|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
8-309 |
1.82e-78 |
|
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: 241.34 E-value: 1.82e-78
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 8 HISIGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGE--VEIVDEVCKLISEVINQIILKYGNDTkfTIGIGVPGLVNQHT 85
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAgpEAVLEAIAELIEELLAEAGISRGRIL--GIGIGVPGPVDPET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 86 GQVSESVNLGS-HSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYY-GSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGV 163
Cdd:COG1940 83 GVVLNAPNLPGwRGVPLAELLEERLGLPVFVENDANAAALAEAWFGaGRGADNVVYLTLGTGIGGGIVINGKLLRGANGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 164 AGEIGHIVADTQGRDCPCGQRGCVETIISGTGLSKLWPA---KNEYPIASLLRNVSAKNKEAEKVWNKFISTLVSALQII 240
Cdd:COG1940 163 AGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARElggAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490216600 241 TVTFDPEIIVIGGGVSKTGAILLKGVKEYIcrleQKSSFLSSLKIPdRVVIANQEVFFGALGAALIGRR 309
Cdd:COG1940 243 INLLDPEVIVLGGGVSAAGDLLLEPIREAL----AKYALPPAREDP-RIVPASLGDDAGLLGAAALALE 306
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
11-305 |
7.44e-59 |
|
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: 190.85 E-value: 7.44e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVST--KQGEVEIVDEVCKLISEVINQIILKygndtkfTIGIGVPGLVNQHTGQV 88
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILEKDSVPTpaSKGGDAILERLLEIIAELKEKYDIE-------GIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 -SESVNL-GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYnYYGS--DSSSLVFLNLGTGVSAGIIINGSIFHGSTGVA 164
Cdd:cd24068 76 iYATDNLpGWTGTNLKEELEERFGLPVAVENDVNCAALAEK-WLGAakGLDDFLCLTLGTGIGGAIILDGRLYRGANGSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 165 GEIGHIVADTQGRDCPCGQRGCVETIISGTGLSKLWPAKNEYPIAS---LLRNVSAKNKEAEKVWNKFISTLVSALQIIT 241
Cdd:cd24068 155 GELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGIDgreIFDLADAGDPLAKEVVEEFAEDLATGLANLV 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490216600 242 VTFDPEIIVIGGGVSKTGAILLKGVKEYIcrleqKSSFLSSLKIPDRVVIANQEVFFGALGAAL 305
Cdd:cd24068 235 HIFDPEVIVIGGGISAQGELFLEELREEL-----RKLLMPPLLDATKIEPAKLGNDAGLLGAAY 293
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
11-309 |
5.41e-56 |
|
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: 183.31 E-value: 5.41e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVE--IVDEVCKLISEVINQIilkygnDTKFTIGIGVPGLVNQHTGQV 88
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEetLVDAIAFFVDSAQRKF------GELIAVGIGSPGLISPKYGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYYGS-DSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEI 167
Cdd:pfam00480 75 TNTPNIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASkDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 168 GHIVADTQGRDCPCGQRGCVETIISGTGLSKLWPAK-NEYPIASLLRNVSAKNKEAEKVWNKFISTLVSALQIITVTFDP 246
Cdd:pfam00480 155 GHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQKgEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDP 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490216600 247 EIIVIGGGVSKTGAILLKGVKEYicrleqKSSFLSSLKIPD-RVVIANQEVFFGALGAALIGRR 309
Cdd:pfam00480 235 QAIVLGGGVSNADGLLEAIRSLV------KKYLNGYLPVPPvIIVAASLGDNAGALGAAALAKQ 292
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
11-269 |
1.18e-55 |
|
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: 182.87 E-value: 1.18e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEivDEVCKLISEVINQIILKYG-NDTKFT-IGIGVPGLVNQHTGQV 88
Cdd:cd24062 3 VGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGG--ENIITDIAESIQQLLEELGySKEDLIgIGVGVPGPVDVETGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFG-AYNYYGSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEI 167
Cdd:cd24062 81 EVAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGeMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 168 GHI-VADTQGRDCPCGQRGCVETIISGTG---LSKLWPAKNEYPIASLLRN----VSAKN-----KE----AEKVWNKFI 230
Cdd:cd24062 161 GHItVNPEGGAPCNCGKTGCLETVASATGivrIAREELEEGKGSSALRILAlggeLTAKDvfeaaKAgdelALAVVDTVA 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 490216600 231 STLVSALQIITVTFDPEIIVIGGGVSKTGAILLKGVKEY 269
Cdd:cd24062 241 RYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEY 279
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
10-268 |
5.59e-53 |
|
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: 176.01 E-value: 5.59e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 10 SIGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEIVDEVCKLISEvinqiiLKYGNDTKfTIGIGVPGLVNQHTGQVS 89
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEE------LREGHDVS-AVGVAAAGFVDADRATVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 90 ESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNY-YGSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIG 168
Cdd:cd24061 74 FAPNIAWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFgAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 169 HIVADTQGRDCPCGQRGCVETIISGTGLSKLWPAK-NEYPIASLLRNVSAKNK----------------EAEKVWNKFIS 231
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAaNATPEGAAVLLADGSVDgitgkhiseaaragdpVALDALRELAR 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 490216600 232 TLVSALQIITVTFDPEIIVIGGGVSKTGAILLKGVKE 268
Cdd:cd24061 234 WLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIRE 270
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
