|
Name |
Accession |
Description |
Interval |
E-value |
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-312 |
8.99e-96 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 285.49 E-value: 8.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA-SDSGK-FTRLLEVSGIPHEA 79
Cdd:COG1105 1 ILTVTLNPALDRTYEVD-ELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLgGFTGEfIEELLDEEGIPTDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEP-DGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVysVNP 158
Cdd:COG1105 80 VPIEGETRINIKIVDPsDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLA--RAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 159 NIRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSEVLATLGEA 238
Cdd:COG1105 158 GAKVVLDTSGEALKAALEA----GPDLIKPNLEELEELLGRPLETLED---------IIAAARELLERGAENVVVSLGAD 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063218607 239 GAVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYPEQVH 312
Cdd:COG1105 225 GALL-VTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVE 297
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-304 |
2.87e-84 |
|
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: 255.92 E-value: 2.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 1 MILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA-SDSGK-FTRLLEVSGIPHE 78
Cdd:cd01164 1 MIYTVTLNPAIDLTIELD-QLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLgGFTGDfFEALLKEEGIPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 79 AINTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYsvNP 158
Cdd:cd01164 80 FVEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAR--EK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 159 NIRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINqdgeeleaaAAEGNYLPVAQAARALNELGVSEVLATLGEA 238
Cdd:cd01164 158 GARVILDTSGEALLAALAA----KPFLIKPNREELEELFG---------RPLGDEEDVIAAARKLIERGAENVLVSLGAD 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063218607 239 GAVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTT 304
Cdd:cd01164 225 GALL-VTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-311 |
3.25e-80 |
|
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: 245.95 E-value: 3.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA-SDSGKF-TRLLEVSGIPHEA 79
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVD-GLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLgGFTGEFiEALLAEEGIKNDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYSVnpN 159
Cdd:TIGR03168 80 VEVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKK--G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 160 IRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSEVLATLGEAG 239
Cdd:TIGR03168 158 AKVILDTSGEALREALAA----KPFLIKPNHEELEELFGRELKTLEE---------IIEAARELLDRGAENVLVSLGADG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063218607 240 AVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYPEQV 311
Cdd:TIGR03168 225 ALL-VTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDV 295
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-299 |
3.03e-29 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 114.02 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLdTELKRGGVFRLPMAEDMAGGKGINVSKALHYAG-EKTLALYPASD-SGKFTRLLEVSGIPHEA 79
Cdd:PRK09513 5 VATITLNPAYDLVGFC-PEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGiDVTVGGFLGKDnQDGFQQLFSELGIANRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYSVNPn 159
Cdd:PRK09513 84 QVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCP- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 160 iRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELgqiinqdgeeleaAAAEGNYLP----VAQAARALNELGVSEVLATL 235
Cdd:PRK09513 163 -CIIFDSSREALVAGLKA----APWLVKPNRREL-------------EIWAGRKLPelkdVIEAAHALREQGIAHVVISL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063218607 236 GEAGAvLSVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATS 299
Cdd:PRK09513 225 GAEGA-LWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVS 287
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
36-305 |
7.16e-25 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 101.65 E-value: 7.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 36 AGGKGINVSKALHYAGEKTLALYPASDS--GKFTR-LLEVSGIPHEAINTTNEARVNLTLAE--PDGTTTKLNSPGMTL- 109
