|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
1-276 |
1.07e-153 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 430.87 E-value: 1.07e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 1 MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQVAIASTGIIRDGSLLALNPHNL 80
Cdd:PRK05082 1 MTTLAIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQADRVAVASTGIINDGILTALNPHNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 81 GGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLAD 160
Cdd:PRK05082 81 GGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTLAD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 161 PQGPVCGCGRTGCVEAIASGRGIAAAAQGELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTDCQCVVVG 240
Cdd:PRK05082 161 PHGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKATLDCQCVVLG 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1610968931 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 |
6.04e-113 |
|
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: 327.32 E-value: 6.04e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGaDGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQVAIASTGIIRDGSLLALNPHNLGGL 83
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSGTPEALADALASLLADYQGQFDRVAVASTGIIRDGVLTALNPKNLGGL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 84 LHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLADPQ 162
Cdd:cd24069 80 SGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGeGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADPP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 163 GPVCGCGRTGCVEAIASGRGIAAAAQGELM-GADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTDCQCVVVGG 241
Cdd:cd24069 160 GPVCGCGRRGCVEAIASGTAIAAAASEILGePVDAKDVFERARSGDEEAARLIDRAARALADLIADLKATLDLDCVVIGG 239
|
250 260 270
....*....|....*....|....*....|....*
gi 1610968931 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 |
2.40e-90 |
|
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: 270.37 E-value: 2.40e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQ---VAIASTGIIRDGSLLALNPHNL 80
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEETLVDAIAFFVDSAQRKFGEliaVGIGSPGLISPKYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 81 GGLlHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQ-ALEGDITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLA 159
Cdd:pfam00480 81 GWD-NFDLVEKLEERFNVPVFFENDANAAALAEAVfGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 160 DPQGPVCGCGRTGCVEAIASGRGIAAAAQGELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTDCQCVVV 239
Cdd:pfam00480 160 DPNGPKCGCGNHGCLETIASGRALEKRYQQKGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQAIVL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1610968931 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 |
3.61e-61 |
|
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: 196.27 E-value: 3.61e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 1 MTTLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQ-------VAIASTGIIRDGSLL 73
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGIsrgrilgIGIGVPGPVDPETGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 74 ALNPHNLGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFvtvstgvgggvvsggKLLTGPGGLAG 152
Cdd:COG1940 85 VLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGrGADNVVYltlgtgigggivingKLLRGANGNAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 153 HIGHTLADPQGPVCGCGRTGCVEAIASGRGIA--AAAQGELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKA 230
Cdd:COG1940 165 EIGHMPVDPDGPLCGCGNRGCLETYASGPALLrrARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLIN 244
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1610968931 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 |
3.37e-41 |
|
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: 144.24 E-value: 3.37e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQVAIA--STGII--RDGSLLALNPhN 79
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGisSAGQVdpKTGEVIYATD-N 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 80 LGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTL 158
Cdd:cd24068 82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAkGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 159 ADPQGPVCGCGRTGCVEAIASGRGIA--AAAQGELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTDCQC 236
Cdd:cd24068 162 VDPGGRPCCCGGKGCLEQYASGTALVrrVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1610968931 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 |
5.26e-36 |
|
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: 130.92 E-value: 5.26e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALV-----SPLHAHAQQVAIASTGIIRDGSLLALNPH 78
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIetllsKAGKDSIEGIGVSSAGPLDLRKGTIVNSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 79 NLGGLLhFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGD-ITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHT 157
Cdd:cd24063 83 NIKGKE-IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRgTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 158 LADPQ-GPVCGCGRTGCVEAIASGRGIAAAAQGELMGAD----------------AKTIFTRAGQGDEQAQQLIHRSARV 220
Cdd:cd24063 162 VVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSsrtslklrnpggegitAKEVFSAARKGDPLALKIIEKLARY 241
|
250 260
....*....|....*....|...
