|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
38-348 |
2.27e-139 |
|
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: 399.04 E-value: 2.27e-139
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEKLRTETPdksKSPKVVEDTIVELVLDLSDRHDVHAVGIGAAGWVDADRNRVLFAPH 117
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPTP---PTADGIVDAIVEAVEELREGHDVSAVGVAAAGFVDADRATVLFAPN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 118 LSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQV 197
Cdd:cd24061 78 IAWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 198 VPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAYGIIEhvKGQIGDITGPMITELARDGDAMCVELLQDIGQWL 277
Cdd:cd24061 158 VPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATPEGAAVLLA--DGSVDGITGKHISEAARAGDPVALDALRELARWL 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692325114 278 GVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGYRPEARIVRAQLGPEAGMVGAADLAR 348
Cdd:cd24061 236 GAGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFERWLPGRGWRPIPRLRTAQLGNDAGLIGAADLAR 306
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
38-348 |
4.36e-112 |
|
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: 329.55 E-value: 4.36e-112
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKVVEDTIVELVLDL-----SDRHDVHAVGIGAAGWVDADRNRV 112
Cdd:COG1940 7 VIGIDIGGTKIKAALVDLDGEVLARERIPTP-AGAGPEAVLEAIAELIEELlaeagISRGRILGIGIGVPGPVDPETGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 113 LFAPHL-SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGE 191
Cdd:COG1940 86 LNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 192 FGHMQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADspvaygiiehvkgqigDITGPMITELARDGDAMCVELLQ 271
Cdd:COG1940 166 IGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGAE----------------KLTAEELFAAARAGDPLALEVLD 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692325114 272 DIGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGyRPEARIVRAQLGPEAGMVGAADLAR 348
Cdd:COG1940 230 EAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPA-REDPRIVPASLGDDAGLLGAAALAL 305
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
39-344 |
1.79e-95 |
|
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: 286.76 E-value: 1.79e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKVVEDTIVELVLDLSDRHDVHAVGIGAAGWVDADRNRVLFA-PH 117
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILEKDSVPTP-ASKGGDAILERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYAtDN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 118 L-SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQ 196
Cdd:cd24068 82 LpGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 197 VVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADspvaygiiehvkgqigDITGPMITELARDGDAMCVELLQDIGQW 276
Cdd:cd24068 162 VDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEP----------------GIDGREIFDLADAGDPLAKEVVEEFAED 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 692325114 277 LGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGYRPeARIVRAQLGPEAGMVGAA 344
Cdd:cd24068 226 LATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDA-TKIEPAKLGNDAGLLGAA 292
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
39-348 |
2.70e-90 |
|
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: 274.47 E-value: 2.70e-90
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPdksKSPKVVEDTI---VELVLDLSDR--HDVHAVGIGAAGWVDADRNRVL 113
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTD---TTPETIVDAIasaVDSFIQHIAKvgHEIVAIGIGAPGPVNRQRGTVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 114 FAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFG 193
Cdd:TIGR00744 78 FAVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 194 HMQVVP-GGHRCPCGNRGCWEQYSSGNALVREARElaaadspvAYGIIEHVKG--QIGD---ITGPMITELARDGDAMCV 267
Cdd:TIGR00744 158 HIRMVPdGRLLCNCGKQGCIETYASATGLVRYAKR--------ANAKPERAEVllALGDgdgISAKHVFVAARQGDPVAV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 268 ELLQDIGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGyRPEARIVRAQLGPEAGMVGAADLA 347
Cdd:TIGR00744 230 DSYREVARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGA-RQVADIIAAQLGNDAGLVGAADLA 308
|
.
gi 692325114 348 R 348
Cdd:TIGR00744 309 R 309
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
39-348 |
2.88e-82 |
|
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: 253.26 E-value: 2.88e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDkSKSPKVVEDTIVELVLDLSDRHDVH-----AVGIGAAGWVDADRNRVL 113
Cdd:cd24076 4 IGVELGVDYITVVVTDLAGEVLWRREVPLPA-SDDPDEVLAQLAALIREALAAAPDSplgilGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 114 FAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFG 193
Cdd:cd24076 83 LAPNLGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 194 HMQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAYgiiehvkgqigditgPMITELARDGDAMCVELLQDI 273
Cdd:cd24076 163 HMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAGGEPLSL---------------AELVEAARAGDPAALAALEEV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692325114 274 GQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGYRPeARIVRAQLGPEAGMVGAADLAR 348
Cdd:cd24076 228 GEYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARD-VRIVVSRLGEDAAALGAAALAI 301
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
39-346 |
3.19e-80 |
|
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: 248.36 E-value: 3.19e-80
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVeDTIVE-----LVLDLSDRHDVHAVGIGAAGWVDADRNRVL 113
Cdd:cd24062 3 VGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENII-TDIAEsiqqlLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 114 FAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAE-WRfGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:cd24062 82 VAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEmWK-GAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVP-GGHRCPCGNRGCWEQYSSGNALVREARE-LAAADSPVAYGIIEHVkgqiGDITGPMITELARDGDAMCVELL 270
