|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
77-384 |
6.42e-94 |
|
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: 283.71 E-value: 6.42e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELlaEAGISRGRILGIGIGVPGPVDPETGVVL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:COG1940 87 NAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGEI 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGR--SAELAARLEAggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:COG1940 167 GHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGAEKltAEELFAAARA---------------GDPLALEVLDEA 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:COG1940 232 ARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAAL 303
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
75-388 |
1.24e-71 |
|
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: 226.29 E-value: 1.24e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 75 LRFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGI 152
Cdd:cd24076 1 GAVIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREAlaAAPDSPLGILGIGVGVPGLVDSEDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24076 81 VLLAPNL-GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALAR---DAEQVAREGRSAELAARLEAggrlsaadvaaaasgGDTAALELI 309
Cdd:cd24076 160 EIGHMTVDPDGPPCSCGNRGCWETYASERALLRaagRLGAGGEPLSLAELVEAARA---------------GDPAALAAL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 310 RRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDH 388
Cdd:cd24076 225 EEVGEYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALAIDH 303
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
78-384 |
3.85e-70 |
|
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: 220.41 E-value: 3.85e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL-KASGLAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELlAEAGVRERILGIGIGVPGPVDPETGIVLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd23763 81 PNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVepdglpcacgnqgcleahfsgsalardaeqvaregrsaelaarleaggrlsaadvaaaasggdtaalelIRRGGRHT 316
Cdd:cd23763 161 ITV---------------------------------------------------------------------LEEAARYL 171
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd23763 172 GIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
77-384 |
9.82e-70 |
|
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: 221.28 E-value: 9.82e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKLKASGLAEGfdgAGIGVPGPVRFPEGIPV-A 155
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKYDIEG---IGISSAGQVDPKTGEVIyA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24068 79 TDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQV--AREGRSAELAARLEAggrlsaadvaaaasgGDTAALELIRRGG 313
Cdd:cd24068 159 HMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEAlgEPGIDGREIFDLADA---------------GDPLAKEVVEEFA 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24068 224 EDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
76-384 |
2.57e-65 |
|
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: 210.61 E-value: 2.57e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 76 RFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEG-I 152
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLleELGYSKEDLIGIGVGVPGPVDVETGtV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPImpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24062 81 EVAVNL--GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPD-GLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRR 311
Cdd:cd24062 159 EIGHITVNPEgGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDT 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674 312 GGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24062 239 VARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
78-391 |
1.52e-64 |
|
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: 208.21 E-value: 1.52e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEK-LKASGLAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd24059 4 IGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRlLEKENIKSKILGIGIGAPGPLDVEKGIILNP 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24059 84 PNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEIGH 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAggrlsaadvaaaaSGGDTAALELIRRGGRHT 316
Cdd:cd24059 164 TSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGSGRSFQLDIVEAL-------------QKGDPIADEVIEEAAKYL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLFS 391
Cdd:cd24059 231 GIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAAALVLNKYFE 305
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
77-390 |
3.46e-63 |
|
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: 204.71 E-value: 3.46e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREgPVAVFEQVLDMAEKL--KASGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGD-PEAVAEAIAEAVAELlaQAGLSPDRLLGIGVGLPGLVDAETGICR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:cd24073 82 WSPLL-GWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAggrlsaadvaaaASGGDTAALELIRRGGR 314
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLRGEPLTIEDLLAA------------ARAGDPAARAILRRAGR 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498326674 315 HTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLF 390
Cdd:cd24073 229 ALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGAAALALQEFF 304
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
78-384 |
4.11e-60 |
|
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: 196.81 E-value: 4.11e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVreGPVAVFEQVLDMAEklkasGLAEGFD--GAGIGVPGPVRFPEGIPVA 155
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVE-----ELREGHDvsAVGVAAAGFVDADRATVLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPgWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24061 75 APNIA-WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVARE-GRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRRGGR 314
Cdd:cd24061 154 HIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANAtPEGAAVLLADGSVDGITGKHISEAARAGDPVALDALRELAR 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674 315 HTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTqVYRQSLPlATGNLP---IVLGELGPAAGVIGGARL 384
Cdd:cd24061 234 WLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIRE-AFERWLP-GRGWRPiprLRTAQLGNDAGLIGAADL 304
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
78-392 |
1.38e-59 |
|
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: 195.89 E-value: 1.38e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAV-----FEQVLDMAEKLKASGLaegfdGAGIGVPGPVRFPEGI 152
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDaiasaVDSFIQHIAKVGHEIV-----AIGIGAPGPVNRQRGT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:TIGR00744 76 VYFAVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDG-LPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRR 311
Cdd:TIGR00744 155 EIGHIRMVPDGrLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYRE 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 312 GGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLFS 391
Cdd:TIGR00744 235 VARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAADLARTYIIE 314
|
.
