterial type; This model represents glucokinase of E. coli and close ... |
14-320 |
1.42e-78 |
|
glucokinase, proteobacterial type; This model represents glucokinase of E. coli and close homologs, mostly from other proteobacteria, presumed to have equivalent function. This glucokinase is more closely related to a number of uncharacterized paralogs than to the glucokinase glcK (fromerly yqgR) of Bacillus subtilis and its closest homologs, so the two sets are represented by separate models. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 129832 [Multi-domain] Cd Length: 316 Bit Score: 242.48 E-value: 1.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWR--GQRLESIEVLACADYPRPELAVRDYLARIGESVAN-IDSVCLACAGPVGAADFRFTNNHWVI 90
Cdd:TIGR00749 1 LVGDIGGTNARLALCEiaPGEISQAKTYSGLDFPSLEAVVRVYLEEHKVELKDpIAKGCFAIACPITGDWVAMTNHTWAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 91 NRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLGGGRWEVLPCEGGH 170
Cdd:TIGR00749 81 SIAELKQNLGFSHLEIINDFTAVSYAIPGLKKEDLIQFGGAEPVEGKPIAILGAGTGLGVAHLIHQVDGRWVVLPGEGGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 171 VDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAE------VGALAMAGD-AQADAVL 243
Cdd:TIGR00749 161 VDFAPNSELEAIILEYLRAKIGHVSAERVLSGPGLVNIYEALVKADPERQFNKLPQEnlkpkdISERALAGScTDCRRAL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489205800 244 EHFFLWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTsGAYLQDVPVWVMTAEHPGLLGAG 320
Cdd:TIGR00749 241 SLFCVIYGRFAGNLALNLGTRGGVYIAGGIVPRFIEFFKASGFRAAFEDKGRM-KEYVHDIPVYVVLHDNPGLLGAG 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| glk |
PRK00292 |
glucokinase; Provisional |
12-326 |
9.91e-157 |
|
glucokinase; Provisional
Pssm-ID: 234716 Cd Length: 316 Bit Score: 441.14 E-value: 9.91e-157
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 12 LGLVGDIGGTNARFAL--WRGQRLESIEVLACADYPRPELAVRDYLARigESVANIDSVCLACAGPVGAADFRFTNNHWV 89
Cdd:PRK00292 3 PALVGDIGGTNARFALcdWANGEIEQIKTYATADYPSLEDAIRAYLAD--EHGVQVRSACFAIAGPVDGDEVRMTNHHWA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 90 INRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLgGGRWEVLPCEGG 169
Cdd:PRK00292 81 FSIAAMKQELGLDHLLLINDFTAQALAIPRLGEEDLVQIGGGEPVPGAPIAVIGPGTGLGVAGLVPV-DGRWIVLPGEGG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 170 HVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVLEHFFL 248
Cdd:PRK00292 160 HVDFAPRSEEEAQILQYLRAEFGHVSAERVLSGPGLVNLYRAICKADGREPELLTPADITERALAGsCPLCRRTLSLFCV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489205800 249 WLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVALQQA 326
Cdd:PRK00292 240 ILGRVAGNLALTLGARGGVYIAGGIVPRFLEFFKASGFRAAFEDKGRFS-AYLADIPVYVITHPQPGLLGAGAYLRQA 316
|
|
| Glucokinase |
pfam02685 |
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes ... |
14-325 |
2.49e-139 |
|
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes phosphorylate glucose using ATP as a donor to give glucose-6-phosphate and ADP.
