|
Name |
Accession |
Description |
Interval |
E-value |
| Glk |
COG0837 |
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway ... |
2-320 |
2.73e-132 |
|
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440599 Cd Length: 320 Bit Score: 379.07 E-value: 2.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 2 SHALIADLGGTNARFALVPI-HQYEPLEVRVLPCKNYEDFFAAAADYIENCSVdmENIDAVVLAIAGPVNQAVIRFSNNP 80
Cdd:COG0837 5 TPILVADIGGTNARLALAEGgGGLELLEIRRYPSADYASLEDALRAYLAELGL--PRPRAACLAVAGPVDGDRVKLTNLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 81 WHFTRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGErSTVDPKAPCWVVGAGTGLGISCVVPQDNGPnMVLP 160
Cdd:COG0837 83 WSISAAALRAALGLER-VLLINDFEALAYALPALSPDDLVQLGG-GEPDPGGPRAVIGPGTGLGVAGLVPDGGGW-IVLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 161 GEGGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGI-ERRLTAPEIGEALKQGNDPIANAALE 239
Cdd:COG0837 160 SEGGHVDFAPRDERELELLRYLRRRYGHVSAERVLSGPGLVNLYRALAALDGApPAPLSPAEITAAALAGSDPLAVEALE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 240 QFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCACYASH 319
Cdd:COG0837 240 LFCRILGRVAGNLALTLGARGGVYLAGGIAPRILPLLDRSGFREAFEDKGRFSALLADIPVYVITHPQPGLLGAAAYAAQ 319
|
.
gi 2126536088 320 L 320
Cdd:COG0837 320 L 320
|
|
| glk |
PRK00292 |
glucokinase; Provisional |
1-320 |
4.90e-119 |
|
glucokinase; Provisional
Pssm-ID: 234716 Cd Length: 316 Bit Score: 345.23 E-value: 4.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 1 MSHALIADLGGTNARFALVPIHQYEPLEVRVLPCKNYEDFFAAAADYIENCSVDmeNIDAVVLAIAGPVNQAVIRFSNNP 80
Cdd:PRK00292 1 MKPALVGDIGGTNARFALCDWANGEIEQIKTYATADYPSLEDAIRAYLADEHGV--QVRSACFAIAGPVDGDEVRMTNHH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 81 WHFTRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGERsTVDPKAPCWVVGAGTGLGISCVVPQDNGpNMVLP 160
Cdd:PRK00292 79 WAFSIAAMKQELGLDH-LLLINDFTAQALAIPRLGEEDLVQIGGG-EPVPGAPIAVIGPGTGLGVAGLVPVDGR-WIVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 161 GEGGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIERR-LTAPEIGEALKQGNDPIANAALE 239
Cdd:PRK00292 156 GEGGHVDFAPRSEEEAQILQYLRAEFGHVSAERVLSGPGLVNLYRAICKADGREPElLTPADITERALAGSCPLCRRTLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 240 QFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCACYASH 319
Cdd:PRK00292 236 LFCVILGRVAGNLALTLGARGGVYIAGGIVPRFLEFFKASGFRAAFEDKGRFSAYLADIPVYVITHPQPGLLGAGAYLRQ 315
|
.