gi 498326674 392 P 392
Cdd:TIGR00744 315 P 315
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
78-384 |
5.63e-56 |
|
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon repressor, xylR, from Bacillus subtilis, Lactobacillus pentosus and Staphylococcus xylosus; N-acetylglucosamine repressor, nagC, from Escherichia coli; glucokinase from Streptomyces coelicolor; fructokinase from from Pediococcus pentosaceus, Streptococcus mutans and Zymomonas mobilis; allokinase and mlc from E. coli; and E. coli hypothetical proteins yajF and yhcI and the corresponding Haemophilus influenzae proteins. The repressor proteins (xylR and nagC) from this family possess an N-terminal region not present in the sugar kinases and which contains an helix-turn-helix DNA-binding motif.
Pssm-ID: 395384 [Multi-domain] Cd Length: 292 Bit Score: 185.62 E-value: 5.63e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHI---TQPMDVREGPVAVFEQVLDMAEklkasGLAEGFDGAGIGVPGPVRFPEGIPV 154
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARErvpTPTTTTEETLVDAIAFFVDSAQ-----RKFGELIAVGIGSPGLISPKYGYIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPiMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDI 234
Cdd:pfam00480 76 NTP-NIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 235 GHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAR--EGRSAELAARLeaggrlsaadvaaaasgGDTAALELIRRG 312
Cdd:pfam00480 155 GHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQKGEdlEGKDIIVLAEQ-----------------GDEVAEEAVERL 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQSL-PLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:pfam00480 218 ARYLAKAIANLINLFDPQAIVLGGGV-SNADGLLEAIRSLVKKYLNgYLPVPPVIIVAASLGDNAGALGAAAL 289
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
78-382 |
9.57e-56 |
|
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: 184.84 E-value: 9.57e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAElEVLGHITQPMDvREGPVAVFEQVLDMAEKLKASglAEGFDGAGIGVPGPVRFPEGIPVAPP 157
Cdd:cd24065 3 IGLDLGGTKIAAGVVDGG-RILSRLVVPTP-REGGEAVLDALARAVEALQAE--APGVEAVGLGVPGPLDFRRGRVRFAP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 158 IMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGHI 237
Cdd:cd24065 79 NIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHT 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 238 QVEPDGLPCACGNQGCLEAHFSGSALARDAEQV-AREGRSAELAARLEAggrlsaadvaaaasgGDTAALELIRRGGRHT 316
Cdd:cd24065 159 TVLPGGPMCGCGLVGCLEALASGRALARDASFAyGRPMSTAELFELAQQ---------------GEPKALRIVEQAAAHL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGnlPIVLGELGPAAGVIGGA 382
Cdd:cd24065 224 GIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYTEGWHAP--PLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
77-390 |
3.52e-55 |
|
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: 184.03 E-value: 3.52e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKL-KASGLAEGFDGAGIGVPGPVRFPEGIPVA 155
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLiKNKHVEKKLLGIGIAVSGLVDSKKGIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMpGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24071 83 STIL-GWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAElaarLEAGGRLSAADVAAAASGGDTAALELIRRGGRH 315
Cdd:cd24071 162 HMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSL----LKELEDFEIEKVREAAEEGDSVATELFKKAGEY 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 316 TGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGARLISDHLF 390