Pssm-ID: 397005 Cd Length: 314 Bit Score: 396.93 E-value: 2.49e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWRGQRLE----SIEVLACADYPRPELAVRDYLARiGESVANIDSVCLACAGPVGAADFRFTNNHWV 89
Cdd:pfam02685 1 LAGDIGGTNARFALVTASGGEpqplSIRTYASADYPSLEEAIQDYLAE-DAGVTQPRHACFAVAGPVDGDRVRLTNLPWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 90 INRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLGGGRWeVLPCEGG 169
Cdd:pfam02685 80 ISIEELRATLGLDAVLLINDFEAVAYAIPRLGADDLVQLGGGKPDPGAPRAVLGPGTGLGVAGLIPRGGRWI-VLPGEGG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 170 HVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVLEHFFL 248
Cdd:pfam02685 159 HVDFAPRSEREIELLRYLRRRFGHVSAERVLSGPGLVNLYRALCALDGITPELLTPADITAAALAGdDPLAREALELFCA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489205800 249 WLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVALQQ 325
Cdd:pfam02685 239 ILGSVAGNLALTLGARGGVYIAGGIAPRILEFLKASGFRAAFEDKGRFS-ALLRDIPVYVITHPQPGLLGAAAAARQ 314
|
|
| Glk |
COG0837 |
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway ... |
8-326 |
2.16e-130 |
|
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440599 Cd Length: 320 Bit Score: 374.45 E-value: 2.16e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 8 SAGGLGLVGDIGGTNARFALWR---GQRLESIEVLACADYPRPELAVRDYLARIGesVANIDSVCLACAGPVGAADFRFT 84
Cdd:COG0837 2 TAPTPILVADIGGTNARLALAEgggGLELLEIRRYPSADYASLEDALRAYLAELG--LPRPRAACLAVAGPVDGDRVKLT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 85 NNHWVINRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPlGGGRWEVL 164
Cdd:COG0837 80 NLPWSISAAALRAALGLERVLLINDFEALAYALPALSPDDLVQLGGGEPDPGGPRAVIGPGTGLGVAGLVP-DGGGWIVL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 165 PCEGGHVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVL 243
Cdd:COG0837 159 PSEGGHVDFAPRDERELELLRYLRRRYGHVSAERVLSGPGLVNLYRALAALDGAPPAPLSPAEITAAALAGsDPLAVEAL 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 244 EHFFLWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVAL 323
Cdd:COG0837 239 ELFCRILGRVAGNLALTLGARGGVYLAGGIAPRILPLLDRSGFREAFEDKGRFS-ALLADIPVYVITHPQPGLLGAAAYA 317
|
...
gi 489205800 324 QQA 326
Cdd:COG0837 318 AQL 320
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
14-319 |
1.18e-101 |
|
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. Glucokinases are mainly found in invertebrates and microorganisms and highly specific for glucose. Glucokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466858 [Multi-domain] Cd Length: 313 Bit Score: 301.45 E-value: 1.18e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWR----GQRLESIEVLACADYPRPELAVRDYLARIGESVanIDSVCLACAGPVGAADFRFTNNHWV 89
Cdd:cd24008 2 LVGDIGGTNARLALADagdgSGDLLFVRKYPSADFASLEDALAAFLAELGAPR--PKAACIAVAGPVDGGRVRLTNLDWS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 90 INRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQV-RAGSAQADRARLIIGPGTGLGVGSLLPLGGGRWEVLPCEG 168
Cdd:cd24008 80 IDAAELRKALGIGRVRLLNDFEAAAYGLPALGPEDLLVLyGGGGPLPGGPRAVLGPGTGLGVALLVPDGDGGYVVLPSEG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 169 GHVDLPVTSPRDFALWQGLQARYGH-VSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAGDAQADAVLEHFF 247
Cdd:cd24008 160 GHADFAPVTEEEAELLEFLRKRFGRsVSYEDVLSGPGLENIYEFLAKLDGAEPPDLTAEEIAEAALAGDPLAREALDLFA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 489205800 248 LWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGA 319
Cdd:cd24008 240 RILGRFAGNLALSFLATGGVYLAGGIAPKNLDLLDSSAFREAFLDKGRMS-DLLEDIPVYLVTNEDLGLLGA 310
|
|
| glk |
TIGR00749 |
glucokinase, proteobacterial type; This model represents glucokinase of E. coli and close ... |
14-320 |
1.42e-78 |
|
glucokinase, proteobacterial type; This model represents glucokinase of E. coli and close homologs, mostly from other proteobacteria, presumed to have equivalent function. This glucokinase is more closely related to a number of uncharacterized paralogs than to the glucokinase glcK (fromerly yqgR) of Bacillus subtilis and its closest homologs, so the two sets are represented by separate models. [Energy metabolism, Glycolysis/gluconeogenesis]
Pssm-ID: 129832 [Multi-domain] Cd Length: 316 Bit Score: 242.48 E-value: 1.42e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWR--GQRLESIEVLACADYPRPELAVRDYLARIGESVAN-IDSVCLACAGPVGAADFRFTNNHWVI 90
Cdd:TIGR00749 1 LVGDIGGTNARLALCEiaPGEISQAKTYSGLDFPSLEAVVRVYLEEHKVELKDpIAKGCFAIACPITGDWVAMTNHTWAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 91 NRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLGGGRWEVLPCEGGH 170
Cdd:TIGR00749 81 SIAELKQNLGFSHLEIINDFTAVSYAIPGLKKEDLIQFGGAEPVEGKPIAILGAGTGLGVAHLIHQVDGRWVVLPGEGGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 171 VDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAE------VGALAMAGD-AQADAVL 243
Cdd:TIGR00749 161 VDFAPNSELEAIILEYLRAKIGHVSAERVLSGPGLVNIYEALVKADPERQFNKLPQEnlkpkdISERALAGScTDCRRAL 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 489205800 244 EHFFLWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTsGAYLQDVPVWVMTAEHPGLLGAG 320
Cdd:TIGR00749 241 SLFCVIYGRFAGNLALNLGTRGGVYIAGGIVPRFIEFFKASGFRAAFEDKGRM-KEYVHDIPVYVVLHDNPGLLGAG 316
|
|
| PRK14101 |
PRK14101 |
bifunctional transcriptional regulator/glucokinase; |
9-330 |
4.64e-69 |
|
bifunctional transcriptional regulator/glucokinase;
Pssm-ID: 184507 [Multi-domain] Cd Length: 638 Bit Score: 227.11 E-value: 4.64e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 9 AGGLGLVGDIGGTNARFALWRG-QRLESIEVLACADYPRPELAVRDYLARIGesVANIDSVCLACAGPVGAADFRFTNNH 87
Cdd:PRK14101 16 ADGPRLLADVGGTNARFALETGpGEITQIRVYPGADYPTLTDAIRKYLKDVK--IGRVNHAAIAIANPVDGDQVRMTNHD 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 88 WVINRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPLgGGRWEVLPCE 167
Cdd:PRK14101 94 WSFSIEATRRALGFDTLLVVNDFTALAMALPGLTDAQRVQVGGGTRRQNSVIGLLGPGTGLGVSGLIPA-DDRWIALGSE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 168 GGHVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRAS-SAAEVGALAMAGDAQADAVLEHF 246
Cdd:PRK14101 173 GGHASFAPQDEREDLVLQYARKKYPHVSFERVCAGPGMEIIYRALAARDKKRVAANvDTAEIVERAHAGDALALEAVECF 252
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 247 FLWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTSgAYLQDVPVWVMTAEHPGLLGAGVALQQA 326
Cdd:PRK14101 253 CAILGTFAGNLALTLGALGGIYIGGGVVPKLGELFTRSSFRARFEAKGRFE-AYLANIPTYLITAEYPAFLGVSAILAEQ 331
|
....