Cdd:cd24062 161 GHITVNPeGGAPCNCGKTGCLETVASATGIVRIAREeLEEGKGSSALRILALG----GELTAKDVFEAAKAGDELALAVV 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692325114 271 QDIGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRgYRPEARIVRAQLGPEAGMVGAADL 346
Cdd:cd24062 237 DTVARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPR-VRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
39-348 |
4.17e-79 |
|
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: 244.94 E-value: 4.17e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKVVEDTIVELVLDLSDR-HDVHAVGIGAAGWVDADRNRVLFAPH 117
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTP-TTTTEETLVDAIAFFVDSAQRKfGELIAVGIGSPGLISPKYGYITNTPN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 118 LSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQV 197
Cdd:pfam00480 80 IGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 198 VPGGHRCPCGNRGCWEQYSSGNALVRearelaaadspvAYGIIEHvkgqigDITGPMITELARDGDAMCVELLQDIGQWL 277
Cdd:pfam00480 160 DPNGPKCGCGNHGCLETIASGRALEK------------RYQQKGE------DLEGKDIIVLAEQGDEVAEEAVERLARYL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692325114 278 GVGIANLAAALDPSCFVVGGGVSAADDLLiGPARDAFKRHLTGRGYRPEARIVRAQLGPEAGMVGAADLAR 348
Cdd:pfam00480 222 AKAIANLINLFDPQAIVLGGGVSNADGLL-EAIRSLVKKYLNGYLPVPPVIIVAASLGDNAGALGAAALAK 291
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
39-344 |
2.21e-74 |
|
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: 230.81 E-value: 2.21e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDkSKSPKVVEDTIVELVLDLSDRH----DVHAVGIGAAGWVDADRNRVLF 114
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPA-EEGPEAVLDRIAELIEELLAEAgvreRILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 115 APHLS-WRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFG 193
Cdd:cd23763 80 APNLPwWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 194 HMQVVpgghrcpcgnrgcweqyssgnalvrearelaaadspvaygiiehvkgqigditgpmitelardgdamcvellQDI 273
Cdd:cd23763 160 HITVL------------------------------------------------------------------------EEA 167
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 692325114 274 GQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHlTGRGYRPEARIVRAQLGPEAGMVGAA 344
Cdd:cd23763 168 ARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRR-ALPPLRRRVRIVPSELGDDAGLLGAA 237
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
38-347 |
5.70e-72 |
|
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: 227.05 E-value: 5.70e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEklRTETPDKSKSPKVVEDTIVELVLDLS-----DRHDVHAVGIGAAGWVDADRNRV 112
Cdd:cd24073 3 VVGVKLTEDRITAVLTDLRGNVLA--SHTLPLDSGDPEAVAEAIAEAVAELLaqaglSPDRLLGIGVGLPGLVDAETGIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 113 LFAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:cd24073 81 RWSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAygiIEHVkgqigditgpmiTELARDGDAMCVELLQD 272
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLRGEPLT---IEDL------------LAAARAGDPAARAILRR 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692325114 273 IGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGrGYRPEARIVRAQLGPEAGMVGAADLA 347
Cdd:cd24073 226 AGRALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFP-GLASDLELVIHPWGDEAWARGAAALA 299
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
37-344 |
1.23e-71 |
|
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: 225.67 E-value: 1.23e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 37 PTVGIDIGGTKVMAGVVDaDGNILEKLRTETPDKSKSPkvVEDTIVELVLDLSDRH-DVHAVGIGAAGWVDADRNRVLFA 115
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTPREGGEA--VLDALARAVEALQAEApGVEAVGLGVPGPLDFRRGRVRFA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 PHL-SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGH 194
Cdd:cd24065 78 PNIpGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 195 MQVVPGGHRCPCGNRGCWEQYSSGNALVREARelaaadspvaygiieHVKGQigDITGPMITELARDGDAMCVELLQDIG 274
Cdd:cd24065 158 TTVLPGGPMCGCGLVGCLEALASGRALARDAS---------------FAYGR--PMSTAELFELAQQGEPKALRIVEQAA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 275 QWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGrgyRPEARIVRAQLGPEAGMVGAA 344
Cdd:cd24065 221 AHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYTEG---WHAPPLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
38-347 |
3.72e-69 |
|
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: 219.76 E-value: 3.72e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEKLRTETPDKsKSPKVVEDTIVELVLDLSDRHD----VHAVGIGAAGWVDADRNRVL 113
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEK-ENPEEVLEKLYELIDRLLEKENikskILGIGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 114 FAPHLS-WRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:cd24059 82 NPPNFPgWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVPGGHRCPCGNRGCWEQYSSGNALVREARElaaadspvaygiiehvKGQIGDITGPMITELARDGDAMCVELLQD 272
Cdd:cd24059 162 GHTSIDINGPRCSCGNRGCLELYASIPAIEKKARS----------------ALGSGRSFQLDIVEALQKGDPIADEVIEE 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692325114 273 IGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGYRpEARIVRAQLGPEAGMVGAADLA 347
Cdd:cd24059 226 AAKYLGIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAR-EVRILKSSLGEDAPLLGAAALV 299
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
39-344 |
2.10e-66 |
|
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: 212.74 E-value: 2.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVEDtIVELVLDLSDRHDVHAVGIGAAGWVDADRNRVLFAPHL 118
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINR-IAETVNELIEEMELLGIGIGSPGSIDRENGIVRFSPNF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 119 -SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQV 197
Cdd:cd24064 81 pDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 198 VPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAYGIIEhvkgqigDITGPMITELARDGDAMCVELLQDIGQWL 277
Cdd:cd24064 161 EPNGPICGCGNRGCVEAFASATAIIRYARESRKRYPDSLAGESE-------KINAKHVFDAARKNDPLATMVFRRVVDAL 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692325114 278 GVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHlTGRGYRPEARIVRAQLGPEAGMVGAA 344