Cdd:cd24071 238 LGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVIDHLF 312
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
78-382 |
1.58e-49 |
|
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: 169.21 E-value: 1.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVldmAEKLKASGLAEGFDGAGIGVPGPVRFPEGIPVAPP 157
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRI---AETVNELIEEMELLGIGIGSPGSIDRENGIVRFSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 158 IMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGHI 237
Cdd:cd24064 79 NFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 238 QVEPDGLPCACGNQGCLEAHFSGSALARdaeqVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRRGGRHTG 317
Cdd:cd24064 159 IVEPNGPICGCGNRGCVEAFASATAIIR----YARESRKRYPDSLAGESEKINAKHVFDAARKNDPLATMVFRRVVDALA 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 318 QVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGPAAGVIGGA 382
Cdd:cd24064 235 IAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAA 299
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
76-384 |
7.85e-46 |
|
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: 159.81 E-value: 7.85e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 76 RFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKLKASGLAEGFDGAGIGVPGPVRFPEGIPVA 155
Cdd:cd24063 1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLSKAGKDSIEGIGVSSAGPLDLRKGTIVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDgFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24063 81 SPNIKGKE-IPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPD-GLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGR-LSAADVAAAASGGDTAALELIRRGG 313
Cdd:cd24063 160 HLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLKLRNPGGEgITAKEVFSAARKGDPLALKIIEKLA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSlplATGNLP-IVLGELGPAAGVIGGARL 384
Cdd:cd24063 240 RYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKNP---AISKGPeIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
76-382 |
5.70e-42 |
|
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: 148.85 E-value: 5.70e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 76 RFLGVDIGATSVDVAVTNAELEVLG---HITQPMDVREGPVAVFEQVLDmaEKLKASGLAegFDGAGIGVPGPVRFPEGI 152
Cdd:cd24070 2 YVLGIDIGGTNIRIGLVDEDGKLLDfekVPSKDLLRAGDPVEVLADLIR--EYIEEAGLK--PAAIVIGVPGTVDKDRRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24070 78 VISTPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARleaggrlsaadvaaaasGGDTAAL-ELIrr 311
Cdd:cd24070 158 ELGHIPVYGNGKPCGCGNTGCLETYASGRALEEIAEEHYPDTPILDIFVD-----------------HGDEPELdEFV-- 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 312 ggRHTGQVIAGLVSFFNPGLVVIGGGVTGLG----HTLLAAIRTQVyRQSLPLatGNLPIVLGELGPAAGVIGGA 382
Cdd:cd24070 219 --EDLALAIATEINILDPDAVILGGGVIDMKgfprETLEEYIRKHL-RKPYPA--DNLKIIYAELGPEAGVIGAA 288
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
78-353 |
1.06e-41 |
|
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: 148.72 E-value: 1.06e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLD-MAEKLKASglAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEFEYRVITLETPEALIDEIIDcIDRLLKLW--KDRVKGIALAIQGLVDSHKGVSLWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPgWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24072 82 PGAP-WRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVaaaasgGDTAALELIRRGGRHT 316
Cdd:cd24072 161 TKVNPDGARCDCGRRGCLETVASNSALKRNARVTLKLGPVSADPEKLTMEQLIEALEE------GEPIATQIFDRAANAI 234
|
250 260 270
....*....|....*....|....*....|....*..
