|
Name |
Accession |
Description |
Interval |
E-value |
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
6-327 |
6.65e-154 |
|
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: 433.94 E-value: 6.65e-154
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 6 LAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDSTGYTLLKGIYDSFVEKVNENNYNfsnVLGVGIGVPGPVDFEKGTVN 85
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVDAIASAVDSFIQHIAKVGHE---IVAIGIGAPGPVNRQRGTVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 86 GAVNLYWPEKVnVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEI 165
Cdd:TIGR00744 78 FAVNLDWKQEP-LKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 166 GHFRADFDQRFKCNCGRSGCIETVASATGVVNLINFYYPKLTFRSSILELIKENKVTAKAVFDAAKAGDQFCIFITEKVA 245
Cdd:TIGR00744 157 GHIRMVPDGRLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDSYREVA 236
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 246 NYIGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAAGLIKTYVLDKE 325
Cdd:TIGR00744 237 RWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAADLARTYIIEPD 316
|
..
gi 586307212 326 GV 327
Cdd:TIGR00744 317 PI 318
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
4-316 |
7.13e-95 |
|
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: 283.80 E-value: 7.13e-95
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 4 IILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDStGYTLLKGIYDSFVEKVNENNYNFSNVLGVGIGVPGPVDFEKGT 83
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEG-GENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGT 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 84 VNGAVNLYWpEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGA 163
Cdd:cd24062 80 VEVAVNLGW-KNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 164 EIGHFRADFDQRFKCNCGRSGCIETVASATGVVNlINFYYPKLTFRSSILELIKEN-KVTAKAVFDAAKAGDQFCIFITE 242
Cdd:cd24062 159 EIGHITVNPEGGAPCNCGKTGCLETVASATGIVR-IAREELEEGKGSSALRILALGgELTAKDVFEAAKAGDELALAVVD 237
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 586307212 243 KVANYIGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAAGL 316
Cdd:cd24062 238 TVARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-318 |
2.91e-82 |
|
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: 251.35 E-value: 2.91e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 1 MTKIILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDsTGYTLLKGIYDSFVEKVNENNYNFSNVLGVGIGVPGPVDFE 80
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGA-GPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 81 KGTVNGAVNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAitlgtglgggiiSNGEIVHGHNG 160
Cdd:COG1940 82 TGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYltlgtgigggivINGKLLRGANG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 161 SGAEIGHFRADFDQRfKCNCGRSGCIETVASATGVVNLINfyypkltfrssilELIKENKVTAKAVFDAAKAGDQFCIFI 240
Cdd:COG1940 162 NAGEIGHMPVDPDGP-LCGCGNRGCLETYASGPALLRRAR-------------ELGGAEKLTAEELFAAARAGDPLALEV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 586307212 241 TEKVANYIGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAAGLIK 318
Cdd:COG1940 228 LDEAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALAL 305
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
5-314 |
8.32e-59 |
|
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: 190.85 E-value: 8.32e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 5 ILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDstGYTLLKGIYDSFVEKVNENnynfSNVLGVGIGVPGPVDFEKGTV 84
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASK--GGDAILERLLEIIAELKEK----YDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 85 NGAV-NLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGA 163
Cdd:cd24068 76 IYATdNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 164 EIGHFRADFDqRFKCNCGRSGCIETVASATGVVNLINfyypkltfrssilELIKENKVTAKAVFDAAKAGDQFCIFITEK 243
Cdd:cd24068 156 ELGHMVVDPG-GRPCCCGGKGCLEQYASGTALVRRVA-------------EALGEPGIDGREIFDLADAGDPLAKEVVEE 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 586307212 244 VANYIG-YLCSIISVTsNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAA 314
Cdd:cd24068 222 FAEDLAtGLANLVHIF-DPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAA 292
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
66-316 |
5.78e-53 |
|
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: 176.22 E-value: 5.78e-53
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 66 VLGVGIGVPGPVDFEKGTVNGAVNLYWpEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLG 145
Cdd:cd24076 63 ILGIGVGVPGLVDSEDGVVLLAPNLGW-RDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIG 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 146 GGIISNGEIVHGHNGSGAEIGHFRADFDQRfKCNCGRSGCIETVASatgvvnlinfyyPKLTFRSSILELIKENKVTAKA 225
Cdd:cd24076 142 AGIILDGELYRGASGFAGEIGHMTVDPDGP-PCSCGNRGCWETYAS------------ERALLRAAGRLGAGGEPLSLAE 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 226 VFDAAKAGDQFCIFITEKVANYIGY-LCSIISvTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKL 304
Cdd:cd24076 209 LVEAARAGDPAALAALEEVGEYLGIgLANLVN-TFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRL 287
|
250
....*....|..
