|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
79-364 |
2.90e-58 |
|
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: 192.03 E-value: 2.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 79 VPASRYALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDA 158
Cdd:COG1940 1 NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 159 TAGWVVDPPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVS 238
Cdd:COG1940 81 ETGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 239 GNAGEVG-------GLGAGCSTRILVEEAVALGVLGTEYAVTNPADAQRGvERLAAMTAEGDARADGILERLAIRIGRGV 311
Cdd:COG1940 161 GNAGEIGhmpvdpdGPLCGCGNRGCLETYASGPALLRRARELGGAEKLTA-EELFAAARAGDPLALEVLDEAARYLGIGL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2770182087 312 CAAATLLDIDTIVFGGPTWHlLADRLLPTIEPMVAGSPFVKATHPTAVVSTTL 364
Cdd:COG1940 240 ANLINLLDPEVIVLGGGVSA-AGDLLLEPIREALAKYALPPAREDPRIVPASL 291
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
86-364 |
1.37e-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: 154.16 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 86 LGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGAdRDRILGLGIAAPGPIDATAGWVVD 165
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGV-RERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 166 PPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG 245
Cdd:cd23763 80 APNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 246 GlgagcstrilveeavalgvlgteyavtnpadaqrgverlaaMTaegdaradgILERLAIRIGRGVCAAATLLDIDTIVF 325
Cdd:cd23763 160 H-----------------------------------------IT---------VLEEAARYLGIGLANLINLLNPELIVL 189
|
250 260 270
....*....|....*....|....*....|....*....
gi 2770182087 326 GGPTWHlLADRLLPTIEPMVAGSPFVKATHPTAVVSTTL 364
Cdd:cd23763 190 GGGVAE-AGDLLLEPIREAVRRRALPPLRRRVRIVPSEL 227
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
95-346 |
1.45e-27 |
|
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.
Pssm-ID: 395384 [Multi-domain] Cd Length: 292 Bit Score: 110.12 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 95 ITCVLVDLLGTVVAQRSRATPrggdTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGWVVDPPELhGWGR 174
Cdd:pfam00480 10 IAAALFDEEGEILARERVPTP----TTTTEETLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITNTPNI-GWDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 175 YPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------GL 247
Cdd:pfam00480 85 FDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGhiqldpnGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 248 GAGCSTRILVEeavalgvlgtEYAvTNPADAQRGVERLAAMTA--------EGDARADGILERLAIRIGRGVCAAATLLD 319
Cdd:pfam00480 165 KCGCGNHGCLE----------TIA-SGRALEKRYQQKGEDLEGkdiivlaeQGDEVAEEAVERLARYLAKAIANLINLFD 233
|
250 260
....*....|....*....|....*..
gi 2770182087 320 IDTIVFGGPTWHllADRLLPTIEPMVA 346
Cdd:pfam00480 234 PQAIVLGGGVSN--ADGLLEAIRSLVK 258
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
95-327 |
5.75e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 71.87 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 95 ITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAEsgADRDRILGLGIAAPGPIDAtagwvVDPPELHGWGR 174
Cdd:PRK05082 13 IAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQ--ADRVAVASTGIINDGILTA-----LNPHNLGGLLH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 175 YPLRDRLSEATGFTAVLDKDVTAAVVAErWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------GL 247
Cdd:PRK05082 86 FPLVQTLEQLTDLPTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGhtladphGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 248 GAGCSTRILVE--------EAVALGVLgteyavtNPADAQRGVERLAAmtaeGDARADGILERLAIRIGRGVCAAATLLD 319
Cdd:PRK05082 165 VCGCGRRGCVEaiasgraiAAAAQGWL-------AGCDAKTIFERAGQ----GDEQAQALINRSAQAIARLIADLKATLD 233
|
....*...