gi 2126536088 320 L 320
Cdd:PRK00292 316 A 316
|
|
| Glucokinase |
pfam02685 |
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes ... |
5-319 |
1.38e-118 |
|
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: 344.16 E-value: 1.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 5 LIADLGGTNARFALV--PIHQYEPLEVRVLPCKNYEDFFAAAADYIENcSVDMENIDAVVLAIAGPVNQAVIRFSNNPWH 82
Cdd:pfam02685 1 LAGDIGGTNARFALVtaSGGEPQPLSIRTYASADYPSLEEAIQDYLAE-DAGVTQPRHACFAVAGPVDGDRVRLTNLPWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 83 FTRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGERSTvDPKAPCWVVGAGTGLGISCVVPQDNGPnMVLPGE 162
Cdd:pfam02685 80 ISIEELRATLGLDA-VLLINDFEAVAYAIPRLGADDLVQLGGGKP-DPGAPRAVLGPGTGLGVAGLIPRGGRW-IVLPGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 163 GGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIE-RRLTAPEIGEALKQGNDPIANAALEQF 241
Cdd:pfam02685 157 GGHVDFAPRSEREIELLRYLRRRFGHVSAERVLSGPGLVNLYRALCALDGITpELLTPADITAAALAGDDPLAREALELF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2126536088 242 FVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCACYASH 319
Cdd:pfam02685 237 CAILGSVAGNLALTLGARGGVYIAGGIAPRILEFLKASGFRAAFEDKGRFSALLRDIPVYVITHPQPGLLGAAAAARQ 314
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
4-314 |
1.11e-108 |
|
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: 318.78 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 4 ALIADLGGTNARFALV--PIHQYEPLEVRVLPCKNYEDFFAAAADYIENCsvDMENIDAVVLAIAGPVNQAVIRFSNNPW 81
Cdd:cd24008 1 ILVGDIGGTNARLALAdaGDGSGDLLFVRKYPSADFASLEDALAAFLAEL--GAPRPKAACIAVAGPVDGGRVRLTNLDW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 82 HFTRDEVQSYFGDDkPVALLNDFDAVGYSLEVLSTKDMVVLGERSTVDPKAPCWVVGAGTGLGISCVVPQDNGPNMVLPG 161
Cdd:cd24008 79 SIDAAELRKALGIG-RVRLLNDFEAAAYGLPALGPEDLLVLYGGGGPLPGGPRAVLGPGTGLGVALLVPDGDGGYVVLPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 162 EGGHVDLSACNDLEDDILKFLRTRHKR-VSAERVLSGMGLENLYEAIALREGIERR-LTAPEIGEALKQGnDPIANAALE 239
Cdd:cd24008 158 EGGHADFAPVTEEEAELLEFLRKRFGRsVSYEDVLSGPGLENIYEFLAKLDGAEPPdLTAEEIAEAALAG-DPLAREALD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2126536088 240 QFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCA 314
Cdd:cd24008 237 LFARILGRFAGNLALSFLATGGVYLAGGIAPKNLDLLDSSAFREAFLDKGRMSDLLEDIPVYLVTNEDLGLLGAA 311
|
|
| glk |
TIGR00749 |
glucokinase, proteobacterial type; This model represents glucokinase of E. coli and close ... |
5-314 |
1.54e-86 |
|
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: 262.51 E-value: 1.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 5 LIADLGGTNARFALVPIHQYEPLEVRVLPCKNYEDFFAAAADYIENCSVDMEN-IDAVVLAIAGPVNQAVIRFSNNPWHF 83
Cdd:TIGR00749 1 LVGDIGGTNARLALCEIAPGEISQAKTYSGLDFPSLEAVVRVYLEEHKVELKDpIAKGCFAIACPITGDWVAMTNHTWAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 84 TRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGErSTVDPKAPCWVVGAGTGLGISCVVPQDNGPNMVLPGEG 163
Cdd:TIGR00749 81 SIAELKQNLGFSH-LEIINDFTAVSYAIPGLKKEDLIQFGG-AEPVEGKPIAILGAGTGLGVAHLIHQVDGRWVVLPGEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 164 GHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIER-------RLTAPEIGEALKQGNDPIANA 236
Cdd:TIGR00749 159 GHVDFAPNSELEAIILEYLRAKIGHVSAERVLSGPGLVNIYEALVKADPERQfnklpqeNLKPKDISERALAGSCTDCRR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2126536088 237 ALEQFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCA 314
Cdd:TIGR00749 239 ALSLFCVIYGRFAGNLALNLGTRGGVYIAGGIVPRFIEFFKASGFRAAFEDKGRMKEYVHDIPVYVVLHDNPGLLGAG 316
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| Glk |
COG0837 |
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway ... |
2-320 |
2.73e-132 |
|
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440599 Cd Length: 320 Bit Score: 379.07 E-value: 2.73e-132
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 2 SHALIADLGGTNARFALVPI-HQYEPLEVRVLPCKNYEDFFAAAADYIENCSVdmENIDAVVLAIAGPVNQAVIRFSNNP 80
Cdd:COG0837 5 TPILVADIGGTNARLALAEGgGGLELLEIRRYPSADYASLEDALRAYLAELGL--PRPRAACLAVAGPVDGDRVKLTNLP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 81 WHFTRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGErSTVDPKAPCWVVGAGTGLGISCVVPQDNGPnMVLP 160
Cdd:COG0837 83 WSISAAALRAALGLER-VLLINDFEALAYALPALSPDDLVQLGG-GEPDPGGPRAVIGPGTGLGVAGLVPDGGGW-IVLP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 161 GEGGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGI-ERRLTAPEIGEALKQGNDPIANAALE 239
Cdd:COG0837 160 SEGGHVDFAPRDERELELLRYLRRRYGHVSAERVLSGPGLVNLYRALAALDGApPAPLSPAEITAAALAGSDPLAVEALE 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 240 QFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCACYASH 319
Cdd:COG0837 240 LFCRILGRVAGNLALTLGARGGVYLAGGIAPRILPLLDRSGFREAFEDKGRFSALLADIPVYVITHPQPGLLGAAAYAAQ 319
|
.