gi 586307212 305 GNDAGITGAAGL 316
Cdd:cd24076 288 GEDAAALGAAAL 299
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-316 |
5.08e-50 |
|
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: 166.48 E-value: 5.08e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 6 LAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDSTGYTL--LKGIYDSFVEKVNENnynfSNVLGVGIGVPGPVDFEKGT 83
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLdrIAELIEELLAEAGVR----ERILGIGIGVPGPVDPETGI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 84 VNGAVNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAitlgtglgggiiSNGEIVHGHNGSGA 163
Cdd:cd23763 77 VLFAPNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYitlgtgigggiiIDGKLYRGANGAAG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 164 EIGHFRAdfdqrfkcncgrsgcIETVAS--ATGVVNLINFYypkltfrssilelikenkvtakavfdaakagdqfcifit 241
Cdd:cd23763 157 EIGHITV---------------LEEAARylGIGLANLINLL--------------------------------------- 182
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586307212 242 ekvanyigylcsiisvtsNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAAGL 316
Cdd:cd23763 183 ------------------NPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAAL 239
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
6-319 |
1.61e-47 |
|
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: 161.74 E-value: 1.61e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 6 LAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDsTGYTLLKGIyDSFVEKVNENnynFSNVLGVGIGVPGPVDFEKGTVN 85
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTT-TEETLVDAI-AFFVDSAQRK---FGELIAVGIGSPGLISPKYGYIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 86 GAVNLYWPEKvNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEI 165
Cdd:pfam00480 76 NTPNIGWDNF-DLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 166 GHFRADFDQrFKCNCGRSGCIETVASATGVVNLInfyypkltfrssileLIKENKVTAKAVFDAAKAGDQFCIFITEKVA 245
Cdd:pfam00480 155 GHIQLDPNG-PKCGCGNHGCLETIASGRALEKRY---------------QQKGEDLEGKDIIVLAEQGDEVAEEAVERLA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 586307212 246 NYIGYLCSIISVTSNPKYIVLGGGMSTAGPILiENIKTEYHNLTF-APAQFETEIVQAKLGNDAGITGAAGLIKT 319
Cdd:pfam00480 219 RYLAKAIANLINLFDPQAIVLGGGVSNADGLL-EAIRSLVKKYLNgYLPVPPVIIVAASLGDNAGALGAAALAKQ 292
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
9-316 |
3.51e-45 |
|
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: 155.97 E-value: 3.51e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 9 DVGGTTCKLGIFTPELEQLHKWSIHTDTSDStgytllkGIYDSFVEKVNENNYNFSnVLGVGIGVPGPVDFEKGTVNGAV 88
Cdd:cd24061 5 DIGGTKIAAGVVDEEGEILATERVPTPPTAD-------GIVDAIVEAVEELREGHD-VSAVGVAAAGFVDADRATVLFAP 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 89 NLYWpEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEIGHF 168
Cdd:cd24061 77 NIAW-RNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 169 RADFDQRFkCNCGRSGCIETVASATGVVNLINFYYPKLTFRSS-ILELIKENKVTAKAVFDAAKAGDQFCIFITEKVANY 247
Cdd:cd24061 156 RVVPDGLL-CGCGSRGCWEQYASGRALVRYAKEAANATPEGAAvLLADGSVDGITGKHISEAARAGDPVALDALRELARW 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 248 IGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEY-HNLTFAPAQFETEIVQAKLGNDAGITGAAGL 316
Cdd:cd24061 235 LGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFeRWLPGRGWRPIPRLRTAQLGNDAGLIGAADL 304
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-314 |
3.93e-45 |
|
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: 155.18 E-value: 3.93e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 4 IILAADVGGTTCKLGIFTPElEQLHKwsihtdTSDSTGYTLLKGIYDSFVEKVNENNYNFSNVLGVGIGVPGPVDFEKGT 83
Cdd:cd24065 1 STIGLDLGGTKIAAGVVDGG-RILSR------LVVPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGR 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 84 VNGAVNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGA 163
Cdd:cd24065 74 VRFAPNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 164 EIGHFRADFDQRFkCNCGRSGCIETVASATGVVNLINFYYPKltfrssilelikenKVTAKAVFDAAKAGDQFCIFITEK 243
Cdd:cd24065 154 EIGHTTVLPGGPM-CGCGLVGCLEALASGRALARDASFAYGR--------------PMSTAELFELAQQGEPKALRIVEQ 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 586307212 244 VANYIGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAqfETEIVQAKLGNDAGITGAA 314
Cdd:cd24065 219 AAAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYTEGWH--APPLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
5-324 |
8.42e-44 |
|
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: 152.35 E-value: 8.42e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 5 ILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDSTGYTLLKgIYDSfVEKVNENNYNFSNVLGVGIGVPGPVDFEKGTV 84
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEK-LYEL-IDRLLEKENIKSKILGIGIGAPGPLDVEKGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 85 NGAVNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAE 164
Cdd:cd24059 81 LNPPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 165 IGHFRADFDQRFkCNCGRSGCIETVASATGVVnlinfyypkltfrSSILELIKENKVTAKAVFDAAKAGDQFCIFITEKV 244
Cdd:cd24059 161 IGHTSIDINGPR-CSCGNRGCLELYASIPAIE-------------KKARSALGSGRSFQLDIVEALQKGDPIADEVIEEA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 245 ANYIGYlcSIISV--TSNPKYIVLGGGMSTAGPILIENIKTE-YHNLTFAPAQfETEIVQAKLGNDAGITGAAglikTYV 321
Cdd:cd24059 227 AKYLGI--GLVNLinLLNPEAIIIGGELIYLGERYLEPIEKEvNSRLFGRNAR-EVRILKSSLGEDAPLLGAA----ALV 299
|
...
