|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
1-276 |
6.92e-158 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 441.27 E-value: 6.92e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 1 MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNL 80
Cdd:PRK05082 1 MTTLAIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQADRVAVASTGIINDGILTALNPHNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 81 GGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDGDITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTLAD 160
Cdd:PRK05082 81 GGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 161 PHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCVVVG 240
Cdd:PRK05082 161 PHGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKATLDCQCVVLG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 90111558 241 GSVGLAEGYLALVETYLAQEPAAFHVDLLAAHYRHD 276
Cdd:PRK05082 241 GSVGLAEGYLELVQAYLAQEPAIYHVPLLAAHYRHD 276
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
4-276 |
2.40e-118 |
|
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: 340.80 E-value: 2.40e-118
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGaDGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNLGGL 83
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGTPEALADALASLLADYQGQFDRVAVASTGIIRDGVLTALNPKNLGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 84 LHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTLADPH 162
Cdd:cd24069 80 SGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGeGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 163 GPVCGCGRTGCVEAIASGRGIAAAAQGELA-GADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCVVVGG 241
Cdd:cd24069 160 GPVCGCGRRGCVEAIASGTAIAAAASEILGePVDAKDVFERARSGDEEAARLIDRAARALADLIADLKATLDLDCVVIGG 239
|
250 260 270
....*....|....*....|....*....|....*
gi 90111558 242 SVGLAEGYLALVETYLAQEPAAFHVDLLAAHYRHD 276
Cdd:cd24069 240 SVGLAEGFLERVEQYLADEPAIFRVSLEPARLGQD 274
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
4-276 |
7.37e-96 |
|
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: 284.23 E-value: 7.37e-96
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQ---RVAIASTGIIRDGSLLALNPHNL 80
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEETLVDAIAFFVDSAQRKFGeliAVGIGSPGLISPKYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 81 GGLlHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQ-ALDGDITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTLA 159
Cdd:pfam00480 81 GWD-NFDLVEKLEERFNVPVFFENDANAAALAEAVfGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 160 DPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCVVV 239
Cdd:pfam00480 160 DPNGPKCGCGNHGCLETIASGRALEKRYQQKGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQAIVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 90111558 240 GGSVGLAEGYL----ALVETYLAQEPAAFHVDLLAAHYRHD 276
Cdd:pfam00480 240 GGGVSNADGLLeairSLVKKYLNGYLPVPPVIIVAASLGDN 280
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-276 |
7.44e-64 |
|
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: 202.82 E-value: 7.44e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 1 MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQR-------VAIASTGIIRDGSLL 73
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGIsrgrilgIGIGVPGPVDPETGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 74 ALNPHNLGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITvstgvgggvvsgcKLLTGPGGLAG 152
Cdd:COG1940 85 VLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGrGADNVVYLTlgtgigggivingKLLRGANGNAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 153 HIGHTLADPHGPVCGCGRTGCVEAIASGRGIA--AAAQGELAGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKA 230
Cdd:COG1940 165 EIGHMPVDPDGPLCGCGNRGCLETYASGPALLrrARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLIN 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 90111558 231 TTDCQCVVVGGSVGLA-EGYLALVETYLAQ---EPAAFHVDLLAAHYRHD 276
Cdd:COG1940 245 LLDPEVIVLGGGVSAAgDLLLEPIREALAKyalPPAREDPRIVPASLGDD 294
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
4-276 |
1.09e-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: 153.10 E-value: 1.09e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQRVAIA--STGII--RDGSLLALNPhN 79
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGisSAGQVdpKTGEVIYATD-N 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 80 LGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTL 158
Cdd:cd24068 82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAkGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 159 ADPHGPVCGCGRTGCVEAIASGRGIA--AAAQGELAGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQC 236
Cdd:cd24068 162 VDPGGRPCCCGGKGCLEQYASGTALVrrVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 90111558 237 VVVGGSVGLA-EGYLALVETYLAQE-PAAFH--VDLLAAHYRHD 276
Cdd:cd24068 242 IVIGGGISAQgELFLEELREELRKLlMPPLLdaTKIEPAKLGND 285
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
4-243 |
5.78e-39 |
|
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: 138.63 E-value: 5.78e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALV-----SPLQAHAQRVAIASTGIIRDGSLLALNPH 78
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIetllsKAGKDSIEGIGVSSAGPLDLRKGTIVNSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 79 NLGGLLhFPLVKTLEQLTNLPTIAINDAQAAAWAE--FQALDGdITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGH 156
Cdd:cd24063 83 NIKGKE-IPLVEPLKEEFNIPVALLNDAVAAALGEhlFGAGRG-TSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 157 TLADPH-GPVCGCGRTGCVEAIASGRGIAAAAQG----------------ELAGADAKTIFTRAGQGDEQAQQLIHRSAR 219
Cdd:cd24063 161 LVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREwaegfssrtslklrnpGGEGITAKEVFSAARKGDPLALKIIEKLAR 240
|
250 260
....*....|....*....|....