gi 2126536088 320 L 320
Cdd:COG0837 320 L 320
|
|
| glk |
PRK00292 |
glucokinase; Provisional |
1-320 |
4.90e-119 |
|
glucokinase; Provisional
Pssm-ID: 234716 Cd Length: 316 Bit Score: 345.23 E-value: 4.90e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 1 MSHALIADLGGTNARFALVPIHQYEPLEVRVLPCKNYEDFFAAAADYIENCSVDmeNIDAVVLAIAGPVNQAVIRFSNNP 80
Cdd:PRK00292 1 MKPALVGDIGGTNARFALCDWANGEIEQIKTYATADYPSLEDAIRAYLADEHGV--QVRSACFAIAGPVDGDEVRMTNHH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 81 WHFTRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGERsTVDPKAPCWVVGAGTGLGISCVVPQDNGpNMVLP 160
Cdd:PRK00292 79 WAFSIAAMKQELGLDH-LLLINDFTAQALAIPRLGEEDLVQIGGG-EPVPGAPIAVIGPGTGLGVAGLVPVDGR-WIVLP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 161 GEGGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIERR-LTAPEIGEALKQGNDPIANAALE 239
Cdd:PRK00292 156 GEGGHVDFAPRSEEEAQILQYLRAEFGHVSAERVLSGPGLVNLYRAICKADGREPElLTPADITERALAGSCPLCRRTLS 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 240 QFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCACYASH 319
Cdd:PRK00292 236 LFCVILGRVAGNLALTLGARGGVYIAGGIVPRFLEFFKASGFRAAFEDKGRFSAYLADIPVYVITHPQPGLLGAGAYLRQ 315
|
.
gi 2126536088 320 L 320
Cdd:PRK00292 316 A 316
|
|
| Glucokinase |
pfam02685 |
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes ... |
5-319 |
1.38e-118 |
|
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: 344.16 E-value: 1.38e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 5 LIADLGGTNARFALV--PIHQYEPLEVRVLPCKNYEDFFAAAADYIENcSVDMENIDAVVLAIAGPVNQAVIRFSNNPWH 82
Cdd:pfam02685 1 LAGDIGGTNARFALVtaSGGEPQPLSIRTYASADYPSLEEAIQDYLAE-DAGVTQPRHACFAVAGPVDGDRVRLTNLPWV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 83 FTRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGERSTvDPKAPCWVVGAGTGLGISCVVPQDNGPnMVLPGE 162
Cdd:pfam02685 80 ISIEELRATLGLDA-VLLINDFEAVAYAIPRLGADDLVQLGGGKP-DPGAPRAVLGPGTGLGVAGLIPRGGRW-IVLPGE 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 163 GGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIE-RRLTAPEIGEALKQGNDPIANAALEQF 241
Cdd:pfam02685 157 GGHVDFAPRSEREIELLRYLRRRFGHVSAERVLSGPGLVNLYRALCALDGITpELLTPADITAAALAGDDPLAREALELF 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2126536088 242 FVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCACYASH 319
Cdd:pfam02685 237 CAILGSVAGNLALTLGARGGVYIAGGIAPRILEFLKASGFRAAFEDKGRFSALLRDIPVYVITHPQPGLLGAAAAARQ 314
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
4-314 |
1.11e-108 |
|
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: 318.78 E-value: 1.11e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 4 ALIADLGGTNARFALV--PIHQYEPLEVRVLPCKNYEDFFAAAADYIENCsvDMENIDAVVLAIAGPVNQAVIRFSNNPW 81
Cdd:cd24008 1 ILVGDIGGTNARLALAdaGDGSGDLLFVRKYPSADFASLEDALAAFLAEL--GAPRPKAACIAVAGPVDGGRVRLTNLDW 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 82 HFTRDEVQSYFGDDkPVALLNDFDAVGYSLEVLSTKDMVVLGERSTVDPKAPCWVVGAGTGLGISCVVPQDNGPNMVLPG 161