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQV 353
Cdd:cd24072 235 GRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAI 271
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
75-374 |
2.66e-41 |
|
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: 147.90 E-value: 2.66e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 75 LRFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREgPVAVFEQVLDMAEKLKASGLAEGFDGAGIGV--PGPVRFPEGI 152
Cdd:cd24075 1 FHILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALN-QEALLSQLIEEIAQFLKSHRRKTQRLIAISItlPGLINPKTGV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 153 PVAPPIMPGWDgFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAG 232
Cdd:cd24075 80 VHYMPHIQVKS-WPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 233 DIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARleaggRLSAADVAAAASGGDTAALELIRRG 312
Cdd:cd24075 159 EIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQGYASQLTLQ-----DCTIKDICQAALNGDQLAQDVIKRA 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 498326674 313 GRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGP 374
Cdd:cd24075 234 GRYLGKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDH 295
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
78-384 |
7.24e-41 |
|
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: 146.41 E-value: 7.24e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPM-DVREGPVAVFEQVLDMAEKlKASGLAEGFDGAGIGVPGPVRFPEGIPV-A 155
Cdd:cd24060 3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNpKTYEERIDLILQMCVEAAS-EAVKLNCRILGVGISTGGRVNPREGIVLhS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24060 82 TKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAGGRLSAADVAAAASGGDTAALELIRRGGRH 315
Cdd:cd24060 162 HIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAGTA 241
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 316 TGQVIAGLVSFFNPGLVVIGGGVTGLGhtlLAAIRTQVYRQSLPlATGNLPIVLGELGPAAgVIGGARL 384
Cdd:cd24060 242 LGLGIVNILHTLNPSLVILSGVLASHY---ENIVKDVIAQRALP-SVQNVDVVVSDLVDPA-LLGAASM 305
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
159-391 |
7.91e-37 |
|
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: 136.29 E-value: 7.91e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 159 MPGWD--GFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24074 84 LPFYDikNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGH 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARleaggRLSAADVAAAASGGDTAALELIRRGGRHT 316
Cdd:cd24074 164 TQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQSPDSMLHGQ-----PISIESLCQAALAGDPLAQDIIIQVGRHL 238
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 498326674 317 GQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSLPLATGNLPIVLGELGpAAGVIGGARLISDHLFS 391
Cdd:cd24074 239 GRILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQSLPAYSQHLQIESTKFY-NDGTMPGAALIKDALYD 312
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
77-370 |
1.35e-29 |
|
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: 116.10 E-value: 1.35e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVREgPVAVFEQVLDMAEKLKAS------GLAegfdGAGIGVPGPVrFPE 150
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLLDIS-FENILEILKSIIQELISQapktpyGLV----GIGIGIHGIV-DEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 151 GIPVAPPIMpgWDGFPVREALSQELGCPVMVDNDVNLMAMGEQhaGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGS 230
Cdd:cd24077 77 EIIFTPYYD--LEDIDLKEKLEEKFNVPVYLENEANLSALAER--TFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 231 AGDIGHIQVEPDGLPCACGNQGCLEAHFSGSALARD-AEQVAREG-RSAELAARLEAggrlsaadvaaaasgGDTAALEL 308
Cdd:cd24077 153 AGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLKElSEKKGLETlTFDDLIQLYNE---------------GDPEALEL 217
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 498326674 309 IRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQV------YRQSLPLATGNLPIVLG 370
Cdd:cd24077 218 IDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEKIKEQLsssfnkYVEILISTLGKNATLLG 285
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
79-384 |
1.39e-29 |
|
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: 115.79 E-value: 1.39e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 79 GVDIGATSVDVAVTNAELEVLGHITQPMDVREGPvAVFEQVLDMAEKLKASGLAEGfdGAGIGVPGPVRFPEGIPVAPPI 158
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYA-AFLAAIAELVAEADARFGVKG--PVGIGIPGVIDPEDGTLITANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 159 mPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH-- 236
Cdd:cd24057 81 -PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHgp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 ----IQVEPDGLP---CACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARLEAggrlsaadvaaaasgGDTAALEL 308
Cdd:cd24057 160 lpadALLLGYDLPvlrCGCGQTGCLETYLSGRGLERLYAHLYGEELDApEIIAAWAA---------------GDPQAVAH 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 498326674 309 IRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGhTLLAAIRTQVYRQSLPLATgnLP-IVLGELGPAAGVIGGARL 384