Cdd:pfam00294 33 PGGKGANVAVALARLGGDVAFIGAVGDDnfGEFLLqELKKEGVDTDYVVIDEDTRTGTALIEvdGDGERTIVFNRGAAAd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 110 TKAHRRRVLEKLIHHAKratWVVFAGSLPPGVPRDFYVQCTEAVYSVNPNIRVAMDTSDGPLTEVVRAFPKVrpFLMKPN 189
Cdd:pfam00294 113 LTPEELEENEDLLENAD---LLYISGSLPLGLPEATLEELIEAAKNGGTFDPNLLDPLGAAREALLELLPLA--DLLKPN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 190 AYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSEVLATLGEAGAVLSVKSGGCFAATSPSIVAQSTVGAGDCA 269
Cdd:pfam00294 188 EEELEALTGAKLDDIEE---------ALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSF 258
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063218607 270 LAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTI 305
Cdd:pfam00294 259 VGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
2-312 |
8.99e-96 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 285.49 E-value: 8.99e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA-SDSGK-FTRLLEVSGIPHEA 79
Cdd:COG1105 1 ILTVTLNPALDRTYEVD-ELEPGEVNRASEVRLDPGGKGINVARVLKALGVDVTALGFLgGFTGEfIEELLDEEGIPTDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEP-DGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVysVNP 158
Cdd:COG1105 80 VPIEGETRINIKIVDPsDGTETEINEPGPEISEEELEALLERLEELLKEGDWVVLSGSLPPGVPPDFYAELIRLA--RAR 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 159 NIRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSEVLATLGEA 238
Cdd:COG1105 158 GAKVVLDTSGEALKAALEA----GPDLIKPNLEELEELLGRPLETLED---------IIAAARELLERGAENVVVSLGAD 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063218607 239 GAVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYPEQVH 312
Cdd:COG1105 225 GALL-VTEDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGLARGLDLEEALRLAVAAGAAAALSPGTGLPDREDVE 297
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
1-304 |
2.87e-84 |
|
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: 255.92 E-value: 2.87e-84
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 1 MILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA-SDSGK-FTRLLEVSGIPHE 78
Cdd:cd01164 1 MIYTVTLNPAIDLTIELD-QLQPGEVNRVSSTRKDAGGKGINVARVLKDLGVEVTALGFLgGFTGDfFEALLKEEGIPDD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 79 AINTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYsvNP 158
Cdd:cd01164 80 FVEVAGETRINVKIKEEDGTETEINEPGPEISEEELEALLEKLKALLKKGDIVVLSGSLPPGVPADFYAELVRLAR--EK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 159 NIRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINqdgeeleaaAAEGNYLPVAQAARALNELGVSEVLATLGEA 238
Cdd:cd01164 158 GARVILDTSGEALLAALAA----KPFLIKPNREELEELFG---------RPLGDEEDVIAAARKLIERGAENVLVSLGAD 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063218607 239 GAVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTT 304
Cdd:cd01164 225 GALL-VTKDGVYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSLEEALRLAVAAGSATAFSPGTG 289
|
|
| 1-PFK |
TIGR03168 |
hexose kinase, 1-phosphofructokinase family; This family consists largely of ... |
2-311 |
3.25e-80 |
|
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: 245.95 E-value: 3.25e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA-SDSGKF-TRLLEVSGIPHEA 79
Cdd:TIGR03168 1 IYTVTLNPAIDLTIEVD-GLTPGEVNRVAAVRKDAGGKGINVARVLARLGAEVVATGFLgGFTGEFiEALLAEEGIKNDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYSVnpN 159
Cdd:TIGR03168 80 VEVKGETRINVKIKESSGEETELNEPGPEISEEELEQLLEKLRELLASGDIVVISGSLPPGVPPDFYAQLIAIARKK--G 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 160 IRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSEVLATLGEAG 239
Cdd:TIGR03168 158 AKVILDTSGEALREALAA----KPFLIKPNHEELEELFGRELKTLEE---------IIEAARELLDRGAENVLVSLGADG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063218607 240 AVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYPEQV 311
Cdd:TIGR03168 225 ALL-VTKEGALKATPPKVEVVNTVGAGDSMVAGFLAGLARGLSLEEALRFAVAAGSAAAFSPGTGLPDPEDV 295
|
|
| pfkB |
TIGR03828 |
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific ... |
2-311 |
6.02e-77 |
|
1-phosphofructokinase; This enzyme acts in concert with the fructose-specific phosphotransferase system (PTS) which imports fructose as fructose-1-phosphate. The action of 1-phosphofructokinase results in beta-D-fructose-1,6-bisphosphate and is an entry point into glycolysis (GenProp0688).