gi 586307212 322 LDK 324
Cdd:cd24059 300 LNK 302
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
5-314 |
5.22e-43 |
|
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: 150.34 E-value: 5.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 5 ILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDstGYTLLKGIYDSFVEKVNENnynfSNVLGVGIGVPGPVDFEKGTV 84
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTIDTKVEN--GKEDVINRIAETVNELIEE----MELLGIGIGSPGSIDRENGIV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 85 NGAVNlyWPEKVN---VREIFEQfVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGS 161
Cdd:cd24064 75 RFSPN--FPDWRNfplVPLIEER-TGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 162 GAEIGHFRADfDQRFKCNCGRSGCIETVASATGVVNLINFYYPKltFRSSILELIKenKVTAKAVFDAAKAGDQF----C 237
Cdd:cd24064 152 AAELGHVIVE-PNGPICGCGNRGCVEAFASATAIIRYARESRKR--YPDSLAGESE--KINAKHVFDAARKNDPLatmvF 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586307212 238 IFITEKVANYIGYLCSIIsvtsNPKYIVLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAA 314
Cdd:cd24064 227 RRVVDALAIAIGGFVHIF----NPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAA 299
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
4-313 |
2.79e-40 |
|
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This subfamily is composed of uncharacterized proteins belonging to the the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this subfamily lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466988 [Multi-domain] Cd Length: 286 Bit Score: 142.71 E-value: 2.79e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 4 IILAADVGGTTCKLGIFTPELEQLHKWSI-HTDTSDSTGYTLLKGIYDSFVEKVNennynfsnvlGVGIGVPGPVDFEKG 82
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIpTPKDSLEEFLDYIKKIIKRYDEEID----------GIAISAPGVIDPETG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 83 TVNGAVNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSG 162
Cdd:cd24152 71 IIYGGGALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFA 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 163 AEIGHFRADFDQRFKCNCGRSgcietvASATGVVNLINfyypkltfrssilELIKENKVTAKAVFDAAKAGDQFCIFIte 242
Cdd:cd24152 151 GEFSYLLTDDDDKDLLFFSGL------ASMFGLVKRYN-------------KAKGLEPLDGEEIFEKYAKGDEAAKKI-- 209
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 586307212 243 kVANYIGYLCSII---SVTSNPKYIVLGGGMSTAgPILIENIKTEYHNLT--FAPAQFETEIVQAKLGNDAGITGA 313
Cdd:cd24152 210 -LDEYIRNLAKLIyniQYILDPEVIVIGGGISEQ-PLFIEDLKKEVNEILanRPGSIPKPEIKACKFGNDANLLGA 283
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
5-316 |
4.41e-39 |
|
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: 140.17 E-value: 4.41e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 5 ILAADVGGTTCKLGIFTPELEQLHKWSIHT--DTSDSTGYTLLKGIYDSFVEKVNennynFSNVLGVGIGVPGPVDFEKG 82
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTpkTGDPGTVSEQVLGLIETLLSKAG-----KDSIEGIGVSSAGPLDLRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 83 TVNGAVNLYWPEKVNVREIFEQFvDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSG 162
Cdd:cd24063 77 TIVNSPNIKGKEIPLVEPLKEEF-NIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 163 AEIGHFRADFDQRFKCNCGRSGCIETVASATGVVNLINFYYPKLTFRSSI-LELIKENKVTAKAVFDAAKAGDQFCIFIT 241
Cdd:cd24063 156 AEVGHLVVDTESGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLkLRNPGGEGITAKEVFSAARKGDPLALKII 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586307212 242 EKVANYIGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEY--HNLTFAPaqfeTEIVQAKLGNDAGITGAAGL 316
Cdd:cd24063 236 EKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLekNPAISKG----PEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