Cdd:cd24008 79 SIDAAELRKALGIG-RVRLLNDFEAAAYGLPALGPEDLLVLYGGGGPLPGGPRAVLGPGTGLGVALLVPDGDGGYVVLPS 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 162 EGGHVDLSACNDLEDDILKFLRTRHKR-VSAERVLSGMGLENLYEAIALREGIERR-LTAPEIGEALKQGnDPIANAALE 239
Cdd:cd24008 158 EGGHADFAPVTEEEAELLEFLRKRFGRsVSYEDVLSGPGLENIYEFLAKLDGAEPPdLTAEEIAEAALAG-DPLAREALD 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2126536088 240 QFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCA 314
Cdd:cd24008 237 LFARILGRFAGNLALSFLATGGVYLAGGIAPKNLDLLDSSAFREAFLDKGRMSDLLEDIPVYLVTNEDLGLLGAA 311
|
|
| glk |
TIGR00749 |
glucokinase, proteobacterial type; This model represents glucokinase of E. coli and close ... |
5-314 |
1.54e-86 |
|
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: 262.51 E-value: 1.54e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 5 LIADLGGTNARFALVPIHQYEPLEVRVLPCKNYEDFFAAAADYIENCSVDMEN-IDAVVLAIAGPVNQAVIRFSNNPWHF 83
Cdd:TIGR00749 1 LVGDIGGTNARLALCEIAPGEISQAKTYSGLDFPSLEAVVRVYLEEHKVELKDpIAKGCFAIACPITGDWVAMTNHTWAF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 84 TRDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGErSTVDPKAPCWVVGAGTGLGISCVVPQDNGPNMVLPGEG 163
Cdd:TIGR00749 81 SIAELKQNLGFSH-LEIINDFTAVSYAIPGLKKEDLIQFGG-AEPVEGKPIAILGAGTGLGVAHLIHQVDGRWVVLPGEG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 164 GHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIER-------RLTAPEIGEALKQGNDPIANA 236
Cdd:TIGR00749 159 GHVDFAPNSELEAIILEYLRAKIGHVSAERVLSGPGLVNIYEALVKADPERQfnklpqeNLKPKDISERALAGSCTDCRR 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2126536088 237 ALEQFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCA 314
Cdd:TIGR00749 239 ALSLFCVIYGRFAGNLALNLGTRGGVYIAGGIVPRFIEFFKASGFRAAFEDKGRMKEYVHDIPVYVVLHDNPGLLGAG 316
|
|
| PRK14101 |
PRK14101 |
bifunctional transcriptional regulator/glucokinase; |
5-324 |
5.03e-56 |
|
bifunctional transcriptional regulator/glucokinase;
Pssm-ID: 184507 [Multi-domain] Cd Length: 638 Bit Score: 192.05 E-value: 5.03e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 5 LIADLGGTNARFALvPIHQYEPLEVRVLPCKNYEDFFAAAADYIENCSVDMENIDAVvlAIAGPVNQAVIRFSNNPWHFT 84
Cdd:PRK14101 21 LLADVGGTNARFAL-ETGPGEITQIRVYPGADYPTLTDAIRKYLKDVKIGRVNHAAI--AIANPVDGDQVRMTNHDWSFS 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 85 RDEVQSYFGDDKpVALLNDFDAVGYSLEVLSTKDMVVLGERSTVdPKAPCWVVGAGTGLGISCVVPQDNgPNMVLPGEGG 164
Cdd:PRK14101 98 IEATRRALGFDT-LLVVNDFTALAMALPGLTDAQRVQVGGGTRR-QNSVIGLLGPGTGLGVSGLIPADD-RWIALGSEGG 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 165 HVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREG--IERRLTAPEIGEALKQGnDPIANAALEQFF 242
Cdd:PRK14101 175 HASFAPQDEREDLVLQYARKKYPHVSFERVCAGPGMEIIYRALAARDKkrVAANVDTAEIVERAHAG-DALALEAVECFC 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 243 VFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGC-ACYASHLV 321
Cdd:PRK14101 254 AILGTFAGNLALTLGALGGIYIGGGVVPKLGELFTRSSFRARFEAKGRFEAYLANIPTYLITAEYPAFLGVsAILAEQLS 333
|
...
