|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
9-293 |
2.70e-74 |
|
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: 229.38 E-value: 2.70e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSAlIMDTQ--IREKRQIETPKTDKDNFILVLVELIRSYQqiEPIEFVGFSVPGAV-KEASTVFFGGAVA 85
Cdd:cd24152 3 LVFDIGGTFIKYA-LVDENgnIIKKGKIPTPKDSLEEFLDYIKKIIKRYD--EEIDGIAISAPGVIdPETGIIYGGGALP 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 86 CLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLIQD 165
Cdd:cd24152 80 YLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLLTD 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 166 rGINGAESFAGINLSAVRLVKELTKLFQCEPE-GPLVFDyLYQKEDDQAQTLYRTYCNQVAILCFNIQCLLDLDKIIIGG 244
Cdd:cd24152 160 -DDDKDLLFFSGLASMFGLVKRYNKAKGLEPLdGEEIFE-KYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGG 237
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 488261292 245 GISKQKRLIRDIQKNYEAIFSVSPmieQTITKMTIEAAAFESEANLIGA 293
Cdd:cd24152 238 GISEQPLFIEDLKKEVNEILANRP---GSIPKPEIKACKFGNDANLLGA 283
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
6-294 |
4.93e-60 |
|
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: 193.57 E-value: 4.93e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 6 MWTLSIDIGGTYIKSALI-MDTQIREKRQIETPK-TDKDNFILVLVELIRSYQQ-----IEPIEFVGFSVPGAV-KEAST 77
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVdLDGEVLARERIPTPAgAGPEAVLEAIAELIEELLAeagisRGRILGIGIGVPGPVdPETGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 78 VFFGGAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAG 157
Cdd:COG1940 85 VLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 158 EVSFLIQDR-------GING-AESFAginlSAVRLVKELTKLFQCEP-EGPLVFDyLYQKEDDQAQTLYRTYCNQVAILC 228
Cdd:COG1940 165 EIGHMPVDPdgplcgcGNRGcLETYA----SGPALLRRARELGGAEKlTAEELFA-AARAGDPLALEVLDEAARYLGIGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488261292 229 FNIQCLLDLDKIIIGGGISKQ-KRLIRDIQKNYEAiFSVSPMIEQTitkmTIEAAAFESEANLIGAA 294
Cdd:COG1940 240 ANLINLLDPEVIVLGGGVSAAgDLLLEPIREALAK-YALPPAREDP----RIVPASLGDDAGLLGAA 301
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
9-295 |
8.15e-44 |
|
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: 151.17 E-value: 8.15e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALIMDT-QIREKRQIETPKTDKDNFILV-LVELIRSYQQIEPIEFVGFSVPGAV--KEASTVFFGGAV 84
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADgEILEKDSVPTPASKGGDAILErLLEIIAELKEKYDIEGIGISSAGQVdpKTGEVIYATDNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 85 ACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFL-I 163
Cdd:cd24068 83 PGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMvV 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 164 QDRGINGAESFAGI-----NLSA-VRLVKELTKLFQCEPEgpLVFDyLYQKEDDQAQTLYRTYCNQVAILCFNIQCLLDL 237
Cdd:cd24068 163 DPGGRPCCCGGKGCleqyaSGTAlVRRVAEALGEPGIDGR--EIFD-LADAGDPLAKEVVEEFAEDLATGLANLVHIFDP 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488261292 238 DKIIIGGGISKQK-RLIRDIQKNYEAIFsvspmIEQTITKMTIEAAAFESEANLIGAAK 295
Cdd:cd24068 240 EVIVIGGGISAQGeLFLEELREELRKLL-----MPPLLDATKIEPAKLGNDAGLLGAAY 293
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
9-294 |
5.38e-38 |
|
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: 134.51 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALI-MDTQIREKRQIETPKT-DKDNFILVLVELIRSYQQ----IEPIEFVGFSVPGAV-KEASTVFFG 81
Cdd:cd23763 1 IGIDIGGTKIRAALVdLDGEILARERVPTPAEeGPEAVLDRIAELIEELLAeagvRERILGIGIGVPGPVdPETGIVLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 82 GAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSF 161
Cdd:cd23763 81 PNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 162 LiqdrgingaesfaginlsavrlvkeltklfqcepegplvfdylyqkeddqaqTLYRTYCNQVAILCFNIQCLLDLDKII 241
Cdd:cd23763 161 I----------------------------------------------------TVLEEAARYLGIGLANLINLLNPELIV 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 488261292 242 IGGGISKQKRLIRDIQKNYEAIFSVSPMIEQTitkmTIEAAAFESEANLIGAA 294
Cdd:cd23763 189 LGGGVAEAGDLLLEPIREAVRRRALPPLRRRV----RIVPSELGDDAGLLGAA 237
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
9-294 |
2.97e-33 |
|
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: 123.16 E-value: 2.97e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALIMDTQIREKRQIETPKT-DKDNFILVLVELIRSYQqiEPIEFVGFSVPGAVKEAS-TVFFGGAVAC 86
Cdd:cd24069 1 LAIDIGGTKIAAALIGNGQIIDRRQIPTPRSgTPEALADALASLLADYQ--GQFDRVAVASTGIIRDGVlTALNPKNLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 87 LNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLIQDR 166