11-306 |
9.49e-53 |
|
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: 173.03 E-value: 9.49e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEveIVDEVCKLISEVINQIILKYGNDTKFT-IGIGVPGLVNQHTGQVS 89
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEE--GPEAVLDRIAELIEELLAEAGVRERILgIGIGVPGPVDPETGIVL 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 90 ESVNL-GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYY-GSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEI 167
Cdd:cd23763 79 FAPNLpWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGaGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 168 GHIVadtqgrdcpcgqrgcvetiisgtglsklwpakneypiasllrnvsaknkeaekVWNKFISTLVSALQIITVTFDPE 247
Cdd:cd23763 159 GHIT-----------------------------------------------------VLEEAARYLGIGLANLINLLNPE 185
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 490216600 248 IIVIGGGVSKTGAILLKGVKEYIcrleQKSSFLSSLKIPdRVVIANQEVFFGALGAALI 306
Cdd:cd23763 186 LIVLGGGVAEAGDLLLEPIREAV----RRRALPPLRRRV-RIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
10-268 |
3.29e-48 |
|
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: 163.50 E-value: 3.29e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 10 SIGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGE--VEIVDEVCKLISEVINQIilkygNDTKFT---IGIGVPGLVNQH 84
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVPLPASDdpDEVLAQLAALIREALAAA-----PDSPLGilgIGVGVPGLVDSE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 85 TGQVSESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYY-GSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGV 163
Cdd:cd24076 78 DGVVLLAPNLGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGaGRGVSDLVYLSAGVGIGAGIILDGELYRGASGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 164 AGEIGHIVADTQGRDCPCGQRGCVETIISGTGLSK----LWPAKNEYPIASLLRNVSAKNKEAEKVWNKFISTLVSALQI 239
Cdd:cd24076 158 AGEIGHMTVDPDGPPCSCGNRGCWETYASERALLRaagrLGAGGEPLSLAELVEAARAGDPAALAALEEVGEYLGIGLAN 237
|
250 260
....*....|....*....|....*....
gi 490216600 240 ITVTFDPEIIVIGGGVSKTGAILLKGVKE 268
Cdd:cd24076 238 LVNTFNPELVVLGGALAPLGPWLLPPLRA 266
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
11-310 |
2.90e-47 |
|
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: 161.61 E-value: 2.90e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEIVDEVCKLISEVInQIILKYGNDTKFtIGIGVPGLVNQHTGQVSE 90
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFI-QHIAKVGHEIVA-IGIGAPGPVNRQRGTVYF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 91 SVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDSS-SLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIGH 169
Cdd:TIGR00744 79 AVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGArDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 170 IVADTQGR-DCPCGQRGCVETIISGTGLSKLwpAKNEYP----IASLLR-----NVSAKN-KEAEK--------VWNKFI 230
Cdd:TIGR00744 159 IRMVPDGRlLCNCGKQGCIETYASATGLVRY--AKRANAkperAEVLLAlgdgdGISAKHvFVAARqgdpvavdSYREVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 231 STLVSALQIITVTFDPEIIVIGGGVSKTGAILLKGV-KEYicrleQKSSFLSSLKIPDrVVIANQEVFFGALGAALIGRR 309
Cdd:TIGR00744 237 RWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIrKSY-----KRWLFGGARQVAD-IIAAQLGNDAGLVGAADLART 310
|
.
gi 490216600 310 Y 310
Cdd:TIGR00744 311 Y 311
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
12-306 |
5.45e-44 |
|
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: 152.39 E-value: 5.45e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 12 GVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVE-IVDEVCKLISEVINQIilkygnDTKFTIGIGVPGLVNQHTGQVSe 90
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAaFLAAIAELVAEADARF------GVKGPVGIGIPGVIDPEDGTLI- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 91 SVNL-GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDSSSLVF-LNLGTGVSAGIIINGSIFHGSTGVAGEIG 168
Cdd:cd24057 77 TANIpAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFgLILGTGVGGGLVVNGRLVGGRSGIAGEWG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 169 H--IVAD--TQGRD-----CPCGQRGCVETIISGTGLSKLW-----PAKNEYPIASLLRnvsAKNKEAEKVWNKFISTLV 234
Cdd:cd24057 157 HgpLPADalLLGYDlpvlrCGCGQTGCLETYLSGRGLERLYahlygEELDAPEIIAAWA---AGDPQAVAHVDRWLDLLA 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 490216600 235 SALQIITVTFDPEIIVIGGGVSKTGAIllkgvkeyICRLEQ--KSSFLSSLKIPdRVVIANQEVFFGALGAALI 306
Cdd:cd24057 234 GCLANILTALDPDVVVLGGGLSNFPAL--------IAELPAalPAHLLSGARTP-RIVPARHGDAGGVRGAAFL 298
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
10-270 |
4.67e-43 |
|
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: 150.04 E-value: 4.67e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 10 SIGVDVGGTKVLCAAFNTNNELIAHSQVSTKqgEVEIVDEVCKLISEVINQIILKYGNDTKFT-IGIGVPGLVNQHTGQV 88
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLD--EKENPEEVLEKLYELIDRLLEKENIKSKILgIGIGAPGPLDVEKGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNL-GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFgAYNYYGS--DSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAG 165
Cdd:cd24059 81 LNPPNFpGWENIPLVELLEEKFGIPVYLDNDANAAAL-AEKWYGKgkNYDNFIYILADEGIGAGIIINGKLYRGVDGYAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 166 EIGHIVADTQGRDCPCGQRGCVETIISGTG-LSKLWPAKNEYP--IASLLRNVSAKNKEAEKVWNKFISTLVSALQIITV 242
Cdd:cd24059 160 EIGHTSIDINGPRCSCGNRGCLELYASIPAiEKKARSALGSGRsfQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLIN 239
|
250 260
....*....|....*....|....*...