Pssm-ID: 274804 [Multi-domain] Cd Length: 304 Bit Score: 237.49 E-value: 6.02e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYP-ASDSGK-FTRLLEVSGIPHEA 79
Cdd:TIGR03828 1 IYTVTLNPAIDLTIELD-GLTLGEVNRVESTRIDAGGKGINVSRVLKNLGVDVVALGFlGGFTGDfIEALLREEGIKTDF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYsvNPN 159
Cdd:TIGR03828 80 VRVPGETRINVKIKEPSGTETKLNGPGPEISEEELEALLEKLRAQLAEGDWLVLSGSLPPGVPPDFYAELIALAR--EKG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 160 IRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELGQIINqdgeeleaaAAEGNYLPVAQAARALNELGVSEVLATLGEAG 239
Cdd:TIGR03828 158 AKVILDTSGEALRDGLKA----KPFLIKPNDEELEELFG---------RELKTLEEIIEAARELLDLGAENVLISLGADG 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1063218607 240 AVLSVKSGGCFaATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYPEQV 311
Cdd:TIGR03828 225 ALLVTKEGALF-AQPPKGEVVSTVGAGDSMVAGFLAGLESGLSLEEALRLAVAAGSAAAFSEGTGLPDPEDI 295
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
2-299 |
3.03e-29 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 114.02 E-value: 3.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRLARLdTELKRGGVFRLPMAEDMAGGKGINVSKALHYAG-EKTLALYPASD-SGKFTRLLEVSGIPHEA 79
Cdd:PRK09513 5 VATITLNPAYDLVGFC-PEIERGEVNLVKTTGLHAAGKGINVAKVLKDLGiDVTVGGFLGKDnQDGFQQLFSELGIANRF 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEAVYSVNPn 159
Cdd:PRK09513 84 QVVQGRTRINVKLTEKDGEVTDFNFSGFEVTPADWERFVTDSLSWLGQFDMVAVSGSLPRGVSPEAFTDWMTRLRSQCP- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 160 iRVAMDTSDGPLTEVVRAfpkvRPFLMKPNAYELgqiinqdgeeleaAAAEGNYLP----VAQAARALNELGVSEVLATL 235
Cdd:PRK09513 163 -CIIFDSSREALVAGLKA----APWLVKPNRREL-------------EIWAGRKLPelkdVIEAAHALREQGIAHVVISL 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1063218607 236 GEAGAvLSVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATS 299
Cdd:PRK09513 225 GAEGA-LWVNASGEWIAKPPACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALAVS 287
|
|
| PRK10294 |
PRK10294 |
6-phosphofructokinase 2; Provisional |
2-303 |
1.07e-28 |
|
6-phosphofructokinase 2; Provisional
Pssm-ID: 182361 [Multi-domain] Cd Length: 309 Bit Score: 112.18 E-value: 1.07e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 2 ILTLTVNPSIDRlARLDTELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYPA--SDSGKFTRLLEVSGIPHEA 79
Cdd:PRK10294 4 IYTLTLAPSLDS-ATITPQIYPEGKLRCSAPVFEPGGGGINVARAIAHLGGSATAIFPAggATGEHLVSLLADENVPVAT 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARVNLTL-AEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVfAGSLPPGVPRDFYVQCTEAVYsvNP 158
Cdd:PRK10294 83 VEAKDWTRQNLHVhVEASGEQYRFVMPGAALNEDEFRQLEEQVLEIESGAILVI-SGSLPPGVKLEKLTQLISAAQ--KQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 159 NIRVAMDTSDGPLTEVVrAFPKVRpfLMKPNAYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSE-VLATLGE 237
Cdd:PRK10294 160 GIRCIIDSSGDALSAAL-AIGNIE--LVKPNQKELSALVNRDLTQPDD---------VRKAAQELVNSGKAKrVVVSLGP 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1063218607 238 AGAvLSVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGT 303