Cdd:cd24069 79 LSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 167 G--------INGAESFAGINLSAVRLVKELTKLFQCepegPLVFDyLYQKEDDQAQTLYRTYCNQVAILCFNIQCLLDLD 238
Cdd:cd24069 159 PgpvcgcgrRGCVEAIASGTAIAAAASEILGEPVDA----KDVFE-RARSGDEEAARLIDRAARALADLIADLKATLDLD 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 488261292 239 KIIIGGGI---SKQKRLIRDIQKNYEAIFSVSpmieqtitkmtIEAAAFESEANLIGAA 294
Cdd:cd24069 234 CVVIGGSVglaEGFLERVEQYLADEPAIFRVS-----------LEPARLGQDAGLLGAA 281
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
7-295 |
7.23e-33 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis 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: 466912 [Multi-domain] Cd Length: 311 Bit Score: 123.17 E-value: 7.23e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 7 WTLSIDIGGTYIKSALI-MDTQIREKRQIETPKTDKDNFILVlvELIRSYQQI--------EPIEFVGFSVPGAVKEAST 77
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLtQEGEIVQKWEIPTNKLEGGENIIT--DIAESIQQLleelgyskEDLIGIGVGVPGPVDVETG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 78 VFFGGAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAG 157
Cdd:cd24062 79 TVEVAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 158 EVSFLIQDR--------GINGA-ESFA---GINLSAVRLVKE---LTKLFQCEPEGPL----VFDyLYQKEDDQAQTLYR 218
Cdd:cd24062 159 EIGHITVNPeggapcncGKTGClETVAsatGIVRIAREELEEgkgSSALRILALGGELtakdVFE-AAKAGDELALAVVD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488261292 219 TYCNQVAILCFNIQCLLDLDKIIIGGGISKQKRLIRDIQKNYEAIFSVSpmieQTITKMTIEAAAFESEANLIGAAK 295
Cdd:cd24062 238 TVARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFP----RVRQDTEIVLATLGNDAGVIGAAW 310
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
8-294 |
3.02e-32 |
|
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; HK (EC 2.7.1.1) possesses the ability to transfer an inorganic phosphate group from ATP to a substrate. It catalyzes the ATP-dependent phosphorylation of aldo- and keto-hexose sugars to the hexose-6-phosphate (H6P). Thermus thermophilus HK possesses significant enzymatic activity against glucose and mannose. However, it shows little catalytic capacity for galactose and fructose. 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: 466915 [Multi-domain] Cd Length: 289 Bit Score: 120.90 E-value: 3.02e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 8 TLSIDIGGTYIKSALIMDTQIREKRQIETPKTDKDNFILVLVELIRSYQQIEP-IEFVGFSVPGAVK-EASTVFFGGAVA 85
Cdd:cd24065 2 TIGLDLGGTKIAAGVVDGGRILSRLVVPTPREGGEAVLDALARAVEALQAEAPgVEAVGLGVPGPLDfRRGRVRFAPNIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 86 CLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLI-- 163
Cdd:cd24065 82 GLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTTvl 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 164 -----QDRGINGA-ESFAginlSAVRLVKELTKLFQCEPEGPLVFDyLYQKEDDQAQTLYRTYCNQVAILCFNIQCLLDL 237
Cdd:cd24065 162 pggpmCGCGLVGClEALA----SGRALARDASFAYGRPMSTAELFE-LAQQGEPKALRIVEQAAAHLGIGLANLQKALDP 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488261292 238 DKIIIGGGISKQkrlirdiqknyeAIFSVSPMIE------QTITKMTIEAAAFESEANLIGAA 294
Cdd:cd24065 237 EVFVLGGGVAQV------------GDYYLLPVQEaarrytEGWHAPPLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
6-294 |
2.86e-31 |
|
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: 118.49 E-value: 2.86e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 6 MWTlSIDIGGTYIKSALI-MDTQIREKRQIETPKTDKDNFILVLVELIRSYQQIEPI-EFVGFSVPGAVKEASTVFFGGA 83
Cdd:cd24057 1 MYY-GFDIGGTKIEFAVFdEALQLVWTKRVPTPTDDYAAFLAAIAELVAEADARFGVkGPVGIGIPGVIDPEDGTLITAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 84 VACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFL- 162
Cdd:cd24057 80 IPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 163 ----------------------------IQDRGING-AESFAGINLSAVRLVKeltklfqcepegplvfdyLYQKEDDQA 213
Cdd:cd24057 160 lpadalllgydlpvlrcgcgqtgcletyLSGRGLERlYAHLYGEELDAPEIIA------------------AWAAGDPQA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 214 QTLYRTYCNQVAILCFNIQCLLDLDKIIIGGGISKQKRLIRDIQKNYEA-IFSVspmieqtITKMTIEAAAFESEANLIG 292
Cdd:cd24057 222 VAHVDRWLDLLAGCLANILTALDPDVVVLGGGLSNFPALIAELPAALPAhLLSG-------ARTPRIVPARHGDAGGVRG 294
|
..
gi 488261292 293 AA 294
Cdd:cd24057 295 AA 296
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
9-294 |
2.00e-28 |
|
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.