gi 490216600 243 TFDPEIIVIGGGVSKTGAILLKGVKEYI 270
Cdd:cd24059 240 LLNPEAIIIGGELIYLGERYLEPIEKEV 267
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
11-306 |
8.91e-42 |
|
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: 146.49 E-value: 8.91e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTK--QGEVEIVDEVCKLISEVINQIILKYgndtkftIGIGVPGLVNQHTGQV 88
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKveNGKEDVINRIAETVNELIEEMELLG-------IGIGSPGSIDRENGIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNL-GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYnYYGS--DSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAG 165
Cdd:cd24064 75 RFSPNFpDWRNFPLVPLIEERTGIKVFLENDANAFALGEW-WFGNakGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 166 EIGHIVADTQGRDCPCGQRGCVETIISGTGLSKLW-PAKNEYP--IASLLRNVSAK---------NKEAEKVWNKFISTL 233
Cdd:cd24064 154 ELGHVIVEPNGPICGCGNRGCVEAFASATAIIRYArESRKRYPdsLAGESEKINAKhvfdaarknDPLATMVFRRVVDAL 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490216600 234 VSALQIITVTFDPEIIVIGGGVSKTGAILLKGVKEyicrlEQKSSFLSSLKIPDRVVIANQEVFFGALGAALI 306
Cdd:cd24064 234 AIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIRE-----KTKKYVMLSFQDTYSIELSNLVEDAGILGAASI 301
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
11-308 |
9.58e-41 |
|
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: 143.84 E-value: 9.58e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQ--GEVEIVDEVCKLISEVINQIILKYGndtkfTIGIGVPGLVNQHTGQV 88
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDllRAGDPVEVLADLIREYIEEAGLKPA-----AIVIGVPGTVDKDRRTV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNLGSHS-IDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDSSSLVF-LNLGTGVSAGIIINGSIFHGSTGVAGE 166
Cdd:cd24070 79 ISTPNIPGLDgVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLgFYIGTGIGNAILINGKPLRGKNGVAGE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 167 IGHIVADTQGRDCPCGQRGCVETIISGTGLSKLwpAKNEYP-IASLLRNVSAKNKEAEKvwnKFISTLvsALQIIT-VT- 243
Cdd:cd24070 159 LGHIPVYGNGKPCGCGNTGCLETYASGRALEEI--AEEHYPdTPILDIFVDHGDEPELD---EFVEDL--ALAIATeINi 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490216600 244 FDPEIIVIGGGVSKTGAILLKGVKEYICRLEQKSSFLSSLKIpdrvVIANQEVFFGALGAALIGR 308
Cdd:cd24070 232 LDPDAVILGGGVIDMKGFPRETLEEYIRKHLRKPYPADNLKI----IYAELGPEAGVIGAAIYAF 292
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
11-306 |
1.23e-40 |
|
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: 144.02 E-value: 1.23e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHsqVSTKQGEVEIVDEVCKLISEVINQIILKYGNDTKFTIGIGVPGLVNQHTGQVSE 90
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLK--IRQPTPKTGDPGTVSEQVLGLIETLLSKAGKDSIEGIGVSSAGPLDLRKGTIVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 91 SVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDS-SSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIGH 169
Cdd:cd24063 81 SPNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGtSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 170 IVADTQGRD-CPCGQRGCVETIISGTGLSKL---WPAKNEYPIASLLRN-----VSAK---------NKEAEKVWNKFIS 231
Cdd:cd24063 161 LVVDTESGLkCGCGGYGHWEAFASGRGIPRFareWAEGFSSRTSLKLRNpggegITAKevfsaarkgDPLALKIIEKLAR 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490216600 232 TLVSALQIITVTFDPEIIVIGGGVSKTGAILLKGVKEYicrLEQKSSFLSslkiPDRVVIANQEVFFGALGAALI 306
Cdd:cd24063 241 YNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEY---LEKNPAISK----GPEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
9-268 |
1.42e-40 |
|
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: 143.24 E-value: 1.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 9 ISIGVDVGGTKVLCAAFnTNNELIAHSQVST-KQGEVEIVDEVCKLISEvinqiiLKYGNDTKFTIGIGVPGLVNQHTGQ 87