Cdd:cd24057 225 VDRWLDLLAGCLANILTALDPDVVVLGGGLSNFP-ALIAELPAALPAHLLSGAR--TPrIVPARHGDAGGVRGAAFL 298
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
78-384 |
1.54e-29 |
|
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: 115.46 E-value: 1.54e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVA-VTNAELEVLGHITQPmdvREGPVAVFEQVLdmaeKLKASGLAEGFDGAGIGVPGPVRFPEGIPVAP 156
Cdd:cd24069 1 LAIDIGGTKIAAAlIGNGQIIDRRQIPTP---RSGTPEALADAL----ASLLADYQGQFDRVAVASTGIIRDGVLTALNP 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:cd24069 74 KNLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 237 IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARleaggrlsaadvaaaASGGDTAALELIRRGGRH 315
Cdd:cd24069 154 TLADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEPVDAkDVFER---------------ARSGDEEAARLIDRAARA 218
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 498326674 316 TGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTqvYRQSLPlATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24069 219 LADLIADLKATLDLDCVVIGGSV-GLAEGFLERVEQ--YLADEP-AIFRVSLEPARLGQDAGLLGAALL 283
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
76-393 |
8.66e-29 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 113.92 E-value: 8.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 76 RFLGVDIGATSVDVAVTNAELEVLGHITQP-MDVREGPVA------VFEQVLDMAEKLKasglaegfdGAGIGVPGPVRF 148
Cdd:PRK09698 5 VVLGIDMGGTHIRFCLVDAEGEILHCEKKRtAEVIAPDLVsglgemIDEYLRRFNARCH---------GIVMGFPALVSK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 149 PEGIPVAPPIMP--GWDGFPVREALSQELGCPVMVDNDVNLMAMGE--QHAGVARTArdfLCVKIGTGIGCGIVVGSTVY 224
Cdd:PRK09698 76 DRRTVISTPNLPltALDLYDLADKLENTLNCPVFFSRDVNLQLLWDvkENNLTQQLV---LGAYLGTGMGFAVWMNGAPW 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 225 RGTTGSAGDIGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVARegrsaelaarleaggrlsaadvaaaasggDTA 304
Cdd:PRK09698 153 TGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQQPR-----------------------------DYP 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 305 ALELIRRGGRH---------TGQVIAGLVSFFNPGLVVIGGGVTGLGHTLLAAIRTQVYRQSL-PLATGNLPIVLGELGP 374
Cdd:PRK09698 204 LSDLFVHAGDHpfiqsllenLARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRkPLPYEVVRFIYASSSD 283
|
330
....*....|....*....
gi 498326674 375 AAGVIGGARLISDHLFSPA 393
Cdd:PRK09698 284 FNGAQGAAILAHQRFLPQS 302
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
78-384 |
5.01e-28 |
|
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: 111.53 E-value: 5.01e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDvREGPVAVFEQVLDMAEKLKASGLAEGfdGAGIGVPGPVrfpegipvAPP 157
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTP-RGDYEATLDAIADLVEEAEEELGAPA--TVGIGTPGSI--------SPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 158 IMPGWD-------GFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGS 230
Cdd:cd24066 71 TGLVKNanstwlnGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 231 AGDIGHIQVEP------DGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARLEAggrlsaadvaaaasgGDT 303
Cdd:cd24066 151 AGEWGHNPLPWpdedelPGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAeEIVALARA---------------GDA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 304 AALELIRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHtLLAAIRTQVYRQ--SLPLATgnlPIVLGELGPAAGVIGG 381
Cdd:cd24066 216 AAVATLDRFLDRLGRALANVINILDPDVIVLGGGLSNIDE-LYTEGPAALARYvfSDEVET---PIVKNKHGDSSGVRGA 291
|
...
gi 498326674 382 ARL 384
Cdd:cd24066 292 AWL 294
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
77-384 |
1.32e-23 |
|
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; Bacillus subtilis FRK (EC 2.7.1.4), also called glucomannan utilization protein E, catalyzes the phosphorylation of fructose to fructose-6-P. It seems to be involved in the degradation of glucomannan. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466917 [Multi-domain] Cd Length: 285 Bit Score: 99.16 E-value: 1.32e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDVregPVAVFEQVLDMAEKLKASglaegFDGAGIGVPGPVRFPEG----- 151
Cdd:cd24067 1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPTTT---PEETLQAVIDFFREQEEP-----IDAIGIASFGPIDLNPTsptyg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 152 -IPVAPPimPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGS 230
Cdd:cd24067 73 yITTTPK--PGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 231 AGdiGHIQVEPDglPCACGNQG-------CLEAHFSGSALArdaeqvAREGRSAELAArleaggrlsaadvaaaasgGDT 303
Cdd:cd24067 151 EM--GHIRVPRH--PDDDGFPGvcpfhgdCLEGLASGPAIA------ARWGIPAEELP-------------------DDH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 304 AALELIrrgGRHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQ-----SLPLATGNLP--IVLGELGPAA 376
Cdd:cd24067 202 PAWDLE---AYYLAQACANLTLTLSPERIVLGGGV-MQRPGLFPRIREKFRKLlngylEVPRLLPDIDeyIVPPALGNDA 277
|
....*...
