|
Name |
Accession |
Description |
Interval |
E-value |
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
1-291 |
0e+00 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 506.37 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 1 MRCLALDIGGTKIAAAIV-AQNQVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDYVAVASTGIINKGILTALNPKNL 79
Cdd:PRK05082 1 MTTLAIDIGGTKIAAALVgEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQADRVAVASTGIINDGILTALNPHNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 80 GGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQdKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVA 159
Cdd:PRK05082 81 GGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQAL-PDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTLA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 160 DPNGPVCGCGRVGCVEAIASGRAIEAVSKQWDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVI 239
Cdd:PRK05082 160 DPHGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKATLDCQCVVL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2310524591 240 GGSVGLAEGYLPLVQAYLQQMPEVYRGAIESAQLGQDAGLIGAASWALAQIQ 291
Cdd:PRK05082 240 GGSVGLAEGYLELVQAYLAQEPAIYHVPLLAAHYRHDAGLLGAALWAQGEKL 291
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
4-285 |
1.12e-146 |
|
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: 412.83 E-value: 1.12e-146
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQNQVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDYVAVASTGIINKGILTALNPKNLGGLA 83
Cdd:cd24069 1 LAIDIGGTKIAAALIGNGQIIDRRQIPTPRSGTPEALADALASLLADYQGQFDRVAVASTGIIRDGVLTALNPKNLGGLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 84 YFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVADPNG 163
Cdd:cd24069 81 GFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADPPG 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 164 PVCGCGRVGCVEAIASGRAIEAVSKQWD-DPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVIGGS 242
Cdd:cd24069 161 PVCGCGRRGCVEAIASGTAIAAAASEILgEPVDAKDVFERARSGDEEAARLIDRAARALADLIADLKATLDLDCVVIGGS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2310524591 243 VGLAEGYLPLVQAYLQQMPEVYRGAIESAQLGQDAGLIGAASW 285
Cdd:cd24069 241 VGLAEGFLERVEQYLADEPAIFRVSLEPARLGQDAGLLGAALL 283
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
4-288 |
5.74e-103 |
|
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: 302.34 E-value: 5.74e-103
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQN-QVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFD---YVAVASTGIINKGILTALNPKNL 79
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEgEILARERVPTPTTTTEETLVDAIAFFVDSAQRKFGeliAVGIGSPGLISPKYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 80 GGlAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVA 159
Cdd:pfam00480 81 GW-DNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 160 DPNGPVCGCGRVGCVEAIASGRAIEAVSKQWDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVI 239
Cdd:pfam00480 160 DPNGPKCGCGNHGCLETIASGRALEKRYQQKGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQAIVL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2310524591 240 GGSVGLAEGYLP----LVQAYLQQMPEVYRGAIESAQLGQDAGLIGAASWALA 288
Cdd:pfam00480 240 GGGVSNADGLLEairsLVKKYLNGYLPVPPVIIVAASLGDNAGALGAAALAKQ 292
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
4-287 |
2.40e-80 |
|
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: 245.19 E-value: 2.40e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIV-AQNQVTQRKQIHTPQENVAAAMHQTLAQLLTDY-------AGQFDYVAVASTGIINKGILTALN 75
Cdd:COG1940 8 IGIDIGGTKIKAALVdLDGEVLARERIPTPAGAGPEAVLEAIAELIEELlaeagisRGRILGIGIGVPGPVDPETGVVLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 76 PKNLGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIG 155
Cdd:COG1940 88 APNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGEIG 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 156 HTVADPNGPVCGCGRVGCVEAIASGRAIEAVSKQW--DDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMD 233
Cdd:COG1940 168 HMPVDPDGPLCGCGNRGCLETYASGPALLRRARELggAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLINLLD 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 2310524591 234 IQKVVIGGSVGLA-EGYLPLVQAYLQQ--MPEVYRGA-IESAQLGQDAGLIGAASWAL 287
Cdd:COG1940 248 PEVIVLGGGVSAAgDLLLEPIREALAKyaLPPAREDPrIVPASLGDDAGLLGAAALAL 305
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-284 |
2.86e-61 |
|
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: 196.01 E-value: 2.86e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQNQVTQRKQIHTPQ---ENVAAAMHQTLAQLLTDyAGQFDYVAVASTGIINKGILTALNPKNLG 80
Cdd:cd24065 3 IGLDLGGTKIAAGVVDGGRILSRLVVPTPReggEAVLDALARAVEALQAE-APGVEAVGLGVPGPLDFRRGRVRFAPNIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 81 GLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVAD 160