gi 2770182087 320 IDTIVFGG 327
Cdd:PRK05082 234 CQCVVLGG 241
|
|
| HTH_24 |
pfam13412 |
Winged helix-turn-helix DNA-binding; |
19-58 |
3.93e-05 |
|
Winged helix-turn-helix DNA-binding;
Pssm-ID: 404317 [Multi-domain] Cd Length: 45 Bit Score: 40.49 E-value: 3.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2770182087 19 VLDAIRRHPtGLSRVELARATGLSSQTVSNITRRLLDQGV 58
Cdd:pfam13412 6 ILNLLQENP-RISQRELAERLGLSPSTVNRRLKRLEEEGV 44
|
|
| HTH_MARR |
smart00347 |
helix_turn_helix multiple antibiotic resistance protein; |
19-61 |
5.93e-05 |
|
helix_turn_helix multiple antibiotic resistance protein;
Pssm-ID: 197670 [Multi-domain] Cd Length: 101 Bit Score: 41.81 E-value: 5.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2770182087 19 VLDAIRRHPtGLSRVELARATGLSSQTVSNITRRLLDQG-VARE 61
Cdd:smart00347 15 VLRILYEEG-PLSVSELAKRLGVSPSTVTRVLDRLEKKGlVRRE 57
|
|
| COG2512 |
COG2512 |
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ... |
15-57 |
5.50e-04 |
|
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only];
Pssm-ID: 442002 [Multi-domain] Cd Length: 80 Bit Score: 38.36 E-value: 5.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2770182087 15 NESVVLDAIRRHPTGLSRVELARATGLSSQTVSNITRRLLDQG 57
Cdd:COG2512 16 DERRVLELLRENGGRMTQSEIVKETGWSKSKVSRLLSRLEERG 58
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
79-364 |
2.90e-58 |
|
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: 192.03 E-value: 2.90e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 79 VPASRYALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDA 158
Cdd:COG1940 1 NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 159 TAGWVVDPPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVS 238
Cdd:COG1940 81 ETGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 239 GNAGEVG-------GLGAGCSTRILVEEAVALGVLGTEYAVTNPADAQRGvERLAAMTAEGDARADGILERLAIRIGRGV 311
Cdd:COG1940 161 GNAGEIGhmpvdpdGPLCGCGNRGCLETYASGPALLRRARELGGAEKLTA-EELFAAARAGDPLALEVLDEAARYLGIGL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2770182087 312 CAAATLLDIDTIVFGGPTWHlLADRLLPTIEPMVAGSPFVKATHPTAVVSTTL 364
Cdd:COG1940 240 ANLINLLDPEVIVLGGGVSA-AGDLLLEPIREALAKYALPPAREDPRIVPASL 291
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
86-364 |
1.37e-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: 154.16 E-value: 1.37e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 86 LGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGAdRDRILGLGIAAPGPIDATAGWVVD 165
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGV-RERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 166 PPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG 245
Cdd:cd23763 80 APNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 246 GlgagcstrilveeavalgvlgteyavtnpadaqrgverlaaMTaegdaradgILERLAIRIGRGVCAAATLLDIDTIVF 325
Cdd:cd23763 160 H-----------------------------------------IT---------VLEEAARYLGIGLANLINLLNPELIVL 189
|
250 260 270
....*....|....*....|....*....|....*....
gi 2770182087 326 GGPTWHlLADRLLPTIEPMVAGSPFVKATHPTAVVSTTL 364
Cdd:cd23763 190 GGGVAE-AGDLLLEPIREAVRRRALPPLRRRVRIVPSEL 227
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
83-342 |
8.93e-42 |
|
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: 148.85 E-value: 8.93e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 83 RYALGVHLDPAVITCVLVDLLGTVVAQRSRATPrGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGW 162
Cdd:cd24073 1 AYVVGVKLTEDRITAVLTDLRGNVLASHTLPLD-SGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 163 VVDPPeLHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAG 242
Cdd:cd24073 80 CRWSP-LLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 243 EVG-------GLGAGCSTRILVEEAVALGVLGTEYAVTNPADAQRGVERLAAMTAEGDARADGILERLAIRIGRGVCAAA 315
Cdd:cd24073 159 EIGhttvdpdGPPCRCGKRGCLEAYASDPAILRQAREAGLRGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLV 238
|
250 260 270
....*....|....*....|....*....|
gi 2770182087 316 TLLDIDTIVFGGP---TWHLLADRLLPTIE 342
Cdd:cd24073 239 NLLDPELIIISGEgvrAGDLLFEPMREALR 268
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
83-383 |
1.84e-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: 148.12 E-value: 1.84e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 83 RYALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGADRdRILGLGIAAPGPIDATAGW 162
Cdd:cd24059 1 PYVIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENIKS-KILGIGIGAPGPLDVEKGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 163 VVDPPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAG 242
Cdd:cd24059 80 ILNPPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 243 EVG-------GLGAGCSTRILVEEAVALGVLgTEYAV----TNPADAQRGVERLaamtAEGDARADGILERLAIRIGRGV 311
Cdd:cd24059 160 EIGhtsidinGPRCSCGNRGCLELYASIPAI-EKKARsalgSGRSFQLDIVEAL----QKGDPIADEVIEEAAKYLGIGL 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2770182087 312 CAAATLLDIDTIVFGGPTwHLLADRLLPTIEPMVAGSPFVKATHPTAVVSTTLGANVAAVGAASLVLDSTLS 383
Cdd:cd24059 235 VNLINLLNPEAIIIGGEL-IYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAAALVLNKYFE 305
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
84-364 |
2.67e-40 |
|
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: 145.02 E-value: 2.67e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 84 YALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGWV 163
Cdd:cd24076 2 AVIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 164 VDPPELhGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGE 243
Cdd:cd24076 82 LLAPNL-GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 244 VG-------GLGAGCSTR----ILVEEAVALGVLGTEYAVTNPADAQRGVERLAAmtaeGDARADGILERLAIRIGRGVC 312
Cdd:cd24076 161 IGhmtvdpdGPPCSCGNRgcweTYASERALLRAAGRLGAGGEPLSLAELVEAARA----GDPAALAALEEVGEYLGIGLA 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2770182087 313 AAATLLDIDTIVFGGPtWHLLADRLLPTIEPMVAGSPFVKATHPTAVVSTTL 364
Cdd:cd24076 237 NLVNTFNPELVVLGGA-LAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRL 287
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
95-346 |
1.45e-27 |
|
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.