gi 1610968931 221 LARLIADIKATTDCQCVVVGGSV 243
Cdd:cd24063 242 NGRGIANVINAYDPELIVIGGSV 264
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
2-250 |
1.45e-34 |
|
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: 126.68 E-value: 1.45e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 2 TTLAIDIGGTKLAAALIgADGQIRDRRELPTPASQTpQALRDALSALVSPLHAHAQQVAIASTGI-----IRDGSLLALN 76
Cdd:cd24065 1 STIGLDLGGTKIAAGVV-DGGRILSRLVVPTPREGG-EAVLDALARAVEALQAEAPGVEAVGLGVpgpldFRRGRVRFAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 77 phNLGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAE--YQALEGdITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHI 154
Cdd:cd24065 79 --NIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEhhYGAARG-TESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 155 GHTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQGELMGA-DAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTD 233
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAYGRPmSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALD 235
|
250
....*....|....*..
gi 1610968931 234 CQCVVVGGSVGLAEGYL 250
Cdd:cd24065 236 PEVFVLGGGVAQVGDYY 252
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
3-265 |
3.54e-32 |
|
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: 120.54 E-value: 3.54e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPAsqTPQALRDALSALVSPLHA-HA-QQVAIASTGII-RDGSLLALNPHN 79
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVEELREgHDvSAVGVAAAGFVdADRATVLFAPNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 80 lgGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTL 158
Cdd:cd24061 79 --AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGrGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIR 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 159 ADPQGPVCGCGRTGCVEAIASGRGI------AAAAQGE---LMGADA-------KTIFTRAGQGDEQAQQLIHRSARVLA 222
Cdd:cd24061 157 VVPDGLLCGCGSRGCWEQYASGRALvryakeAANATPEgaaVLLADGsvdgitgKHISEAARAGDPVALDALRELARWLG 236
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1610968931 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 |
1.28e-29 |
|
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: 113.81 E-value: 1.28e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQ-------VAIASTGIIRDGSLLALN 76
Cdd:cd24076 4 IGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPDsplgilgIGVGVPGLVDSEDGVVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 77 PHNLGgLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITE-MVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIG 155
Cdd:cd24076 84 APNLG-WRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSdLVYLSAGVGIGAGIILDGELYRGASGFAGEIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 156 HTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQ---GELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATT 232
Cdd:cd24076 163 HMTVDPDGPPCSCGNRGCWETYASERALLRAAGrlgAGGEPLSLAELVEAARAGDPAALAALEEVGEYLGIGLANLVNTF 242
|
250
....*....|....*...
gi 1610968931 233 DCQCVVVGGSVGLAEGYL 250
Cdd:cd24076 243 NPELVVLGGALAPLGPWL 260
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
5-246 |
2.42e-28 |
|
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: 110.40 E-value: 2.42e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 5 AIDIGGTKLAAALIGADGQIRDRRELPTPAsQTPQALRDALSALVSPLHAHAQQ---VAIASTGII--RDGSLLALNphn 79
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPT-DDYAAFLAAIAELVAEADARFGVkgpVGIGIPGVIdpEDGTLITAN--- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 80 LGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITEMVFVTVSTG-VGGGVVSGGKLLTGPGGLAGHIGHT- 157
Cdd:cd24057 80 IPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTgVGGGLVVNGRLVGGRSGIAGEWGHGp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 158 ------LADPQGPV--CGCGRTGCVEAIASGRGIAAAAQ---GElmGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIA 226
Cdd:cd24057 160 lpadalLLGYDLPVlrCGCGQTGCLETYLSGRGLERLYAhlyGE--ELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLA 237
|
250 260
....*....|....*....|
gi 1610968931 227 DIKATTDCQCVVVGGsvGLA 246
Cdd:cd24057 238 NILTALDPDVVVLGG--GLS 255
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-246 |
1.30e-27 |
|
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: 108.83 E-value: 1.30e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPasQTPQALRDALSALVSPLHAHAQQ-------VAIASTGIIRDGSLLALN 76
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTD--TTPETIVDAIASAVDSFIQHIAKvgheivaIGIGAPGPVNRQRGTVYF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 77 PHNLGgLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGD-ITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIG 155
Cdd:TIGR00744 79 AVNLD-WKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKgARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 156 HTLADPQGPV-CGCGRTGCVEAIASGRGIAAAAQ---------------GELMGADAKTIFTRAGQGDEQAQQLIHRSAR 219
Cdd:TIGR00744 158 HIRMVPDGRLlCNCGKQGCIETYASATGLVRYAKranakperaevllalGDGDGISAKHVFVAARQGDPVAVDSYREVAR 237
|
250 260
....*....|....*....|....*..