gi 90111558 220 TLARLIADIKATTDCQCVVVGGSV 243
Cdd:cd24063 241 YNGRGIANVINAYDPELIVIGGSV 264
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
2-250 |
1.10e-37 |
|
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: 134.76 E-value: 1.10e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 2 TTLAIDIGGTKLAAALIgADGQIRDRRELPTPASQTpEALRDALSALVSPLQAHA---QRVAIASTG--IIRDGSLLALN 76
Cdd:cd24065 1 STIGLDLGGTKIAAGVV-DGGRILSRLVVPTPREGG-EAVLDALARAVEALQAEApgvEAVGLGVPGplDFRRGRVRFAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 77 phNLGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIG 155
Cdd:cd24065 79 --NIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAArGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 156 HTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGA-DAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDC 234
Cdd:cd24065 157 HTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRPmSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALDP 236
|
250
....*....|....*.
gi 90111558 235 QCVVVGGSVGLAEGYL 250
Cdd:cd24065 237 EVFVLGGGVAQVGDYY 252
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
3-265 |
2.71e-33 |
|
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: 123.62 E-value: 2.71e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPAsqTPEALRDALSALVSPLQA-HA-QRVAIASTGII-RDGSLLALNPHN 79
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVEELREgHDvSAVGVAAAGFVdADRATVLFAPNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 80 lgGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTL 158
Cdd:cd24061 79 --AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGrGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 159 ADPHGPVCGCGRTGCVEAIASGRGIAAAAQ----------------GELAGADAKTIFTRAGQGDEQAQQLIHRSARTLA 222
Cdd:cd24061 157 VVPDGLLCGCGSRGCWEQYASGRALVRYAKeaanatpegaavlladGSVDGITGKHISEAARAGDPVALDALRELARWLG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 90111558 223 RLIADIKATTDCQCVVVGGSVGlAEGYLALVETYLAQEPAAFH 265
Cdd:cd24061 237 AGLASLAALLDPELFVIGGGVS-DAGDLLLDPIREAFERWLPG 278
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
4-250 |
3.46e-32 |
|
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: 120.75 E-value: 3.46e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQR-------VAIASTGIIRDGSLLALN 76
Cdd:cd24076 4 IGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPDsplgilgIGVGVPGLVDSEDGVVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 77 PHNLGgLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQ---ALDGDitDMVFITVSTGVGGGVVSGCKLLTGPGGLAGH 153
Cdd:cd24076 84 APNLG-WRDVPLRDLLEEALGVPVFVDNEANAAALAEKRfgaGRGVS--DLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 154 IGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADAKT---IFTRAGQGDEQAQQLIHRSARTLARLIADIKA 230
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAGGEPLSlaeLVEAARAGDPAALAALEEVGEYLGIGLANLVN 240
|
250 260
....*....|....*....|
gi 90111558 231 TTDCQCVVVGGSVGLAEGYL 250
Cdd:cd24076 241 TFNPELVVLGGALAPLGPWL 260
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-246 |
7.58e-29 |
|
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: 112.30 E-value: 7.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPasQTPEALRDALSALVSPLQAHAQR-------VAIASTGIIRDGSLLALN 76
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTD--TTPETIVDAIASAVDSFIQHIAKvgheivaIGIGAPGPVNRQRGTVYF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 77 PHNLGgLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDGD-ITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIG 155
Cdd:TIGR00744 79 AVNLD-WKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKgARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 156 HTLADPHGPV-CGCGRTGCVEAIASGRGI---AAAAQGELA------------GADAKTIFTRAGQGDEQAQQLIHRSAR 219
Cdd:TIGR00744 158 HIRMVPDGRLlCNCGKQGCIETYASATGLvryAKRANAKPEraevllalgdgdGISAKHVFVAARQGDPVAVDSYREVAR 237
|
250 260
....*....|....*....|....*..