Pssm-ID: 395384 [Multi-domain] Cd Length: 292 Bit Score: 110.12 E-value: 1.45e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 95 ITCVLVDLLGTVVAQRSRATPrggdTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGWVVDPPELhGWGR 174
Cdd:pfam00480 10 IAAALFDEEGEILARERVPTP----TTTTEETLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITNTPNI-GWDN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 175 YPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------GL 247
Cdd:pfam00480 85 FDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGhiqldpnGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 248 GAGCSTRILVEeavalgvlgtEYAvTNPADAQRGVERLAAMTA--------EGDARADGILERLAIRIGRGVCAAATLLD 319
Cdd:pfam00480 165 KCGCGNHGCLE----------TIA-SGRALEKRYQQKGEDLEGkdiivlaeQGDEVAEEAVERLARYLAKAIANLINLFD 233
|
250 260
....*....|....*....|....*..
gi 2770182087 320 IDTIVFGGPTWHllADRLLPTIEPMVA 346
Cdd:pfam00480 234 PQAIVLGGGVSN--ADGLLEAIRSLVK 258
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
84-327 |
2.01e-27 |
|
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: 110.46 E-value: 2.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 84 YALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGWV 163
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 164 VDPPELhGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGE 243
Cdd:cd24062 81 EVAVNL-GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 244 VG------GLGAGCS---TRILVEEAVALG-VLGTEYAVTNPADAQRGV-----ERLAAMTA-----EGDARADGILERL 303
Cdd:cd24062 160 IGhitvnpEGGAPCNcgkTGCLETVASATGiVRIAREELEEGKGSSALRilalgGELTAKDVfeaakAGDELALAVVDTV 239
|
250 260
....*....|....*....|....
gi 2770182087 304 AIRIGRGVCAAATLLDIDTIVFGG 327
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGG 263
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
84-364 |
3.27e-27 |
|
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: 109.74 E-value: 3.27e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 84 YALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAAdmaaSVSGLVAE--SGADRDRILGLGIAAPGPIDATAG 161
Cdd:cd24063 1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSE----QVLGLIETllSKAGKDSIEGIGVSSAGPLDLRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 162 WVVDPPELHGwGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNA 241
Cdd:cd24063 77 TIVNSPNIKG-KEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 242 GEVG---------------------GLGAGCSTRILVEEAVALGVLGTEYAVTNPADAQRGVERLAAMTAEGDARADGIL 300
Cdd:cd24063 156 AEVGhlvvdtesglkcgcggyghweAFASGRGIPRFAREWAEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKII 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2770182087 301 ERLAIRIGRGVCAAATLLDIDTIVFGGPTWHLLADRLLPTIEPMVAGSPFVKathPTAVVSTTL 364
Cdd:cd24063 236 EKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKNPAISK---GPEIVLSEL 296
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
85-327 |
1.09e-25 |
|
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: 105.51 E-value: 1.09e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 85 ALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGD--TDKIAAdmaaSVSGLvaesgADRDRILGLGIAAPGPIDATAGW 162
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTPPTADgiVDAIVE----AVEEL-----REGHDVSAVGVAAAGFVDADRAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 163 VVDPPELhGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAG 242
Cdd:cd24061 72 VLFAPNI-AWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 243 EVG-------GLGAGC----------STRILVEEAVALGVLGTEYAVTNPADAQRGV---ERLAAMTAEGDARADGILER 302
Cdd:cd24061 151 EFGhirvvpdGLLCGCgsrgcweqyaSGRALVRYAKEAANATPEGAAVLLADGSVDGitgKHISEAARAGDPVALDALRE 230
|
250 260
....*....|....*....|....*
gi 2770182087 303 LAIRIGRGVCAAATLLDIDTIVFGG 327
Cdd:cd24061 231 LARWLGAGLASLAALLDPELFVIGG 255
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
99-327 |
4.94e-25 |
|
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: 103.41 E-value: 4.94e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 99 LVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESgadrdRILGLGIAAPGPIDATAGWVVDP-PELHGWGRYPL 177
Cdd:cd24068 16 LVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKY-----DIEGIGISSAGQVDPKTGEVIYAtDNLPGWTGTNL 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 178 RDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------GLGAG 250
Cdd:cd24068 91 KEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGhmvvdpgGRPCC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2770182087 251 CSTRILVEEAVALGVLGTEYAVTNPADAQRGVErLAAMTAEGDARADGILERLAIRIGRGVCAAATLLDIDTIVFGG 327