gi 498326674 377 GVIGGARL 384
Cdd:cd24067 278 GILGALAL 285
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
79-384 |
3.89e-22 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 95.44 E-value: 3.89e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 79 GVDIGATSVDVAVTNAELEVLGHITQPMdvregPVAVFEQVLDMAEKLKASGLAEgFDGAG---IGVPGPVRFPEGIPVA 155
Cdd:PRK13310 4 GFDIGGTKIELGVFNEKLELQWEERVPT-----PRDSYDAFLDAVCELVAEADQR-FGCKGsvgIGIPGMPETEDGTLYA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPImPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:PRK13310 78 ANV-PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDGL----------PCACGNQGCLEAHFSGSALARDAEQVAREGRSA-ELAARLEAggrlsaadvaaaasgGDTA 304
Cdd:PRK13310 157 HMRLPVDALtllgwdaplrRCGCGQKGCIENYLSGRGFEWLYQHYYGEPLQApEIIALYYQ---------------GDEQ 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 305 ALELIRRGGRHTGQVIAGLVSFFNPGLVVIGGGVTGLGHTllaairTQVYRQSLP---LATGNLP-IVLGELGPAAGVIG 380
Cdd:PRK13310 222 AVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLSNFDAI------YEQLPKRLPrhlLPVARVPrIEKARHGDAGGVRG 295
|
....
gi 498326674 381 GARL 384
Cdd:PRK13310 296 AAFL 299
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
78-339 |
2.89e-21 |
|
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: 92.63 E-value: 2.89e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVL--GHITQPMDVREgpvAVFEQVLDMAEKLKasglaEGFDGAGIGVPGPVRFPEGIPVA 155
Cdd:cd24152 3 LVFDIGGTFIKYALVDENGNIIkkGKIPTPKDSLE---EFLDYIKKIIKRYD-----EEIDGIAISAPGVIDPETGIIYG 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIG 235
Cdd:cd24152 75 GGALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 236 HIQVEPDglpcacGNQGCLEAHF-SGSALARDAEQVARE----GRsaELAARLEAggrlsaadvaaaasgGDTAALELIR 310
Cdd:cd24152 155 YLLTDDD------DKDLLFFSGLaSMFGLVKRYNKAKGLepldGE--EIFEKYAK---------------GDEAAKKILD 211
|
250 260
....*....|....*....|....*....
gi 498326674 311 RGGRHTGQVIAGLVSFFNPGLVVIGGGVT 339
Cdd:cd24152 212 EYIRNLAKLIYNIQYILDPEVIVIGGGIS 240
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
76-389 |
9.35e-21 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 91.51 E-value: 9.35e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 76 RFLGVDIGATSVDVAVTNAELEVLGHITQPMDVREGPVAVFEQVLDMAEKLKASglaegFDGAGIGVPGPVRfpEGIPVA 155
Cdd:PRK05082 2 TTLAIDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQAQ-----ADRVAVASTGIIN--DGILTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 156 --PPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAgVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGD 233
Cdd:PRK05082 75 lnPHNLGGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQA-LPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 234 IGHIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARLEAggrlsaadvaaaasgGDTAALELIRRGG 313
Cdd:PRK05082 154 IGHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIFERAGQ---------------GDEQAQALINRSA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVtGLGHTLLAaiRTQVYRQSLPLATgNLPIVLGELGPAAGVIGGARLISDHL 389
Cdd:PRK05082 219 QAIARLIADLKATLDCQCVVLGGSV-GLAEGYLE--LVQAYLAQEPAIY-HVPLLAAHYRHDAGLLGAALWAQGEK 290
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
78-339 |
2.20e-19 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 87.77 E-value: 2.20e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVL--GHITQPMDVREGPVAVFEQVLDMAEKlkasglAEGFDGA-GIGVPGPVRFPEGipV 154
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELfrKRLPTPRDDYQQTIEAIATLVDMAEQ------ATGQRGTvGVGIPGSISPYTG--L 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGW-DGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGD 233
Cdd:PRK09557 75 VKNANSTWlNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 234 IGHIQV---EPDGL------PCACGNQGCLEAHFSGSALARDAEQVAREGRS-AELAARLEAGGRLSaadvaaaasggdT 303
Cdd:PRK09557 155 WGHNPLpwmDEDELryrnevPCYCGKQGCIETFISGTGFATDYRRLSGKALKgSEIIRLVEEGDPVA------------E 222
|
250 260 270
....*....|....*....|....*....|....*..