gi 90111558 220 TLARLIADIKATTDCQCVVVGGSVGLA 246
Cdd:TIGR00744 238 WAGAGLADLASLFNPSAIVLGGGLSDA 264
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
5-246 |
2.38e-27 |
|
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: 107.70 E-value: 2.38e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 5 AIDIGGTKLAAALIGADGQIRDRRELPTPAsQTPEALRDALSALVSPLQAHAQ---RVAIASTGII--RDGSLLALNphn 79
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPT-DDYAAFLAAIAELVAEADARFGvkgPVGIGIPGVIdpEDGTLITAN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 80 LGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDGDITDMVF-ITVSTGVGGGVVSGCKLLTGPGGLAGHIGHT- 157
Cdd:cd24057 80 IPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFgLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 158 -----LADPHG-PV--CGCGRTGCVEAIASGRGIAAAAQ---GElaGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIA 226
Cdd:cd24057 160 lpadaLLLGYDlPVlrCGCGQTGCLETYLSGRGLERLYAhlyGE--ELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLA 237
|
250 260
....*....|....*....|
gi 90111558 227 DIKATTDCQCVVVGGsvGLA 246
Cdd:cd24057 238 NILTALDPDVVVLGG--GLS 255
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-250 |
2.05e-26 |
|
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: 103.70 E-value: 2.05e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQR------VAIASTGII--RDGSLlaL 75
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGVrerilgIGIGVPGPVdpETGIV--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NPHNLGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITvstgvgggvvsgcKLLTGPGGLAGHI 154
Cdd:cd23763 79 FAPNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGrGVRNFVYITlgtgigggiiidgKLYRGANGAAGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 155 GHTladphgpvcgcgrtgcveaiasgrgiaaaaqgelagadaktiftragqgdeqaqQLIHRSARTLARLIADIKATTDC 234
Cdd:cd23763 159 GHI------------------------------------------------------TVLEEAARYLGIGLANLINLLNP 184
|
250
....*....|....*.
gi 90111558 235 QCVVVGGSVGLAEGYL 250
Cdd:cd23763 185 ELIVLGGGVAEAGDLL 200
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
4-250 |
3.11e-26 |
|
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: 104.89 E-value: 3.11e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPL--QAHAQRVAIASTGII-RDGSLLALNPhNL 80
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELieEMELLGIGIGSPGSIdRENGIVRFSP-NF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 81 GGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAE--FQALDGdITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTL 158
Cdd:cd24064 81 PDWRNFPLVPLIEERTGIKVFLENDANAFALGEwwFGNAKG-SNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 159 ADPHGPVCGCGRTGCVEAIASGRGIAAAAQ-----------GELAGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIAD 227
Cdd:cd24064 160 VEPNGPICGCGNRGCVEAFASATAIIRYAResrkrypdslaGESEKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGG 239
|
250 260
....*....|....*....|...
gi 90111558 228 IKATTDCQCVVVGGSVGLAEGYL 250
Cdd:cd24064 240 FVHIFNPEIIIIGGGISRAGSFL 262
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
3-241 |
6.91e-26 |
|
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: 103.82 E-value: 6.91e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALVSPLQAHAQR------VAIASTGIIRDGSLLALN 76
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENIkskilgIGIGAPGPLDVEKGIILN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 77 PHNLGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAE--FQAlDGDITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHI 154
Cdd:cd24059 83 PPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEkwYGK-GKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 155 GHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELA--GADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATT 232
Cdd:cd24059 162 GHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGsgRSFQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLINLL 241
|
....*....
gi 90111558 233 DCQCVVVGG 241
Cdd:cd24059 242 NPEAIIIGG 250
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
2-276 |
7.75e-25 |
|
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: 100.72 E-value: 7.75e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 2 TTLAIDIGGTKLAAALIGADGQIRDRRELPTPAsQTPEALRDALSALVSPLQAHAQRVAI-------ASTGIIRDGSLla 74
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPK-DSLEEFLDYIKKIIKRYDEEIDGIAIsapgvidPETGIIYGGGA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 75 lNPHNLGgllhFPLVKTLEQLTNLPTIAINDAQAAAWAEFQAldG---DITDMVFITvstgvgggvvsgckLLTGPGG-- 149
Cdd:cd24152 78 -LPYLKG----FNLKEELEERCNLPVSIENDAKCAALAELWL--GslkGIKNGAVIV--------------LGTGIGGai 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 150 ------------LAGHIGHTLADP--HGPVCGCGRTGCVEAIasgRGIAAAAQGELagADAKTIFTRAGQGDEQAQQLIH 215
Cdd:cd24152 137 iidgklyrgshfFAGEFSYLLTDDddKDLLFFSGLASMFGLV---KRYNKAKGLEP--LDGEEIFEKYAKGDEAAKKILD 211
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 90111558 216 RSARTLARLIADIKATTDCQCVVVGGSVGLAEGYLALV-----ETYLAQEPAAFHVDLLAAHYRHD 276