Cdd:cd24068 171 CGGKGCLEQYASGTALVRRVAEALGEPGIDGRE-IFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEVIVIGG 246
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
83-327 |
1.96e-23 |
|
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: 99.28 E-value: 1.96e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 83 RYALGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESgADRDRILGLGIAAPGPIDATAGW 162
Cdd:cd24071 1 GYIIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLIKNK-HVEKKLLGIGIAVSGLVDSKKGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 163 VVDPPELhGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAG 242
Cdd:cd24071 80 VIRSTIL-GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 243 EVGGL-----GAGC------------STRILVEEAVALGVLGTEYAVTNPADAQrgVERLAAMTAEGDARADGILERLAI 305
Cdd:cd24071 159 EIGHMtiqpdGRKCycgqkgcleayaSFEALVNEIKELTESYPLSLLKELEDFE--IEKVREAAEEGDSVATELFKKAGE 236
|
250 260
....*....|....*....|..
gi 2770182087 306 RIGRGVCAAATLLDIDTIVFGG 327
Cdd:cd24071 237 YLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
86-327 |
1.18e-22 |
|
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: 96.63 E-value: 1.18e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 86 LGVHLDPAVITCVLVDllGTVVAQRS-RATPRGGdTDKIAADMAASVSGLVAESGadrdRILGLGIAAPGPIDATAGWVV 164
Cdd:cd24065 3 IGLDLGGTKIAAGVVD--GGRILSRLvVPTPREG-GEAVLDALARAVEALQAEAP----GVEAVGLGVPGPLDFRRGRVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 165 DPPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEV 244
Cdd:cd24065 76 FAPNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 245 G-------GLGAGCSTRILVeEAVALGVL---GTEYAVTNPADaqrgVERLAAMTAEGDARADGILERLAIRIGRGVCAA 314
Cdd:cd24065 156 GhttvlpgGPMCGCGLVGCL-EALASGRAlarDASFAYGRPMS----TAELFELAQQGEPKALRIVEQAAAHLGIGLANL 230
|
250
....*....|...
gi 2770182087 315 ATLLDIDTIVFGG 327
Cdd:cd24065 231 QKALDPEVFVLGG 243
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
86-364 |
5.28e-21 |
|
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: 92.48 E-value: 5.28e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 86 LGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAESgadRDRILGLGIAAPGPIDATAGWVVD 165
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEFEYRVITLETPEALIDEIIDCIDRLLKLW---KDRVKGIALAIQGLVDSHKGVSLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 166 PPELHgWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG 245
Cdd:cd24072 81 SPGAP-WRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 246 -------GLGAGCSTRILVEEAVALGVLGTEYAVTNP------ADAQRGVERLAAMTAEGDARADGILERLAIRIGRGVC 312
Cdd:cd24072 160 htkvnpdGARCDCGRRGCLETVASNSALKRNARVTLKlgpvsaDPEKLTMEQLIEALEEGEPIATQIFDRAANAIGRSLA 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 2770182087 313 AAATLLDIDTIVFGGPTWHlLADRLLPTIEPMVAGSPFvkATHPTAVVSTTL 364
Cdd:cd24072 240 NILNLLNPEQVLLYGRGCR-AGDLLLPAIRRAIAENPF--SQHATQIGFGQL 288
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
84-342 |
2.38e-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: 90.50 E-value: 2.38e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 84 YALGVHLDPAVITCVLVDLLGTVVAQRSRATPrGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGWV 163
Cdd:cd24075 2 HILAVRLGRHDLTLGLYDLSGELLAEHTVPLT-ALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 164 VDPPeLHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGE 243
Cdd:cd24075 81 HYMP-HIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 244 VGglgagcstRILVEEAVA------LGVLGTEyaVTNPADAQRGVERLAA------------------MTAEGDARADGI 299
Cdd:cd24075 160 IG--------HIQIEPLGErchcgnFGCLETV--ASNAAIEQRVKKLLKQgyasqltlqdctikdicqAALNGDQLAQDV 229
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 2770182087 300 LERLAIRIGRGVCAAATLLDIDTIVFGG---PTWHLladrLLPTIE 342
Cdd:cd24075 230 IKRAGRYLGKVIAILINLLNPQKIIIAGeitQADKV----LLPVIK 271
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
85-327 |
3.01e-20 |
|
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: 90.25 E-value: 3.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 85 ALGVHLDPAVITCVLVDLLGTVVAQRSRATprggDTDKIAADMAASVSGLVAESgADRDRILGLGIAAPGPIDATAGWVV 164
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTIDT----KVENGKEDVINRIAETVNEL-IEEMELLGIGIGSPGSIDRENGIVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 165 DPPELHGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEV 244
Cdd:cd24064 76 FSPNFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAEL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 245 G-------GLGAGCSTRILVE---EAVALGVLGTEYAVTNPADAQRGVERLAAMTA-----EGDARADGILERLAIRIGR 309
Cdd:cd24064 156 GhvivepnGPICGCGNRGCVEafaSATAIIRYARESRKRYPDSLAGESEKINAKHVfdaarKNDPLATMVFRRVVDALAI 235
|
250
....*....|....*...