Cdd:cd24065 82 GLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTTVL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 161 PNGPVCGCGRVGCVEAIASGRAIEA-VSKQWDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVI 239
Cdd:cd24065 162 PGGPMCGCGLVGCLEALASGRALARdASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALDPEVFVL 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 2310524591 240 GGSVGLAEGYL--PLVQAYLQQMPEVYRGAIESAQLGQDAGLIGAAS 284
Cdd:cd24065 242 GGGVAQVGDYYllPVQEAARRYTEGWHAPPLRLAHLGTDAGVIGAAL 288
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
4-285 |
2.46e-60 |
|
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: 193.54 E-value: 2.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQN-QVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDYVAVA--STGIIN--KGILTALNPkN 78
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADgEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEGIGisSAGQVDpkTGEVIYATD-N 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 79 LGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTV 158
Cdd:cd24068 82 LPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 159 ADPNGPVCGCGRVGCVEAIASGRAIEAVSKQW--DDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQK 236
Cdd:cd24068 162 VDPGGRPCCCGGKGCLEQYASGTALVRRVAEAlgEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2310524591 237 VVIGGSVGLA-EGYLPLVQAYLQQ--MPEVYRG-AIESAQLGQDAGLIGAASW 285
Cdd:cd24068 242 IVIGGGISAQgELFLEELREELRKllMPPLLDAtKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
4-284 |
8.53e-52 |
|
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: 172.14 E-value: 8.53e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQNQVTQRKQ-IHTPQENVAAAMHQTLAQLLTDYAGQFDYVAVASTGIINKGIL-----TALNPK 77
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIrQPTPKTGDPGTVSEQVLGLIETLLSKAGKDSIEGIGVSSAGPLdlrkgTIVNSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 78 NLGGlAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHT 157
Cdd:cd24063 83 NIKG-KEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 158 VADPN-GPVCGCGRVGCVEAIASGRAIEAVSKQWDDPCEP----------------KEVFARFRKTDEKATVLVSRSAKA 220
Cdd:cd24063 162 VVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSrtslklrnpggegitaKEVFSAARKGDPLALKIIEKLARY 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524591 221 IANLVADLVIGMDIQKVVIGGSVGLAEGYL--PLVQaYLQQMPEVYRGA-IESAQLGQDAGLIGAAS 284
Cdd:cd24063 242 NGRGIANVINAYDPELIVIGGSVFNNNKDIldPLIE-YLEKNPAISKGPeIVLSELGDDVGLIGALA 307
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
4-284 |
5.61e-45 |
|
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: 154.19 E-value: 5.61e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQN-QVTQRKQIHTPQENVAAAMHQTLAQLLTDYA--GQFDYVAVASTGIINK--GILTaLNPkN 78
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENgDILKKKTIDTKVENGKEDVINRIAETVNELIeeMELLGIGIGSPGSIDRenGIVR-FSP-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 79 LGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTV 158
Cdd:cd24064 80 FPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 159 ADPNGPVCGCGRVGCVEAIASGRAIEAVSKQW-----------DDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVAD 227
Cdd:cd24064 160 VEPNGPICGCGNRGCVEAFASATAIIRYARESrkrypdslageSEKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310524591 228 LVIGMDIQKVVIGGSVGLAEGYL--PLVQAYLQQMPEVYRG--AIESAQLGQDAGLIGAAS 284
Cdd:cd24064 240 FVHIFNPEIIIIGGGISRAGSFLldPIREKTKKYVMLSFQDtySIELSNLVEDAGILGAAS 300
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-285 |
2.41e-44 |
|
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: 150.69 E-value: 2.41e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIV-AQNQVTQRKQIHTP----QENVAAAMHQTLAQLL--TDYAGQFDYVAVASTGIIN--KGILtaL 74
Cdd:cd23763 1 IGIDIGGTKIRAALVdLDGEILARERVPTPaeegPEAVLDRIAELIEELLaeAGVRERILGIGIGVPGPVDpeTGIV--L 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 75 NPKNLGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHI 154
Cdd:cd23763 79 FAPNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 155 GHtvadpngpvcgcgrvgcveaiasgraieavskqwddpcepkevfarfrktdekaTVLVSRSAKAIANLVADLVIGMDI 234
Cdd:cd23763 159 GH------------------------------------------------------ITVLEEAARYLGIGLANLINLLNP 184
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2310524591 235 QKVVIGGSVGLAEGYL--PLVQAYLQQMPEVYRGA--IESAQLGQDAGLIGAASW 285
Cdd:cd23763 185 ELIVLGGGVAEAGDLLlePIREAVRRRALPPLRRRvrIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
4-287 |
5.03e-44 |
|
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: 151.74 E-value: 5.03e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIV-AQNQVTQRKQIHTPQEnvAAAMHQTLAQLLTDYAGQFDYVA--VASTGIINKGILTALNPKNLG 80