Cdd:cd24065 1 STIGLDLGGTKIAAGVV-DGGRILSRLVVPTpREGGEAVLDALARAVEA------LQAEAPGVEAVGLGVPGPLDFRRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 88 VSESVNL-GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNY---YGSDSSslVFLNLGTGVSAGIIINGSIFHGSTGV 163
Cdd:cd24065 74 VRFAPNIpGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYgaaRGTESS--VYVTISTGIGGGLVLGGRVLRGRHGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 164 AGEIGHIVADTQGRDCPCGQRGCVETIISGTGLSKL--WPAKNEYPIASLLRNVSAKNKEAEK-VWN--KFISTLVSALQ 238
Cdd:cd24065 152 AGEIGHTTVLPGGPMCGCGLVGCLEALASGRALARDasFAYGRPMSTAELFELAQQGEPKALRiVEQaaAHLGIGLANLQ 231
|
250 260 270
....*....|....*....|....*....|
gi 490216600 239 IitvTFDPEIIVIGGGVSKTGAILLKGVKE 268
Cdd:cd24065 232 K---ALDPEVFVLGGGVAQVGDYYLLPVQE 258
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
11-257 |
8.16e-39 |
|
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: 138.49 E-value: 8.16e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVE-IVDEVCKLISEVINQIilkygnDTKFTIGIGVPGLVNQHTGQV- 88
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEaTLDAIADLVEEAEEEL------GAPATVGIGTPGSISPRTGLVk 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 -SESVNLGSHSidFKTEIRKRFGLNSVIDNDVN---------AAAFGAynyygsdssSLVF-LNLGTGVSAGIIINGSIF 157
Cdd:cd24066 76 nANSTWLNGKP--LKADLEARLGRPVRIENDANcfalseatdGAGAGA---------GVVFgVILGTGVGGGIVVNGRVL 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 158 HGSTGVAGEIGH------IVADTQGRDCPCGQRGCVETIISGTGLSKLWPAKN--EYPIASLLRNVSAKNKEAEKVWNKF 229
Cdd:cd24066 145 TGANGIAGEWGHnplpwpDEDELPGPPCYCGKRGCVETFLSGPALERDYARLTgkTLSAEEIVALARAGDAAAVATLDRF 224
|
250 260
....*....|....*....|....*...
gi 490216600 230 ISTLVSALQIITVTFDPEIIVIGGGVSK 257
Cdd:cd24066 225 LDRLGRALANVINILDPDVIVLGGGLSN 252
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
8-268 |
2.46e-37 |
|
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: 134.99 E-value: 2.46e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 8 HISIGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEIVDEvckLISEVINQIILKYGNDTK--FTIGIGVPGLVNQHT 85
Cdd:cd24073 1 AYVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAE---AIAEAVAELLAQAGLSPDrlLGIGVGLPGLVDAET 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 86 GQVSESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAA-----FGAynyyGSDSSSLVFLNLGTGVSAGIIINGSIFHGS 160
Cdd:cd24073 78 GICRWSPLLGWRDVPLAELLEERLGLPVYVENDVNALAlaehwFGA----GRGLDNFAVVTIGRGIGCGLVVDGRLYRGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 161 TGVAGEIGHIVADTQGRDCPCGQRGCVETIISGTGLSKLW----PAKNEYPIASLLRNVSAKNKEAEKVWNK-------F 229
Cdd:cd24073 154 HGGAGEIGHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAreagLRGEPLTIEDLLAAARAGDPAARAILRRagralglA 233
|
250 260 270
....*....|....*....|....*....|....*....
gi 490216600 230 ISTLVSalqiitvTFDPEIIVIGGGVSKTGAILLKGVKE 268
Cdd:cd24073 234 LANLVN-------LLDPELIIISGEGVRAGDLLFEPMRE 265
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
12-256 |
2.69e-37 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 134.73 E-value: 2.69e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 12 GVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVE-IVDEVCKLISEVinqiilkygnDTKF----TIGIGVPGLVNQHTG 86
Cdd:PRK13310 4 GFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDaFLDAVCELVAEA----------DQRFgckgSVGIGIPGMPETEDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 87 QVsESVNLGSHSIDFkteIRK----RFGLNSVIDNDVNAAAFG-AYNYYGSDSSSLVFLNLGTGVSAGIIINGSIFHGST 161
Cdd:PRK13310 74 TL-YAANVPAASGKP---LRAdlsaRLGRDVRLDNDANCFALSeAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRS 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 162 GVAGEIGHIV----------ADTQGRDCPCGQRGCVETIISGTGLSKLW--------PAKNeypiasLLRNVSAKNKEAE 223
Cdd:PRK13310 150 YITGEFGHMRlpvdaltllgWDAPLRRCGCGQKGCIENYLSGRGFEWLYqhyygeplQAPE------IIALYYQGDEQAV 223
|
250 260 270
....*....|....*....|....*....|....