gi 2770182087 310 GVCAAATLLDIDTIVFGG 327
Cdd:cd24064 236 AIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
104-327 |
1.15e-16 |
|
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: 79.64 E-value: 1.15e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 104 GTVVAQRSRATPRGGDtdkiAADMAASVSGLVAESGADRDRIlglGIAAPGPIDATAGWVVDPPELHGWGRYPLRDRLSE 183
Cdd:cd24069 18 GQIIDRRQIPTPRSGT----PEALADALASLLADYQGQFDRV---AVASTGIIRDGVLTALNPKNLGGLSGFPLADALQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 184 ATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------GLGAGCSTRIL 256
Cdd:cd24069 91 LLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGhtladppGPVCGCGRRGC 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2770182087 257 VE---EAVALGVLGTEyAVTNPADAQRGVERLAAmtaeGDARADGILERLAIRIGRGVCAAATLLDIDTIVFGG 327
Cdd:cd24069 171 VEaiaSGTAIAAAASE-ILGEPVDAKDVFERARS----GDEEAARLIDRAARALADLIADLKATLDLDCVVIGG 239
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
111-327 |
2.82e-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: 78.36 E-value: 2.82e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 111 SRATPRGGDTDKIAADMaasVSGLVAESGadrDRILGLGIAAPGPIDATAGWVVDPPELHGWGRYPLRDRLSEATGFTAV 190
Cdd:cd24070 32 SKDLLRAGDPVEVLADL---IREYIEEAG---LKPAAIVIGVPGTVDKDRRTVISTPNIPGLDGVNLADILENKLGIPVI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 191 LDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-----GLGA-------GCStrilve 258
Cdd:cd24070 106 LERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGhipvyGNGKpcgcgntGCL------ 179
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 259 EAVALGVLGTEYAVTNPADaqrgVERLAAMTAEGDARA-DGILERLAIrigrGVCAAATLLDIDTIVFGG 327
Cdd:cd24070 180 ETYASGRALEEIAEEHYPD----TPILDIFVDHGDEPElDEFVEDLAL----AIATEINILDPDAVILGG 241
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
142-327 |
1.14e-15 |
|
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: 76.45 E-value: 1.14e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 142 RDRILGLGIAAPGPIDATAGWVVD---PPELHGwgrYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFY 218
Cdd:cd24152 51 DEEIDGIAISAPGVIDPETGIIYGggaLPYLKG---FNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIV 127
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 219 FGTGTGMGMVVDDAVLRGVSGNAGEVG------------GLGAGCSTRILVEEAVALGVLgteyavtNPADAQRGVERLa 286
Cdd:cd24152 128 LGTGIGGAIIIDGKLYRGSHFFAGEFSylltddddkdllFFSGLASMFGLVKRYNKAKGL-------EPLDGEEIFEKY- 199
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2770182087 287 amtAEGDARADGILERLAIRIGRGVCAAATLLDIDTIVFGG 327
Cdd:cd24152 200 ---AKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
104-327 |
3.43e-14 |
|
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: 72.65 E-value: 3.43e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 104 GTVVAQRSRATPRGgDTDKIAADMAAsvsgLVAESGADRDRILGLGIAAPGPIDATAGWVV--DPPELHGWgryPLRDRL 181
Cdd:cd24057 21 LQLVWTKRVPTPTD-DYAAFLAAIAE----LVAEADARFGVKGPVGIGIPGVIDPEDGTLItaNIPAAKGR---PLRADL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 182 SEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVGGLGAGCSTRILVEEA- 260
Cdd:cd24057 93 SARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPLPADALLLGYDLp 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 261 -VALGVlGTEYAVTNPADAqRGVERL--------------AAMTAEGDARADGILERLAIRIGRGVCAAATLLDIDTIVF 325
Cdd:cd24057 173 vLRCGC-GQTGCLETYLSG-RGLERLyahlygeeldapeiIAAWAAGDPQAVAHVDRWLDLLAGCLANILTALDPDVVVL 250
|
..