gi 1610968931 220 VLARLIADIKATTDCQCVVVGGSVGLA 246
Cdd:TIGR00744 238 WAGAGLADLASLFNPSAIVLGGGLSDA 264
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
4-250 |
9.10e-24 |
|
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: 97.95 E-value: 9.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPL--HAHAQQVAIASTGII-RDGSLLALNPhNL 80
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELieEMELLGIGIGSPGSIdRENGIVRFSP-NF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 81 GGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAE--YQALEGdITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTL 158
Cdd:cd24064 81 PDWRNFPLVPLIEERTGIKVFLENDANAFALGEwwFGNAKG-SNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 159 ADPQGPVCGCGRTGCVEAIASGRGIAAAAQ-----------GELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIAD 227
Cdd:cd24064 160 VEPNGPICGCGNRGCVEAFASATAIIRYAResrkrypdslaGESEKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGG 239
|
250 260
....*....|....*....|...
gi 1610968931 228 IKATTDCQCVVVGGSVGLAEGYL 250
Cdd:cd24064 240 FVHIFNPEIIIIGGGISRAGSFL 262
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-250 |
1.03e-23 |
|
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: 96.38 E-value: 1.03e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQ------VAIASTGII--RDGSLLal 75
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGVrerilgIGIGVPGPVdpETGIVL-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 76 NPHNLGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFvtvstgvgggvvsggKLLTGPGGLAGHI 154
Cdd:cd23763 79 FAPNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGrGVRNFVYitlgtgigggiiidgKLYRGANGAAGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 155 GHTladpqgpvcgcgrtgcveaiasgrgiaaaaqgelmgadaktiftragqgdeqaqQLIHRSARVLARLIADIKATTDC 234
Cdd:cd23763 159 GHI------------------------------------------------------TVLEEAARYLGIGLANLINLLNP 184
|
250
....*....|....*.
gi 1610968931 235 QCVVVGGSVGLAEGYL 250
Cdd:cd23763 185 ELIVLGGGVAEAGDLL 200
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
6-256 |
5.52e-23 |
|
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: 96.20 E-value: 5.52e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 6 IDIGGTKLAAALIGADGQIRDRRELPTP----ASQTPQALRDALSALVSPLHAHAQQVAIASTGI-----IRDGSL-LAL 75
Cdd:cd24062 5 IDVGGTTIKMAFLTQEGEIVQKWEIPTNklegGENIITDIAESIQQLLEELGYSKEDLIGIGVGVpgpvdVETGTVeVAV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 76 NPhnlgGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEY--QALEGdITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGH 153
Cdd:cd24062 85 NL----GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMwkGAGQG-AKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 154 IGHTLADPQGPV-CGCGRTGCVEAIASGRGIAAAAQGELMGA---------------DAKTIFTRAGQGDEQAQQLIHRS 217
Cdd:cd24062 160 IGHITVNPEGGApCNCGKTGCLETVASATGIVRIAREELEEGkgssalrilalggelTAKDVFEAAKAGDELALAVVDTV 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1610968931 218 ARVLARLIADIKATTDCQCVVVGGSVGLA-EGYLALVETY 256
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSAAgEFLLSPVKEY 279
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
2-276 |
1.08e-22 |
|
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: 94.94 E-value: 1.08e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 2 TTLAIDIGGTKLAAALIGADGQIRDRRELPTPAsQTPQALRDALSALVSPLHAHAQQVAI-------ASTGIIRDGSLla 74
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPK-DSLEEFLDYIKKIIKRYDEEIDGIAIsapgvidPETGIIYGGGA-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 75 lNPHNLGgllhFPLVKTLEQLTDLPTIAINDAQAAAWAE--YQALEGdITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAG 152
Cdd:cd24152 78 -LPYLKG----FNLKEELEERCNLPVSIENDAKCAALAElwLGSLKG-IKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 153 HIGHTLADPQGP--VCGCGRTGCVEAIasgRGIAAAAQGELMgaDAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKA 230
Cdd:cd24152 152 EFSYLLTDDDDKdlLFFSGLASMFGLV---KRYNKAKGLEPL--DGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQY 226