Cdd:cd24064 234 AIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKY-VMLSFQDTYSIELSNLVEDAGILGAA 299
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
39-347 |
3.95e-66 |
|
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: 212.15 E-value: 3.95e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVEdTIVELVLDLSDRHDV--HAVGIGAA--GWVDADRNRVLF 114
Cdd:cd24071 4 IGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIE-LIAENIKKLIKNKHVekKLLGIGIAvsGLVDSKKGIVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 115 APHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGH 194
Cdd:cd24071 83 STILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 195 MQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAYgiiehvkGQIGDITGPMITELARDGDAMCVELLQDIG 274
Cdd:cd24071 163 MTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSLL-------KELEDFEIEKVREAAEEGDSVATELFKKAG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692325114 275 QWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGYRpEARIVRAQLGPEAGMVGAADLA 347
Cdd:cd24071 236 EYLGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGR-NVIILVDSLGEDAWVLGAALLV 307
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
39-346 |
1.08e-65 |
|
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: 211.04 E-value: 1.08e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKVVEDTIVELVLDL---SDRHDVHAVGIGAAGWVDADRNRVLFA 115
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTP-KTGDPGTVSEQVLGLIETLlskAGKDSIEGIGVSSAGPLDLRKGTIVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 PHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHM 195
Cdd:cd24063 82 PNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 196 QVVPGGH-RCPCGNRGCWEQYSSGNALVREARELAAADSpvaYGIIEHVKGQIGD-ITGPMITELARDGDAMCVELLQDI 273
Cdd:cd24063 162 VVDTESGlKCGCGGYGHWEAFASGRGIPRFAREWAEGFS---SRTSLKLRNPGGEgITAKEVFSAARKGDPLALKIIEKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692325114 274 GQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLtgRGYRPeARIVRAQLGPEAGMVGAADL 346
Cdd:cd24063 239 ARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKNP--AISKG-PEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
39-348 |
3.17e-54 |
|
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: 180.82 E-value: 3.17e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVEdTIVELVLDLSDRHDVH--AVGIGAAGWVDADRNRVLFAP 116
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVE-VLADLIREYIEEAGLKpaAIVIGVPGTVDKDRRTVISTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 117 HL-SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHM 195
Cdd:cd24070 83 NIpGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 196 QVVPGGHRCPCGNRGCWEQYSSGNALVREARElaaadspvaygiiEHVKGQIGDItgpmiteLARDGDAmcvELLQDIGQ 275
Cdd:cd24070 163 PVYGNGKPCGCGNTGCLETYASGRALEEIAEE-------------HYPDTPILDI-------FVDHGDE---PELDEFVE 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692325114 276 WLGVGIANLAAALDPSCFVVGGGVSAADDLligPaRDAFKRHLTGRGYRPEAR----IVRAQLGPEAGMVGAADLAR 348
Cdd:cd24070 220 DLALAIATEINILDPDAVILGGGVIDMKGF---P-RETLEEYIRKHLRKPYPAdnlkIIYAELGPEAGVIGAAIYAF 292
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
40-343 |
2.13e-52 |
|
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: 175.83 E-value: 2.13e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 40 GIDIGGTKVMAGVVDADGNILEKLRTETPDKSKspkvveDTIVELVLDLSDRHD--VHAVGIGAAGWVDADRNRVLFAPH 117
Cdd:cd24152 4 VFDIGGTFIKYALVDENGNIIKKGKIPTPKDSL------EEFLDYIKKIIKRYDeeIDGIAISAPGVIDPETGIIYGGGA 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 118 LSW-RNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQ 196
Cdd:cd24152 78 LPYlKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 197 VVPGGHrcpcgNRGCWEQYSSGNALVREARElaAADSPVAYGIIehvkgqigditgpmITELARDGDAMCVELLQDIGQW 276
Cdd:cd24152 158 TDDDDK-----DLLFFSGLASMFGLVKRYNK--AKGLEPLDGEE--------------IFEKYAKGDEAAKKILDEYIRN 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 692325114 277 LGVGIANLAAALDPSCFVVGGGVSAADDLLigparDAFKRHLT-----GRGYRPEARIVRAQLGPEAGMVGA 343
Cdd:cd24152 217 LAKLIYNIQYILDPEVIVIGGGISEQPLFI-----EDLKKEVNeilanRPGSIPKPEIKACKFGNDANLLGA 283
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
40-344 |
4.59e-51 |
|
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: 172.80 E-value: 4.59e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 40 GIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVveDTIVELVLDLSDRHDVHA-VGIGAAGWVDADRNRVLFAPHL 118
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAFL--AAIAELVAEADARFGVKGpVGIGIPGVIDPEDGTLITANIP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 119 SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQVV 198
Cdd:cd24057 82 AAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 199 PGG---------HRCPCGNRGCWEQYSSGNALVREARelaaadspvaygiieHVKGQigDITGPMITELARDGDAMCVEL 269
Cdd:cd24057 162 ADAlllgydlpvLRCGCGQTGCLETYLSGRGLERLYA---------------HLYGE--ELDAPEIIAAWAAGDPQAVAH 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692325114 270 LQDIGQWLGVGIANLAAALDPSCFVVGGGVSAADDlLIGPARDAFKRHLTGRGYRPeaRIVRAQLGPEAGMVGAA 344
Cdd:cd24057 225 VDRWLDLLAGCLANILTALDPDVVVLGGGLSNFPA-LIAELPAALPAHLLSGARTP--RIVPARHGDAGGVRGAA 296
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
37-306 |
7.58e-49 |
|
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: 167.21 E-value: 7.58e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 37 PTVGIDIGGTKVMAGVVDADGNILEKLrTETPDKSKSPKVVEDTIVELVLDLSD--RHDVHAVGIGAAGWVDADRNRVLF 114
Cdd:cd24072 2 WVLGIVVSPNSLRAQVGNACGELLGEF-EYRVITLETPEALIDEIIDCIDRLLKlwKDRVKGIALAIQGLVDSHKGVSLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 115 APHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGH 194
Cdd:cd24072 81 SPGAPWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 195 MQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAygiiehvkgQIGDITGPMITELARDGDAMCVELLQDIG 274
Cdd:cd24072 161 TKVNPDGARCDCGRRGCLETVASNSALKRNARVTLKLGPVSA---------DPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270
....*....|....*....|....*....|...