gi 2770182087 326 GG 327
Cdd:cd24057 251 GG 252
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
95-327 |
5.75e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 71.87 E-value: 5.75e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 95 ITCVLVDLLGTVVAQRSRATPRGGDTDKIAADMAASVSGLVAEsgADRDRILGLGIAAPGPIDAtagwvVDPPELHGWGR 174
Cdd:PRK05082 13 IAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQ--ADRVAVASTGIINDGILTA-----LNPHNLGGLLH 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 175 YPLRDRLSEATGFTAVLDKDVTAAVVAErWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------GL 247
Cdd:PRK05082 86 FPLVQTLEQLTDLPTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGhtladphGP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 248 GAGCSTRILVE--------EAVALGVLgteyavtNPADAQRGVERLAAmtaeGDARADGILERLAIRIGRGVCAAATLLD 319
Cdd:PRK05082 165 VCGCGRRGCVEaiasgraiAAAAQGWL-------AGCDAKTIFERAGQ----GDEQAQALINRSAQAIARLIADLKATLD 233
|
....*...
gi 2770182087 320 IDTIVFGG 327
Cdd:PRK05082 234 CQCVVLGG 241
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
85-245 |
2.65e-13 |
|
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: 69.75 E-value: 2.65e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 85 ALGVHLDPAVITCVLVDLLGTVVAQRSRATPrGGDTDKIAADMAASVSgLVAESGADRDRILGLGIAAPGPIDATAGWVV 164
Cdd:cd24060 2 ALAVDLGGTNLRVAIVSMKGEIVKKYTQPNP-KTYEERIDLILQMCVE-AASEAVKLNCRILGVGISTGGRVNPREGIVL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 165 DPPEL-HGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGE 243
Cdd:cd24060 80 HSTKLiQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAE 159
|
..
gi 2770182087 244 VG 245
Cdd:cd24060 160 LG 161
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
86-328 |
7.99e-13 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 68.49 E-value: 7.99e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 86 LGVHLDPAVITCVLVDLLGTVVAQRSRATPRGGDTDKIAAdMAASVSGLVAESGADRDRILGLGIAAPGPIDATAGWVVD 165
Cdd:cd24074 5 LSIRIGRGYITLALRDLNGRLLAEERYPLPAKDNDPFLDR-LLESISEFFSRHQKKLERLTAIAITLPGIIDPESGIVHR 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 166 PP--ELHGWgryPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGE 243
Cdd:cd24074 84 LPfyDIKNL---PLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 244 VGGL------------GAGC-----STRILVEEAVALGVLGTEYAVTNPADAqrgVERLAAMTAEGDARADGILERLAIR 306
Cdd:cd24074 161 LGHTqidpygkrcycgNHGCletvaSIPAILEQANQLLEQSPDSMLHGQPIS---IESLCQAALAGDPLAQDIIIQVGRH 237
|
250 260
....*....|....*....|..
gi 2770182087 307 IGRGVCAAATLLDIDTIVFGGP 328
Cdd:cd24074 238 LGRILAILVNLFNPEKILIGSP 259
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
86-327 |
2.36e-10 |
|
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: 61.07 E-value: 2.36e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 86 LGVHLDPAVITCVLVDLLGTVVAQRSRATPRGgDTDKIAADMAASVSGLVAESGADrdriLGLGIAAPGPIDATAGWVVD 165
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRG-DYEATLDAIADLVEEAEEELGAP----ATVGIGTPGSISPRTGLVKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 166 PPELHGWGRyPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG 245
Cdd:cd24066 77 ANSTWLNGK-PLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 246 -------------GLGAGCSTRILVEEAVALGVLGTEYAVTNPadAQRGVERLAAMTAEGDARADGILERLAIRIGRGVC 312
Cdd:cd24066 156 hnplpwpdedelpGPPCYCGKRGCVETFLSGPALERDYARLTG--KTLSAEEIVALARAGDAAAVATLDRFLDRLGRALA 233
|
250
....*....|....*
gi 2770182087 313 AAATLLDIDTIVFGG 327
Cdd:cd24066 234 NVINILDPDVIVLGG 248
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
143-236 |
6.01e-10 |
|
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: 59.48 E-value: 6.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 143 DRILGLGIAAPGPID-----ATAGWVVDPPELhGWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFF 217
Cdd:cd24067 49 EPIDAIGIASFGPIDlnptsPTYGYITTTPKP-GWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYI 127
|
90
....*....|....*....