27-317 |
3.12e-38 |
|
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: 137.80 E-value: 3.12e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 27 LHKWSIHTD-TSDSTgyTLLKGIYDSfVEKVNENNYNFSNVLGVGIGVPGPVDFEKGTVNGAVNLYWpEKVNVREIFEQF 105
Cdd:cd24071 25 LEKTRIPFDhETDPE--KVIELIAEN-IKKLIKNKHVEKKLLGIGIAVSGLVDSKKGIVIRSTILGW-ENVELKKILKEK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 106 VDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEIGHFRADFDQRfKCNCGRSGC 185
Cdd:cd24071 101 FKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIGHMTIQPDGR-KCYCGQKGC 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 186 IETVASATGVVNLINfyypKLTFRSSILELIKENKVTAKAVFDAAKAGDQFCIFITEKVANYIGY-LCSIISvTSNPKYI 264
Cdd:cd24071 180 LEAYASFEALVNEIK----ELTESYPLSLLKELEDFEIEKVREAAEEGDSVATELFKKAGEYLGIgIKNLIN-IFNPEAI 254
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 586307212 265 VLGGGMSTAGPILIENIKTEYHNLTFAPAQFETEIVQAKLGNDAGITGAAGLI 317
Cdd:cd24071 255 IIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLV 307
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
66-317 |
2.15e-36 |
|
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: 132.68 E-value: 2.15e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 66 VLGVGIGVPGPVDFEKGTVNGAVNLYWPEkVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLG 145
Cdd:cd24073 62 LLGIGVGLPGLVDAETGICRWSPLLGWRD-VPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIG 140
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 146 GGIISNGEIVHGHNGSGAEIGHFRADFDQRfKCNCGRSGCIETVASATGVVnlinfyypkltfRSSILELIKENKVTAKA 225
Cdd:cd24073 141 CGLVVDGRLYRGAHGGAGEIGHTTVDPDGP-PCRCGKRGCLEAYASDPAIL------------RQAREAGLRGEPLTIED 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 226 VFDAAKAGDQFCIFITEKVANYIGY-LCSIISVTsNPKYIVLGG-GMStAGPILIENIKTEYHNLTFAPAQFETEIVQAK 303
Cdd:cd24073 208 LLAAARAGDPAARAILRRAGRALGLaLANLVNLL-DPELIIISGeGVR-AGDLLFEPMREALRAHVFPGLASDLELVIHP 285
|
250
....*....|....
gi 586307212 304 LGNDAGITGAAGLI 317
Cdd:cd24073 286 WGDEAWARGAAALA 299
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
4-314 |
1.19e-33 |
|
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: 125.42 E-value: 1.19e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 4 IILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDstgYTLLkgiYDSFVEKVNENNYNFSNVLGVGIGVPGPVDFEKGT 83
Cdd:cd24057 1 MYYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDD---YAAF---LAAIAELVAEADARFGVKGPVGIGIPGVIDPEDGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 84 VNGAvNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGA 163
Cdd:cd24057 75 LITA-NIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 164 EIGHFRADFDQ--------RFKCNCGRSGCIETVASATGVVNLINFYYpkltfrssileliKENKvTAKAVFDAAKAGDQ 235
Cdd:cd24057 154 EWGHGPLPADAlllgydlpVLRCGCGQTGCLETYLSGRGLERLYAHLY-------------GEEL-DAPEIIAAWAAGDP 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 586307212 236 FCIFITEKVANYIGYLCSIISVTSNPKYIVLGGGMSTAgPILIENIKTEYHNLTFAPAQFEtEIVQAKLGNDAGITGAA 314
Cdd:cd24057 220 QAVAHVDRWLDLLAGCLANILTALDPDVVVLGGGLSNF-PALIAELPAALPAHLLSGARTP-RIVPARHGDAGGVRGAA 296
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
6-316 |
3.64e-32 |
|
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: 121.75 E-value: 3.64e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 6 LAADVGGTTCKLGIFTPELEQLHKWSIHT-DTSDSTGYTLLKGIYDSFVEKVNENnynfSNVLGVGIGVPGPVDFEKGTV 84
Cdd:cd24060 3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNpKTYEERIDLILQMCVEAASEAVKLN----CRILGVGISTGGRVNPREGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 85 NGAVNLY--WPEkVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSG 162