Pssm-ID: 395384 [Multi-domain] Cd Length: 292 Bit Score: 110.89 E-value: 2.00e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALI-MDTQIREKRQIETPKTD-KDNFILVLVELIRSYQQ-IEPIEFVGFSVPGAVKEASTVFFGGAVA 85
Cdd:pfam00480 1 IGIDIGGTKIAAALFdEEGEILARERVPTPTTTtEETLVDAIAFFVDSAQRkFGELIAVGIGSPGLISPKYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 86 CLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLIQD 165
Cdd:pfam00480 81 GWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQLD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 166 RgiNGAESFAG------INLSAVRLVKEL-TKLFQCEPEGPLVfdyLYQKEDDQAQTLYRTYCNQVAILCFNIQCLLDLD 238
Cdd:pfam00480 161 P--NGPKCGCGnhgcleTIASGRALEKRYqQKGEDLEGKDIIV---LAEQGDEVAEEAVERLARYLAKAIANLINLFDPQ 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 239 KIIIGGGISKQKRLIRDIQKNYEAI----FSVSPMIeqtitkmtIEAAAFESEANLIGAA 294
Cdd:pfam00480 236 AIVLGGGVSNADGLLEAIRSLVKKYlngyLPVPPVI--------IVAASLGDNAGALGAA 287
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
11-294 |
2.05e-25 |
|
nucleotide-binding domain (NBD) of Aeropyrum pernix 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: 466913 [Multi-domain] Cd Length: 308 Bit Score: 102.80 E-value: 2.05e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 11 IDIGGTYIKSALI-MDTQIREKRQIETPKT-DKDNFILVLVELIR---SYQQIEPIEFVGFSVPGAVKEASTVFFGGAVA 85
Cdd:cd24063 5 VDIGGTWIRAGLVdEDGRILLKIRQPTPKTgDPGTVSEQVLGLIEtllSKAGKDSIEGIGVSSAGPLDLRKGTIVNSPNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 86 CLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLIQD 165
Cdd:cd24063 85 KGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHLVVD 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 166 RGINGA---------ESFAG-----------INLSAVRLVKELTKLFQCEPEGPLVFDyLYQKEDDQAQTLYRTYCNQVA 225
Cdd:cd24063 165 TESGLKcgcggyghwEAFASgrgiprfarewAEGFSSRTSLKLRNPGGEGITAKEVFS-AARKGDPLALKIIEKLARYNG 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 226 ILCFNIQCLLDLDKIIIGGGISK-QKRLIRDIQKNYEAIFSVSPMIEqtitkmtIEAAAFESEANLIGAA 294
Cdd:cd24063 244 RGIANVINAYDPELIVIGGSVFNnNKDILDPLIEYLEKNPAISKGPE-------IVLSELGDDVGLIGAL 306
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
9-294 |
2.21e-25 |
|
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]
Pssm-ID: 273246 [Multi-domain] Cd Length: 318 Bit Score: 103.06 E-value: 2.21e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALI-MDTQIREKRQIETPKTDkDNFILVLVELIRSYQQI-----EPIEFVGFSVPGAV-KEASTVFFG 81
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVdEEGNILSKWKVPTDTTP-ETIVDAIASAVDSFIQHiakvgHEIVAIGIGAPGPVnRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 82 GAVACLNEVnLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSF 161
Cdd:TIGR00744 80 VNLDWKQEP-LKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 162 L--IQDRG----------INGAESFAGInlsaVRLVK----------ELTKLFQCEP-EGPLVFDylYQKEDDQ-AQTLY 217
Cdd:TIGR00744 159 IrmVPDGRllcncgkqgcIETYASATGL----VRYAKranakperaeVLLALGDGDGiSAKHVFV--AARQGDPvAVDSY 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488261292 218 RTYCNQVAILCFNIQCLLDLDKIIIGGGISKQKRLIRD-IQKNYEAiFSVSPMIEQTitkmTIEAAAFESEANLIGAA 294
Cdd:TIGR00744 233 REVARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDpIRKSYKR-WLFGGARQVA----DIIAAQLGNDAGLVGAA 305
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
8-294 |
2.07e-24 |
|
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: 100.12 E-value: 2.07e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 8 TLSIDIGGTYIKSALIMDT-QIREKRQIETPKtDKDNFILVLVELIRSYQQIEPIEFVGFSVPGAV-KEASTVFFGGAVA 85
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEgEILATERVPTPP-TADGIVDAIVEAVEELREGHDVSAVGVAAAGFVdADRATVLFAPNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 86 CLNEvNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFL--I 163
Cdd:cd24061 80 WRNE-PLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIrvV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 164 QDR-----GINGA-ESFAginlSAVRLVKELTKLFQCEPEGPLVfdyLYQKEDDQ-----------------AQTLYRTY 220
Cdd:cd24061 159 PDGllcgcGSRGCwEQYA----SGRALVRYAKEAANATPEGAAV---LLADGSVDgitgkhiseaaragdpvALDALREL 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488261292 221 CNQVAILCFNIQCLLDLDKIIIGGGISKQKRLIRD-IQKNYEAIFSVSPmieqTITKMTIEAAAFESEANLIGAA 294
Cdd:cd24061 232 ARWLGAGLASLAALLDPELFVIGGGVSDAGDLLLDpIREAFERWLPGRG----WRPIPRLRTAQLGNDAGLIGAA 302
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
6-294 |
6.70e-24 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 98.45 E-value: 6.70e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 6 MWTLSIDIGGTYIKSALIM-DTQIREKRQIETPKT-DKDNFILVLVELIRSYQQiePIEFVGFSVPGAVKEastvffgGA 83