Cdd:PRK10294 228 QGA-LGVDSENCIQVVPPPVKSQSTVGAGDSMVGAMTLKLAENASLEEMVRFGVAAGSAATLNQGT 292
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
36-305 |
7.16e-25 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 101.65 E-value: 7.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 36 AGGKGINVSKALHYAGEKTLALYPASDS--GKFTR-LLEVSGIPHEAINTTNEARVNLTLAE--PDGTTTKLNSPGMTL- 109
Cdd:pfam00294 33 PGGKGANVAVALARLGGDVAFIGAVGDDnfGEFLLqELKKEGVDTDYVVIDEDTRTGTALIEvdGDGERTIVFNRGAAAd 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 110 TKAHRRRVLEKLIHHAKratWVVFAGSLPPGVPRDFYVQCTEAVYSVNPNIRVAMDTSDGPLTEVVRAFPKVrpFLMKPN 189
Cdd:pfam00294 113 LTPEELEENEDLLENAD---LLYISGSLPLGLPEATLEELIEAAKNGGTFDPNLLDPLGAAREALLELLPLA--DLLKPN 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 190 AYELGQIINQDGEELEAaaaegnylpVAQAARALNELGVSEVLATLGEAGAVLSVKSGGCFAATSPSIVAQSTVGAGDCA 269
Cdd:pfam00294 188 EEELEALTGAKLDDIEE---------ALAALHKLLAKGIKTVIVTLGADGALVVEGDGEVHVPAVPKVKVVDTTGAGDSF 258
|
250 260 270
....*....|....*....|....*....|....*.
gi 1063218607 270 LAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTI 305
Cdd:pfam00294 259 VGGFLAGLLAGKSLEEALRFANAAAALVVQKSGAQT 294
|
|
| PRK13508 |
PRK13508 |
tagatose-6-phosphate kinase; Provisional |
1-294 |
8.43e-22 |
|
tagatose-6-phosphate kinase; Provisional
Pssm-ID: 237405 [Multi-domain] Cd Length: 309 Bit Score: 93.63 E-value: 8.43e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 1 MILTLTVNPSIDRLARLDtELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLAL-YPASDSGKFTRLLEVSGIPHEA 79
Cdd:PRK13508 1 MILTVTLNPSIDISYPLD-ELKLDTVNRVVDVSKTAGGKGLNVTRVLSEFGENVLATgLIGGELGQFIAEHLDDQIKHAF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 80 INTTNEARvNLTLAEPDGTTTKLNSPGMTLTKAHRRRVLEKLIHHAKRATWVVFAGSLPPGVPRDFYVQCTEavYSVNPN 159
Cdd:PRK13508 80 YKIKGETR-NCIAILHEGQQTEILEKGPEISVQEADGFLHHFKQLLESVEVVAISGSLPAGLPVDYYAQLIE--LANQAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 160 IRVAMDTSDGPLTEVVRAfpKVRPFLMKPNAYELGQIINQdgeeleaaaaegnylPVAQAARALNEL-------GVSEVL 232
Cdd:PRK13508 157 KPVVLDCSGAALQAVLES--PYKPTVIKPNIEELSQLLGK---------------EVSEDLDELKEVlqqplfeGIEWII 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063218607 233 ATLGEAGAVlsVKSGGCF-AATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYG 294
Cdd:PRK13508 220 VSLGADGAF--AKHNDTFyKVDIPKIEVVNPVGSGDSTVAGIASGLLHQEDDADLLKKANVLG 280
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
11-309 |
3.28e-17 |
|
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: 80.31 E-value: 3.28e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 11 IDRLARLDTELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKT--LALYPASDSGKFTR-LLEVSGIPHEAINTTNEAR 87
Cdd:COG0524 10 VDLVARVDRLPKGGETVLAGSFRRSPGGAAANVAVALARLGARValVGAVGDDPFGDFLLaELRAEGVDTSGVRRDPGAP 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 88 VNLTLAE--PDGTTTKLNSPG--MTLTKAHrrrVLEKLIhhaKRATWVVFAG-SLPPGVPRDFYVQCTEA------VYSV 156