gi 498326674 304 AALE-LIRRGGRHTGQVIaglvSFFNPGLVVIGGGVT 339
Cdd:PRK09557 223 LAFRrYEDRLAKSLAHVI----NILDPDVIVLGGGMS 255
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
77-260 |
7.48e-18 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 82.38 E-value: 7.48e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHITQPMDvREGPVAVFEQVLDMAEKLKASGLAEGfdGAGIGVPGPVRFPEGIpVAP 156
Cdd:PRK13311 2 YYGFDMGGTKIELGVFDENLQRIWHKRVPTP-REDYPQLLQILRDLTEEADTYCGVQG--SVGIGIPGLPNADDGT-VFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 157 PIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCVKIGTGIGCGIVVGSTVYRGTTGSAGDIGH 236
Cdd:PRK13311 78 ANVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
|
170 180 190
....*....|....*....|....*....|....
gi 498326674 237 IQVEPDGL----------PCACGNQGCLEAHFSG 260
Cdd:PRK13311 158 FRLPVDALdilgadiprvPCGCGHRGCIENYISG 191
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
78-384 |
8.47e-13 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 67.59 E-value: 8.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 78 LGVDIGATSVDVAVTNAELEVLGHITQPMDVREG--PVAVFEQVLDMAEKLKAsglaegFDGAGIGVPGPVRfpEGI-PV 154
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTDTGELLSERIRIPTPQPatPEAVADVVAELVAHFPW------FGPVGVGFPGVVR--RGVvRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 155 APPIMPGWDGFPVREALSQELGCPVMVDNDVNLMAMGEQHAGVARTARDFLCV-KIGTGIGCGIVVGSTVYRGTtgsagD 233
Cdd:cd24058 74 AANLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVLVlTLGTGIGSALFVDGHLVPNT-----E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 234 IGHIQVepDGlpcacgnqgcleahfsgsalaRDAEQVAregrSAELAARLEAGgrlsaadvaaaasggdtaalelIRRGG 313
Cdd:cd24058 149 LGHLEI--RG---------------------KDAEERA----SLGVRAREDLG----------------------WKRWA 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 498326674 314 RHTGQVIAGLVSFFNPGLVVIGGGVTGLghtllaairtqvYRQSLPLATGNLPIVLGELGPAAGVIGGARL 384
Cdd:cd24058 180 KRVNKYLQYLERLFNPDLFIIGGGNSKK------------ADKFLPLLDVKTPVVPAVLRNDAGIVGAALL 238
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
77-383 |
1.48e-05 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 46.41 E-value: 1.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGHIT----QPMDVreGPVAVFEQVLDMAEK-LKASGLAEGFDGAGIGVPGpVRFPEG 151
Cdd:COG2971 3 ILGVDGGGTKTRAVLVDADGEVLGRGRaggaNPQSV--GLEEALASLREALEEaLAAAGDPADIEAVGFGLAG-AGTPED 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 152 IPVappimpgwdgfpVREALSQELG-CPVMVDNDVNLMAMG--EQHAGVArtardflCVkIGTG-IGCGIVVGSTVYR-- 225
Cdd:COG2971 80 AEA------------LEAALRELFPfARVVVVNDALAALAGalGGEDGIV-------VI-AGTGsIAAGRDGDGRTARvg 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 226 ------GTTGSAGDIG-----HIQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARL-----EAggrl 289
Cdd:COG2971 140 gwgyllGDEGSGAWLGrealrAALRALDGRGPPTALTEAVLAEFGLDDPEELIAWVYRGPAPPADLASLaplvfEA---- 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 290 saadvaaaASGGDTAALELIRRGGRHTGQVIAGLVSfFNPGLVVIGGGVTGLGHTLLAAIRTQvyrqslpLATGNLPIVL 369
Cdd:COG2971 216 --------AEAGDPVARAILEEAADELAELARALLE-RGALPVVLAGGVAAAQPLLREALRAR-------LAAGGAEIVP 279
|
330
....*....|....