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1610968931 231 TTDCQCVVVGGSVGLAEGYLALV-----ETYLAQEPAAFHVDLLAAHYRHD 276
Cdd:cd24152 227 ILDPEVIVIGGGISEQPLFIEDLkkevnEILANRPGSIPKPEIKACKFGND 277
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
3-241 |
1.38e-22 |
|
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: 94.96 E-value: 1.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHAQQ------VAIASTGIIRDGSLLALN 76
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENIkskilgIGIGAPGPLDVEKGIILN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 77 PHNLGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAE--YQAlEGDITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHI 154
Cdd:cd24059 83 PPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEkwYGK-GKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 155 GHTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQGELM--GADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATT 232
Cdd:cd24059 162 GHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGsgRSFQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLINLL 241
|
....*....
gi 1610968931 233 DCQCVVVGG 241
Cdd:cd24059 242 NPEAIIIGG 250
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
3-251 |
1.03e-20 |
|
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: 89.73 E-value: 1.03e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPAsQTPQALRDALSALVSPLHAHAQQ-------VAIASTGIIRDGS-LLA 74
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEHTVPLTA-LNQEALLSQLIEEIAQFLKSHRRktqrliaISITLPGLINPKTgVVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 75 LNPHNlgGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAE-YQALEGDITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGH 153
Cdd:cd24075 82 YMPHI--QVKSWPIVEELEQRFNVPCFIGNDIRSLALAEhYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 154 IGHTLADPQGPVCGCGRTGCVEAIASGRGI----------AAAAQGELMGADAKTIFTRAGQGDEQAQQLIHRSARVLAR 223
Cdd:cd24075 160 IGHIQIEPLGERCHCGNFGCLETVASNAAIeqrvkkllkqGYASQLTLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGK 239
|
250 260
....*....|....*....|....*...
gi 1610968931 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 |
6.39e-19 |
|
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: 84.53 E-value: 6.39e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 10 GTKLAAALIGADGQIRDRRELPTPaSQTPQALRDALSALVSPLHAHAQQ-------VAIASTGIIRDGSLLALNPHNLGg 82
Cdd:cd24073 10 EDRITAVLTDLRGNVLASHTLPLD-SGDPEAVAEAIAEAVAELLAQAGLspdrllgIGVGLPGLVDAETGICRWSPLLG- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 83 LLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIGHTLADP 161
Cdd:cd24073 88 WRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGrGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTTVDP 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 162 QGPVCGCGRTGCVEAIASGRGIAAAAQ---GELMGADAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTDCQCVV 238
Cdd:cd24073 168 DGPPCRCGKRGCLEAYASDPAILRQAReagLRGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELII 247
|
250
....*....|..
gi 1610968931 239 VGGSVGLAEGYL 250
Cdd:cd24073 248 ISGEGVRAGDLL 259
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
1-249 |
2.19e-16 |
|
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: 77.59 E-value: 2.19e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 1 MTTLAIDIGGTKLAAALIGADGQIRDRRELPT----PASQTPQALRDALSALVSPLHAHAQQVAIASTGII-RDGSLLaL 75
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSkdllRAGDPVEVLADLIREYIEEAGLKPAAIVIGVPGTVdKDRRTV-I 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 76 NPHNLGGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITEMV------------FVTVStgvgggvvsggKL 143
Cdd:cd24070 80 STPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVlgfyigtgignaILING-----------KP 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 144 LTGPGGLAGHIGHTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQGELMGADAKTIFTRAGQGDEqaqqlIHRSARVLAR 223
Cdd:cd24070 149 LRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEEHYPDTPILDIFVDHGDEPE-----LDEFVEDLAL 223
|
250 260
....*....|....*....|....*.