gi 490216600 224 KVWNKFISTL-VSALQIITVtFDPEIIVIGGGVS 256
Cdd:PRK13310 224 AHVERYLDLLaICLGNILTI-VDPHLVVLGGGLS 256
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
14-256 |
5.05e-37 |
|
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: 133.85 E-value: 5.05e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 14 DVGGTKVLCAAFNTNNELIAHSQVSTKQGEV-EIVDEVCKLISEVINQIIlkygndtkfTIGIGVPGLVNQHTGQV-SES 91
Cdd:cd24152 6 DIGGTFIKYALVDENGNIIKKGKIPTPKDSLeEFLDYIKKIIKRYDEEID---------GIAISAPGVIDPETGIIyGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 92 VNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYnYYGS--DSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIGH 169
Cdd:cd24152 77 ALPYLKGFNLKEELEERCNLPVSIENDAKCAALAEL-WLGSlkGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 170 IVADTQGRD-CPCGQRGCVETIISGTGLSKLWPAKNEYPIASLLRNvsaKNKEAEKVWNKFISTLVSALQIITVTFDPEI 248
Cdd:cd24152 156 LLTDDDDKDlLFFSGLASMFGLVKRYNKAKGLEPLDGEEIFEKYAK---GDEAAKKILDEYIRNLAKLIYNIQYILDPEV 232
|
....*...
gi 490216600 249 IVIGGGVS 256
Cdd:cd24152 233 IVIGGGIS 240
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
11-270 |
3.70e-35 |
|
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: 129.33 E-value: 3.70e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEivDEVCKLISEVINQIILKYGNDTKFT-IGIGVPGLVNQHTGQVS 89
Cdd:cd24071 4 IGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDP--EKVIELIAENIKKLIKNKHVEKKLLgIGIAVSGLVDSKKGIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 90 ESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNY-YGSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIG 168
Cdd:cd24071 82 RSTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKgKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 169 HIVADTQGRDCPCGQRGCVET----------IISGTGLSKLWPAKNEYPI-ASLLRNvSAKNKE--AEKVWNKFISTLVS 235
Cdd:cd24071 162 HMTIQPDGRKCYCGQKGCLEAyasfealvneIKELTESYPLSLLKELEDFeIEKVRE-AAEEGDsvATELFKKAGEYLGI 240
|
250 260 270
....*....|....*....|....*....|....*
gi 490216600 236 ALQIITVTFDPEIIVIGGGVSKTGAILLKGVKEYI 270
Cdd:cd24071 241 GIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIA 275
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
13-255 |
3.36e-34 |
|
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: 126.24 E-value: 3.36e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 13 VDVGGTKVlCAAFNTNNELIAHSQVSTkqgeveIVDEVCKLISEVINQIILKYGNDTKFtIGIGVPGLVNQHTGQVSESV 92
Cdd:cd24069 3 IDIGGTKI-AAALIGNGQIIDRRQIPT------PRSGTPEALADALASLLADYQGQFDR-VAVASTGIIRDGVLTALNPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 93 NLGSHS-IDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYY-GSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIGHI 170
Cdd:cd24069 75 NLGGLSgFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGdGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 171 VADTQGRDCPCGQRGCVETIISGTGLSKLWPAKNEYPI--ASLLRNVSAKNKEAEKVWNKFISTLVSALQIITVTFDPEI 248
Cdd:cd24069 155 LADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEPVdaKDVFERARSGDEEAARLIDRAARALADLIADLKATLDLDC 234
|
....*..
gi 490216600 249 IVIGGGV 255
Cdd:cd24069 235 VVIGGSV 241
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
10-251 |
2.26e-33 |
|
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: 124.19 E-value: 2.26e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 10 SIGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVE-IVDEVCKLISEVINQIilkygNDTKFT---IGIGVPGLVNQHT 85
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFEnILEILKSIIQELISQA-----PKTPYGlvgIGIGIHGIVDENE 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 86 GQVSESVNLgsHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNYYgSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAG 165
Cdd:cd24077 78 IIFTPYYDL--EDIDLKEKLEEKFNVPVYLENEANLSALAERTFS-EDYDNLISISIHSGIGAGIIINNQLYRGYNGFAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 166 EIGHIVADTQGRDCPCGQRGCVETIISGTGLSKLWPAKNEYPIAS---LLRNVSAKNKEAEKVWNKFISTLVSALQIITV 242
Cdd:cd24077 155 EIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSEKKGLETLTfddLIQLYNEGDPEALELIDQFIKYLAIGINNIIN 234
|
....*....