gi 498326674 370 GELGPAAGVIGGAR 383
Cdd:COG2971 280 PAGDPVDGALLLAL 293
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
77-376 |
6.65e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 38.05 E-value: 6.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 77 FLGVDIGATSVDVAVTNAELEVLGH-ITQPMDVREGPVAVFEQVLDMA--EKLKASGLAEGFDGAGIGvpgpvrfpegip 153
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRgKGGPSNPASVGIEEAKENLKEAvrEALSQAGSLGEIDAICLG------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 154 vappiMPGWDGFPVREALSQEL-----GCPVMVDNDVNLMamgeqHAGVARTARDFLCVkIGTG-IGCGIVVGSTVYR-- 225
Cdd:cd24007 69 -----LAGIDSEEDRERLRSALkelflSGRIIIVNDAEIA-----LAAALGGGPGIVVI-AGTGsVAYGRNGDGEEARvg 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 226 ------GTTGSAGDIGH-----IQVEPDGLPCACGNQGCLEAHFSGSALARDAEQVAREGRSAELAARL-----EAggrl 289
Cdd:cd24007 138 gwghllGDEGSGYWIGRralraALRALDGRGPKTPLLDAILKFLGLDSIEELITAIYRSSDRKKEIASLaplvfEA---- 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 498326674 290 saadvaaaASGGDTAALELIRRGGRHTGQVIAGLVS---FFNPGLVVIGGGVtGLGHTLLAAIRTQVYRQSLPLATGNLP 366
Cdd:cd24007 214 --------AEEGDPVAQAILKEAAEELAKLVVALAKlllLGEKLPLALSGGV-FKNNYYLAEFLEELLKKKKPNAKVVEP 284
|
330
....*....|
gi 498326674 367 IVLGELGPAA 376
Cdd:cd24007 285 KGSPVVGALL 294
|
|
| Lrp |
COG1522 |
DNA-binding transcriptional regulator, Lrp family [Transcription]; |
12-52 |
7.04e-03 |
|
DNA-binding transcriptional regulator, Lrp family [Transcription];
Pssm-ID: 441131 [Multi-domain] Cd Length: 138 Bit Score: 36.68 E-value: 7.04e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 498326674 12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:COG1522 9 RILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVI 49
|
|
| MarR |
COG1846 |
DNA-binding transcriptional regulator, MarR family [Transcription]; |
10-73 |
7.04e-03 |
|
DNA-binding transcriptional regulator, MarR family [Transcription];
Pssm-ID: 441451 [Multi-domain] Cd Length: 142 Bit Score: 36.49 E-value: 7.04e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 498326674 10 QARLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLVVadgLAASRGGRRSHNIRLAP 73
Cdd:COG1846 40 QFRVLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLVE---REPDPEDRRAVLVRLTE 100
|
|
| HTH_24 |
pfam13412 |
Winged helix-turn-helix DNA-binding; |
12-52 |
8.59e-03 |
|
Winged helix-turn-helix DNA-binding;
Pssm-ID: 404317 [Multi-domain] Cd Length: 45 Bit Score: 33.95 E-value: 8.59e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 498326674 12 RLLRLLRDGGAHSRAQLGEEVDLSRSKLAVEVDRLLETGLV 52
Cdd:pfam13412 5 KILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
|
|
|