gi 489205800 327 LDAE 330
Cdd:PRK14101 332 LSNR 335
|
|
| PRK12408 |
PRK12408 |
glucokinase; Provisional |
14-321 |
3.85e-52 |
|
glucokinase; Provisional
Pssm-ID: 237092 Cd Length: 336 Bit Score: 174.94 E-value: 3.85e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWRGQR--LESIEVL-----ACADYPRPELAVRDYLArigeSVANIDSVCLACAGpVGAADFRFTNN 86
Cdd:PRK12408 19 VAADVGGTHVRVALVCASPdaAKPVELLdyrtyRCADYPSLAAILADFLA----ECAPVRRGVIASAG-YALDDGRVITA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 87 H--WVINRAAFREELGLDHLLLVNDFSTMAWAASRLGADELVQVRAGSAQADRARLIIGPGTGLGVGSLLPlGGGRWEVL 164
Cdd:PRK12408 94 NlpWTLSPEQIRAQLGLQAVHLVNDFEAVAYAAPYMEGNQVLQLSGPAQAAAGPALVLGPGTGLGAALWIP-NGGRPVVL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 165 PCEGGHVDLPVTSPRDFALWQGLQARYGHVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVL 243
Cdd:PRK12408 173 PTEAGQAALAAASELEMQLLQHLLRTRTHVPIEHVLSGPGLLNLYRALCALRGATPVHASPAAITAAALAGdDALAHEAL 252
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 489205800 244 EHFFLWLARVAGNAVLTVGALGGVYITGGIVPRFLERFIASGFAEAFASRGKTsGAYLQDVPVWVMTAEHPGLLGAGV 321
Cdd:PRK12408 253 QVFCGFLGSVVGDMALAYGARGGVYLAGGILPQIADFLARSDFVERFLNKGPM-RPALEQVPVKLVEHGQLGVLGAAS 329
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
17-283 |
7.67e-12 |
|
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate transport and metabolism, Transcription];
Pssm-ID: 441543 [Multi-domain] Cd Length: 306 Bit Score: 64.92 E-value: 7.67e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 17 DIGGTNARFALW--RGQRLESIEVLACADYPRPEL------AVRDYLARIGESVANIDSVCLACAGPVGAAD--FRFTNN 86
Cdd:COG1940 11 DIGGTKIKAALVdlDGEVLARERIPTPAGAGPEAVleaiaeLIEELLAEAGISRGRILGIGIGVPGPVDPETgvVLNAPN 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 87 HWVIN----RAAFREELGLDhLLLVNDFSTMAWAASRLGAdelvqvraGSAQADRARLIIGPGTGLGV---GSLLP---L 156
Cdd:COG1940 91 LPGWRgvplAELLEERLGLP-VFVENDANAAALAEAWFGA--------GRGADNVVYLTLGTGIGGGIvinGKLLRganG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 157 GGGrwevlpcEGGHVdlpVTSPRDFALWQGlqaRYGHVsaERALSGNGLLALYEISCALDGVavrasSAAEVGALAMAGD 236
Cdd:COG1940 162 NAG-------EIGHM---PVDPDGPLCGCG---NRGCL--ETYASGPALLRRARELGGAEKL-----TAEELFAAARAGD 221
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 489205800 237 AQADAVLEHFFLWLARVAGNAVLTVGAlgGVYITGGIVPRFLERFIA 283
Cdd:COG1940 222 PLALEVLDEAARYLGIGLANLINLLDP--EVIVLGGGVSAAGDLLLE 266
|
|
| PTZ00288 |
PTZ00288 |
glucokinase 1; Provisional |
4-265 |
2.09e-09 |
|
glucokinase 1; Provisional
Pssm-ID: 240346 [Multi-domain] Cd Length: 405 Bit Score: 58.40 E-value: 2.09e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 4 DNKRSAGGLGLVGDIGGTNARFALWRGQRLESIEVLACadYPRPELAVRDY----------LARIGESVANIDSVCL--- 70
Cdd:PTZ00288 19 DASWSSGPIFVGCDVGGTNARVGFAREVQHDDSGVHII--YVRFNVTKTDIrelleffdevLQKLKKNLSFIQRVAAgai 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 71 ACAGPV--GAADFRFTNNHWVINRAAFREELGLDH-LLLVND--------------------FSTMAWAASRLGADElvQ 127