Cdd:cd24152 212 EYIRNLAKLIYNIQYILDPEVIVIGGGISEQPLFIEDLkkevnEILANRPGSIPKPEIKACKFGND 277
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
6-256 |
1.10e-22 |
|
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: 95.05 E-value: 1.10e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 6 IDIGGTKLAAALIGADGQIRDRRELPTP----ASQTPEALRDALSALVSPLQAHAQRVAIASTGI-----IRDGSL-LAL 75
Cdd:cd24062 5 IDVGGTTIKMAFLTQEGEIVQKWEIPTNklegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVpgpvdVETGTVeVAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NPhnlgGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEF--QALDGdITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGH 153
Cdd:cd24062 85 NL----GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMwkGAGQG-AKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 154 IGHTLADPHGPV-CGCGRTGCVEAIASGRGIAAAAQGELAGA---------------DAKTIFTRAGQGDEQAQQLIHRS 217
Cdd:cd24062 160 IGHITVNPEGGApCNCGKTGCLETVASATGIVRIAREELEEGkgssalrilalggelTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 90111558 218 ARTLARLIADIKATTDCQCVVVGGSVGLA-EGYLALVETY 256
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSAAgEFLLSPVKEY 279
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
3-251 |
1.15e-22 |
|
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: 95.13 E-value: 1.15e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPAsQTPEALRDALSALVSPLQAHAQR-------VAIASTGIIRDGS-LLA 74
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEHTVPLTA-LNQEALLSQLIEEIAQFLKSHRRktqrliaISITLPGLINPKTgVVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 75 LNPHNlgGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAE-FQALDGDITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGH 153
Cdd:cd24075 82 YMPHI--QVKSWPIVEELEQRFNVPCFIGNDIRSLALAEhYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 154 IGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGEL-AGA---------DAKTIFTRAGQGDEQAQQLIHRSARTLAR 223
Cdd:cd24075 160 IGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLkQGYasqltlqdcTIKDICQAALNGDQLAQDVIKRAGRYLGK 239
|
250 260
....*....|....*....|....*...
gi 90111558 224 LIADIKATTDCQCVVVGGSVGLAEGYLA 251
Cdd:cd24075 240 VIAILINLLNPQKIIIAGEITQADKVLL 267
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
10-250 |
2.35e-21 |
|
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: 91.46 E-value: 2.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 10 GTKLAAALIGADGQIRDRRELPTPaSQTPEALRDALSALVSPLQAHAQR-------VAIASTGIIRDGSLLALNPHNLGg 82
Cdd:cd24073 10 EDRITAVLTDLRGNVLASHTLPLD-SGDPEAVAEAIAEAVAELLAQAGLspdrllgIGVGLPGLVDAETGICRWSPLLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 83 LLHFPLVKTLEQLTNLPTIAINDAQAAAWAE--FQALDGdITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTLAD 160
Cdd:cd24073 88 WRDVPLAELLEERLGLPVYVENDVNALALAEhwFGAGRG-LDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTTVD 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 161 PHGPVCGCGRTGCVEAIASGRGIAAAAQ---GELAGADAKTIFTRAGQGDEQAQQLIHRSARTLARLIADIKATTDCQCV 237
Cdd:cd24073 167 PDGPPCRCGKRGCLEAYASDPAILRQAReagLRGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELI 246
|
250
....*....|...
gi 90111558 238 VVGGSVGLAEGYL 250
Cdd:cd24073 247 IISGEGVRAGDLL 259
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
4-243 |
1.20e-18 |
|
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: 83.79 E-value: 1.20e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPA---SQTPEALRDALSALVSPLQAHAqRVAIASTGII--RDGSLLALNPH 78
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgdyEATLDAIADLVEEAEEELGAPA-TVGIGTPGSIspRTGLVKNANST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 79 NLGGLlhfPLVKTLEQLTNLPTIAINDAQAAAWAEfqALDGDIT--DMVF-ITVSTGVGGGVVSGCKLLTGPGGLAGHIG 155
Cdd:cd24066 81 WLNGK---PLKADLEARLGRPVRIENDANCFALSE--ATDGAGAgaGVVFgVILGTGVGGGIVVNGRVLTGANGIAGEWG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 156 HTLADPH------GPVCGCGRTGCVEAIASGRGIAAAAQgELAGA--DAKTIFTRAGQGDEQAQQLIHRSARTLARLIAD 227
Cdd:cd24066 156 HNPLPWPdedelpGPPCYCGKRGCVETFLSGPALERDYA-RLTGKtlSAEEIVALARAGDAAAVATLDRFLDRLGRALAN 234
|
250
....*....|....*.
gi 90111558 228 IKATTDCQCVVVGGSV 243
Cdd:cd24066 235 VINILDPDVIVLGGGL 250
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
1-249 |
1.83e-18 |
|
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: 83.37 E-value: 1.83e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 1 MTTLAIDIGGTKLAAALIGADGQIRDRRELPT----PASQTPEALRDALSALVSPLQAHAQRVAIASTGII-RDGSLLaL 75
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSkdllRAGDPVEVLADLIREYIEEAGLKPAAIVIGVPGTVdKDRRTV-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NPHNLGGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDGDITDMVFitvstgvgggvvsGC-------------- 141
Cdd:cd24070 80 STPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVL-------------GFyigtgignailing 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 142 KLLTGPGGLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGELAGADAKTIFTRAGQGDEqaqqlIHRSARTL 221
Cdd:cd24070 147 KPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEEHYPDTPILDIFVDHGDEPE-----LDEFVEDL 221
|
250 260
....*....|....*....|....*...