gi 1610968931 224 LIADIKATTDCQCVVVGGSVGLAEGY 249
Cdd:cd24070 224 AIATEINILDPDAVILGGGVIDMKGF 249
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
4-243 |
6.72e-16 |
|
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: 76.09 E-value: 6.72e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPA---SQTPQALRDALSALVSPLHAHAQqVAIASTGII--RDGSLLALNPH 78
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgdyEATLDAIADLVEEAEEELGAPAT-VGIGTPGSIspRTGLVKNANST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 79 NLGGLlhfPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITEMVFVTVSTGVGGG-VVSGGKLLTGPGGLAGHIGHT 157
Cdd:cd24066 81 WLNGK---PLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGgIVVNGRVLTGANGIAGEWGHN 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 158 LADPQ------GPVCGCGRTGCVEAIASGRGIAAAAQgELMGA--DAKTIFTRAGQGDEQAQQLIHRSARVLARLIADIK 229
Cdd:cd24066 158 PLPWPdedelpGPPCYCGKRGCVETFLSGPALERDYA-RLTGKtlSAEEIVALARAGDAAAVATLDRFLDRLGRALANVI 236
|
250
....*....|....
gi 1610968931 230 ATTDCQCVVVGGSV 243
Cdd:cd24066 237 NILDPDVIVLGGGL 250
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
4-269 |
8.32e-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: 75.92 E-value: 8.32e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPasQTPQALRDALSALVSPLHAHAQQVA--IASTGIIRDGSLlalNPHNlG 81
Cdd:cd24060 3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNP--KTYEERIDLILQMCVEAASEAVKLNcrILGVGISTGGRV---NPRE-G 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 82 GLLH----------FPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGPGGL 150
Cdd:cd24060 77 IVLHstkliqewssVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGkGVENFVTVITGTGIGGGIILNHELIHGSSFC 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 151 AGHIGHTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQ-----GELM----------GADAKTIFTRAGQGDEQAQQLIH 215
Cdd:cd24060 157 AAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKklhdeDLLLvegmsvtndeEVTAKHLIQAAKLGNAKAQKILR 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1610968931 216 RSARVLARLIADIKATTDCQCVVVGGSvgLAEGYLALVETYLAQ--EPAAFHVDLL 269
Cdd:cd24060 237 TAGTALGLGIVNILHTLNPSLVILSGV--LASHYENIVKDVIAQraLPSVQNVDVV 290
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
3-233 |
6.89e-13 |
|
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: 67.44 E-value: 6.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 3 TLAIDIGGTKLAAALIGADGQI--RDRRELPTPAsqTPQALRDALSALVSPL----HAHAQQVAIASTGII--RDGSLLA 74
Cdd:cd24072 3 VLGIVVSPNSLRAQVGNACGELlgEFEYRVITLE--TPEALIDEIIDCIDRLlklwKDRVKGIALAIQGLVdsHKGVSLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 75 LNPHNLGGllhFPLVKTLEQLTDLPTIAINDAQAAAWAE-----YQALEGDITEMVfvtvSTGVGGGVVSGGKLLTGPGG 149
Cdd:cd24072 81 SPGAPWRN---IEIKYLLEERYGIPVFVENDCNMLALAEkwqgeLRQSRDFCVINL----DYGIGSAIVIDNKLYIGASS 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 150 LAGHIGHTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQGEL-MGADAKTI-------FTRA-GQGDEQAQQLIHRSARV 220
Cdd:cd24072 154 GSGEIGHTKVNPDGARCDCGRRGCLETVASNSALKRNARVTLkLGPVSADPekltmeqLIEAlEEGEPIATQIFDRAANA 233
|
250
....*....|...