gi 2770182087 218 YFGTGTGMGMVVDDAVLRG 236
Cdd:cd24067 128 TVGTGIGVGLVVNGKPVHG 146
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
99-327 |
4.96e-08 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 53.83 E-value: 4.96e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 99 LVDLLGTVVAQRSRATprggdTDKIAADMAASVSGLVAESGADRD-RILGLGIAAPGPIDATAGWVVDPPELHGWG--RY 175
Cdd:PRK09698 20 LVDAEGEILHCEKKRT-----AEVIAPDLVSGLGEMIDEYLRRFNaRCHGIVMGFPALVSKDRRTVISTPNLPLTAldLY 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 176 PLRDRLSEATGFTAVLDKDVTAAVvaeRWTGAA--TDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG-------G 246
Cdd:PRK09698 95 DLADKLENTLNCPVFFSRDVNLQL---LWDVKEnnLTQQLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGhiplgdmT 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 247 LGAGCSTRILVEEAVALGVLGTEYAvTNPADAqrGVERLaaMTAEGDARA-DGILERLAIRIGRGVcaaaTLLDIDTIVF 325
Cdd:PRK09698 172 QHCGCGNPGCLETNCSGMALRRWYE-QQPRDY--PLSDL--FVHAGDHPFiQSLLENLARAIATSI----NLFDPDAIIL 242
|
..
gi 2770182087 326 GG 327
Cdd:PRK09698 243 GG 244
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
84-245 |
1.15e-07 |
|
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: 52.93 E-value: 1.15e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 84 YALGVHLDPAVITCVLVDLLGTVVAQRSRATPrGGDTDKIAADMAASVSGLVAESGADRDRILGLGIAAPGpidatagwV 163
Cdd:cd24077 2 YSIGIDLGYNYISLMLTYLDGEIISSKQIKLL-DISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHG--------I 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 164 VD-------PPELhgWGRYPLRDRLSEATGFTAVLDKDVTAAVVAERwtGAATDSRNLLFFYFGTGTGMGMVVDDAVLRG 236
Cdd:cd24077 73 VDeneiiftPYYD--LEDIDLKEKLEEKFNVPVYLENEANLSALAER--TFSEDYDNLISISIHSGIGAGIIINNQLYRG 148
|
....*....
gi 2770182087 237 VSGNAGEVG 245
Cdd:cd24077 149 YNGFAGEIG 157
|
|
| HTH_24 |
pfam13412 |
Winged helix-turn-helix DNA-binding; |
19-58 |
3.93e-05 |
|
Winged helix-turn-helix DNA-binding;
Pssm-ID: 404317 [Multi-domain] Cd Length: 45 Bit Score: 40.49 E-value: 3.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|
gi 2770182087 19 VLDAIRRHPtGLSRVELARATGLSSQTVSNITRRLLDQGV 58
Cdd:pfam13412 6 ILNLLQENP-RISQRELAERLGLSPSTVNRRLKRLEEEGV 44
|
|
| HTH_MARR |
smart00347 |
helix_turn_helix multiple antibiotic resistance protein; |
19-61 |
5.93e-05 |
|
helix_turn_helix multiple antibiotic resistance protein;
Pssm-ID: 197670 [Multi-domain] Cd Length: 101 Bit Score: 41.81 E-value: 5.93e-05
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2770182087 19 VLDAIRRHPtGLSRVELARATGLSSQTVSNITRRLLDQG-VARE 61
Cdd:smart00347 15 VLRILYEEG-PLSVSELAKRLGVSPSTVTRVLDRLEKKGlVRRE 57
|
|
| MarR_2 |
pfam12802 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
13-63 |
7.03e-05 |
|
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.