Cdd:cd24060 79 LHSTKLIqeWSS-VDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 163 AEIGHFRADFDQRfKCNCGRSGCIETVASATGVVNLINFYYPK--LTFRSSILEliKENKVTAKAVFDAAKAGDQFCIFI 240
Cdd:cd24060 158 AELGHIVVSLDGP-DCMCGSHGCVEAYASGMALQREAKKLHDEdlLLVEGMSVT--NDEEVTAKHLIQAAKLGNAKAQKI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 586307212 241 TEKVANYIGY-LCSIISvTSNPKYIVLGGGMStagPILIENIKTEYHNLTFAPAQfETEIVQAKLgNDAGITGAAGL 316
Cdd:cd24060 235 LRTAGTALGLgIVNILH-TLNPSLVILSGVLA---SHYENIVKDVIAQRALPSVQ-NVDVVVSDL-VDPALLGAASM 305
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
44-321 |
5.11e-30 |
|
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: 115.98 E-value: 5.11e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 44 LLKGIYDSFVEKVNENNynfSNVLGVGIGVPGPVDFEKGTVNGAVNLYWpEKVNVREIFEQFVDCPVYVDNDANIAALGE 123
Cdd:cd24072 41 LIDEIIDCIDRLLKLWK---DRVKGIALAIQGLVDSHKGVSLWSPGAPW-RNIEIKYLLEERYGIPVFVENDCNMLALAE 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 124 KHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEIGHFRADFDQRfKCNCGRSGCIETVASATGVVNLINFYY 203
Cdd:cd24072 117 KWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGHTKVNPDGA-RCDCGRRGCLETVASNSALKRNARVTL 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 204 PKLTFRSSILELIKEnkvtakAVFDAAKAGDQFCIFITEKVANYIGY-LCSIISVTsNPKYIVLGGGMSTAGPILIENIK 282
Cdd:cd24072 196 KLGPVSADPEKLTME------QLIEALEEGEPIATQIFDRAANAIGRsLANILNLL-NPEQVLLYGRGCRAGDLLLPAIR 268
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 586307212 283 TEYHNLtfAPAQFETEIVQAKLGNDAGITG-AAGLIKTYV 321
Cdd:cd24072 269 RAIAEN--PFSQHATQIGFGQLSTEQGCAQqALGLVYLYI 306
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
65-323 |
5.33e-26 |
|
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: 105.14 E-value: 5.33e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 65 NVLGVGIGVPGPVDFEKGTVNgavnlYWPE-KVN---VREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITL 140
Cdd:cd24075 61 RLIAISITLPGLINPKTGVVH-----YMPHiQVKswpIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 141 GTGLGGGIISNGEIVHGHNGSGAEIGHFRAD-FDQRfkCNCGRSGCIETVASATGVVNlinfyypkltfrsSILELIKE- 218
Cdd:cd24075 136 HHGIGAGIIIDGKLFLGQNGNAGEIGHIQIEpLGER--CHCGNFGCLETVASNAAIEQ-------------RVKKLLKQg 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 219 -------NKVTAKAVFDAAKAGDQFCIFITEKVANYIGYLCSIISVTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFA 291
Cdd:cd24075 201 yasqltlQDCTIKDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALP 280
|
250 260 270
....*....|....*....|....*....|..
gi 586307212 292 PAQFETEIVQAKLGNDAGItGAAGLIKTYVLD 323
Cdd:cd24075 281 DFRQELKIVASQLDHNSAI-GAFALVKRALLE 311
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
69-314 |
6.09e-26 |
|
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: 104.29 E-value: 6.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 69 VGIGVPGPVDfeKGTVNGAVN---LYWPEKVNVREIfEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLG 145
Cdd:cd24069 55 VAVASTGIIR--DGVLTALNPknlGGLSGFPLADAL-QQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVG 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 146 GGIISNGEIVHGHNGSGAEIGHFRADFDQRfKCNCGRSGCIETVASATGVVnlinfyypkltfRSSILELIKEnkVTAKA 225
Cdd:cd24069 132 GGLVLNGQLLTGPNGLAGHIGHTLADPPGP-VCGCGRRGCVEAIASGTAIA------------AAASEILGEP--VDAKD 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 226 VFDAAKAGDQFCIFITEKVANYIGYLCSIISVTSNPKYIVLGGGMSTAgPILIENIKTEYHNLtfaPAQFETEIVQAKLG 305
Cdd:cd24069 197 VFERARSGDEEAARLIDRAARALADLIADLKATLDLDCVVIGGSVGLA-EGFLERVEQYLADE---PAIFRVSLEPARLG 272
|
....*....