gi 90111558 222 ARLIADIKATTDCQCVVVGGSVGLAEGY 249
Cdd:cd24070 222 ALAIATEINILDPDAVILGGGVIDMKGF 249
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
4-269 |
4.46e-16 |
|
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: 76.69 E-value: 4.46e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPasQTPEALRDALSALVspLQAHAQRVA----IASTGIIRDGSLlalNPHN 79
Cdd:cd24060 3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNP--KTYEERIDLILQMC--VEAASEAVKlncrILGVGISTGGRV---NPRE 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 80 lGGLLH----------FPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGPG 148
Cdd:cd24060 76 -GIVLHstkliqewssVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGkGVENFVTVITGTGIGGGIILNHELIHGSS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 149 GLAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQgELAGAD----------------AKTIFTRAGQGDEQAQQ 212
Cdd:cd24060 155 FCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAK-KLHDEDlllvegmsvtndeevtAKHLIQAAKLGNAKAQK 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 90111558 213 LIHRSARTLARLIADIKATTDCQCVVVGGSvgLAEGYLALVETYLAQ--EPAAFHVDLL 269
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGV--LASHYENIVKDVIAQraLPSVQNVDVV 290
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
3-233 |
1.54e-14 |
|
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: 72.45 E-value: 1.54e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 3 TLAIDIGGTKLAAALIGADGQI--RDRRELPTPAsqTPEALRDALSALVSPL----QAHAQRVAIASTGII--RDGSLLA 74
Cdd:cd24072 3 VLGIVVSPNSLRAQVGNACGELlgEFEYRVITLE--TPEALIDEIIDCIDRLlklwKDRVKGIALAIQGLVdsHKGVSLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 75 LNPHNLGGllhFPLVKTLEQLTNLPTIAINDAQAAAWAE-FQALDGDITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGH 153
Cdd:cd24072 81 SPGAPWRN---IEIKYLLEERYGIPVFVENDCNMLALAEkWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGE 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 154 IGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQGEL-AGADAKTI-------FTRA-GQGDEQAQQLIHRSARTLARL 224
Cdd:cd24072 158 IGHTKVNPDGARCDCGRRGCLETVASNSALKRNARVTLkLGPVSADPekltmeqLIEAlEEGEPIATQIFDRAANAIGRS 237
|
....*....
gi 90111558 225 IADIKATTD 233
Cdd:cd24072 238 LANILNLLN 246
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
3-113 |
4.77e-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: 67.21 E-value: 4.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 3 TLAIDIGGTKLAAALIGAD-GQ-IRDRRELPTPASQTPEALRDALSALVSPLQAHAqRVAIASTGIIRDGslLALNPHNL 80
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDTDtGElLSERIRIPTPQPATPEAVADVVAELVAHFPWFG-PVGVGFPGVVRRG--VVRTAANL 77
|
90 100 110
....*....|....*....|....*....|....
gi 90111558 81 G-GLLHFPLVKTLEQLTNLPTIAINDAQAAAWAE 113
Cdd:cd24058 78 DkSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAE 111
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
4-226 |
7.71e-13 |
|
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: 67.72 E-value: 7.71e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQ--IRDRRELPT-PASQTPEALRDALSALVSPLQAHAQRV-AIAstgIIRDGsllALNPHN 79
Cdd:cd24074 5 LSIRIGRGYITLALRDLNGRllAEERYPLPAkDNDPFLDRLLESISEFFSRHQKKLERLtAIA---ITLPG---IIDPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 80 lgGLLH---------FPLVKTLEQLTNLPTIAINDAQAAAWAE-FQALDGDITDMVFITVSTGVGGGVVSGCKLLTGPGG 149
Cdd:cd24074 79 --GIVHrlpfydiknLPLGEALEQHTGLPVYVQHDISAWTLAErFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSS 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 150 LAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAAQgELAGADAKTIFTR-----------AGQGDEQAQQLIHRSA 218
Cdd:cd24074 157 RLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQAN-QLLEQSPDSMLHGqpisieslcqaALAGDPLAQDIIIQVG 235
|
....*...