Pssm-ID: 432797 [Multi-domain] Cd Length: 60 Bit Score: 40.26 E-value: 7.03e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 2770182087 13 DFNESVVLDAIRRHPtGLSRVELARATGLSSQTVSNITRRLLDQG-VARESG 63
Cdd:pfam12802 4 TPAQFRVLLALARNP-GLTVAELARRLGISKQTVSRLVKRLEAKGlVEREPS 54
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
131-327 |
9.13e-05 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 43.82 E-value: 9.13e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 131 VSGLVAESGADRDRILGLGIAAPGPIDATAG--WVVDPPELHGwgrYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAA 208
Cdd:PRK13310 43 VCELVAEADQRFGCKGSVGIGIPGMPETEDGtlYAANVPAASG---KPLRADLSARLGRDVRLDNDANCFALSEAWDDEF 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 209 TDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVGglgagcSTRILVEeavALGVLGTEYAVTNPADAQRGV------ 282
Cdd:PRK13310 120 TQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFG------HMRLPVD---ALTLLGWDAPLRRCGCGQKGCienyls 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2770182087 283 -------------ERLAAMT-----AEGDARADGILER----LAIRIGRGVcaaaTLLDIDTIVFGG 327
Cdd:PRK13310 191 grgfewlyqhyygEPLQAPEiialyYQGDEQAVAHVERyldlLAICLGNIL----TIVDPHLVVLGG 253
|
|
| COG2512 |
COG2512 |
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ... |
15-57 |
5.50e-04 |
|
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only];
Pssm-ID: 442002 [Multi-domain] Cd Length: 80 Bit Score: 38.36 E-value: 5.50e-04
10 20 30 40
....*....|....*....|....*....|....*....|...
gi 2770182087 15 NESVVLDAIRRHPTGLSRVELARATGLSSQTVSNITRRLLDQG 57
Cdd:COG2512 16 DERRVLELLRENGGRMTQSEIVKETGWSKSKVSRLLSRLEERG 58
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
100-355 |
1.07e-03 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 40.78 E-value: 1.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 100 VDLLGT---VVAQ--------RSR-ATPRGGDTDKIAAdmaasVSGLVAESGADRDRILGLGIAAPGPIDATAGWVVDPP 167
Cdd:PRK09557 5 IDLGGTkieVIALddageelfRKRlPTPRDDYQQTIEA-----IATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 168 E--LHGwgrYPLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNLLFFYFGTGTGMGMVVDDAVLRGVSGNAGEVG 245
Cdd:PRK09557 80 StwLNG---QPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 246 ----------------GLGAGCSTRILVEEAVAlgvlGTEYAV---TNPADAQRGVErLAAMTAEGDARADGILERLAIR 306
Cdd:PRK09557 157 hnplpwmdedelryrnEVPCYCGKQGCIETFIS----GTGFATdyrRLSGKALKGSE-IIRLVEEGDPVAELAFRRYEDR 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2770182087 307 IGRGVCAAATLLDIDTIVFGGPTWHLlaDRLLPT----IEPMVAG----SPFVKATH 355
Cdd:PRK09557 232 LAKSLAHVINILDPDVIVLGGGMSNV--DRLYPTlpalLKQYVFGgeceTPVRKALH 286
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
99-230 |
3.38e-03 |
|
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: 38.70 E-value: 3.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2770182087 99 LVDLL-GTVVAQRSR-ATPRGGDTDKIAADMAASVSGLvaesgADRDRIlglGIAAPGPIdaTAGWVVDPPELH-GWGRY 175
Cdd:cd24058 15 IVDTDtGELLSERIRiPTPQPATPEAVADVVAELVAHF-----PWFGPV---GVGFPGVV--RRGVVRTAANLDkSWIGF 84
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2770182087 176 PLRDRLSEATGFTAVLDKDVTAAVVAERWTGAATDSRNL-LFFYFGTGTGMGMVVD 230
Cdd:cd24058 85 DAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVvLVLTLGTGIGSALFVD 140
|
|
| HTH_IclR |
pfam09339 |
IclR helix-turn-helix domain; |
19-60 |
4.03e-03 |
|
IclR helix-turn-helix domain;
Pssm-ID: 430539 [Multi-domain] Cd Length: 52 Bit Score: 35.08 E-value: 4.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|..
gi 2770182087 19 VLDAIRRHPTGLSRVELARATGLSSQTVSNITRRLLDQGVAR 60
Cdd:pfam09339 8 ILDALAEAPGPLTLTEIARRTGLPKSTAHRLLQTLVELGYVE 49
|
|
| MarR |
COG1846 |
DNA-binding transcriptional regulator, MarR family [Transcription]; |
19-61 |
5.13e-03 |
|
DNA-binding transcriptional regulator, MarR family [Transcription];
Pssm-ID: 441451 [Multi-domain] Cd Length: 142 Bit Score: 37.26 E-value: 5.13e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 2770182087 19 VLDAIRRHPtGLSRVELARATGLSSQTVSNITRRLLDQG-VARE 61
Cdd:COG1846 43 VLAALAEAG-GLTQSELAERLGLTKSTVSRLLDRLEEKGlVERE 85
|
|
| |