Cdd:PRK05082 1 MTTLAIDIGGTKIAAALVGeDGQIRQRRQIPTPASqTPEALRQALSALVSPLQA--QADRVAVASTGIIND-------GI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 84 VACLNEVNL--------KQEIEKHLPVRVFVENDAKAAVLGEasFGHLKG-IENGAGIILGTGVGVGLLLDGQVRKGPHC 154
Cdd:PRK05082 72 LTALNPHNLggllhfplVQTLEQLTDLPTIALNDAQAAAWAE--YQALPDdIRNMVFITVSTGVGGGIVLNGKLLTGPGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 155 QAGEVSFLIQDrgINGA----------ESFA---GINLSAvrlvkeLTKLFQCEPEgpLVFDyLYQKEDDQAQTLYRTYC 221
Cdd:PRK05082 150 LAGHIGHTLAD--PHGPvcgcgrrgcvEAIAsgrAIAAAA------QGWLAGCDAK--TIFE-RAGQGDEQAQALINRSA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488261292 222 NQVAILCFNIQCLLDLDKIIIGGGISKQK---RLIRDIQKNYEAIFSVspmieqtitkmTIEAAAFESEANLIGAA 294
Cdd:PRK05082 219 QAIARLIADLKATLDCQCVVLGGSVGLAEgylELVQAYLAQEPAIYHV-----------PLLAAHYRHDAGLLGAA 283
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
6-294 |
2.89e-21 |
|
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1.55), also called allokinase, catalyzes the phosphorylation of D-allose to D-allose 6-phosphate. It has also low level glucokinase activity in vitro. 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: 466920 [Multi-domain] Cd Length: 293 Bit Score: 91.46 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 6 MWTLSIDIGGTYIKSALIMDTQIREKRQIETPKT--DKDNFILVLVELIRSY--QQIEPIEFVGFSVPGAV-KEASTVFF 80
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDllRAGDPVEVLADLIREYieEAGLKPAAIVIGVPGTVdKDRRTVIS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 81 GGAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGE-- 158
Cdd:cd24070 81 TPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGElg 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 159 -VSFLIQDR-----GINGAESFA-GINLsaVRLVKE------LTKLFQCEPEGPLVFDYLyqkeDDQAqtlyRTYCNQVA 225
Cdd:cd24070 161 hIPVYGNGKpcgcgNTGCLETYAsGRAL--EEIAEEhypdtpILDIFVDHGDEPELDEFV----EDLA----LAIATEIN 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488261292 226 IlcfniqclLDLDKIIIGGGISK-----QKRLIRDIQKNyeaifSVSPMIEQTItkmTIEAAAFESEANLIGAA 294
Cdd:cd24070 231 I--------LDPDAVILGGGVIDmkgfpRETLEEYIRKH-----LRKPYPADNL---KIIYAELGPEAGVIGAA 288
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
9-265 |
3.28e-21 |
|
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: 91.11 E-value: 3.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKsALIMDTQIRE--KRQIETPKTDKDNFILVLVELI-RSYQQIEPIEFVGFSVPGA-------VKEASTV 78
Cdd:cd24066 2 IGIDLGGTKIE-GIALDRAGREllRRRVPTPRGDYEATLDAIADLVeEAEEELGAPATVGIGTPGSisprtglVKNANST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 79 ffggavaCLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGE 158
Cdd:cd24066 81 -------WLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 159 VSFLI----QDRGINGAESFAGIN------LSAVRLVKELTKLFQCEPEGPLVFDyLYQKEDDQAQTLYRTYCNQVAILC 228
Cdd:cd24066 154 WGHNPlpwpDEDELPGPPCYCGKRgcvetfLSGPALERDYARLTGKTLSAEEIVA-LARAGDAAAVATLDRFLDRLGRAL 232
|
250 260 270
....*....|....*....|....*....|....*...
gi 488261292 229 FNIQCLLDLDKIIIGGGISKQKRLIRD-IQKNYEAIFS 265
Cdd:cd24066 233 ANVINILDPDVIVLGGGLSNIDELYTEgPAALARYVFS 270
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
8-294 |
1.77e-20 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to N-acetylglucosamine kinase (Tm1224; EC 2.7.1.59) from Thermotoga maritima, which belongs to kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Tm1224 lacks the cysteine-rich zinc-binding motif, which presents in other family members.
Pssm-ID: 466909 [Multi-domain] Cd Length: 305 Bit Score: 89.18 E-value: 1.77e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 8 TLSIDIGGTYIKSALI-MDTQIREKRQIETP-KTDKDNFILVLVELIRSYQQIEPIEF----VGFSVPGAVKEASTV--- 78
Cdd:cd24059 3 VIGVEIGRDLLSAVLCdLSGNILAREKYPLDeKENPEEVLEKLYELIDRLLEKENIKSkilgIGIGAPGPLDVEKGIiln 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 79 ---FFGGavaclNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQ 155
Cdd:cd24059 83 ppnFPGW-----ENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 156 AGEVSFLIQDrgINGA----------ESFAGINlsavRLVKELTKLFQCEPEGPLVFDYLYQKEDDQAQTLYRTYCNQVA 225
Cdd:cd24059 158 AGEIGHTSID--INGPrcscgnrgclELYASIP----AIEKKARSALGSGRSFQLDIVEALQKGDPIADEVIEEAAKYLG 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 226 ILCFNIQCLLDLDKIIIGG-GISKQKRLIRDIQKNYEaifsvSPMIEQTITKMTIEAAAFESEANLIGAA 294
Cdd:cd24059 232 IGLVNLINLLNPEAIIIGGeLIYLGERYLEPIEKEVN-----SRLFGRNAREVRILKSSLGEDAPLLGAA 296
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
7-294 |
2.37e-20 |
|
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.