gi 90111558 219 RTLARLIA 226
Cdd:cd24074 236 RHLGRILA 243
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
4-241 |
3.54e-12 |
|
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: 65.38 E-value: 3.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRDALSALV------SPLQAHAQRVAIASTGII-------RDG 70
Cdd:cd24071 4 IGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIkkliknKHVEKKLLGIGIAVSGLVdskkgivIRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 71 SLLalnphnlgGLLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGPGG 149
Cdd:cd24071 84 TIL--------GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGkGYSNFICVTVGAGIGSSLVIDGKLYTGNFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 150 LAGHIGHTLADPHGPVCGCGRTGCVEAIASGRGIAAAA-----QGELAGADAKTIFT------RAGQGDEQAQQLIHRSA 218
Cdd:cd24071 156 GAGEIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIkelteSYPLSLLKELEDFEiekvreAAEEGDSVATELFKKAG 235
|
250 260
....*....|....*....|...
gi 90111558 219 RTLARLIADIKATTDCQCVVVGG 241
Cdd:cd24071 236 EYLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
3-243 |
3.77e-12 |
|
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: 65.25 E-value: 3.77e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPaSQTPEALRDALSALVSPL--QAHAQR-----VAIASTGIIRDGSLLAL 75
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLL-DISFENILEILKSIIQELisQAPKTPyglvgIGIGIHGIVDENEIIFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NPHNLGGLlhfPLVKTLEQLTNLPTIAINDAQAAAWAEfQALDGDITDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIG 155
Cdd:cd24077 82 PYYDLEDI---DLKEKLEEKFNVPVYLENEANLSALAE-RTFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 156 HTLADPHGPVCGCGRTGCVEAIASGRGIAAaaqgELAGADAKTIFTRA------GQGDEQAQQLIHRSARTLARLIADIK 229
Cdd:cd24077 158 HMIIVPNGKPCPCGNKGCLEQYASEKALLK----ELSEKKGLETLTFDdliqlyNEGDPEALELIDQFIKYLAIGINNII 233
|
250
....*....|....
gi 90111558 230 ATTDCQCVVVGGSV 243
Cdd:cd24077 234 NTFNPEIIIINSSL 247
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-243 |
1.41e-11 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 63.85 E-value: 1.41e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTP---EALRDALSALVSPLQAHAQRVAIASTGIIRDGSLLALNPHNL 80
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPdlvSGLGEMIDEYLRRFNARCHGIVMGFPALVSKDRRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 81 --GGLLHFPLVKTLEQLTNLPtIAIN---------DAQaaawaEFQaLDGDI-------TDM---VFITVstgvgggvvs 139
Cdd:PRK09698 87 plTALDLYDLADKLENTLNCP-VFFSrdvnlqllwDVK-----ENN-LTQQLvlgaylgTGMgfaVWMNG---------- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 140 gcKLLTGPGGLAGHIGHT-LADPHGPvCGCGRTGCVEAIASGRGIAAAAQGELAGADAKTIFTRAgqGDEQA-QQLIHRs 217
Cdd:PRK09698 150 --APWTGAHGVAGELGHIpLGDMTQH-CGCGNPGCLETNCSGMALRRWYEQQPRDYPLSDLFVHA--GDHPFiQSLLEN- 223
|
250 260
....*....|....*....|....*.
gi 90111558 218 artLARLIADIKATTDCQCVVVGGSV 243
Cdd:PRK09698 224 ---LARAIATSINLFDPDAIILGGGV 246
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
7-241 |
6.62e-10 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 58.85 E-value: 6.62e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 7 DIGGTKLAAALIGADGQIRDRRELPTPASQTPEALrDALSALVSplQAHAQRVAIASTGI-------IRDGSLLALN-PH 78
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFL-DAVCELVA--EADQRFGCKGSVGIgipgmpeTEDGTLYAANvPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 79 NLGGllhfPLVKTLEQLTNLPTIAINDAQAAAWAEfqALDGDITDMVFITVSTGVGG---GVVSGCKLLTGPGGLAGHIG 155
Cdd:PRK13310 83 ASGK----PLRADLSARLGRDVRLDNDANCFALSE--AWDDEFTQYPLVMGLILGTGvggGLVFNGKPISGRSYITGEFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 156 HTLADPHG--------PV--CGCGRTGCVEAIASGRGIA---AAAQGElaGADAKTIFTRAGQGDEQAQQLIHRSARTLA 222
Cdd:PRK13310 157 HMRLPVDAltllgwdaPLrrCGCGQKGCIENYLSGRGFEwlyQHYYGE--PLQAPEIIALYYQGDEQAVAHVERYLDLLA 234
|
250
....*....|....*....