Cdd:cd24061 2 IGVDIGGTKIAAGVVdEEGEILATERVPTPPT--ADGIVDAIVEAVEELREGHDVSAvgVAAAGFVDADRATVLFAPNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 81 gLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVAD 160
Cdd:cd24061 80 -WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRVV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 161 PNGPVCGCGRVGCVEAIASGRAI--EAVSKQWDDPCEPKEVFARF--------------RKTDEKATVLVSRSAKAIANL 224
Cdd:cd24061 159 PDGLLCGCGSRGCWEQYASGRALvrYAKEAANATPEGAAVLLADGsvdgitgkhiseaaRAGDPVALDALRELARWLGAG 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2310524591 225 VADLVIGMDIQKVVIGGSVGLAEGYL--PLVQAYLQQMPEV-YRGA--IESAQLGQDAGLIGAASWAL 287
Cdd:cd24061 239 LASLAALLDPELFVIGGGVSDAGDLLldPIREAFERWLPGRgWRPIprLRTAQLGNDAGLIGAADLAR 306
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
4-289 |
1.41e-42 |
|
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: 148.10 E-value: 1.41e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIV-AQNQVTQRKQIHTPQENVAAAMHQTLAQLLTD---YAGQFDY----VAVASTGIINKGILTALN 75
Cdd:cd24076 4 IGVELGVDYITVVVTdLAGEVLWRREVPLPASDDPDEVLAQLAALIREalaAAPDSPLgilgIGVGVPGLVDSEDGVVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 76 PKNLGgLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIG 155
Cdd:cd24076 84 APNLG-WRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 156 HTVADPNGPVCGCGRVGCVEAIASGRAIEAVSKQ---WDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGM 232
Cdd:cd24076 163 HMTVDPDGPPCSCGNRGCWETYASERALLRAAGRlgaGGEPLSLAELVEAARAGDPAALAALEEVGEYLGIGLANLVNTF 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2310524591 233 DIQKVVIGGSVGLAEGYL-PLVQAYLQQ--MPEVYRGA-IESAQLGQDAGLIGAASWALAQ 289
Cdd:cd24076 243 NPELVVLGGALAPLGPWLlPPLRAEVARraLPAPARDVrIVVSRLGEDAAALGAAALAIDH 303
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
4-290 |
7.56e-41 |
|
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: 143.50 E-value: 7.56e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIV-AQNQVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDY------VAVASTGIIN--KGILtaL 74
Cdd:cd24059 4 IGVEIGRDLLSAVLCdLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENIkskilgIGIGAPGPLDveKGII--L 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 75 NPKNLGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHI 154
Cdd:cd24059 82 NPPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 155 GHTVADPNGPVCGCGRVGCVEAIASGRAIE--AVSKQWDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGM 232
Cdd:cd24059 162 GHTSIDINGPRCSCGNRGCLELYASIPAIEkkARSALGSGRSFQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLINLL 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524591 233 DIQKVVIGG-SVGLAEGYLPLVQAYLQQ---MPEVYRGAIESAQLGQDAGLIGAASWALAQI 290
Cdd:cd24059 242 NPEAIIIGGeLIYLGERYLEPIEKEVNSrlfGRNAREVRILKSSLGEDAPLLGAAALVLNKY 303
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
7-284 |
1.14e-40 |
|
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: 143.20 E-value: 1.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 7 DIGGTKIAAAIVAQN-QVTQRKQIHTPQENVAAAMHQTLA----QLLTDY---AGQFDYVAVASTGIINKGILTALNPKN 78
Cdd:cd24062 6 DVGGTTIKMAFLTQEgEIVQKWEIPTNKLEGGENIITDIAesiqQLLEELgysKEDLIGIGVGVPGPVDVETGTVEVAVN 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 79 LGgLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGH-T 157
Cdd:cd24062 86 LG-WKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEIGHiT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 158 VADPNGPVCGCGRVGCVEAIASGRAI-----EAVSKQWDDPCE----------PKEVFARFRKTDEKATVLVSRSAKAIA 222
Cdd:cd24062 165 VNPEGGAPCNCGKTGCLETVASATGIvriarEELEEGKGSSALrilalggeltAKDVFEAAKAGDELALAVVDTVARYLG 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524591 223 NLVADLVIGMDIQKVVIGGSVGLA-EGYLPLVQAYLQQM--PEVYRGA-IESAQLGQDAGLIGAAS 284
Cdd:cd24062 245 LALANLANTLNPEKIVIGGGVSAAgEFLLSPVKEYFDRFtfPRVRQDTeIVLATLGNDAGVIGAAW 310
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
3-285 |
1.29e-40 |
|
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: 142.32 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 3 CLALDIGGTKIAAAIV-AQNQVTQRKQIHTPQeNVAAAMHQTLAQLLTDYAGQFDYVAVASTGIIN--KGILT--ALNPK 77
Cdd:cd24152 2 YLVFDIGGTFIKYALVdENGNIIKKGKIPTPK-DSLEEFLDYIKKIIKRYDEEIDGIAISAPGVIDpeTGIIYggGALPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 78 NLGglayFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHT 157
Cdd:cd24152 81 LKG----FNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 158 VADPNGPV-CGCGRVGCVEAIASGRAIEAVSKQWDDpcepKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQK 236
Cdd:cd24152 157 LTDDDDKDlLFFSGLASMFGLVKRYNKAKGLEPLDG----EEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEV 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 2310524591 237 VVIGGSVGLAEGYLPLVQAYLQQMPEVYRG-----AIESAQLGQDAGLIGAASW 285
Cdd:cd24152 233 IVIGGGISEQPLFIEDLKKEVNEILANRPGsipkpEIKACKFGNDANLLGALYN 286