Pssm-ID: 466910 [Multi-domain] Cd Length: 305 Bit Score: 89.01 E-value: 2.37e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 7 WTLSIDIGGTYIKSALI-MDTQIREKRQIETPKTDKDNFILVLVELIRSYQQIEP----IEFVGFSVPGAV--KEASTVF 79
Cdd:cd24060 1 SALAVDLGGTNLRVAIVsMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAVKlncrILGVGISTGGRVnpREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 80 FGGAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEV 159
Cdd:cd24060 81 STKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 160 SFLIQDR-------GINGA-ESFAginlSAVRLVKELTKLFQcepEGPLVFDYLYQKEDDQ----------------AQT 215
Cdd:cd24060 161 GHIVVSLdgpdcmcGSHGCvEAYA----SGMALQREAKKLHD---EDLLLVEGMSVTNDEEvtakhliqaaklgnakAQK 233
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 216 LYRTYCNQVAILCFNIQCLLDLDKIIIGGGISKQkrlirdiqknYEAIfsVSPMIEQTITKMTIEAAAFES---EANLIG 292
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGVLASH----------YENI--VKDVIAQRALPSVQNVDVVVSdlvDPALLG 301
|
..
gi 488261292 293 AA 294
Cdd:cd24060 302 AA 303
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
9-294 |
2.03e-19 |
|
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: 86.47 E-value: 2.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALI-MDTQIREKRQIETPKTDK-DNFILVLVELIRSYQQIEP-----IEFVGFSVPGAV-KEASTVFF 80
Cdd:cd24076 4 IGVELGVDYITVVVTdLAGEVLWRREVPLPASDDpDEVLAQLAALIREALAAAPdsplgILGIGVGVPGLVdSEDGVVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 81 ----GgavacLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQA 156
Cdd:cd24076 84 apnlG-----WRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 157 GEVS-FLIQDRGIN---GA----ESFAGINlSAVRLVKELTklfqcEPEGPLVFDYLYQ---KEDDQAQTLYRTYCNQVA 225
Cdd:cd24076 159 GEIGhMTVDPDGPPcscGNrgcwETYASER-ALLRAAGRLG-----AGGEPLSLAELVEaarAGDPAALAALEEVGEYLG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488261292 226 ILCFNIQCLLDLDKIIIGGGISKQKRLIRdiqknyeaifsvsPMIEQTITKMT---------IEAAAFESEANLIGAA 294
Cdd:cd24076 233 IGLANLVNTFNPELVVLGGALAPLGPWLL-------------PPLRAEVARRAlpapardvrIVVSRLGEDAAALGAA 297
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
8-294 |
4.11e-19 |
|
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Staphylococcus aureus xylose repressor (SaXylR), which belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. SaXylR acts as a transcriptional repressor of xylose-utilizing enzymes. It lacks the cysteine-rich zinc-binding motif, which presents in other family members.
Pssm-ID: 466927 [Multi-domain] Cd Length: 295 Bit Score: 85.28 E-value: 4.11e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 8 TLSIDIGGTYIKSALI-MDTQIREKRQIETPKTDKDNFILVLVELIRSYQQIEP-----IEFVGFSVPGAVKEASTVFFG 81
Cdd:cd24077 3 SIGIDLGYNYISLMLTyLDGEIISSKQIKLLDISFENILEILKSIIQELISQAPktpygLVGIGIGIHGIVDENEIIFTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 82 GAVacLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHlkGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVS- 160
Cdd:cd24077 83 YYD--LEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSE--DYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIGh 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 161 FLIQDRGINGA-------ESFAginlSAVRLVKELTKLFQCEPEGPLVFDYLYQKEDDQAQTLYRTYCNQVAILCFNIQC 233
Cdd:cd24077 159 MIIVPNGKPCPcgnkgclEQYA----SEKALLKELSEKKGLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNIIN 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488261292 234 LLDLDKIIIGGGISKQ-KRLIRDIQKNYEAIFSvspmieqtiTKMTIEAAAFESEANLIGAA 294
Cdd:cd24077 235 TFNPEIIIINSSLINEiPELLEKIKEQLSSSFN---------KYVEILISTLGKNATLLGGA 287
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
9-294 |
4.33e-19 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima 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: 466914 [Multi-domain] Cd Length: 301 Bit Score: 85.24 E-value: 4.33e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALI-MDTQIREKRQIETP-KTDKDNFILVLVELIRSYQQIEPIEFVGFSVPGAV-KEASTVFFGGAVA 85
Cdd:cd24064 2 IGIDLGGTDTKIGIVdENGDILKKKTIDTKvENGKEDVINRIAETVNELIEEMELLGIGIGSPGSIdRENGIVRFSPNFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 86 CLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLIQD 165
Cdd:cd24064 82 DWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIVE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 166 ----------RG-INGAESFAGINLSAVRLVKELTKLFQCEPE---GPLVFDyLYQKEDDQAQTLYRTYCNQVAILCFNI 231
Cdd:cd24064 162 pngpicgcgnRGcVEAFASATAIIRYARESRKRYPDSLAGESEkinAKHVFD-AARKNDPLATMVFRRVVDALAIAIGGF 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488261292 232 QCLLDLDKIIIGGGISKQKRL----IRDIQKNYeaifsVSPMIEQTitkMTIEAAAFESEANLIGAA 294
Cdd:cd24064 241 VHIFNPEIIIIGGGISRAGSFlldpIREKTKKY-----VMLSFQDT---YSIELSNLVEDAGILGAA 299
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
9-244 |
4.91e-16 |
|