gi 490216600 243 TFDPEIIVI 251
Cdd:cd24077 235 TFNPEIIII 243
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
11-308 |
1.94e-32 |
|
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: 122.48 E-value: 1.94e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEIVDEvckLISEVINQIILKYGNDTKFTIGIGV--PGLVNQHTGQV 88
Cdd:cd24075 4 LAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLS---QLIEEIAQFLKSHRRKTQRLIAISItlPGLINPKTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFgAYNYYGS--DSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGE 166
Cdd:cd24075 81 HYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLAL-AEHYFGAskDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 167 IGHIVADTQGRDCPCGQRGCVETIISGTGL-------------SKLWPakNEYPIASLLRNVSAKNKEAEKVWNKFISTL 233
Cdd:cd24075 160 IGHIQIEPLGERCHCGNFGCLETVASNAAIeqrvkkllkqgyaSQLTL--QDCTIKDICQAALNGDQLAQDVIKRAGRYL 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 490216600 234 VSALQIITVTFDPEIIVIGGGVSKTGAILLKGVKEYICRlEQKSSFLSSLKIPDRVVIANQevffgALGA-ALIGR 308
Cdd:cd24075 238 GKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQS-QALPDFRQELKIVASQLDHNS-----AIGAfALVKR 307
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
11-309 |
5.79e-32 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 120.86 E-value: 5.79e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKV-LC---AAFNTNNELIAHSQVSTKQGEVeivdevcKLISEVINQIILKYGNDTKfTIGIGVPGLVNQHTG 86
Cdd:PRK09698 7 LGIDMGGTHIrFClvdAEGEILHCEKKRTAEVIAPDLV-------SGLGEMIDEYLRRFNARCH-GIVMGFPALVSKDRR 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 87 QVSESVNLGSHSIDF---KTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGV 163
Cdd:PRK09698 79 TVISTPNLPLTALDLydlADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQQLVLGAYLGTGMGFAVWMNGAPWTGAHGV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 164 AGEIGHIVADTQGRDCPCGQRGCVETIISGTGLSKlWPAKN--EYPIASLLrnVSAKNkeaekvwNKFISTLVS--ALQI 239
Cdd:PRK09698 159 AGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRR-WYEQQprDYPLSDLF--VHAGD-------HPFIQSLLEnlARAI 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 490216600 240 ITVT--FDPEIIVIGGGVsktgaILLKGV-KEYICRLEQKSSFLSSLKIPDRVVIANQEVFFGALGAALIGRR 309
Cdd:PRK09698 229 ATSInlFDPDAIILGGGV-----MDMPAFpRETLIAMIQKYLRKPLPYEVVRFIYASSSDFNGAQGAAILAHQ 296
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
11-270 |
2.33e-30 |
|
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: 116.75 E-value: 2.33e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQ--VSTKQGEVEIVDEVCKLISEvinqiILKYGNDTKFTIGIGVPGLVNQHTGQV 88
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEFEyrVITLETPEALIDEIIDCIDR-----LLKLWKDRVKGIALAIQGLVDSHKGVS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 SESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFgAYNYYGSDSSS--LVFLNLGTGVSAGIIINGSIFHGSTGVAGE 166
Cdd:cd24072 79 LWSPGAPWRNIEIKYLLEERYGIPVFVENDCNMLAL-AEKWQGELRQSrdFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 167 IGHIVADTQGRDCPCGQRGCVETIISGTGLSKLW------PAKNEYP----IASLLRNVSAKNKEAEKVWNKFISTLVSA 236
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNArvtlklGPVSADPekltMEQLIEALEEGEPIATQIFDRAANAIGRS 237
|
250 260 270
....*....|....*....|....*....|....
gi 490216600 237 LQIITVTFDPEIIVIGGGVSKTGAILLKGVKEYI 270
Cdd:cd24072 238 LANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAI 271
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
13-255 |
7.91e-30 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 114.62 E-value: 7.91e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 13 VDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVeiVDEvcklISEVINQIILKYGNDTKFtIGIGVPGLVNQHTGQVSESV 92
Cdd:PRK05082 6 IDIGGTKIAAALVGEDGQIRQRRQIPTPASQT--PEA----LRQALSALVSPLQAQADR-VAVASTGIINDGILTALNPH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 93 NLGShSIDF--KTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIGHI 170
Cdd:PRK05082 79 NLGG-LLHFplVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 171 VADTQGRDCPCGQRGCVETIISGTGL---SKLWpaKNEYPIASLLRNVSAKNKEAEKVWNKFISTLVSALQIITVTFDPE 247
Cdd:PRK05082 158 LADPHGPVCGCGRRGCVEAIASGRAIaaaAQGW--LAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKATLDCQ 235
|
....*...