gi 586307212 306 NDAGITGAA 314
Cdd:cd24069 273 QDAGLLGAA 281
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
69-316 |
2.00e-25 |
|
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: 103.05 E-value: 2.00e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 69 VGIGVPGPVDFEKGTVNGAvNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGI 148
Cdd:cd24066 59 VGIGTPGSISPRTGLVKNA-NSTWLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGI 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 149 ISNGEIVHGHNGSGAEIGHFRADFDQRFK-----CNCGRSGCIETVASATGVVNlinfYYPKLTfrssilelikENKVTA 223
Cdd:cd24066 138 VVNGRVLTGANGIAGEWGHNPLPWPDEDElpgppCYCGKRGCVETFLSGPALER----DYARLT----------GKTLSA 203
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 224 KAVFDAAKAGDQFCIFITEKVANYIGY-LCSIISVTsNPKYIVLGGGMS------TAGPILIEnikteyhNLTFAPAqFE 296
Cdd:cd24066 204 EEIVALARAGDAAAVATLDRFLDRLGRaLANVINIL-DPDVIVLGGGLSnidelyTEGPAALA-------RYVFSDE-VE 274
|
250 260
....*....|....*....|
gi 586307212 297 TEIVQAKLGNDAGITGAAGL 316
Cdd:cd24066 275 TPIVKNKHGDSSGVRGAAWL 294
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-314 |
2.02e-25 |
|
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: 103.01 E-value: 2.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 3 KIILAADVGGTTCKLGIFTPELEQLHKWSIHTDTSDSTGYTL--LKGIYDSFVEKVNennynfSNVLGVGIGVPGPVDFE 80
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVevLADLIREYIEEAG------LKPAAIVIGVPGTVDKD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 81 KGTVNGAVNLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNG 160
Cdd:cd24070 75 RRTVISTPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 161 SGAEIGH--FRADFDqrfKCNCGRSGCIETVASATGVVNLINFYYPKltfrSSILELikenkvtakavfdAAKAGDQfci 238
Cdd:cd24070 155 VAGELGHipVYGNGK---PCGCGNTGCLETYASGRALEEIAEEHYPD----TPILDI-------------FVDHGDE--- 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 239 fitEKVANYIGYLcSIISVTS----NPKYIVLGGG--MSTAGPI--LIENIkteYHNLTF-APAQfETEIVQAKLGNDAG 309
Cdd:cd24070 212 ---PELDEFVEDL-ALAIATEinilDPDAVILGGGviDMKGFPRetLEEYI---RKHLRKpYPAD-NLKIIYAELGPEAG 283
|
....*
gi 586307212 310 ITGAA 314
Cdd:cd24070 284 VIGAA 288
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
9-316 |
7.20e-21 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 90.86 E-value: 7.20e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 9 DVGGTTCKLGIFTPELEQLHKWSIHTDTSDSTGyTLlkgiyDSFVEKVNENNYNFSNVLGVGIGVPGPVDFEKGTVNGAv 88
Cdd:PRK09557 6 DLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQ-TI-----EAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNA- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 89 NLYW----PEKVNVREIFEQfvdcPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAE 164
Cdd:PRK09557 79 NSTWlngqPLDKDLSARLNR----EVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 165 IGH-----FRAD---FDQRFKCNCGRSGCIETVASATGVVNLINFYYPKLTFRSSILELIKENKVTAKAVFDA-----AK 231
Cdd:PRK09557 155 WGHnplpwMDEDelrYRNEVPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEIIRLVEEGDPVAELAFRRyedrlAK 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 232 AgdqfcifitekVANYIGYLcsiisvtsNPKYIVLGGGMStagpilieNIKTEYHNLTFAPAQF------ETEIVQAKLG 305
Cdd:PRK09557 235 S-----------LAHVINIL--------DPDVIVLGGGMS--------NVDRLYPTLPALLKQYvfggecETPVRKALHG 287
|
330
....*....|.