gi 2126536088 322 SKA 324
Cdd:PRK14101 334 NRT 336
|
|
| PRK12408 |
PRK12408 |
glucokinase; Provisional |
5-314 |
2.01e-52 |
|
glucokinase; Provisional
Pssm-ID: 237092 Cd Length: 336 Bit Score: 175.71 E-value: 2.01e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 5 LIADLGGTNARFALV-----PIHQYEPLEVRVLPCKNYEDFFAAAADYIENCSVdmenIDAVVLAIAG-PVNQAVIRFSN 78
Cdd:PRK12408 19 VAADVGGTHVRVALVcaspdAAKPVELLDYRTYRCADYPSLAAILADFLAECAP----VRRGVIASAGyALDDGRVITAN 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 79 NPWHFTRDEVQSYFGDdKPVALLNDFDAVGYSLEVLSTKDMVVL-GERSTVDpkAPCWVVGAGTGLGISCVVPQDNGPnM 157
Cdd:PRK12408 95 LPWTLSPEQIRAQLGL-QAVHLVNDFEAVAYAAPYMEGNQVLQLsGPAQAAA--GPALVLGPGTGLGAALWIPNGGRP-V 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 158 VLPGEGGHVDLSACNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIERRLTAPE-IGEALKQGNDPIANA 236
Cdd:PRK12408 171 VLPTEAGQAALAAASELEMQLLQHLLRTRTHVPIEHVLSGPGLLNLYRALCALRGATPVHASPAaITAAALAGDDALAHE 250
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2126536088 237 ALEQFFVFLGRVIGDLVLSVESRGGVYIAGGIVPRYVNEILESGFREAMQDKGRMKEFVSPIPTFIVMSEYPGLMGCA 314
Cdd:PRK12408 251 ALQVFCGFLGSVVGDMALAYGARGGVYLAGGILPQIADFLARSDFVERFLNKGPMRPALEQVPVKLVEHGQLGVLGAA 328
|
|
| PTZ00288 |
PTZ00288 |
glucokinase 1; Provisional |
8-324 |
6.34e-18 |
|
glucokinase 1; Provisional
Pssm-ID: 240346 [Multi-domain] Cd Length: 405 Bit Score: 83.82 E-value: 6.34e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 8 DLGGTNARFALVPIHQYEPLEVR--VLPCKN-----YE--DFFAAAADYIENCSVDMENIDAVVLAIAGPV-NQAVIRFS 77
Cdd:PTZ00288 32 DVGGTNARVGFAREVQHDDSGVHiiYVRFNVtktdiREllEFFDEVLQKLKKNLSFIQRVAAGAISVPGPVtGGQLAGPF 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 78 NNPWHFTR--DEVQSYFGDDKPvALLNDFDAVGYSLEVLST--------KDMVVLGERSTVDPKAP---------CWVVG 138
Cdd:PTZ00288 112 NNLKGIARltDYPVELFPPGRS-ALLNDLEAGAYGVLAVSNagrlseyfKVMWKGTQWDALSEGKPagsvigrgrCMVLA 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 139 AGTGLGISCVV-PQDNGPNMVLPGEGGHVDLSAC----NDLEDDILKFLR--------TRHKRVSAERVLSGMGLENLYE 205
Cdd:PTZ00288 191 PGTGLGSSLIHyVGVSDQYIVIPLECGHLSISWPanedSDYVQALAGYLAskalskgiDSTVYPIYEDIVSGRGLEFNYA 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 206 aIALREGIE--RRLTAPEIGEALKQGNDPIANAALEQFFVFLGRV-----IGDLVLSVesrggVYIAGGIV--------P 270
Cdd:PTZ00288 271 -YEKRGNKPsaPLKEAAEVAKLAKYGSDVAAVKAMKRHYKYLMRLaaeisMQFLPLTV-----VLMGDNIVynsfffdnP 344
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*
gi 2126536088 271 RYVNEILesgfREAMQDKGRMKEFVSPIPTFIVMSEYP-GLMGCACYASHLVSKA 324
Cdd:PTZ00288 345 ENVKQLQ----ARITEHKMERLKFLSRTTFLRQKKSVNlNLLGCLQFGSQLSHLK 395