gi 692325114 275 QWLGVGIANLAAALDPS-CFVVGGGVSAADDLL 306
Cdd:cd24072 232 NAIGRSLANILNLLNPEqVLLYGRGCRAGDLLL 264
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
41-346 |
3.44e-47 |
|
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: 162.07 E-value: 3.44e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 41 IDIGGTKVMAGVVDaDGNILEKLRTETPdKSKSPKVVEDTIVELVLDLSDRHDvhAVGIGAAGWVDADRNRVLFAPHLSW 120
Cdd:cd24069 3 IDIGGTKIAAALIG-NGQIIDRRQIPTP-RSGTPEALADALASLLADYQGQFD--RVAVASTGIIRDGVLTALNPKNLGG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 121 RNE-PLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQVVP 199
Cdd:cd24069 79 LSGfPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 200 GGHRCPCGNRGCWEQYSSGNALVREARELAAAdspvaygiiehvkgqigDITGPMITELARDGDAMCVELLQDIGQWLGV 279
Cdd:cd24069 159 PGPVCGCGRRGCVEAIASGTAIAAAASEILGE-----------------PVDAKDVFERARSGDEEAARLIDRAARALAD 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 692325114 280 GIANLAAALDPSCFVVGGGVSAADDLLigpARDAFKRHLTGRGYRPEarIVRAQLGPEAGMVGAADL 346
Cdd:cd24069 222 LIADLKATLDLDCVVIGGSVGLAEGFL---ERVEQYLADEPAIFRVS--LEPARLGQDAGLLGAALL 283
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
38-295 |
1.16e-46 |
|
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: 161.17 E-value: 1.16e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPkvVEDTIVELVLDLSDR-----HDVHAVGIGAAGWVDadRNRV 112
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFEN--ILEILKSIIQELISQapktpYGLVGIGIGIHGIVD--ENEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 113 LFAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRgeDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:cd24077 79 IFTPYYDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDY--DNLISISIHSGIGAGIIINNQLYRGYNGFAGEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVPGGHRCPCGNRGCWEQYSSGNALVREARElaaadspvaygiiehvKGQIGDITGPMITELARDGDAMCVELLQD 272
Cdd:cd24077 157 GHMIIVPNGKPCPCGNKGCLEQYASEKALLKELSE----------------KKGLETLTFDDLIQLYNEGDPEALELIDQ 220
|
250 260
....*....|....*....|...
gi 692325114 273 IGQWLGVGIANLAAALDPSCFVV 295
Cdd:cd24077 221 FIKYLAIGINNIINTFNPEIIII 243
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
41-346 |
1.33e-46 |
|
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: 161.43 E-value: 1.33e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 41 IDIGGTKVMAGVVDADGNILEKLRTETPdksKSPKVVEDTIVELVLDLSDRHD-----VHAVGIGAAGWVDADRNRVLFA 115
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPNP---KTYEERIDLILQMCVEAASEAVklncrILGVGISTGGRVNPREGIVLHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 PHL--SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFG 193
Cdd:cd24060 82 TKLiqEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 194 HMQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVAYGIIEHvKGQIgdITGPMITELARDGDAMCVELLQDI 273
Cdd:cd24060 162 HIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEDLLLVEGMSVT-NDEE--VTAKHLIQAAKLGNAKAQKILRTA 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 692325114 274 GQWLGVGIANLAAALDPSCFVVGGGVSaadDLLIGPARDAFKRHltGRGYRPEARIVRAQLgPEAGMVGAADL 346
Cdd:cd24060 239 GTALGLGIVNILHTLNPSLVILSGVLA---SHYENIVKDVIAQR--ALPSVQNVDVVVSDL-VDPALLGAASM 305
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
39-344 |
1.99e-42 |
|
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: 150.05 E-value: 1.99e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVveDTIVELVLDLSDR-HDVHAVGIGAAGWVDAdRNRVLFAPH 117
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEATL--DAIADLVEEAEEElGAPATVGIGTPGSISP-RTGLVKNAN 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 118 LSWRN-EPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHMQ 196
Cdd:cd24066 79 STWLNgKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 197 VVPG------GHRCPCGNRGCWEQYSSGNALVREARELAAADSPvaygiiehvkgqigditGPMITELARDGDAMCVELL 270
Cdd:cd24066 159 LPWPdedelpGPPCYCGKRGCVETFLSGPALERDYARLTGKTLS-----------------AEEIVALARAGDAAAVATL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692325114 271 QDIGQWLGVGIANLAAALDPSCFVVGGGVSAAdDLLIGPARDAFKRHLTGRgyRPEARIVRAQLGPEAGMVGAA 344
Cdd:cd24066 222 DRFLDRLGRALANVINILDPDVIVLGGGLSNI-DELYTEGPAALARYVFSD--EVETPIVKNKHGDSSGVRGAA 292
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
38-348 |
3.87e-42 |
|
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: 149.82 E-value: 3.87e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEKlRTEtPDKSKSPKVVEDTIVELVLDL-----SDRHDVHAVGIGAAGWVDADRNRV 112
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAE-HTV-PLTALNQEALLSQLIEEIAQFlkshrRKTQRLIAISITLPGLINPKTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 113 LFAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:cd24075 81 HYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAAdspvayGIIEHVKGQigDITGPMITELARDGDAMCVELLQD 272
Cdd:cd24075 161 GHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQ------GYASQLTLQ--DCTIKDICQAALNGDQLAQDVIKR 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692325114 273 IGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIgPARDAFKRHLTGRGYRPEARIVRAQLGPEAgMVGAADLAR 348
Cdd:cd24075 233 AGRYLGKVIAILINLLNPQKIIIAGEITQADKVLL-PVIKKCIQSQALPDFRQELKIVASQLDHNS-AIGAFALVK 306
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
37-348 |
1.38e-37 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 136.97 E-value: 1.38e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 37 PTVGIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKVVEDTIVELVLDLsdRHDVHAVGIGAAGWVdadRNRVLFA- 115