Cdd:PTZ00288 97 SVPGPVtgGQLAGPFNNLKGIARLTDYPVELFPPGrSALLNDleagaygvlavsnagrlseyFKVMWKGTQWDALSE--G 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 128 VRAGSA-QADRArLIIGPGTGLGVGSLLPLG-GGRWEVLPCEGGHVDL--PVTSPRDF-----------ALWQGLQARYG 192
Cdd:PTZ00288 175 KPAGSViGRGRC-MVLAPGTGLGSSLIHYVGvSDQYIVIPLECGHLSIswPANEDSDYvqalagylaskALSKGIDSTVY 253
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 489205800 193 hVSAERALSGNGLLALYEISCALDGVAVRASSAAEVGALAMAG-DAQADAVLEHFFLWLARVAGNAvlTVGALG 265
Cdd:PTZ00288 254 -PIYEDIVSGRGLEFNYAYEKRGNKPSAPLKEAAEVAKLAKYGsDVAAVKAMKRHYKYLMRLAAEI--SMQFLP 324
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
14-320 |
1.07e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466919 [Multi-domain] Cd Length: 283 Bit Score: 40.35 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWRGQRLESIEVLACADYPRPElAVRDYLAR-IGESVANIDSVCLACAGPVGAADFRFTNNHWVINR 92
Cdd:cd24069 1 LAIDIGGTKIAAALIGNGQIIDRRQIPTPRSGTPE-ALADALASlLADYQGQFDRVAVASTGIIRDGVLTALNPKNLGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 93 AAFREELGLDHLL-----LVNDFSTMAWAASRLGAdelvqvragsAQADRARLIIGPGTGLGVGSLLplgGGRwevlpce 167
Cdd:cd24069 80 SGFPLADALQQLLgvpvvLLNDAQAAAWGEYQAGD----------GEGVGNLVFITVSTGVGGGLVL---NGQ------- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 168 gghvdlPVTSPRdfalwqGLQARYGHVSAER--ALSGNGLLALYEISCALDGVAVRAS-------SAAEVGALAMAGDAQ 238
Cdd:cd24069 140 ------LLTGPN------GLAGHIGHTLADPpgPVCGCGRRGCVEAIASGTAIAAAASeilgepvDAKDVFERARSGDEE 207
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 239 ADAVLEHFFLWLARVAGNAVLTVGaLGGVYITGGIvprflerfiasGFAEAFASRGKtsgAYLQDVP----VWVMTA--- 311
Cdd:cd24069 208 AARLIDRAARALADLIADLKATLD-LDCVVIGGSV-----------GLAEGFLERVE---QYLADEPaifrVSLEPArlg 272
|
....*....
gi 489205800 312 EHPGLLGAG 320
Cdd:cd24069 273 QDAGLLGAA 281
|
|
| ASKHA_NBD_PanK-III |
cd24015 |
nucleotide-binding domain (NBD) of type III pantothenate kinase (PanK-III) and similar ... |
14-133 |
5.65e-03 |
|
nucleotide-binding domain (NBD) of type III pantothenate kinase (PanK-III) and similar proteins; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to PanK-III that belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466865 [Multi-domain] Cd Length: 241 Bit Score: 37.63 E-value: 5.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 489205800 14 LVGDIGGTNARFALWRGQRLESIevlACADYPRPELAVRDYLARIGESVANIDSVCLACAGP---------------VGA 78
Cdd:cd24015 1 LVIDIGNTNIKLGLFDGGELVKI---WRLSTDKELTEDELLLLLAGIELEDISGVVISSVVPsltevleealkkyfgISP 77
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 489205800 79 ADFRFTNNHWVINRAAFREELGLDhlLLVNdfstmAWAASRLGADELVQVRAGSA 133
Cdd:cd24015 78 LVVGPGLKLGVKIAYDNPKELGAD--RLAN-----AVAAAKLYGRPVIVVDFGTA 125
|
|
| |