gi 1610968931 221 LARLIADIKATTD 233
Cdd:cd24072 234 IGRSLANILNLLN 246
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
3-113 |
1.91e-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: 1.91e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 3 TLAIDIGGTKLAAALIGAD-GQ-IRDRRELPTPASQTPQALRDALSALVSPLHAHAQqVAIASTGIIRDGslLALNPHNL 80
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDTDtGElLSERIRIPTPQPATPEAVADVVAELVAHFPWFGP-VGVGFPGVVRRG--VVRTAANL 77
|
90 100 110
....*....|....*....|....*....|....
gi 1610968931 81 G-GLLHFPLVKTLEQLTDLPTIAINDAQAAAWAE 113
Cdd:cd24058 78 DkSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAE 111
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
7-241 |
6.33e-11 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 61.93 E-value: 6.33e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 7 DIGGTKLAAALIGADGQIRDRRELPTPASQTPQALrDALSALVSPLHAHAQQVAIASTGI-----IRDGSLLALN-PHNL 80
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFL-DAVCELVAEADQRFGCKGSVGIGIpgmpeTEDGTLYAANvPAAS 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 81 GGllhfPLVKTLEQLTDLPTIAINDAQ----AAAW----AEYQALEGDITEMVFVTVstgvgggVVSGGKLLTGPGGLAG 152
Cdd:PRK13310 85 GK----PLRADLSARLGRDVRLDNDANcfalSEAWddefTQYPLVMGLILGTGVGGG-------LVFNGKPISGRSYITG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 153 HIGHTladpQGPV--------------CGCGRTGCVEAIASGRGIA---AAAQGELMgaDAKTIFTRAGQGDEQAQQLIH 215
Cdd:PRK13310 154 EFGHM----RLPVdaltllgwdaplrrCGCGQKGCIENYLSGRGFEwlyQHYYGEPL--QAPEIIALYYQGDEQAVAHVE 227
|
250 260
....*....|....*....|....*.
gi 1610968931 216 RSARVLARLIADIKATTDCQCVVVGG 241
Cdd:PRK13310 228 RYLDLLAICLGNILTIVDPHLVVLGG 253
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
4-241 |
1.99e-10 |
|
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: 60.38 E-value: 1.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALV------SPLHAHAQQVAIASTGII-------RDG 70
Cdd:cd24071 4 IGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIkkliknKHVEKKLLGIGIAVSGLVdskkgivIRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 71 SLLalnphnlgGLLHFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGPGG 149
Cdd:cd24071 84 TIL--------GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGkGYSNFICVTVGAGIGSSLVIDGKLYTGNFG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 150 LAGHIGHTLADPQGPVCGCGRTGCVEAIASGRGIAAAA-----QGELMGADAKTIFT------RAGQGDEQAQQLIHRSA 218
Cdd:cd24071 156 GAGEIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIkelteSYPLSLLKELEDFEiekvreAAEEGDSVATELFKKAG 235
|
250 260
....*....|....*....|...
gi 1610968931 219 RVLARLIADIKATTDCQCVVVGG 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 |
2.20e-10 |
|
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: 60.25 E-value: 2.20e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 3 TLAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALrDALSALVSPLHAHAQQ-------VAIASTGIIRDGSLLAL 75
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENIL-EILKSIIQELISQAPKtpyglvgIGIGIHGIVDENEIIFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 76 NPHNLGGLlhfPLVKTLEQLTDLPTIAINDAQAAAWAEYqALEGDITEMVFVTVSTGVGGGVVSGGKLLTGPGGLAGHIG 155
Cdd:cd24077 82 PYYDLEDI---DLKEKLEEKFNVPVYLENEANLSALAER-TFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 156 HTLADPQGPVCGCGRTGCVEAIASGRGI----AAAAQGELMGADaktIFTRA-GQGDEQAQQLIHRSARVLARLIADIKA 230
Cdd:cd24077 158 HMIIVPNGKPCPCGNKGCLEQYASEKALlkelSEKKGLETLTFD---DLIQLyNEGDPEALELIDQFIKYLAIGINNIIN 234
|
250
....*....|...