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-286 |
1.38e-36 |
|
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: 132.72 E-value: 1.38e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQNQVTQRKQiHTPQENVAAAMHQTLAQLLTDYAGQFD-------YVAVASTGIINKGILTALNP 76
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKW-KVPTDTTPETIVDAIASAVDSFIQHIAkvgheivAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 77 KNLGGLAYfPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGH 156
Cdd:TIGR00744 80 VNLDWKQE-PLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 157 TVADPNGPV-CGCGRVGCVEAIASGRAIEAVSKQW---------------DDPCEPKEVFARFRKTDEKATVLVSRSAKA 220
Cdd:TIGR00744 159 IRMVPDGRLlCNCGKQGCIETYASATGLVRYAKRAnakperaevllalgdGDGISAKHVFVAARQGDPVAVDSYREVARW 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 221 IANLVADLVIGMDIQKVVIGGSVGLAEGYL--PLVQAY--LQQMPEVYRGAIESAQLGQDAGLIGAASWA 286
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGGGLSDAGDLLldPIRKSYkrWLFGGARQVADIIAAQLGNDAGLVGAADLA 308
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
5-283 |
1.48e-36 |
|
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: 131.97 E-value: 1.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 5 ALDIGGTKIAAAIV-AQNQVTQRKQIHTPQENVAAAMhQTLAQLLTDYAGQFDY---VAVASTGIINK--GILTAlnpKN 78
Cdd:cd24057 4 GFDIGGTKIEFAVFdEALQLVWTKRVPTPTDDYAAFL-AAIAELVAEADARFGVkgpVGIGIPGVIDPedGTLIT---AN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 79 LGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHT- 157
Cdd:cd24057 80 IPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 158 -VAD-----PNGPV--CGCGRVGCVEAIASGRAIEAVSKQW-DDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADL 228
Cdd:cd24057 160 lPADalllgYDLPVlrCGCGQTGCLETYLSGRGLERLYAHLyGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLANI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310524591 229 VIGMDIQKVVIGGsvGLAEgylplVQAYLQQMPEVYRGA---------IESAQLGQDAGLIGAA 283
Cdd:cd24057 240 LTALDPDVVVLGG--GLSN-----FPALIAELPAALPAHllsgartprIVPARHGDAGGVRGAA 296
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
4-286 |
1.39e-31 |
|
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: 118.81 E-value: 1.39e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQNQVTQRKQIhTPQENVAAAMH--QTLAQLLTDYAGQFDYV--AVAST--GIINKGILTALNPK 77
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLDFEK-VPSKDLLRAGDpvEVLADLIREYIEEAGLKpaAIVIGvpGTVDKDRRTVISTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 78 NLGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHT 157
Cdd:cd24070 83 NIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 158 VADPNGPVCGCGRVGCVEAIASGRAIEAVSKQWDDPCEPKEVFARfRKTDEKATVLVSRSAKAIANLVADLvigmDIQKV 237
Cdd:cd24070 163 PVYGNGKPCGCGNTGCLETYASGRALEEIAEEHYPDTPILDIFVD-HGDEPELDEFVEDLALAIATEINIL----DPDAV 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 2310524591 238 VIGGSVGLAEGYlP---LVQAYLQQMPEVYRGA---IESAQLGQDAGLIGAASWA 286
Cdd:cd24070 238 ILGGGVIDMKGF-PretLEEYIRKHLRKPYPADnlkIIYAELGPEAGVIGAAIYA 291
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
86-290 |
9.45e-30 |
|
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: 114.19 E-value: 9.45e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 86 PLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVADPNGPV 165
Cdd:cd24073 92 PLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTTVDPDGPP 171
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 166 CGCGRVGCVEAIASGRAIEAVSKQ---WDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVIGGS 242
Cdd:cd24073 172 CRCGKRGCLEAYASDPAILRQAREaglRGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELIIISGE 251
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 2310524591 243 VGLAEGYL--PLVQAYLQQMPEVYRGA--IESAQLGQDAGLIGAASWALAQI 290
Cdd:cd24073 252 GVRAGDLLfePMREALRAHVFPGLASDleLVIHPWGDEAWARGAAALALQEF 303
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
58-290 |
5.78e-29 |
|
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: 112.38 E-value: 5.78e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 58 VAVASTGIIN--KGIL---TALNPKNLgglayfPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTG 132
Cdd:cd24071 65 IGIAVSGLVDskKGIVirsTILGWENV------ELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 133 VGGGLILNRRLLTEPNGIAGHIGHTVADPNGPVCGCGRVGCVEAIASGRAIEAVSKQWDD-----------PCEPKEVFA 201
Cdd:cd24071 139 IGSSLVIDGKLYTGNFGGAGEIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTEsyplsllkeleDFEIEKVRE 218
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 202 RFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVIGGSvGLAEG--YLPLVQAYLQQ-----MPEvyRGAIESAQLG 274
Cdd:cd24071 219 AAEEGDSVATELFKKAGEYLGIGIKNLINIFNPEAIIIGGE-GLEFKdyFLPKIIEIAKEnffgkAGR--NVIILVDSLG 295
|
250
....*....|....*.