gi 90111558 223 RLIADIKATTDCQCVVVGG 241
Cdd:PRK13310 235 ICLGNILTIVDPHLVVLGG 253
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
6-243 |
9.09e-10 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 58.50 E-value: 9.09e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 6 IDIGGTKLAAALIGADGQIRDRRELPTPASQTPEALrDALSALVSPL-QAHAQR----VAIAS-----TGIIRDGSLLAL 75
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTI-EAIATLVDMAeQATGQRgtvgVGIPGsispyTGLVKNANSTWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NPHnlggllhfPLVKTLEQLTNLPTIAINDAQAAAWAEfqALDGDIT--DMVFitvstgvGGGVVSGC--------KLLT 145
Cdd:PRK09557 84 NGQ--------PLDKDLSARLNREVRLANDANCLAVSE--AVDGAAAgkQTVF-------AVIIGTGCgagvaingRVHI 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 146 GPGGLAGHIGHT---------LADPHGPVCGCGRTGCVEAIASGRGIAAAAQgeLAGADAKT---IFTRAGQGDEQAQQL 213
Cdd:PRK09557 147 GGNGIAGEWGHNplpwmdedeLRYRNEVPCYCGKQGCIETFISGTGFATDYR--RLSGKALKgseIIRLVEEGDPVAELA 224
|
250 260 270
....*....|....*....|....*....|
gi 90111558 214 IHRSARTLARLIADIKATTDCQCVVVGGSV 243
Cdd:PRK09557 225 FRRYEDRLAKSLAHVINILDPDVIVLGGGM 254
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
5-259 |
3.32e-09 |
|
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: 56.40 E-value: 3.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 5 AIDIGGTKLAAALIGADGQIRDRRELPTP-ASQTPEALRDALSALVSPLQAhaqrVAIASTGIIRdgsllaLNPH--NLG 81
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIERTEFPTTtPEETLQAVIDFFREQEEPIDA----IGIASFGPID------LNPTspTYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 82 GLL--------HFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDG-DITDMVFITVSTGVGGGVVSGCKLLTGpgglAG 152
Cdd:cd24067 73 YITttpkpgwrNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAkGLDSLAYITVGTGIGVGLVVNGKPVHG----LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 153 H--IGHTL------ADPHGPVCGCGRtGCVEAIASGRGIAAaaqgelagadaktiftRAGQGDEQAQQlIHRS----ART 220
Cdd:cd24067 149 HpeMGHIRvprhpdDDGFPGVCPFHG-DCLEGLASGPAIAA----------------RWGIPAEELPD-DHPAwdleAYY 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 90111558 221 LARLIADIKATTDCQCVVVGGSVGLAEGYLALVETYLAQ 259
Cdd:cd24067 211 LAQACANLTLTLSPERIVLGGGVMQRPGLFPRIREKFRK 249
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
4-228 |
7.75e-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: 46.45 E-value: 7.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGAD---GQIRDRRELPTPASQTPE-ALRDALSALVSPLQAHAqRVAIAstGIIRDGSLLALNPHn 79
Cdd:cd24008 2 LVGDIGGTNARLALADAGdgsGDLLFVRKYPSADFASLEdALAAFLAELGAPRPKAA-CIAVA--GPVDGGRVRLTNLD- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 80 lgglLHFPLVKTLEQLTNLPTIAINDAQAAAWAEFQALDGDITDMvfitvsTGVGGGVVSGCKLLTGPG-GL-------- 150
Cdd:cd24008 78 ----WSIDAAELRKALGIGRVRLLNDFEAAAYGLPALGPEDLLVL------YGGGGPLPGGPRAVLGPGtGLgvallvpd 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 151 --------AGHIGHTLADPHGPV---------CGCGRTGCVEAIASGRGIAAAAQ--GELAGA-----DAKTIFTRAGQG 206
Cdd:cd24008 148 gdggyvvlPSEGGHADFAPVTEEeaelleflrKRFGRSVSYEDVLSGPGLENIYEflAKLDGAeppdlTAEEIAEAALAG 227
|
250 260
....*....|....*....|..