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-317 |
8.29e-16 |
|
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: 76.47 E-value: 8.29e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 1 MSHALIADLGGTNARFALVPiHQYEPLEVRVLP---CKNYEDFFAAAADYIE----NCSVDMENIDAVVLAIAGPVNQA- 72
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVD-LDGEVLARERIPtpaGAGPEAVLEAIAELIEellaEAGISRGRILGIGIGVPGPVDPEt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 73 -VIRFSNNPWHFT----RDEVQSYFGddKPVALLNDFDAVGYSlEVL-----STKDMVVLgerstvdpkapcwVVGAGTG 142
Cdd:COG1940 83 gVVLNAPNLPGWRgvplAELLEERLG--LPVFVENDANAAALA-EAWfgagrGADNVVYL-------------TLGTGIG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 143 LGIscVVpqdNGpnMVLPG------EGGHV------DLSACNdleddilkflrtrhKRVSAERVLSGMGLENLYEAIALR 210
Cdd:COG1940 147 GGI--VI---NG--KLLRGangnagEIGHMpvdpdgPLCGCG--------------NRGCLETYASGPALLRRARELGGA 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 211 EgierRLTAPEIGEALKQGnDPIANAALEQFFVFLGRVIGDLV--LSVESrggVYIAGGIVPRYvnEILESGFREAMqDK 288
Cdd:COG1940 206 E----KLTAEELFAAARAG-DPLALEVLDEAARYLGIGLANLInlLDPEV---IVLGGGVSAAG--DLLLEPIREAL-AK 274
|
330 340 350
....*....|....*....|....*....|..
gi 2126536088 289 GRMKEFVSPIPtfIVMSEY---PGLMGCACYA 317
Cdd:COG1940 275 YALPPAREDPR--IVPASLgddAGLLGAAALA 304
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
8-314 |
1.17e-04 |
|
nucleotide-binding domain (NBD) of Streptomyces griseus 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. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466911 [Multi-domain] Cd Length: 306 Bit Score: 43.11 E-value: 1.17e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 8 DLGGTNARFALVPiHQYEPLEVRVLPCknyedffAAAADYIENCSVDM-------ENIDAVVLAIAGPVN--QAVIRFSN 78
Cdd:cd24061 5 DIGGTKIAAGVVD-EEGEILATERVPT-------PPTADGIVDAIVEAveelregHDVSAVGVAAAGFVDadRATVLFAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 79 N-PW--HFTRDEVQSYFGddKPVALLNDFDAVGYSlEVL-----STKDMVVLgersTVdpkapcwvvgaGTGLGISCVVp 150
Cdd:cd24061 77 NiAWrnEPLKDLLEARIG--LPVVIENDANAAAWA-EYRfgagrGTDDMVMI----TV-----------GTGLGGGIVI- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 151 qdNGP----NMVLPGEGGHV------DLSACNdleddilkflrtrhKRVSAERVLSGMGLENLYEAIA----------LR 210
Cdd:cd24061 138 --GGKllrgAFGIAGEFGHIrvvpdgLLCGCG--------------SRGCWEQYASGRALVRYAKEAAnatpegaavlLA 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 211 EGIERRLTAPEIGEALKQGnDPIANAALEQFFVFLGRVIGDL--VLSVEsrggVYIAGGIVPRYVNEILESgFREAMQDK 288
Cdd:cd24061 202 DGSVDGITGKHISEAARAG-DPVALDALRELARWLGAGLASLaaLLDPE----LFVIGGGVSDAGDLLLDP-IREAFERW 275
|
330 340
....*....|....*....|....*...