gi 2310524591 275 QDAGLIGAASWALAQI 290
Cdd:cd24071 296 EDAWVLGAALLVIDHL 311
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
5-283 |
1.10e-28 |
|
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: 111.10 E-value: 1.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 5 ALDIGGTKIAAAI-VAQNQVTQRKQI--HTPQENVAAamhqtLAQLLTDYAGQFDYVAVASTG--IINK-----GILTAl 74
Cdd:cd24067 3 GIEAGGTKFVCAVgTGDGNIIERTEFptTTPEETLQA-----VIDFFREQEEPIDAIGIASFGpiDLNPtsptyGYITT- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 75 NPKNlgGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLL-----TEpng 149
Cdd:cd24067 77 TPKP--GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVhgllhPE--- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 150 iAGHIG---HTVADPNGPVCGCGRvGCVEAIASGRAIEAvskQWDdpCEPKEVfarfrKTDEKATVLVsrsAKAIANLVA 226
Cdd:cd24067 152 -MGHIRvprHPDDDGFPGVCPFHG-DCLEGLASGPAIAA---RWG--IPAEEL-----PDDHPAWDLE---AYYLAQACA 216
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2310524591 227 DLVIGMDIQKVVIGGSVGLAEGYLPLVQAYLQQM----PEVYRGA------IESAQLGQDAGLIGAA 283
Cdd:cd24067 217 NLTLTLSPERIVLGGGVMQRPGLFPRIREKFRKLlngyLEVPRLLpdideyIVPPALGNDAGILGAL 283
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
4-283 |
4.24e-27 |
|
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: 106.90 E-value: 4.24e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIV-AQNQVTQRKQIHTPQENVAAAMH--QTLAQLLTDYAGQFDYVAVASTGIINK--GIL-----TA 73
Cdd:cd24066 2 IGIDLGGTKIEGIALdRAGRELLRRRVPTPRGDYEATLDaiADLVEEAEEELGAPATVGIGTPGSISPrtGLVknansTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 74 LNPKnlgglayfPLKESLSKHTSKPVYLLNDAQAATYAEYQL---QDKNNIqnFAFItVSTGVGGGLILNRRLLTEPNGI 150
Cdd:cd24066 82 LNGK--------PLKADLEARLGRPVRIENDANCFALSEATDgagAGAGVV--FGVI-LGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 151 AGHIGHTVADP------NGPVCGCGRVGCVEAIASGRAIEA----VSKQWDDpcePKEVFARFRKTDEKAT----VLVSR 216
Cdd:cd24066 151 AGEWGHNPLPWpdedelPGPPCYCGKRGCVETFLSGPALERdyarLTGKTLS---AEEIVALARAGDAAAVatldRFLDR 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2310524591 217 SAKAIANLVADLvigmDIQKVVIGGSVG-LAEGYLPLVQAYLQQmpeVYRGAIES----AQLGQDAGLIGAA 283
Cdd:cd24066 228 LGRALANVINIL----DPDVIVLGGGLSnIDELYTEGPAALARY---VFSDEVETpivkNKHGDSSGVRGAA 292
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
27-282 |
1.94e-24 |
|
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: 100.13 E-value: 1.94e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 27 KQIHTPQENVAAAMHQTLAQLLTDYAGQF-----------DYVAVASTGIIN--KGILTaLNPKNlgGLAYFPLKESLSK 93
Cdd:cd24075 23 ELLAEHTVPLTALNQEALLSQLIEEIAQFlkshrrktqrlIAISITLPGLINpkTGVVH-YMPHI--QVKSWPIVEELEQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 94 HTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVADPNGPVCGCGRVGC 173
Cdd:cd24075 100 RFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGHIQIEPLGERCHCGNFGC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 174 VEAIASGRAIE----------AVSKQWDDPCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVIGGSV 243
Cdd:cd24075 180 LETVASNAAIEqrvkkllkqgYASQLTLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGEI 259
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 2310524591 244 GLAEGYL-PLVQAYLQQ--MPEVYRGA-IESAQLGQDAgLIGA 282
Cdd:cd24075 260 TQADKVLlPVIKKCIQSqaLPDFRQELkIVASQLDHNS-AIGA 301
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
85-281 |
2.03e-24 |
|
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: 100.18 E-value: 2.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 85 FPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVADPNGP 164
Cdd:cd24072 89 IEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGHTKVNPDGA 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 165 VCGCGRVGCVEAIASGRAIEAVSKQW--------DDPCEPKEVFAR-FRKTDEKATVLVSRSAKAIANLVADLVIGMDIQ 235