gi 1610968931 231 TTDCQCVVVGGSV 243
Cdd:cd24077 235 TFNPEIIIINSSL 247
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-243 |
3.05e-10 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 59.61 E-value: 3.05e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTP---QALRDALSALVSPLHAHAQQVAIASTGIIRDGSLLALNPHNL 80
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPdlvSGLGEMIDEYLRRFNARCHGIVMGFPALVSKDRRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 81 --GGLLHFPLVKTLEQLTDLPtIAIN---------DAQaaawaEYQaLEGDI-------TEMVFVTVSTGvgggvvsggK 142
Cdd:PRK09698 87 plTALDLYDLADKLENTLNCP-VFFSrdvnlqllwDVK-----ENN-LTQQLvlgaylgTGMGFAVWMNG---------A 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 143 LLTGPGGLAGHIGHT-LADPQGPvCGCGRTGCVEAIASGRGIAAAAQGELMGADAKTIFTRAgqGDEQA-QQLIHRsarv 220
Cdd:PRK09698 151 PWTGAHGVAGELGHIpLGDMTQH-CGCGNPGCLETNCSGMALRRWYEQQPRDYPLSDLFVHA--GDHPFiQSLLEN---- 223
|
250 260
....*....|....*....|...
gi 1610968931 221 LARLIADIKATTDCQCVVVGGSV 243
Cdd:PRK09698 224 LARAIATSINLFDPDAIILGGGV 246
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
4-226 |
3.34e-09 |
|
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: 56.94 E-value: 3.34e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQ--IRDRRELPT-PASQTPQALRDALSALVSPLHAHAQQV-AIAstgIIRDGsllALNPHN 79
Cdd:cd24074 5 LSIRIGRGYITLALRDLNGRllAEERYPLPAkDNDPFLDRLLESISEFFSRHQKKLERLtAIA---ITLPG---IIDPES 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 80 lgGLLH---------FPLVKTLEQLTDLPTIAINDAQAAAWAEYqaLEG---DITEMVFVTVSTGVGGGVVSGGKLLTGP 147
Cdd:cd24074 79 --GIVHrlpfydiknLPLGEALEQHTGLPVYVQHDISAWTLAER--FFGaakGAKNIIQIVIDDDIGAGVITDGQLLHAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 148 GGLAGHIGHTLADPQGPVCGCGRTGCVEAIASGRGIAAAAQgELMGADAKTIFTR-----------AGQGDEQAQQLIHR 216
Cdd:cd24074 155 SSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQAN-QLLEQSPDSMLHGqpisieslcqaALAGDPLAQDIIIQ 233
|
250
....*....|
gi 1610968931 217 SARVLARLIA 226
Cdd:cd24074 234 VGRHLGRILA 243
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
6-243 |
8.59e-09 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 55.42 E-value: 8.59e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 6 IDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALrDALSALVSPLHAHAQQ-----VAIAS-----TGIIRDGSLLAL 75
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTI-EAIATLVDMAEQATGQrgtvgVGIPGsispyTGLVKNANSTWL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 76 NPHnlggllhfPLVKTLEQLTDLPTIAINDAQAAAWAEyqALEGDIT--EMVFVTVSTGV-GGGVVSGGKLLTGPGGLAG 152
Cdd:PRK09557 84 NGQ--------PLDKDLSARLNREVRLANDANCLAVSE--AVDGAAAgkQTVFAVIIGTGcGAGVAINGRVHIGGNGIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 153 HIGHT---------LADPQGPVCGCGRTGCVEAIASGRGIAA---AAQGE-LMGADaktIFTRAGQGDEQAQQLIHRSAR 219
Cdd:PRK09557 154 EWGHNplpwmdedeLRYRNEVPCYCGKQGCIETFISGTGFATdyrRLSGKaLKGSE---IIRLVEEGDPVAELAFRRYED 230
|
250 260
....*....|....*....|....