gi 490216600 248 IIVIGGGV 255
Cdd:PRK05082 236 CVVLGGSV 243
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
11-261 |
1.22e-29 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 114.35 E-value: 1.22e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKV-LCAAFNTNNELIAHsQVSTKQGEVE-IVDEVCKLISEVINQIilkygnDTKFTIGIGVPGLVNQHTGQV 88
Cdd:PRK09557 3 IGIDLGGTKIeVIALDDAGEELFRK-RLPTPRDDYQqTIEAIATLVDMAEQAT------GQRGTVGVGIPGSISPYTGLV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 89 --SESVNLGSHSIDfkTEIRKRFGLNSVIDNDVNAAAFGAYNYYGSDSSSLVF-LNLGTGVSAGIIINGSIFHGSTGVAG 165
Cdd:PRK09557 76 knANSTWLNGQPLD--KDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFaVIIGTGCGAGVAINGRVHIGGNGIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 166 EIGH-----IVAD----TQGRDCPCGQRGCVETIISGTGLSKLW-----PAKNEYPIASLlrnVSAKNKEAEKVWNKFIS 231
Cdd:PRK09557 154 EWGHnplpwMDEDelryRNEVPCYCGKQGCIETFISGTGFATDYrrlsgKALKGSEIIRL---VEEGDPVAELAFRRYED 230
|
250 260 270
....*....|....*....|....*....|
gi 490216600 232 TLVSALQIITVTFDPEIIVIGGGVSKTGAI 261
Cdd:PRK09557 231 RLAKSLAHVINILDPDVIVLGGGMSNVDRL 260
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
10-270 |
3.39e-29 |
|
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: 113.28 E-value: 3.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 10 SIGVDVGGTKVLCAAFNTNNELI-AHSQVSTKQGE--VEIVDEVCKL---ISEVINQIILKygndtkftIGIGVPGLVNQ 83
Cdd:cd24060 2 ALAVDLGGTNLRVAIVSMKGEIVkKYTQPNPKTYEerIDLILQMCVEaasEAVKLNCRILG--------VGISTGGRVNP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 84 HTGQVSESVNL--GSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNY-YGSDSSSLVFLNLGTGVSAGIIINGSIFHGS 160
Cdd:cd24060 74 REGIVLHSTKLiqEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFgHGKGVENFVTVITGTGIGGGIILNHELIHGS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 161 TGVAGEIGHIVADTQGRDCPCGQRGCVETIISGTGLS----KLWPA----------KNEYPIASLLRNVSAK--NKEAEK 224
Cdd:cd24060 154 SFCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQreakKLHDEdlllvegmsvTNDEEVTAKHLIQAAKlgNAKAQK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 490216600 225 VWNKFISTLVSALQIITVTFDPEIIVIGGGVSKTGailLKGVKEYI 270
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGVLASHY---ENIVKDVI 276
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
12-269 |
2.36e-23 |
|
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: 97.23 E-value: 2.36e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 12 GVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEvEIVDEVCKLISEVINQIIlkygndtkfTIGIGVPGLV-----NQHTG 86
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIERTEFPTTTPE-ETLQAVIDFFREQEEPID---------AIGIASFGPIdlnptSPTYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 87 QVSESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFGAYNY-YGSDSSSLVFLNLGTGVSAGIIINGSIFHGstgvAG 165
Cdd:cd24067 73 YITTTPKPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWgAAKGLDSLAYITVGTGIGVGLVVNGKPVHG----LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 166 --EIGHIVADTQGRD------CPcGQRGCVETIISGTGLSKLWpakneypiasllrNVSAKNKEAEK-VWNKFISTLVSA 236
Cdd:cd24067 149 hpEMGHIRVPRHPDDdgfpgvCP-FHGDCLEGLASGPAIAARW-------------GIPAEELPDDHpAWDLEAYYLAQA 214
|
250 260 270
....*....|....*....|....*....|...
gi 490216600 237 LQIITVTFDPEIIVIGGGVSKtGAILLKGVKEY 269
Cdd:cd24067 215 CANLTLTLSPERIVLGGGVMQ-RPGLFPRIREK 246
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
12-237 |
8.68e-21 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 89.70 E-value: 8.68e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 12 GVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEIVDEVCKLISEVINQIILKYGndtkfTIGIGVPGLVNQHTGQVSES 91
Cdd:PRK13311 4 GFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQG-----SVGIGIPGLPNADDGTVFTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 92 VNLGSHSIDFKTEIRKRFGLNSVIDNDVNAAAFG-AYNYYGSDSSSLVFLNLGTGVSAGIIINGSIFHGSTGVAGEIGHI 170
Cdd:PRK13311 79 NVPSAMGQPLQADLSRLIQREVRIDNDANCFALSeAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHF 158
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490216600 171 -----VADTQGRD-----CPCGQRGCVETIISGTGLSKLWPA--KNEYPIASLLRNVSAKNKEAEKVWNKFISTLVSAL 237
Cdd:PRK13311 159 rlpvdALDILGADiprvpCGCGHRGCIENYISGRGFEWMYSHfyQHTLPATDIIAHYAAGEPKAVAHVERFMDVLAVCL 237
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
73-285 |
1.12e-20 |
|
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: 90.45 E-value: 1.12e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 73 IGIGVPGLVNQHTGQVSESVNLGSHSIDFKTEIRKRFGLNSVIDNDVNA-----AAFGAynyyGSDSSSLVFLNLGTGVS 147
Cdd:cd24074 66 IAITLPGIIDPESGIVHRLPFYDIKNLPLGEALEQHTGLPVYVQHDISAwtlaeRFFGA----AKGAKNIIQIVIDDDIG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 148 AGIIINGSIFHGSTGVAGEIGHIVADTQGRDCPCGQRGCVETIISGTGLSKLWPA-----------KNEYPIASLLRNVS 216
Cdd:cd24074 142 AGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQlleqspdsmlhGQPISIESLCQAAL 221
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 490216600 217 AKNKEAEKVWNKFISTLVSALQIITVTFDPEIIVIGGGVSKTGAILLKGVKEYIcRLEQKSSFLSSLKI 285
Cdd:cd24074 222 AGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNNAAEILFPALSQSI-RQQSLPAYSQHLQI 289
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
12-257 |
2.44e-11 |
|
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: 62.59 E-value: 2.44e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 12 GVDVGGTKVLCAAFNTNN-ELIAHSQ-VSTKQGEVEivdevcKLISEVINQIILKYGNDTKftIGIGVPGLVNQhtGQVS 89
Cdd:cd24058 3 GIDIGGSGIKGAIVDTDTgELLSERIrIPTPQPATP------EAVADVVAELVAHFPWFGP--VGVGFPGVVRR--GVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 90 ESVNLGSHSIDFKTE--IRKRFGLNSVIDNDVNAAAFGAYNY-YGSDSSSLV-FLNLGTGVSAGIIINGSIFHGStgvag 165
Cdd:cd24058 73 TAANLDKSWIGFDAAklLSKRLGRPVRVLNDADAAGLAEMKGgAGKGEKGVVlVLTLGTGIGSALFVDGHLVPNT----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 166 EIGHIVADtqgrdcpcgqRGCVETiisgtglsklwpakneypIASLLrnVSAKNKEAEKVWNKFISTLVSALQIItvtFD 245
Cdd:cd24058 148 ELGHLEIR----------GKDAEE------------------RASLG--VRAREDLGWKRWAKRVNKYLQYLERL---FN 194
|
250
....*....|..