gi 2126536088 289 GRMKEFvSPIPTFIVMSEYP--GLMGCA 314
Cdd:cd24061 276 LPGRGW-RPIPRLRTAQLGNdaGLIGAA 302
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
8-256 |
2.21e-04 |
|
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called GlcNAc kinase, catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding 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: 466907 [Multi-domain] Cd Length: 298 Bit Score: 42.22 E-value: 2.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 8 DLGGTNARFA-----LVPIHQYeplevRV-LPCKNYEDFFAAAADYIENCSVDMENIDAVVLAIAG---PVNQAVIRfSN 78
Cdd:cd24057 6 DIGGTKIEFAvfdeaLQLVWTK-----RVpTPTDDYAAFLAAIAELVAEADARFGVKGPVGIGIPGvidPEDGTLIT-AN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 79 NP----WHFTRDEVQSYfgdDKPVALLNDFDAVgysleVLS-TKDMVVLGERStvdpkapcwVVGA--GTGLGISCVV-- 149
Cdd:cd24057 80 IPaakgRPLRADLSARL---GRPVRIDNDANCF-----ALSeAWDGAGRGYPS---------VFGLilGTGVGGGLVVng 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 150 ---PQDNGpnmvLPGEGGHVDLSA-CNDLEDDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREgierrLTAPEIGEA 225
Cdd:cd24057 143 rlvGGRSG----IAGEWGHGPLPAdALLLGYDLPVLRCGCGQTGCLETYLSGRGLERLYAHLYGEE-----LDAPEIIAA 213
|
250 260 270
....*....|....*....|....*....|.
gi 2126536088 226 LKQGnDPIANAALEQFFVFLGRVIGDLVLSV 256
Cdd:cd24057 214 WAAG-DPQAVAHVDRWLDLLAGCLANILTAL 243
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
8-103 |
6.40e-04 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong 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: 466849 [Multi-domain] Cd Length: 239 Bit Score: 40.52 E-value: 6.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 8 DLGGTNARFALVPIHqYEPLEVRVLPC---KNYEDFFAAAADYIENCSVD---MENIDAVVLAIAGPVNQA--VIRFSNN 79
Cdd:cd23763 4 DIGGTKIRAALVDLD-GEILARERVPTpaeEGPEAVLDRIAELIEELLAEagvRERILGIGIGVPGPVDPEtgIVLFAPN 82
|
90 100
....*....|....*....|....*...
gi 2126536088 80 PWHFT----RDEVQSYFGddKPVALLND 103
Cdd:cd23763 83 LPWWKnvplRELLEERLG--LPVVVEND 108
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-285 |
1.37e-03 |
|
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and similar proteins; The family includes Fusobacterium nucleatum N-acetylmannosamine kinase (NanK; EC 2.7.1.60) and beta-glucoside kinase (BglK; EC 2.7.1.85) from Klebsiella pneumoniae and Listeria innocua. NanK catalyzes the second step of the sialic acid catabolic pathway, transferring a phosphate group from adenosine 5'-triphosphate to the C6 position of N-acetylmannosamine to generate N-acetylmannosamine 6-phosphate. Unlike other NanK enzymes and ROK family members, F. nucleatum NanK does not have a conserved zinc-binding site. BglK catalyzes the ATP-dependent phosphorylation of cellobiose to produce cellobiose-6'-P. It may have a dual role of kinase and transcriptional regulator of the cellobiose-PTS operon. The subfamily belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466918 [Multi-domain] Cd Length: 294 Bit Score: 39.85 E-value: 1.37e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 3 HALIADLGGTNARFALVPiHQYEPLEVRVLP-----CKNY--EDFFAAAADYIENCsvdmeNIDAVVLAIAGPVNQA--- 72