Cdd:cd24072 169 RCDCGRRGCLETVASNSALKRNARVTlklgpvsaDPEKLTMEQLIEaLEEGEPIATQIFDRAANAIGRSLANILNLLNPE 248
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 2310524591 236 KVVIGGSvglaegylpLVQAYLQQMPEVYRgAIESAQLGQDAGLIG 281
Cdd:cd24072 249 QVLLYGR---------GCRAGDLLLPAIRR-AIAENPFSQHATQIG 284
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
4-290 |
3.10e-24 |
|
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: 99.15 E-value: 3.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIG-------GTKIAAAIVAQNQVtqrKQIHTPQENVAAAMHQTLaQLLTDYAGQFDY----VAVASTGIINKGILT 72
Cdd:cd24077 4 IGIDLGynyislmLTYLDGEIISSKQI---KLLDISFENILEILKSII-QELISQAPKTPYglvgIGIGIHGIVDENEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 73 ALNPKNLGGLayfPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDknNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAG 152
Cdd:cd24077 80 FTPYYDLEDI---DLKEKLEEKFNVPVYLENEANLSALAERTFSE--DYDNLISISIHSGIGAGIIINNQLYRGYNGFAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 153 HIGHTVADPNGPVCGCGRVGCVEAIASGRAIE---AVSKQWDDpCEPKEVFARFRKTDEKATVLVSRSAKAIANLVADLV 229
Cdd:cd24077 155 EIGHMIIVPNGKPCPCGNKGCLEQYASEKALLkelSEKKGLET-LTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNII 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2310524591 230 IGMDIQKVVIGGSVgLAE--GYLPLVQAYLQQMPEVYRgAIESAQLGQDAGLIGAASWALAQI 290
Cdd:cd24077 234 NTFNPEIIIINSSL-INEipELLEKIKEQLSSSFNKYV-EILISTLGKNATLLGGAAVAIKNF 294
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
4-284 |
9.36e-24 |
|
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: 98.26 E-value: 9.36e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVA-QNQVTQRKQIHTPQEN-----VAAAMHQTLAQLLTDYAGQFDYVAVASTGIINKGILTALNP- 76
Cdd:cd24060 3 LAVDLGGTNLRVAIVSmKGEIVKKYTQPNPKTYeeridLILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLHSt 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 77 KNLGGLAYFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGH 156
Cdd:cd24060 83 KLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 157 TVADPNGPVCGCGRVGCVEAIASGRAIEAVSKQWDDPCE----------PKEVFARF-----RKTDEKATVLVSRSAKAI 221
Cdd:cd24060 163 IVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLllvegmsvtnDEEVTAKHliqaaKLGNAKAQKILRTAGTAL 242
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2310524591 222 ANLVADLVIGMDIQKVVIGGSvgLAEGYLPLVQAYLQQ--MPEVYRGAIESAQLgQDAGLIGAAS 284
Cdd:cd24060 243 GLGIVNILHTLNPSLVILSGV--LASHYENIVKDVIAQraLPSVQNVDVVVSDL-VDPALLGAAS 304
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
6-283 |
2.43e-21 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 91.59 E-value: 2.43e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 6 LDIGGTKIA-AAIVAQNQVTQRKQIHTPQENVAAAMhQTLAQLLTDYAGQFD---YVAVASTGIINK--GILTALNPKNL 79
Cdd:PRK13310 5 FDIGGTKIElGVFNEKLELQWEERVPTPRDSYDAFL-DAVCELVAEADQRFGckgSVGIGIPGMPETedGTLYAANVPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 80 GGLayfPLKESLSKHTSKPVYLLNDAQAatYAEYQLQDKNNIQnfaFITV-----STGVGGGLILNRRLLTEPNGIAGHI 154
Cdd:PRK13310 84 SGK---PLRADLSARLGRDVRLDNDANC--FALSEAWDDEFTQ---YPLVmglilGTGVGGGLVFNGKPISGRSYITGEF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 155 GHT--------VADPNGPV--CGCGRVGCVEAIASGRAIEAVSKQ-WDDPCEPKEVFARFRKTDEKATVLVSRSAKAIAN 223
Cdd:PRK13310 156 GHMrlpvdaltLLGWDAPLrrCGCGQKGCIENYLSGRGFEWLYQHyYGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAI 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2310524591 224 LVADLVIGMDIQKVVIGGSVG----LAEGYLPLVQAYLQQMPEVYRgaIESAQLGQDAGLIGAA 283
Cdd:PRK13310 236 CLGNILTIVDPHLVVLGGGLSnfdaIYEQLPKRLPRHLLPVARVPR--IEKARHGDAGGVRGAA 297
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
41-283 |
1.19e-20 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 89.68 E-value: 1.19e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 41 HQTLAQLLTDYAGQFDYVAVASTGIINKgiLTALNPKNLgglayfPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNN 120