gi 1610968931 220 VLARLIADIKATTDCQCVVVGGSV 243
Cdd:PRK09557 231 RLAKSLAHVINILDPDVIVLGGGM 254
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
5-259 |
2.66e-08 |
|
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: 53.70 E-value: 2.66e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 5 AIDIGGTKLAAALIGADGQIRDRRELPTP-ASQTPQALRDALSALVSPLHAhaqqVAIASTGIIRdgsllaLNPH--NLG 81
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIERTEFPTTtPEETLQAVIDFFREQEEPIDA----IGIASFGPID------LNPTspTYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 82 GLL--------HFPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEG-DITEMVFVTVSTGVGGGVVSGGKLLTGpgglAG 152
Cdd:cd24067 73 YITttpkpgwrNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAkGLDSLAYITVGTGIGVGLVVNGKPVHG----LL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 153 H--IGHTL------ADPQGPVCGCGRtGCVEAIASGRGIAAaaqgelmgadaktiftRAGQGDEQAQQlIHRS----ARV 220
Cdd:cd24067 149 HpeMGHIRvprhpdDDGFPGVCPFHG-DCLEGLASGPAIAA----------------RWGIPAEELPD-DHPAwdleAYY 210
|
250 260 270
....*....|....*....|....*....|....*....
gi 1610968931 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 |
1.94e-05 |
|
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: 45.29 E-value: 1.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 4 LAIDIGGTKLAAALIGADGQIRDRRELPTPASQTPQALRDALSALVSPLHAHA-QQVAIASTGIIRDGSLLALNPHnlgg 82
Cdd:cd24008 2 LVGDIGGTNARLALADAGDGSGDLLFVRKYPSADFASLEDALAAFLAELGAPRpKAACIAVAGPVDGGRVRLTNLD---- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 83 lLHFPLVKtLEQLTDLPTIA-INDAQAAAWAEYQALEGDITEMvfvtvsTGVGGGVVSGGKLLTGPG-GL---------- 150
Cdd:cd24008 78 -WSIDAAE-LRKALGIGRVRlLNDFEAAAYGLPALGPEDLLVL------YGGGGPLPGGPRAVLGPGtGLgvallvpdgd 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 151 ------AGHIGHTLADPQGPV---------CGCGRTGCVEAIASGRGIAAAAQ-------GELMGADAKTIFTRAGQGDE 208
Cdd:cd24008 150 ggyvvlPSEGGHADFAPVTEEeaelleflrKRFGRSVSYEDVLSGPGLENIYEflakldgAEPPDLTAEEIAEAALAGDP 229
|
250 260
....*....|....*....|
gi 1610968931 209 QAQQLIHRSARVLARLIADI 228
Cdd:cd24008 230 LAREALDLFARILGRFAGNL 249
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
196-266 |
2.06e-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: 2.06e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1610968931 196 AKTIFTRAGQGDEQAQQLIHRSARVLARLIADIKATTDCQcVVVGGSVGLAEGYL-ALVETYLAQEPAAFHV 266
Cdd:COG2971 209 APLVFEAAEAGDPVARAILEEAADELAELARALLERGALP-VVLAGGVAAAQPLLrEALRARLAAGGAEIVP 279
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
7-182 |
2.14e-03 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 38.86 E-value: 2.14e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 7 DIGGTKLAAALIGADGQIRDRRELPTPASQTPQ---ALRDaLSALVSPLHAHAQQVAIASTGI--IRDGSLLALN-PHNL 80
Cdd:PRK13311 6 DMGGTKIELGVFDENLQRIWHKRVPTPREDYPQllqILRD-LTEEADTYCGVQGSVGIGIPGLpnADDGTVFTANvPSAM 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1610968931 81 GGllhfPLVKTLEQLTDLPTIAINDAQAAAWAEYQALEGDITEMVFVTVSTGVGGGVVSG-GKLLTGPGGLAGHIGHTL- 158
Cdd:PRK13311 85 GQ----PLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVnGSIVSGRNHITGEFGHFRl 160
|
170 180 190
....*....|....*....|....*....|....
gi 1610968931 159 ---------AD-PQGPvCGCGRTGCVEAIASGRG 182
Cdd:PRK13311 161 pvdaldilgADiPRVP-CGCGHRGCIENYISGRG 193
|
|
| |