Cdd:cd24068 1 KILGIDIGGTKIKYGLVD-ADGEILEKDSVPtpaskGGDAilERLLEIIAELKEKY-----DIEGIGISSAGQVDPKtge 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 73 VIRFSNNPWHFT----RDEVQSYFGddKPVALLNDFDAVGYSLEVL----STKDMVVLgersTVdpkapcwvvgaGTGLG 144
Cdd:cd24068 75 VIYATDNLPGWTgtnlKEELEERFG--LPVAVENDVNCAALAEKWLgaakGLDDFLCL----TL-----------GTGIG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 145 ISCVVpqdNGpNMV-----LPGEGGHVDLsacndledDILKFLRTRHKRVSAERVLSGMGLENLYEAIALREGIerrlTA 219
Cdd:cd24068 138 GAIIL---DG-RLYrgangSAGELGHMVV--------DPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGI----DG 201
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2126536088 220 PEIGEALKQGnDPIANAALEQFFVFLGRVIGDLVlSVESRGGVYIAGGIV---PRYVNEILESGFREAM 285
Cdd:cd24068 202 REIFDLADAG-DPLAKEVVEEFAEDLATGLANLV-HIFDPEVIVIGGGISaqgELFLEELREELRKLLM 268
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
192-253 |
1.58e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; Escherichia coli FRK (EC 2.7.1.4), also called D-fructose kinase, manno(fructo)kinase, or MAK, catalyzes the phosphorylation of fructose to fructose-6-phosphate. It has also low level glucokinase activity in vitro. It is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine. 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: 466916 [Multi-domain] Cd Length: 294 Bit Score: 39.49 E-value: 1.58e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2126536088 192 ERVLSGMGLENLYEAIAlregiERRLTAPEIGEALKQGnDPIANAALEQFFVFLGRVIGDLV 253
Cdd:cd24066 181 ETFLSGPALERDYARLT-----GKTLSAEEIVALARAG-DAAAVATLDRFLDRLGRALANVI 236
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
199-253 |
6.58e-03 |
|
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Bacillus subtilis xylose repressor (BsXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. BsXylR acts as transcriptional repressor of xylose-utilizing enzymes.
Pssm-ID: 466926 [Multi-domain] Cd Length: 303 Bit Score: 37.93 E-value: 6.58e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 2126536088 199 GLENLYEAIALREGIERRLTAPEIGEALKQGnDPIANAALEQFFVFLGRVIGDLV 253
Cdd:cd24076 186 SERALLRAAGRLGAGGEPLSLAELVEAARAG-DPAALAALEEVGEYLGIGLANLV 239
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
8-286 |
8.23e-03 |
|
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466988 [Multi-domain] Cd Length: 286 Bit Score: 37.55 E-value: 8.23e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 8 DLGGTNARFALVPiHQYEPLEVRVLPCK--NYEDFFAAAADYIENCSvdmENIDAVVLAIAGPVNQA---VIRFSNNPWH 82
Cdd:cd24152 6 DIGGTFIKYALVD-ENGNIIKKGKIPTPkdSLEEFLDYIKKIIKRYD---EEIDGIAISAPGVIDPEtgiIYGGGALPYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 83 FTRD---EVQSYFGddKPVALLNDFDAVGYS---LEVL-STKDMVVLgerstvdpkapcwVVGAGTGLGIscVVPQD--N 153
Cdd:cd24152 82 KGFNlkeELEERCN--LPVSIENDAKCAALAelwLGSLkGIKNGAVI-------------VLGTGIGGAI--IIDGKlyR 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2126536088 154 GPNMvLPGEGGHVdlsacndLEDDIlkflrtRHKRVSAERVLSGMGLENLYEAIALREGierrLTAPEIGEALKQGnDPI 233
Cdd:cd24152 145 GSHF-FAGEFSYL-------LTDDD------DKDLLFFSGLASMFGLVKRYNKAKGLEP----LDGEEIFEKYAKG-DEA 205
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2126536088 234 ANAALEQFFVFLGRVIGDL--VLSVESrggVYIAGGI---------VPRYVNEILESGFREAMQ 286
Cdd:cd24152 206 AKKILDEYIRNLAKLIYNIqyILDPEV---IVIGGGIseqplfiedLKKEVNEILANRPGSIPK 266
|
|
| |