gi 90111558 207 DEQAQQLIHRSARTLARLIADI 228
Cdd:cd24008 228 DPLAREALDLFARILGRFAGNL 249
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
4-258 |
6.95e-04 |
|
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: 40.37 E-value: 6.95e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPT--PASQTPEALRDALSALVSPLQAHA------QRVAIASTGIIRDGSLLAL 75
Cdd:cd24007 2 LGVDGGGTKTRAVLADEDGKILGRGKGGPsnPASVGIEEAKENLKEAVREALSQAgslgeiDAICLGLAGIDSEEDRERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NPHnlggllhfplvktLEQLTNLPTIAI-NDAQAAAWAEFQALDGditdMVFITVstgvgggvvsgckllTGPGGLAGHI 154
Cdd:cd24007 82 RSA-------------LKELFLSGRIIIvNDAEIALAAALGGGPG----IVVIAG---------------TGSVAYGRNG 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 155 GHTLA--DPHGPVCG-------CGRTGCVEAIAS--GRG---------------------IAAAAQG-----ELAGAdAK 197
Cdd:cd24007 130 DGEEArvGGWGHLLGdegsgywIGRRALRAALRAldGRGpktplldailkflgldsieelITAIYRSsdrkkEIASL-AP 208
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90111558 198 TIFTRAGQGDEQAQQLIHRSARTLARLI---ADIKATTDCQCVVVGGSVGLAEGYLALVETYLA 258
Cdd:cd24007 209 LVFEAAEEGDPVAQAILKEAAEELAKLVvalAKLLLLGEKLPLALSGGVFKNNYYLAEFLEELL 272
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
4-266 |
2.22e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 39.09 E-value: 2.22e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 4 LAIDIGGTKLAAALIGADGQIRDRRELPT--PASQTPEALRDALSALVSPLQAHA------QRVAIASTGIIRDGSLLAL 75
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLGRGRAGGanPQSVGLEEALASLREALEEALAAAgdpadiEAVGFGLAGAGTPEDAEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 76 NphnlgGLLHfplvktlEQLTNLPTIAINDAQAAAWAEFQALDGDI----TDMVFITVSTGVGGGVVsgcklltgpGGL- 150
Cdd:COG2971 84 E-----AALR-------ELFPFARVVVVNDALAALAGALGGEDGIVviagTGSIAAGRDGDGRTARV---------GGWg 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 151 --------AGHIGHTL-------ADPHGPvcgcgRTGCVEAIA------SGRGIAAAAQGELAGAD-----AKTIFTRAG 204
Cdd:COG2971 143 yllgdegsGAWLGREAlraalraLDGRGP-----PTALTEAVLaefgldDPEELIAWVYRGPAPPAdlaslAPLVFEAAE 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90111558 205 QGDEQAQQLIHRSARTLARLIADIKATTDCQcVVVGGSVGLAEGYL-ALVETYLAQEPAAFHV 266
Cdd:COG2971 218 AGDPVARAILEEAADELAELARALLERGALP-VVLAGGVAAAQPLLrEALRARLAAGGAEIVP 279
|
|
| Glk |
COG0837 |
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway ... |
1-228 |
8.24e-03 |
|
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440599 Cd Length: 320 Bit Score: 37.40 E-value: 8.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 1 MTTLAIDIGGTK--LAAALIGADGQIRDRRELPTPASQTPE-ALRDALSALVSPlqaHAQRVAIASTGIIRDGSLLALNp 77
Cdd:COG0837 5 TPILVADIGGTNarLALAEGGGGLELLEIRRYPSADYASLEdALRAYLAELGLP---RPRAACLAVAGPVDGDRVKLTN- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 78 hnlgglLHFPL-VKTLEQLTNLPTIA-INDAQAAAWAeFQALDGDitDMVFITVSTGVGGGVvsgcKLLTGPG---GLAG 152
Cdd:COG0837 81 ------LPWSIsAAALRAALGLERVLlINDFEALAYA-LPALSPD--DLVQLGGGEPDPGGP----RAVIGPGtglGVAG 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 153 HI-------------GHT---------------LADPHGPVcgcgrtgCVEAIASGRGI-------AAAAQGELAGADAK 197
Cdd:COG0837 148 LVpdgggwivlpsegGHVdfaprderelellryLRRRYGHV-------SAERVLSGPGLvnlyralAALDGAPPAPLSPA 220
|
250 260 270
....*....|....*....|....*....|..
gi 90111558 198 TIFTRAGQG-DEQAQQLIHRSARTLARLIADI 228
Cdd:COG0837 221 EITAAALAGsDPLAVEALELFCRILGRVAGNL 252
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
7-182 |
9.71e-03 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 36.93 E-value: 9.71e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 7 DIGGTKLAAALIGADGQIRDRRELPTPASQTPEALRdALSALVSPLQAHAQRVAIASTGI-----IRDGSLLALN-PHNL 80
Cdd:PRK13311 6 DMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQ-ILRDLTEEADTYCGVQGSVGIGIpglpnADDGTVFTANvPSAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90111558 81 GGLLHFPLVKTLEQLTNLPTIAINDAQAAAW-AEFQALdgdiTDMVFITVSTGVGGGVVSGCKLLTGPGGLAGHIGHTL- 158
Cdd:PRK13311 85 GQPLQADLSRLIQREVRIDNDANCFALSEAWdPEFRTY----PTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRl 160
|
170 180 190
....*....|....*....|....*....|....
gi 90111558 159 ---------AD-PHGPvCGCGRTGCVEAIASGRG 182
Cdd:PRK13311 161 pvdaldilgADiPRVP-CGCGHRGCIENYISGRG 193
|
|
| |