Cdd:COG0524 90 TGLAFILvdPDGERTIVFYRGanAELTPED---LDEALL---AGADILHLGGiTLASEPPREALLAALEAaraagvPVSL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 157 NPNIRVAMDTSDGPLTEvvRAFPKVRpfLMKPNAYELGQIINQDGeeleaaaaegnylpVAQAARALNELGVSEVLATLG 236
Cdd:COG0524 164 DPNYRPALWEPARELLR--ELLALVD--ILFPNEEEAELLTGETD--------------PEEAAAALLARGVKLVVVTLG 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1063218607 237 EAGAVLSVKsGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYPE 309
Cdd:COG0524 226 AEGALLYTG-GEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRPGAQPALPT 297
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
188-307 |
2.95e-09 |
|
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: 57.17 E-value: 2.95e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 188 PNAYELGQIINQDGeeleaaaaeGNYLPVAQAARALNELGVSEVLATLGEAGAVLSVKsGGCFAATSPSIVAQSTVGAGD 267
Cdd:cd01174 181 PNETEAALLTGIEV---------TDEEDAEKAARLLLAKGVKNVIVTLGAKGALLASG-GEVEHVPAFKVKAVDTTGAGD 250
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1063218607 268 CALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGT--TIPY 307
Cdd:cd01174 251 TFIGALAAALARGLSLEEAIRFANAAAALSVTRPGAqpSIPT 292
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
179-308 |
3.74e-07 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 50.89 E-value: 3.74e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 179 PKVRPFL-----MKPNAYELGQIINQDGEELEAAaaegnylpvAQAARALNELGVSEVLATLGEAGAVLSVKSGGCFAAT 253
Cdd:PTZ00292 190 EIIKPFLkyvslFCVNEVEAALITGMEVTDTESA---------FKASKELQQLGVENVIITLGANGCLIVEKENEPVHVP 260
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1063218607 254 SPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGAAATSLPGTTIPYP 308
Cdd:PTZ00292 261 GKRVKAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAISVTRHGTQSSYP 315
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
216-302 |
8.12e-07 |
|
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: 49.88 E-value: 8.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 216 VAQAARALNeLGVSEVLATLGEAGAVLSVKSGGCFAATSPSIVAQsTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGA 295
Cdd:cd01166 208 AAERALALA-LGVKAVVVKLGAEGALVYTGGGRVFVPAYPVEVVD-TTGAGDAFAAGFLAGLLEGWDLEEALRFANAAAA 285
|
....*..
gi 1063218607 296 AATSLPG 302
Cdd:cd01166 286 LVVTRPG 292
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
151-308 |
2.31e-05 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 45.69 E-value: 2.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 151 EAVYSVNPNIRVAMDT-SDGPLTEVVRAFPKVRPflMKPNAYEL----GQIINQDGEELeaaaaegnylpvaQAARALNE 225
Cdd:PRK09954 203 EWVFTLADEIPVFVDTvSEFKAGKIKHWLAHIHT--LKPTQPELeilwGQAITSDADRN-------------AAVNALHQ 267
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 226 LGVSEVLATLGEAGAVLSVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAygAAATSLPGTTI 305
Cdd:PRK09954 268 QGVQQIFVYLPDESVFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFLEGYSFRDSARFAMA--CAAISRASGSL 345
|
...