Cdd:cd24074 56 HQKKLERLTAIAITLPGIIDPESGIVHR--LPFYDIKNL------PLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKG 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 121 IQNFAFITVSTGVGGGLILNRRLLTEPNGIAGHIGHTVADPNGPVCGCGRVGCVEAIASGRAIEA----VSKQWDDPCEP 196
Cdd:cd24074 128 AKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEqanqLLEQSPDSMLH 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 197 KEV--FARF----RKTDEKATVLVSRSAKAIANLVADLVIGMDIQKVVIGGSVG-LAEGYLPLVQAYL-QQMPEVYRG-- 266
Cdd:cd24074 208 GQPisIESLcqaaLAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNnAAEILFPALSQSIrQQSLPAYSQhl 287
|
250
....*....|....*..
gi 2310524591 267 AIESAQLGQDAGLIGAA 283
Cdd:cd24074 288 QIESTKFYNDGTMPGAA 304
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
3-286 |
3.63e-18 |
|
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: 81.46 E-value: 3.63e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 3 CLALDIGGTKIAAAIVAQNQ---VTQRKQIHTPQENVAAAMHQTLAQLLTDYAGqFDYVAVASTGIINKGI-LTALN--P 76
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDTDTgelLSERIRIPTPQPATPEAVADVVAELVAHFPW-FGPVGVGFPGVVRRGVvRTAANldK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 77 KNLGglayFPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFA-FITVSTGVGGGLILNRRLLtePNGIAGHig 155
Cdd:cd24058 80 SWIG----FDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVlVLTLGTGIGSALFVDGHLV--PNTELGH-- 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 156 HTVadpngpvcgcgRVGCVEAIASG--RAIEAVS-KQWDdpcepkevfARFRKtdekatVLVsrsakAIANLVA-DLVIg 231
Cdd:cd24058 152 LEI-----------RGKDAEERASLgvRAREDLGwKRWA---------KRVNK------YLQ-----YLERLFNpDLFI- 199
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 2310524591 232 mdiqkvvIGGSVG-LAEGYLPLVQAylqQMPEVyrgaieSAQLGQDAGLIGAASWA 286
Cdd:cd24058 200 -------IGGGNSkKADKFLPLLDV---KTPVV------PAVLRNDAGIVGAALLA 239
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-292 |
2.08e-17 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 80.41 E-value: 2.08e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVAQNQVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDY----VAVASTGIINKGILTALNPKNL 79
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIDEYLRRFNArchgIVMGFPALVSKDRRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 80 --GGLAYFPLKESLSKHTSKPVYLLNDAQAATYaeYQLQDKNNIQNFAF-ITVSTGVGGGLILNRRLLTEPNGIAGHIGH 156
Cdd:PRK09698 87 plTALDLYDLADKLENTLNCPVFFSRDVNLQLL--WDVKENNLTQQLVLgAYLGTGMGFAVWMNGAPWTGAHGVAGELGH 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 157 TVADPNGPVCGCGRVGCVEAIASGRAIEAV--SKQWDDPCEpkEVFARFrkTDEKAT-VLVSRSAKAIA---NLvadlvi 230
Cdd:PRK09698 165 IPLGDMTQHCGCGNPGCLETNCSGMALRRWyeQQPRDYPLS--DLFVHA--GDHPFIqSLLENLARAIAtsiNL------ 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 231 gMDIQKVVIGGSVGLAEGYlP------LVQAYLQQ-MP-EVYRgaIESAQLGQDAGLIGAASWALAQIQA 292
Cdd:PRK09698 235 -FDPDAIILGGGVMDMPAF-PretliaMIQKYLRKpLPyEVVR--FIYASSSDFNGAQGAAILAHQRFLP 300
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
5-229 |
6.83e-16 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 75.45 E-value: 6.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 5 ALDIGGTKIAAAIVAQN-QVTQRKQIHTPQENvaaamHQTLAQLLTD-------YAGQFDYVAVASTGIINKG---ILTA 73
Cdd:PRK13311 4 GFDMGGTKIELGVFDENlQRIWHKRVPTPRED-----YPQLLQILRDlteeadtYCGVQGSVGIGIPGLPNADdgtVFTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 74 LNPKNLGGlayfPLKESLSKHTSKPVYLLNDAQAATYAEYQLQDKNNIQNFAFITVSTGVGGGLILNRRLLTEPNGIAGH 153
Cdd:PRK13311 79 NVPSAMGQ----PLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 154 IGH----------TVAD-PNGPvCGCGRVGCVEAIASGRAIEAVSKQWDDPCEP-KEVFARFRKTDEKATVLVSRSAKAI 221
Cdd:PRK13311 155 FGHfrlpvdaldiLGADiPRVP-CGCGHRGCIENYISGRGFEWMYSHFYQHTLPaTDIIAHYAAGEPKAVAHVERFMDVL 233
|
....*...