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Listeria monocytogenes Lmo0178 protein, which is a predicted transcription repressor belonging to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466921 [Multi-domain] Cd Length: 312 Bit Score: 76.94 E-value: 4.91e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALI-MDTQIREKRQIETPKTDKDNFILVLV-----ELIRSYQQIEPIEFVGFSVPGAVKEASTVFFGG 82
Cdd:cd24071 4 IGVKIEEGYLVLALTdLKGKILEKTRIPFDHETDPEKVIELIaenikKLIKNKHVEKKLLGIGIAVSGLVDSKKGIVIRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 83 AVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFL 162
Cdd:cd24071 84 TILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIGHM 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 163 IQDrgINGAE-------------SFAGINLSAVRLvKELTKLFQCEPEGPLVFDYLYQ--KEDDQ-AQTLYRTYCNQVAI 226
Cdd:cd24071 164 TIQ--PDGRKcycgqkgcleayaSFEALVNEIKEL-TESYPLSLLKELEDFEIEKVREaaEEGDSvATELFKKAGEYLGI 240
|
250
....*....|....*...
gi 488261292 227 LCFNIQCLLDLDKIIIGG 244
Cdd:cd24071 241 GIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
10-294 |
1.45e-15 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; Bacillus subtilis FRK (EC 2.7.1.4), also called glucomannan utilization protein E, catalyzes the phosphorylation of fructose to fructose-6-P. It seems to be involved in the degradation of glucomannan. 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: 466917 [Multi-domain] Cd Length: 285 Bit Score: 75.27 E-value: 1.45e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 10 SIDIGGTYIKSAL-IMDTQIREKRQIETpkTDKDNFILVLVELIRSYQqiEPIEFVGFSVPGAVkeastvffggavaCLN 88
Cdd:cd24067 3 GIEAGGTKFVCAVgTGDGNIIERTEFPT--TTPEETLQAVIDFFREQE--EPIDAIGIASFGPI-------------DLN 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 89 E------------------VNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRK 150
Cdd:cd24067 66 PtsptygyitttpkpgwrnFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVH 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 151 GP-HCQAGEVSFLIQ--DRGINGAESF---------AGINLSAvRLVKELTKLFQCEPEGPLVFDYLyqkeddqaqtlyr 218
Cdd:cd24067 146 GLlHPEMGHIRVPRHpdDDGFPGVCPFhgdcleglaSGPAIAA-RWGIPAEELPDDHPAWDLEAYYL------------- 211
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488261292 219 tycnqvAILCFNIQCLLDLDKIIIGGGISKQKRLIRDIQKNYEAI---FSVSPMIEQTITKMtIEAAAFESEANLIGAA 294
Cdd:cd24067 212 ------AQACANLTLTLSPERIVLGGGVMQRPGLFPRIREKFRKLlngYLEVPRLLPDIDEY-IVPPALGNDAGILGAL 283
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
12-268 |
7.60e-14 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 70.40 E-value: 7.60e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 12 DIGGTYIKSAlIMDTQIR---EKRqIETPKTDKDNFILVLVELIRSYQQiepiEF-----VGFSVPGAVKEASTVFFGGA 83
Cdd:PRK13310 6 DIGGTKIELG-VFNEKLElqwEER-VPTPRDSYDAFLDAVCELVAEADQ----RFgckgsVGIGIPGMPETEDGTLYAAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 84 VACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSFLi 163
Cdd:PRK13310 80 VPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 164 qdrgingaesfaGINLSAVRLVKELTKLFQ--CEPEGPLV-------FDYLYQ---------KE--------DDQAQTLY 217
Cdd:PRK13310 159 ------------RLPVDALTLLGWDAPLRRcgCGQKGCIEnylsgrgFEWLYQhyygeplqaPEiialyyqgDEQAVAHV 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 488261292 218 RTYCNQVAILCFNIQCLLDLDKIIIGGGISkqkrlirdiqkNYEAIFSVSP 268
Cdd:PRK13310 227 ERYLDLLAICLGNILTIVDPHLVVLGGGLS-----------NFDAIYEQLP 266
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
8-295 |
1.25e-13 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 69.14 E-value: 1.25e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 8 TLSIDIGGTYIKSAlIMDTQ----IREKRQIETPKTDKDNFIL-VLVELIRSYQQIEPIEfVGFsvPGAVKEastvffGG 82
Cdd:cd24058 1 ILGIDIGGSGIKGA-IVDTDtgelLSERIRIPTPQPATPEAVAdVVAELVAHFPWFGPVG-VGF--PGVVRR------GV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 83 AVACLN------EVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIEnGAGII--LGTGVGVGLLLDGQVrkGPHC 154
Cdd:cd24058 71 VRTAANldkswiGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEK-GVVLVltLGTGIGSALFVDGHL--VPNT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 155 QAGEVSFliqdRGiNGAESFAginLSAVRLVKELTklfqcepegplvfdylYQKEDDQAQTLYRTYcnqVAILCFniqcl 234
Cdd:cd24058 148 ELGHLEI----RG-KDAEERA---SLGVRAREDLG----------------WKRWAKRVNKYLQYL---ERLFNP----- 195
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488261292 235 ldlDKIIIGGGISKQkrlirdiqknyeaIFSVSPMIEqtiTKMTIEAAAFESEANLIGAAK 295
Cdd:cd24058 196 ---DLFIIGGGNSKK-------------ADKFLPLLD---VKTPVVPAVLRNDAGIVGAAL 237
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
64-159 |
3.28e-13 |
|
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; CYANR acts as transcriptional repressor of cyclobis-(1-6)-alpha-nigerosyl (CNN) degrading enzymes. 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: 466923 [Multi-domain] Cd Length: 304 Bit Score: 68.73 E-value: 3.28e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 64 VGFSVPGAVKEAS-----TVFFGgavacLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGV 138
Cdd:cd24073 65 IGVGLPGLVDAETgicrwSPLLG-----WRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGI 139
|
90 100
....*....|....*....|.