Cdd:PRK05082 2 TTLAIDIGGTKIAAALVGEDGQIRQRRQIPTP-ASQTPEALRQALSALVSPL--QAQADRVAVASTGII---NDGILTAl 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 -PH-LSWRNE-PLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDhLVMITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:PRK05082 76 nPHnLGGLLHfPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRN-MVFITVSTGVGGGIVLNGKLLTGPGGLAGHI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVPGGHRCPCGNRGCWEQYSSGNALVREArelaaadspvaygiiehvKGQIGDITGPMITELARDGDAMCVELLQD 272
Cdd:PRK05082 155 GHTLADPHGPVCGCGRRGCVEAIASGRAIAAAA------------------QGWLAGCDAKTIFERAGQGDEQAQALINR 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692325114 273 IGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLigPARDAFKRHLTGrGYRPEarIVRAQLGPEAGMVGAADLAR 348
Cdd:PRK05082 217 SAQAIARLIADLKATLDCQCVVLGGSVGLAEGYL--ELVQAYLAQEPA-IYHVP--LLAAHYRHDAGLLGAALWAQ 287
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
39-348 |
2.00e-35 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 131.64 E-value: 2.00e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNIL--EKLRTETPDKSKSPKVVEDTIVELVLDLSDRhdVHAVGIGAAGWVDADRNRVLFAP 116
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILhcEKKRTAEVIAPDLVSGLGEMIDEYLRRFNAR--CHGIVMGFPALVSKDRRTVISTP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 117 HLSWRNE---PLRDRVADRLAVPVLVDNDANTAAwaEWRFGAGRGEDHLVM-ITLGTGIGGAILEDGQVKRGKFGVAGEF 192
Cdd:PRK09698 85 NLPLTALdlyDLADKLENTLNCPVFFSRDVNLQL--LWDVKENNLTQQLVLgAYLGTGMGFAVWMNGAPWTGAHGVAGEL 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 193 GHMQVVPGGHRCPCGNRGCWEQYSSGNALVREARElaaadspvaygiiehvkgQIGDItgPMITELARDGDAmcvELLQD 272
Cdd:PRK09698 163 GHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQ------------------QPRDY--PLSDLFVHAGDH---PFIQS 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692325114 273 IGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIGPARDAFKRHLTGRGYRPEARIVRAQLGPEAGMVGAADLAR 348
Cdd:PRK09698 220 LLENLARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRKPLPYEVVRFIYASSSDFNGAQGAAILAH 295
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
39-346 |
2.52e-35 |
|
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: 130.74 E-value: 2.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLR--TETPdkskspkvvEDTIVELVLDLSDRHD-VHAVGIGAAGWVDADRN----- 110
Cdd:cd24067 2 GGIEAGGTKFVCAVGTGDGNIIERTEfpTTTP---------EETLQAVIDFFREQEEpIDAIGIASFGPIDLNPTsptyg 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 111 RVLFAPHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKfgVAG 190
Cdd:cd24067 73 YITTTPKPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGL--LHP 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 191 EFGHMQVVPggHR--------CPCGNrGCWEQYSSGNALvrEARelaaadspvaygiiehvkgqigdiTGPMITELARDG 262
Cdd:cd24067 151 EMGHIRVPR--HPdddgfpgvCPFHG-DCLEGLASGPAI--AAR------------------------WGIPAEELPDDH 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 263 DAMCVEllqdiGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLiGPARDAFKRHLTGRGYRPEAR------IVRAQLGP 336
Cdd:cd24067 202 PAWDLE-----AYYLAQACANLTLTLSPERIVLGGGVMQRPGLF-PRIREKFRKLLNGYLEVPRLLpdideyIVPPALGN 275
|
330
....*....|
gi 692325114 337 EAGMVGAADL 346
Cdd:cd24067 276 DAGILGALAL 285
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
40-346 |
7.77e-34 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 127.41 E-value: 7.77e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 40 GIDIGGTKVMAGVVDADgniLEKL---RTETPDKSKSPKVveDTIVELVLDLSDRHDVH-AVGIGAAGWVDADRNRVLFA 115
Cdd:PRK13310 4 GFDIGGTKIELGVFNEK---LELQweeRVPTPRDSYDAFL--DAVCELVAEADQRFGCKgSVGIGIPGMPETEDGTLYAA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 PHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEwrfgAGRGEDH---LVM-ITLGTGIGGAILEDGQVKRGKFGVAGE 191
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSE----AWDDEFTqypLVMgLILGTGVGGGLVFNGKPISGRSYITGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 192 FGHMQV------VPGG----HRCPCGNRGCWEQYSSGNALvrearELaaadspvaygIIEHVKGQigDITGPMITELARD 261
Cdd:PRK13310 155 FGHMRLpvdaltLLGWdaplRRCGCGQKGCIENYLSGRGF-----EW----------LYQHYYGE--PLQAPEIIALYYQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 262 GDAMCVELLQDIGQWLGVGIANLAAALDPSCFVVGGGVSAAdDLLIGPARDAFKRHLTGRGYRPeaRIVRAQLGPEAGMV 341
Cdd:PRK13310 218 GDEQAVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLSNF-DAIYEQLPKRLPRHLLPVARVP--RIEKARHGDAGGVR 294
|
....*
gi 692325114 342 GAADL 346
Cdd:PRK13310 295 GAAFL 299
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
41-306 |
1.12e-31 |
|
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: 122.03 E-value: 1.12e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 41 IDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPkvVEDTIVELVLDLSDRHD-----VHAVGIGAAGWVDADRNRVLFA 115
Cdd:cd24074 7 IRIGRGYITLALRDLNGRLLAEERYPLPAKDNDP--FLDRLLESISEFFSRHQkklerLTAIAITLPGIIDPESGIVHRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 PHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGHM 195
Cdd:cd24074 85 PFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHT 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 196 QVVPGGHRCPCGNRGCWEQYSSGNALVREARELAAADSPVaygiIEHVKgqigDITGPMITELARDGDAMCVELLQDIGQ 275
Cdd:cd24074 165 QIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQSPDS----MLHGQ----PISIESLCQAALAGDPLAQDIIIQVGR 236
|
250 260 270
....*....|....*....|....*....|.