gi 586307212 306 NDAGITGAAGL 316
Cdd:PRK09557 288 DSSGVRGAAWL 298
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
33-317 |
1.94e-20 |
|
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: 89.52 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 33 HTDTSDSTGYTLLKGIYDSFVEKVNENNYNfsnVLGVGIGVPGPVDFEKgtvngavNLYWP----EKVNVREIFEQFVDC 108
Cdd:cd24077 32 LLDISFENILEILKSIIQELISQAPKTPYG---LVGIGIGIHGIVDENE-------IIFTPyydlEDIDLKEKLEEKFNV 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 109 PVYVDNDANIAALGEK--------------HKGAGEGaddVVAitlgtglgggiisNGEIVHGHNGSGAEIGHFRADFDQ 174
Cdd:cd24077 102 PVYLENEANLSALAERtfsedydnlisisiHSGIGAG---III-------------NNQLYRGYNGFAGEIGHMIIVPNG 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 175 RfKCNCGRSGCIETVASATGVVNLINfyypkltfrssilELIKENKVTAKAVFDAAKAGDQFCIFITEKVANYIGYLCSI 254
Cdd:cd24077 166 K-PCPCGNKGCLEQYASEKALLKELS-------------EKKGLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINN 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586307212 255 ISVTSNPKYIVLGGGMSTAGPILIENIKTEYHNLTFApaqfETEIVQAKLGNDAGITGAAGLI 317
Cdd:cd24077 232 IINTFNPEIIIINSSLINEIPELLEKIKEQLSSSFNK----YVEILISTLGKNATLLGGAAVA 290
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
11-316 |
4.59e-20 |
|
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: 88.37 E-value: 4.59e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 11 GGTTCKLGIFTPELEQLHKWSIHTDTSDSTgytlLKGIYDSFvekvNENNYNFSnvlGVGIGVPGPVDFEK-----GTVN 85
Cdd:cd24067 7 GGTKFVCAVGTGDGNIIERTEFPTTTPEET----LQAVIDFF----REQEEPID---AIGIASFGPIDLNPtsptyGYIT 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 86 GAVNLYWPEKVNVREIFEQFvDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHG--HngsgA 163
Cdd:cd24067 76 TTPKPGWRNFDILGALKRAF-PVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGllH----P 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 164 EIGHF---RADFDQRFKCNCGRSG-CIETVASATGVVnlinfyypkltfrssileliKENKVTAKAVFDAAKagdqfcif 239
Cdd:cd24067 151 EMGHIrvpRHPDDDGFPGVCPFHGdCLEGLASGPAIA--------------------ARWGIPAEELPDDHP-------- 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 240 ITEKVANYIGYLCSIISVTSNPKYIVLGGGMStAGPILIENIKTE-------YHNLTFAPAQFETEIVQAKLGNDAGITG 312
Cdd:cd24067 203 AWDLEAYYLAQACANLTLTLSPERIVLGGGVM-QRPGLFPRIREKfrkllngYLEVPRLLPDIDEYIVPPALGNDAGILG 281
|
....
gi 586307212 313 AAGL 316
Cdd:cd24067 282 ALAL 285
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
66-318 |
9.92e-20 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 88.14 E-value: 9.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 66 VLGVGIGVPGPVDFEKGTVNgAVNLY----WPEKvnvrEIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLG 141
Cdd:cd24074 63 LTAIAITLPGIIDPESGIVH-RLPFYdiknLPLG----EALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVID 137
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 142 TGLGGGIISNGEIVHGHNGSGAEIGHFRADFDQRfKCNCGRSGCIETVASATGVVNLINfyypKLTFRSSILELIKEnKV 221
Cdd:cd24074 138 DDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGK-RCYCGNHGCLETVASIPAILEQAN----QLLEQSPDSMLHGQ-PI 211
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 222 TAKAVFDAAKAGDQFCIFITEKVANYIGYLCSIISVTSNPKYIVLGGGMSTAG----PILIENIKT----EYH-NLTFAP 292
Cdd:cd24074 212 SIESLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNNAAeilfPALSQSIRQqslpAYSqHLQIES 291
|
250 260
....*....|....*....|....*.
gi 586307212 293 AQFEteivqaklgNDAGITGAAgLIK 318
Cdd:cd24074 292 TKFY---------NDGTMPGAA-LIK 307
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
9-316 |
2.56e-18 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 83.88 E-value: 2.56e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 9 DVGGTTCKLGIFTPELEQLHKWSIHTDTSDstgYTLLkgiYDSFVEKVNENNYNFSNVLGVGIGVPGPVDFEKGTVNgAV 88
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPRDS---YDAF---LDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLY-AA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 89 NLYWPEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAEIGHF 168
Cdd:PRK13310 79 NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHM 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 169 RADFDQ---------RFKCNCGRSGCIETVASATGVVNLINFYYPKltfrssilelikenKVTAKAVFDAAKAGDQFCIf 239
Cdd:PRK13310 159 RLPVDAltllgwdapLRRCGCGQKGCIENYLSGRGFEWLYQHYYGE--------------PLQAPEIIALYYQGDEQAV- 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 240 itEKVANYIGYLC----SIISVTsNPKYIVLGGGMSTagpilIENIKTEY------HNLTFAPAqfeTEIVQAKLGNDAG 309
Cdd:PRK13310 224 --AHVERYLDLLAiclgNILTIV-DPHLVVLGGGLSN-----FDAIYEQLpkrlprHLLPVARV---PRIEKARHGDAGG 292
|
....*..