gi 1063218607 306 PYP 308
Cdd:PRK09954 346 NNP 348
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
1-274 |
1.14e-04 |
|
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: 42.47 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 1 MILTLTvNPSIDRLARLDTELKRGGVFRLPMAEDMAGGKGINVSKALHYAGEKTLALYpasdsgkftrllevsgipHEAI 80
Cdd:cd00287 1 RVLVVG-SLLVDVILRVDALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVG------------------ADAV 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 81 NTTNEARVnltlaepdgtttklnspgmtltkahrRRVLEKLIHHAKRATWVVFAGSLPPGVPRDfyvqcteavysvnpni 160
Cdd:cd00287 62 VISGLSPA--------------------------PEAVLDALEEARRRGVPVVLDPGPRAVRLD---------------- 99
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 161 rvamdtsdgpLTEVVRAFPKVRpfLMKPNAYELGQIINQDGEELEAAaaegnylpvAQAARALNELGVSEVLATLGEAGA 240
Cdd:cd00287 100 ----------GEELEKLLPGVD--ILTPNEEEAEALTGRRDLEVKEA---------AEAAALLLSKGPKVVIVTLGEKGA 158
|
250 260 270
....*....|....*....|....*....|....
gi 1063218607 241 VLSVKSGGCFAATSPSIVAQSTVGAGDCALAGYV 274
Cdd:cd00287 159 IVATRGGTEVHVPAFPVKVVDTTGAGDAFLAALA 192
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
217-300 |
2.58e-04 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 42.00 E-value: 2.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 217 AQAARALNELGVSEVLATLGEAGAVLsVKSGGCFAATSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAvaygAA 296
Cdd:cd01937 173 TELARLIKETGVKEIIVTDGEEGGYI-FDGNGKYTIPASKKDVVDPTGAGDVFLAAFLYSRLSGKDIKEAAEFA----AA 247
|
....
gi 1063218607 297 ATSL 300
Cdd:cd01937 248 AAAK 251
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
214-302 |
4.04e-04 |
|
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: 41.47 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 214 LPVAQAARALNELGVSEVLATLGEAGAVLSVKSG-GCFAATSPSIVaqSTVGAGDCALAGyVMSR--ERGDSYQD----- 285
Cdd:cd01167 199 EDPEEIAALLLLFGLKLVLVTRGADGALLYTKGGvGEVPGIPVEVV--DTTGAGDAFVAG-LLAQllSRGLLALDedela 275
|
90
....*....|....*...
gi 1063218607 286 -ALTTAVAYGAAATSLPG 302
Cdd:cd01167 276 eALRFANAVGALTCTKAG 293
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
217-311 |
1.32e-03 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 39.85 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 217 AQAARALNELGVSEVLATLGEAGAVLSVKS-GGCFAAtsPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGA 295
Cdd:PRK11142 204 AKAAQVLHQKGIETVLITLGSRGVWLSENGeGQRVPG--FRVQAVDTIAAGDTFNGALVTALLEGKPLPEAIRFAHAAAA 281
|
90
....*....|....*...
gi 1063218607 296 AATSLPG--TTIPYPEQV 311
Cdd:PRK11142 282 IAVTRKGaqPSIPWREEI 299
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
218-311 |
4.05e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 38.66 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 218 QAARAL--NELGVSEVLATLGEAGAVLSVKSGGCFAAtSPSIVAQSTVGAGDCALAGYVMSRERGDSYQDALTTAVAYGA 295
Cdd:PLN02341 307 LAGQELlrPGIRTKWVVVKMGSKGSILVTRSSVSCAP-AFKVNVVDTVGCGDSFAAAIALGYIHNLPLVNTLTLANAVGA 385
|
90
....*....|....*...
gi 1063218607 296 A-ATSL-PGTTIPYPEQV 311
Cdd:PLN02341 386 AtAMGCgAGRNVATLEKV 403
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
216-297 |
7.19e-03 |
|
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: 37.33 E-value: 7.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1063218607 216 VAQAARALNELGVSEVLATLGEAGAVLSvkSGGCFAATSPSIVAQ-STVGAGDCALAGYVMSRERGDsyqDALTTAVAYG 294
Cdd:cd01940 176 VKAKLKEAVSRGAKLVIVTRGEDGAIAY--DGAVFYSVAPRPVEVvDTLGAGDSFIAGFLLSLLAGG---TAIAEAMRQG 250
|
...
gi 1063218607 295 AAA 297
Cdd:cd01940 251 AQF 253
|
|
| |