gi 692325114 276 WLGVGIANLAAALDPSCFVVGGGVSAADDLL 306
Cdd:cd24074 237 HLGRILAILVNLFNPEKILIGSPLNNAAEIL 267
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
38-347 |
1.82e-30 |
|
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: 116.51 E-value: 1.82e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNIL--EKLRTETPDKSkSPKVVEDTIVELVLDLSDRHDVhavGIGAAGWVDadRNRVLFA 115
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDTDTGELlsERIRIPTPQPA-TPEAVADVVAELVAHFPWFGPV---GVGFPGVVR--RGVVRTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 116 PHL--SWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLV-MITLGTGIGGAILEDGQVkrgkfgVAG-E 191
Cdd:cd24058 75 ANLdkSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVlVLTLGTGIGSALFVDGHL------VPNtE 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 192 FGHMQVvpgghrcpcgNRGCWEQYSSgnALVREARELaaadSPVAYgiiehvkgqigditgpmitelardgdamcvellq 271
Cdd:cd24058 149 LGHLEI----------RGKDAEERAS--LGVRAREDL----GWKRW---------------------------------- 178
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 692325114 272 diGQWLGVGIANLAAALDPSCFVVGGGVSAADdlligparDAFKRHLTGRgyrpeARIVRAQLGPEAGMVGAADLA 347
Cdd:cd24058 179 --AKRVNKYLQYLERLFNPDLFIIGGGNSKKA--------DKFLPLLDVK-----TPVVPAVLRNDAGIVGAALLA 239
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
39-344 |
1.50e-23 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 99.33 E-value: 1.50e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKVVeDTIVELVLDLSDRHDVHA-VGIGAAGWVDADRNRVLFApH 117
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTP-RDDYQQTI-EAIATLVDMAEQATGQRGtVGVGIPGSISPYTGLVKNA-N 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 118 LSWRN-EPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGH-- 194
Cdd:PRK09557 80 STWLNgQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGHnp 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 195 ---MQ----VVPGGHRCPCGNRGCWEQYSSGNALVREARELAA-ADSpvaygiiehvkgqigditGPMITELARDGDAMC 266
Cdd:PRK09557 160 lpwMDedelRYRNEVPCYCGKQGCIETFISGTGFATDYRRLSGkALK------------------GSEIIRLVEEGDPVA 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 692325114 267 VELLQDIGQWLGVGIANLAAALDPSCFVVGGGVSAADDLLIG-PARdaFKRHLTGRGYRPEarIVRAQLGPEAGMVGAA 344
Cdd:PRK09557 222 ELAFRRYEDRLAKSLAHVINILDPDVIVLGGGMSNVDRLYPTlPAL--LKQYVFGGECETP--VRKALHGDSSGVRGAA 296
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
40-221 |
2.86e-19 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 86.24 E-value: 2.86e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 40 GIDIGGTKVMAGVVDADGNILEKLRTETPdKSKSPKvvedtIVELVLDLSDRHDVH-----AVGIGAAGWVDADRNRVLF 114
Cdd:PRK13311 4 GFDMGGTKIELGVFDENLQRIWHKRVPTP-REDYPQ-----LLQILRDLTEEADTYcgvqgSVGIGIPGLPNADDGTVFT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 115 APHLSWRNEPLRDRVADRLAVPVLVDNDANTAAWAEWRFGAGRGEDHLVMITLGTGIGGAILEDGQVKRGKFGVAGEFGH 194
Cdd:PRK13311 78 ANVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 692325114 195 MQV--------------VPgghrCPCGNRGCWEQYSSGNAL 221
Cdd:PRK13311 158 FRLpvdaldilgadiprVP----CGCGHRGCIENYISGRGF 194
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
39-348 |
3.51e-15 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 75.30 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTE-----TPDKSKSPKVVEDTIVELVLDLSDRHDVHAVGIGAAGwVDADRNRvl 113
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLGRGRAGganpqSVGLEEALASLREALEEALAAAGDPADIEAVGFGLAG-AGTPEDA-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 114 faphlswrnEPLRDRVADR-LAVPVLVDNDANTAAwaewrFGAGRGEDHLVMItLGTG-IGGAILEDGQVKRgkfgvage 191
Cdd:COG2971 81 ---------EALEAALRELfPFARVVVVNDALAAL-----AGALGGEDGIVVI-AGTGsIAAGRDGDGRTAR-------- 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 192 fghmqvVPG-GHrcPCGNRGcweqysSGNALVREA----------RE---------LAAADSPVAYGIIEHV------KG 245
Cdd:COG2971 138 ------VGGwGY--LLGDEG------SGAWLGREAlraalraldgRGpptalteavLAEFGLDDPEELIAWVyrgpapPA 203
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 246 QIGDITgPMITELARDGDAMCVELLQDIGQWLgVGIANLAAALDPSCFVVGGGVSAADDLLigpaRDAFKRHLTGRGyrp 325
Cdd:COG2971 204 DLASLA-PLVFEAAEAGDPVARAILEEAADEL-AELARALLERGALPVVLAGGVAAAQPLL----REALRARLAAGG--- 274
|
330 340
....*....|....*....|...