gi 488261292 139 GVGLLLDGQVRKGPHCQAGEV 159
Cdd:cd24073 140 GCGLVVDGRLYRGAHGGAGEI 160
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-259 |
1.13e-11 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 64.23 E-value: 1.13e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 4 KSMWtLSIDIGGTYIKSALIMDT-QIREKRQIETPKTDKDNFILVLVELIRSY--QQIEPIEFVGFSVPGAV-KEASTVF 79
Cdd:PRK09698 3 KNVV-LGIDMGGTHIRFCLVDAEgEILHCEKKRTAEVIAPDLVSGLGEMIDEYlrRFNARCHGIVMGFPALVsKDRRTVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 80 FGGAVAC--LNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGiENGAGIILGTGVGVGLLLDGQVRKGPHCQAG 157
Cdd:PRK09698 82 STPNLPLtaLDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQ-QLVLGAYLGTGMGFAVWMNGAPWTGAHGVAG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 158 EVSFLIQ-DRGIN---GAESFAGINLSAVRLVKELTK---------LFQCEPEGPLVFDYLyqkeddqaQTLYRTYCNQV 224
Cdd:PRK09698 161 ELGHIPLgDMTQHcgcGNPGCLETNCSGMALRRWYEQqprdyplsdLFVHAGDHPFIQSLL--------ENLARAIATSI 232
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488261292 225 AIlcfniqclLDLDKIIIGGGISKQK-----RLIRDIQKN 259
Cdd:PRK09698 233 NL--------FDPDAIILGGGVMDMPafpreTLIAMIQKY 264
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
9-294 |
6.53e-10 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. 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: 466924 [Multi-domain] Cd Length: 322 Bit Score: 59.25 E-value: 6.53e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSAL--IMDTQIREKRQiETPKTDKDNFILVLVELI-----RSYQQIEPIEFVGFSVPGAVKEASTVFFG 81
Cdd:cd24074 5 LSIRIGRGYITLALrdLNGRLLAEERY-PLPAKDNDPFLDRLLESIseffsRHQKKLERLTAIAITLPGIIDPESGIVHR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 82 GAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEVSF 161
Cdd:cd24074 84 LPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 162 L-IQDRGIN---G----AESFAGINlSAVRLVKELTKLFQ--CEPEGPLVFDYLYQ---KEDDQAQTLYRTYCNQVAILC 228
Cdd:cd24074 164 TqIDPYGKRcycGnhgcLETVASIP-AILEQANQLLEQSPdsMLHGQPISIESLCQaalAGDPLAQDIIIQVGRHLGRIL 242
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488261292 229 FNIQCLLDLDKIIIGGGISKQKRLIrdiqknyeaifsvSPMIEQTI---------TKMTIEAAAFESEANLIGAA 294
Cdd:cd24074 243 AILVNLFNPEKILIGSPLNNAAEIL-------------FPALSQSIrqqslpaysQHLQIESTKFYNDGTMPGAA 304
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
59-281 |
1.33e-08 |
|
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Escherichia coli protein YphH that belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466922 [Multi-domain] Cd Length: 308 Bit Score: 55.11 E-value: 1.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 59 EPIEFVGFSVPGAVKEASTVFFGGAVACLNEVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGV 138
Cdd:cd24072 58 DRVKGIALAIQGLVDSHKGVSLWSPGAPWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 139 GVGLLLDGQVRKGPHCQAGEVSFLIQDrgINGA----------ESFAGIN--LSAVRLVKELTKLFQCEPEGPL-VFDYL 205
Cdd:cd24072 138 GSAIVIDNKLYIGASSGSGEIGHTKVN--PDGArcdcgrrgclETVASNSalKRNARVTLKLGPVSADPEKLTMeQLIEA 215
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488261292 206 YQKEDDQAQTLYRTYCNQVAILCFNIQCLLDLDKIII-GGGISKQKRLIRDIQKnyeAIFSVSPMIEQTITKMTIEA 281
Cdd:cd24072 216 LEEGEPIATQIFDRAANAIGRSLANILNLLNPEQVLLyGRGCRAGDLLLPAIRR---AIAENPFSQHATQIGFGQLS 289
|
|
| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
81-259 |
5.15e-08 |
|
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.
Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 52.92 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 81 GGAVACLNEVNLKQEIEKHLPV--RVFVENDAKAAVLGeASFGhlkgiENGAGIILGTGVGVGLLLDGQVRkgphcQAGE 158
Cdd:cd24082 69 GLGLAGANVPEARAAFLAALPPfaSLVVVSDAHIACLG-AHGG-----EDGAIIILGTGSVGAALDGGEVR-----QVGG 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 159 VSFLIQDRGingaeSFAGINLSAVR--------------LVKELTKLFQCEPEG-----------------PLVFDYlYQ 207
Cdd:cd24082 138 WGFPLGDEG-----SGAWLGLRALRhtllaldglapsspLTRAVLARFGGDPAEivawantatpadfaalaPLVFEA-AE 211
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 488261292 208 KEDDQAQTLYRTYCNQVAILcfnIQCLLDL--DKIIIGGGISK--QKRLIRDIQKN 259
Cdd:cd24082 212 QGDPVALAILQEAAAYIERL---LRALGAQgaLPLCLLGGLAErlAPYLPEDLQAR 264
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
11-158 |
2.13e-07 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 51.18 E-value: 2.13e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 11 IDIGGTYIKS-ALIMDTQIREKRQIETPKTDKDNFILVLVELIR-SYQQIEPIEFVGFSVPGAVKEastvfFGGAVACLN 88
Cdd:PRK09557 5 IDLGGTKIEViALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDmAEQATGQRGTVGVGIPGSISP-----YTGLVKNAN 79
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488261292 89 EVNLK-QEIEKHLPVR----VFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGE 158
Cdd:PRK09557 80 STWLNgQPLDKDLSARlnreVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
12-158 |
4.32e-07 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 50.03 E-value: 4.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 12 DIGGTYIKSAlIMDTQIRE--KRQIETPKTDKDNFILVLVELIRSYQQIEPIE-FVGFSVPGAVKEASTVFFGGAVACLN 88
Cdd:PRK13311 6 DMGGTKIELG-VFDENLQRiwHKRVPTPREDYPQLLQILRDLTEEADTYCGVQgSVGIGIPGLPNADDGTVFTANVPSAM 84
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 89 EVNLKQEIEKHLPVRVFVENDAKAAVLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGE 158
Cdd:PRK13311 85 GQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGE 154
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
9-158 |
9.46e-07 |
|
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: 49.53 E-value: 9.46e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTYIKSALIMDT--QIREKRQIETPKTDKDNFILVLVELIRSYqQIEPIEFVGFSVPGAVKEASTVFFggavac 86
Cdd:cd24008 2 LVGDIGGTNARLALADAGdgSGDLLFVRKYPSADFASLEDALAAFLAEL-GAPRPKAACIAVAGPVDGGRVRLT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 87 lnevNLK-----QEIEKHLPV-RVFVEND--AKA---AVLGEASFGHLKG----IENGAGIIL--GTGVGVGLLLDGQvR 149
Cdd:cd24008 75 ----NLDwsidaAELRKALGIgRVRLLNDfeAAAyglPALGPEDLLVLYGgggpLPGGPRAVLgpGTGLGVALLVPDG-D 149
|
....*....
gi 488261292 150 KGPHCQAGE 158
Cdd:cd24008 150 GGYVVLPSE 158
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
9-150 |
1.88e-06 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 48.34 E-value: 1.88e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 9 LSIDIGGTyiKS-ALIMDTQIREKRQIET---------PKTDKDNFILVLVELIRSYQQIEPIEFVGFSVPGAVKEAstv 78
Cdd:COG2971 4 LGVDGGGT--KTrAVLVDADGEVLGRGRAgganpqsvgLEEALASLREALEEALAAAGDPADIEAVGFGLAGAGTPE--- 78
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488261292 79 ffggavaclNEVNLKQEIEKHLPV-RVFVENDAKAAVLGeaSFGHlkgiENGAGIILGTG-VGVGLLLDGQVRK 150
Cdd:COG2971 79 ---------DAEALEAALRELFPFaRVVVVNDALAALAG--ALGG----EDGIVVIAGTGsIAAGRDGDGRTAR 137
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
35-159 |
3.33e-06 |
|
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as a repressor of the nagEBACD operon involved in the uptake and degradation of the amino sugars, N-acetyl-D-glucosamine (GlcNAc) and glucosamine (GlcN). It acts both as an activator and a repressor for the transcription of the glmSU operon, encoding proteins necessary for the synthesis of GlcN (glmS) and the formation of UDP-GlcNAc (glmU). 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: 466925 [Multi-domain] Cd Length: 315 Bit Score: 47.75 E-value: 3.33e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488261292 35 ETPKTDKDNFILVLVELIRSYQQI-EPIEFVGFSVPGAVKEASTVFFGGAVACLNEVNLKQEIEKHLPVRVFVENDAKAA 113
Cdd:cd24075 35 LNQEALLSQLIEEIAQFLKSHRRKtQRLIAISITLPGLINPKTGVVHYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSL 114
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 488261292 114 VLGEASFGHLKGIENGAGIILGTGVGVGLLLDGQVRKGPHCQAGEV 159
Cdd:cd24075 115 ALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
|
|