gi 2310524591 222 ANLVADLV 229
Cdd:PRK13311 234 AVCLGNLL 241
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
1-259 |
4.57e-10 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 59.27 E-value: 4.57e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 1 MRcLALDIGGTKI-AAAIVAQNQVTQRKQIHTPQENVAAAMhQTLAQLLTD---YAGQFDYVAVASTGIIN--KGILTAL 74
Cdd:PRK09557 1 MR-IGIDLGGTKIeVIALDDAGEELFRKRLPTPRDDYQQTI-EAIATLVDMaeqATGQRGTVGVGIPGSISpyTGLVKNA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 75 NPKNLGGlayFPLKESLSKHTSKPVYLLNDAQAATYAEY---QLQDKNNIqnFAFItVSTGVGGGLILNRRLLTEPNGIA 151
Cdd:PRK09557 79 NSTWLNG---QPLDKDLSARLNREVRLANDANCLAVSEAvdgAAAGKQTV--FAVI-IGTGCGAGVAINGRVHIGGNGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 152 GHIGHT---------VADPNGPVCGCGRVGCVEAIASG----RAIEAVSKQwddPCEPKEVFARFRKTDEKATVLVSRSA 218
Cdd:PRK09557 153 GEWGHNplpwmdedeLRYRNEVPCYCGKQGCIETFISGtgfaTDYRRLSGK---ALKGSEIIRLVEEGDPVAELAFRRYE 229
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 2310524591 219 KAIANLVADLVIGMDIQKVVIGGSVGLAEGYLPLVQAYLQQ 259
Cdd:PRK09557 230 DRLAKSLAHVINILDPDVIVLGGGMSNVDRLYPTLPALLKQ 270
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
4-285 |
3.73e-06 |
|
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. Glucokinases are mainly found in invertebrates and microorganisms and highly specific for glucose. Glucokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466858 [Multi-domain] Cd Length: 313 Bit Score: 47.60 E-value: 3.73e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 4 LALDIGGTKIAAAIVaqnQVTQRKQIHTPQENVAAAMHQTLAQLLTDYAGQFDY-------VAVASTGIINKGILTalnp 76
Cdd:cd24008 2 LVGDIGGTNARLALA---DAGDGSGDLLFVRKYPSADFASLEDALAAFLAELGAprpkaacIAVAGPVDGGRVRLT---- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 77 kNLGGLAYFplkESLSKHTS-KPVYLLNDAQAATYAEYQLQDKNNIQ-----------NFAFITVSTGVG-GGLILNRRL 143
Cdd:cd24008 75 -NLDWSIDA---AELRKALGiGRVRLLNDFEAAAYGLPALGPEDLLVlyggggplpggPRAVLGPGTGLGvALLVPDGDG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 144 LTEPngIAGHIGHTvadPNGPVCG------------CGRVGCVEAIASGRAIEAV-------SKQWDDPCEPKEVFARFR 204
Cdd:cd24008 151 GYVV--LPSEGGHA---DFAPVTEeeaelleflrkrFGRSVSYEDVLSGPGLENIyeflaklDGAEPPDLTAEEIAEAAL 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2310524591 205 KTDEKATVLVSRSAKAIANLVADLVIG-MDIQKVVIGGSV-----------GLAEGYL--PLVQAYLQQMPeVYRgaies 270
Cdd:cd24008 226 AGDPLAREALDLFARILGRFAGNLALSfLATGGVYLAGGIapknldlldssAFREAFLdkGRMSDLLEDIP-VYL----- 299
|
330
....*....|....*
gi 2310524591 271 aQLGQDAGLIGAASW 285
Cdd:cd24008 300 -VTNEDLGLLGAAAY 313
|
|
| |