gi 692325114 326 eARIVRAQLGPeagMVGAADLAR 348
Cdd:COG2971 275 -AEIVPPAGDP---VDGALLLAL 293
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
39-344 |
3.63e-12 |
|
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. Glucokinases are mainly found in invertebrates and microorganisms and highly specific for glucose. Glucokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466858 [Multi-domain] Cd Length: 313 Bit Score: 66.48 E-value: 3.63e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVEdtIVELVLDLSDRHDVHAVGIGAAGWVDADRNRVlfaPHL 118
Cdd:cd24008 2 LVGDIGGTNARLALADAGDGSGDLLFVRKYPSADFASLED--ALAAFLAELGAPRPKAACIAVAGPVDGGRVRL---TNL 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 119 SWRNEplRDRVADRL-AVPVLVDNDANTAAWA---------EWRFGAGRGEDHLVMITL--GTGIGGAILEDGQVKRGKF 186
Cdd:cd24008 77 DWSID--AAELRKALgIGRVRLLNDFEAAAYGlpalgpedlLVLYGGGGPLPGGPRAVLgpGTGLGVALLVPDGDGGYVV 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 187 gVAGEFGHMQVVPGG---------HRCPCGNRGCWEQYSSGNALVREARELAAADSPVAygiiehvkgqiGDITGPMITE 257
Cdd:cd24008 155 -LPSEGGHADFAPVTeeeaellefLRKRFGRSVSYEDVLSGPGLENIYEFLAKLDGAEP-----------PDLTAEEIAE 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 258 LARDGDAMCVELLQDIGQWLGVGIANLAAALDPS--CFVVGG-GVSAADDLLIGPARDAFKRHLTGRGYRpeARI-VRAQ 333
Cdd:cd24008 223 AALAGDPLAREALDLFARILGRFAGNLALSFLATggVYLAGGiAPKNLDLLDSSAFREAFLDKGRMSDLL--EDIpVYLV 300
|
330
....*....|.
gi 692325114 334 LGPEAGMVGAA 344
Cdd:cd24008 301 TNEDLGLLGAA 311
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
39-339 |
3.16e-11 |
|
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: 63.48 E-value: 3.16e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPD-KSKSPKVVEDTIVELVLDL----SDRHDVHAVGIGAAG-WVDADRNRv 112
Cdd:cd24007 2 LGVDGGGTKTRAVLADEDGKILGRGKGGPSNpASVGIEEAKENLKEAVREAlsqaGSLGEIDAICLGLAGiDSEEDRER- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 113 lfaphlswrnepLRDRVADRL-AVPVLVDNDANTAAWAEWRFGAGrgedhlVMITLGTG-IGGAILEDGQVKRgkfgvAG 190
Cdd:cd24007 81 ------------LRSALKELFlSGRIIIVNDAEIALAAALGGGPG------IVVIAGTGsVAYGRNGDGEEAR-----VG 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 191 EFGHMqvvpgghrcpCGNRGcweqysSGNALVREA-RELAAA------DSPVAYGIIEH------------------VKG 245
Cdd:cd24007 138 GWGHL----------LGDEG------SGYWIGRRAlRAALRAldgrgpKTPLLDAILKFlgldsieelitaiyrssdRKK 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 246 QIGDITgPMITELARDGDAMCVELLQDIGQWLGVGIANLAAALD---PSCFVVGGGVSAADDLLIgpardAFKRHLTGRG 322
Cdd:cd24007 202 EIASLA-PLVFEAAEEGDPVAQAILKEAAEELAKLVVALAKLLLlgeKLPLALSGGVFKNNYYLA-----EFLEELLKKK 275
|
330
....*....|....*..
gi 692325114 323 YrPEARIVRAQLGPEAG 339
Cdd:cd24007 276 K-PNAKVVEPKGSPVVG 291
|
|
| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
39-297 |
3.17e-08 |
|
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.
Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 54.46 E-value: 3.17e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVEDTIVELV--------LDLSDRHDVHAvGIGAAG-WVDADR 109
Cdd:cd24082 3 IGIDGGGTKCRARLADADGTVLGEATGGPANLSSDLDQAWASILAAIkqalaqagLDAAALSDLHA-GLGLAGaNVPEAR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 110 NRVLFAPHlswrnePLRDrvadrlavpVLVDNDANTAAwaewrFGAGRGEDHlVMITLGTGIGGAILEDGQVKRGkfgva 189
Cdd:cd24082 82 AAFLAALP------PFAS---------LVVVSDAHIAC-----LGAHGGEDG-AIIILGTGSVGAALDGGEVRQV----- 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 190 gefghmqvvpGGHRCPCGNRGcweqysSGNALVREA--RELAAAD-----SPVAYGIIEHVKGQIGDITG---------- 252
Cdd:cd24082 136 ----------GGWGFPLGDEG------SGAWLGLRAlrHTLLALDglapsSPLTRAVLARFGGDPAEIVAwantatpadf 199
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 692325114 253 ----PMITELARDGDAMCVELLQDIGQWLGVGIANLAAALDPSCFVVGG 297
Cdd:cd24082 200 aalaPLVFEAAEQGDPVALAILQEAAAYIERLLRALGAQGALPLCLLGG 248
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
39-133 |
7.68e-05 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466793 [Multi-domain] Cd Length: 443 Bit Score: 44.50 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVE-------DTIVELVLDLSDRHDVHAV-GIGAAGW------ 104
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASASRETPLIHPGPGWAEldpeelwEAVKEAIREAAAQAGPDPIaAISVSSQgesgvp 82
|
90 100 110
....*....|....*....|....*....|..