gi 490216600 246 PEIIVIGGGVSK 257
Cdd:cd24058 195 PDLFIIGGGNSK 206
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
11-173 |
1.76e-07 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs 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: 466857 [Multi-domain] Cd Length: 295 Bit Score: 51.54 E-value: 1.76e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQGEVEIVDEVCKLISEVINQIILKYGNDTKFT-IGIGVPGLVNQHTGQVs 89
Cdd:cd24007 2 LGVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAGSLGEIDaICLGLAGIDSEEDRER- 80
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90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 90 esvnlgshsidFKTEIRKRFGLNSV-IDNDVNAAAFGAynYYGSDSSSLVflnLGTGvSAGIIINGsifHGSTGVAGEIG 168
Cdd:cd24007 81 -----------LRSALKELFLSGRIiIVNDAEIALAAA--LGGGPGIVVI---AGTG-SVAYGRNG---DGEEARVGGWG 140
|
....*
gi 490216600 169 HIVAD 173
Cdd:cd24007 141 HLLGD 145
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| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
11-255 |
3.03e-06 |
|
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: 47.99 E-value: 3.03e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNN---ELIAHSQVSTKQgeveivdevCKLISEVINQIILKYGNDTKFTIGIGVPGLVNqhtGQ 87
Cdd:cd24008 2 LVGDIGGTNARLALADAGDgsgDLLFVRKYPSAD---------FASLEDALAAFLAELGAPRPKAACIAVAGPVD---GG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 88 VSESVNLGsHSIDFkTEIRKRFGLNSV-IDNDVNAAAFGAYNYYGSDSSSL------------VFLNLGTGV-SAGIIIN 153
Cdd:cd24008 70 RVRLTNLD-WSIDA-AELRKALGIGRVrLLNDFEAAAYGLPALGPEDLLVLyggggplpggprAVLGPGTGLgVALLVPD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 154 GSifHGSTGVAGEIGHI-VADTQGRDC--------PCGQRGCVETIISGTGLSKLW--------PAKNEYPIASLLRNVS 216
Cdd:cd24008 148 GD--GGYVVLPSEGGHAdFAPVTEEEAelleflrkRFGRSVSYEDVLSGPGLENIYeflakldgAEPPDLTAEEIAEAAL 225
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490216600 217 AKNKEAEKVWNKFISTLVSALQIITVTFDP-EIIVIGGGV 255
Cdd:cd24008 226 AGDPLAREALDLFARILGRFAGNLALSFLAtGGVYLAGGI 265
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|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
11-173 |
3.70e-05 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 44.49 E-value: 3.70e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAhsQVSTKQGEVEIV--DEVCKLISEVINQIILKYGNDTKFT-IGIGVPGLVNQHTGQ 87
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLG--RGRAGGANPQSVglEEALASLREALEEALAAAGDPADIEaVGFGLAGAGTPEDAE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490216600 88 VsesvnlgshsidFKTEIRKRFGLNSV-IDNDVNAAAFGAYNyyGSDSSSLVflnLGTGvSAGIIINGsifHGSTGVAGE 166
Cdd:COG2971 82 A------------LEAALRELFPFARVvVVNDALAALAGALG--GEDGIVVI---AGTG-SIAAGRDG---DGRTARVGG 140
|
....*..
gi 490216600 167 IGHIVAD 173
Cdd:COG2971 141 WGYLLGD 147
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
11-79 |
4.37e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 41.77 E-value: 4.37e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 490216600 11 IGVDVGGTKVLCAAFNTNNELIAHSQVSTKQ-----GEVEI-VDEVCKLISEVINQIILKYGNDTKFTIGIGVPG 79
Cdd:cd07802 3 LGIDNGTTNVKAVLFDLDGREIAVASRPTPVisprpGWAERdMDELWQATAEAIRELLEKSGVDPSDIAGVGVTG 77
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