gi 692325114 105 VDADRNRVlfAPHLSW---RNEPLRDRVADRL 133
Cdd:cd07773 83 VDRDGEPL--GPAIVWfdpRGKEEAEELAERI 112
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
38-123 |
1.67e-04 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466796 [Multi-domain] Cd Length: 436 Bit Score: 43.36 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDAD-GNILEKLRTETPDKSKS---------PKVVEDTIVELVLDLSDRHDVHAVGIGAAG---- 103
Cdd:cd07777 2 VLGIDIGTTSIKAALLDLEsGRILESVSRPTPAPISSddpgrseqdPEKILEAVRNLIDELPREYLSDVTGIGITGqmhg 81
|
90 100
....*....|....*....|..
gi 692325114 104 --WVDADRNRVlfAPHLSWRNE 123
Cdd:cd07777 82 ivLWDEDGNPV--SPLITWQDQ 101
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
39-166 |
2.34e-03 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 39.82 E-value: 2.34e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVE-------DTIVELVLDLSDRH-----DVHAVGIGAAGW-- 104
Cdd:COG1070 4 LGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPHPGWAEqdpedwwEAVVEAIRELLAKAgvdpeEIAAIGVSGQMHgl 83
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 692325114 105 --VDADrnrvlfaphlswrNEPLRdrvadrlavPVLVDNDANTAAWAEWRFGAGrGEDHLVMIT 166
Cdd:COG1070 84 vlLDAD-------------GEPLR---------PAILWNDTRAAAEAAELREEL-GEEALYEIT 124
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
39-112 |
3.69e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 39.07 E-value: 3.69e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 39 VGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVE-------DTIVELVLDLSDRHDVHA---VGIGAAG----- 103
Cdd:cd07802 3 LGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGWAErdmdelwQATAEAIRELLEKSGVDPsdiAGVGVTGhgngl 82
|
90
....*....|
gi 692325114 104 W-VDADRNRV 112
Cdd:cd07802 83 YlVDKDGKPV 92
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
38-102 |
3.79e-03 |
|
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 39.08 E-value: 3.79e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVE---DTIVELVLDL-------SDRHDVHAVGIGAA 102
Cdd:cd07770 2 ILGIDIGTTSTKAVLFDEDGRVVASSSAEYPLIRPEPGWAEqdpEEILEAVLEAlkevlakLGGGEVDAIGFSSA 76
|
|
| ASKHA_NBD_FGGY_NaCK-like |
cd07772 |
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and ... |
41-124 |
7.45e-03 |
|
nucleotide-binding domain (NBD) of Novosphingobium aromaticivorans carbohydrate kinase and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to carbohydrate kinase from Novosphingobium aromaticivorans (NaCK). These proteins may catalyze the transfer of a phosphate group from ATP to their carbohydrate substrates. They belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466792 [Multi-domain] Cd Length: 424 Bit Score: 38.01 E-value: 7.45e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 41 IDIGGTKVMAGVVDADGNILEKLRTETPDKSKSPKVVEDT--IVELVLD----LSDRHDVHAVGI---GAAG-WVDADRN 110
Cdd:cd07772 5 FDIGKTNKKLLLFDENGEVLAERSTPNPEIEEDGYPCEDVeaIWEWLLDslaeLAKRHRIDAINFtthGATFaLLDENGE 84
|
90
....*....|....
gi 692325114 111 RVLfaPHLSWRNEP 124
Cdd:cd07772 85 LAL--PVYDYEKPI 96
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| ASKHA_NBD_BcrAD_BadFG_HgdC_HadI |
cd24036 |
nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and ... |
38-115 |
9.76e-03 |
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nucleotide-binding domain (NBD) of the BcrAD/BadFG and HgdC/HadI family; The BcrAD/BadFG and HgdC/HadI family includes BcrA/BadF/BzdQ and BcrD/BadG/BzdP proteins which are subunits of benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also contains some dehydratase activators, such as Acidaminococcus fermentans (R)-2-hydroxyglutaryl-CoA dehydratase activating ATPase (HgdC), Clostridioides difficile 2-hydroxyisocaproyl-CoA dehydratase activator (HadI), Clostridium sporogenes (R)-phenyllactate dehydratase activator (FldI), and Anaerotignum propionicum activator of lactoyl-CoA dehydratase (LcdC). Uncharacterized proteins, such as Escherichia coli protein YjiL and Methanocaldococcus jannaschii protein MJ0800, are also included in this family.
Pssm-ID: 466886 [Multi-domain] Cd Length: 250 Bit Score: 37.13 E-value: 9.76e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 692325114 38 TVGIDIGGTKVMAGVVDADGNILEK--LRTETPDKSKSPKVVEDTIVELVLDLSDRHDVHAVGIGaagwvdadRNRVLFA 115
Cdd:cd24036 1 FAGIDVGSTTTKAVILDDKGKILGKavIRTGTDPEKTAERALEEALEEAGLSREDIEYIVATGYG--------RNSVPFA 72
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