gi 586307212 310 ITGAAGL 316
Cdd:PRK13310 293 VRGAAFL 299
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
1-318 |
1.62e-15 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 75.79 E-value: 1.62e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 1 MTKIILAADVGGTTCKLGIFTpELEQLHKWSIHTDTSDSTGyTLLKGIYDSFVEKVNENNYNFSnvlGVGIGVPGPVDFE 80
Cdd:PRK09698 2 QKNVVLGIDMGGTHIRFCLVD-AEGEILHCEKKRTAEVIAP-DLVSGLGEMIDEYLRRFNARCH---GIVMGFPALVSKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 81 KGTVNGAVNLYWP--EKVNVREIFEQFVDCPVYVDNDANIAALGE--KHKGAGegaDDVVAITLGTGLGGGIISNGEIVH 156
Cdd:PRK09698 77 RRTVISTPNLPLTalDLYDLADKLENTLNCPVFFSRDVNLQLLWDvkENNLTQ---QLVLGAYLGTGMGFAVWMNGAPWT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 157 GHNGSGAEIGHFRAdFDQRFKCNCGRSGCIETVASATgvvNLINFYypKLTFRSSILElikenkvtakAVFDaaKAGD-Q 235
Cdd:PRK09698 154 GAHGVAGELGHIPL-GDMTQHCGCGNPGCLETNCSGM---ALRRWY--EQQPRDYPLS----------DLFV--HAGDhP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 236 FCIFITEKVANYIGYLCSIIsvtsNPKYIVLGGG--MSTAGPI--LIENIKTeyhNLtFAPAQFET-EIVQAKLGNDAGI 310
Cdd:PRK09698 216 FIQSLLENLARAIATSINLF----DPDAIILGGGvmDMPAFPRetLIAMIQK---YL-RKPLPYEVvRFIYASSSDFNGA 287
|
....*...
gi 586307212 311 TGAAGLIK 318
Cdd:PRK09698 288 QGAAILAH 295
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
9-203 |
4.75e-13 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 68.13 E-value: 4.75e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 9 DVGGTTCKLGIFTPELEQLHKWSIHTDTSDstgYTLLKGIYDSFVEKVNennyNFSNVLG-VGIGVPGPVDFEKGTV--- 84
Cdd:PRK13311 6 DMGGTKIELGVFDENLQRIWHKRVPTPRED---YPQLLQILRDLTEEAD----TYCGVQGsVGIGIPGLPNADDGTVfta 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 85 NGAVNLYWPEKVNVREIFEQfvdcPVYVDNDANIAALGEKHKGAGEGADDVVAITLGTGLGGGIISNGEIVHGHNGSGAE 164
Cdd:PRK13311 79 NVPSAMGQPLQADLSRLIQR----EVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGE 154
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 586307212 165 IGHFRADFDQ---------RFKCNCGRSGCIETVASATGVVNLINFYY 203
Cdd:PRK13311 155 FGHFRLPVDAldilgadipRVPCGCGHRGCIENYISGRGFEWMYSHFY 202
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
99-314 |
4.27e-12 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 65.70 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 99 REIFEQFVDCPVYVDNDANIAALGEKHKGAGEGaDDVVAITLGTGLGGGIISNGEIVHGHNGSGAEIGHFRADfDQRFKC 178
Cdd:PRK05082 89 VQTLEQLTDLPTIALNDAQAAAWAEYQALPDDI-RNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTLAD-PHGPVC 166
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 179 NCGRSGCIETVASATGVvnlinfyypkltfrsSILELIKENKVTAKAVFDAAKAGDQFCIFITEKVANYIGYLCSIISVT 258
Cdd:PRK05082 167 GCGRRGCVEAIASGRAI---------------AAAAQGWLAGCDAKTIFERAGQGDEQAQALINRSAQAIARLIADLKAT 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 586307212 259 SNPKYIVLGGGMSTAG---PILIENIKTEyhnltfaPAQFETEIVQAKLGNDAGITGAA 314
Cdd:PRK05082 232 LDCQCVVLGGSVGLAEgylELVQAYLAQE-------PAIYHVPLLAAHYRHDAGLLGAA 283
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
69-314 |
2.90e-09 |
|
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: 56.42 E-value: 2.90e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 69 VGIGVPGPVdfEKGTVNGAVNLY--WpEKVNVREIFEQFVDCPVYVDNDANIAALGEKHKGAGEGADDVV---------- 136
Cdd:cd24058 58 VGVGFPGVV--RRGVVRTAANLDksW-IGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVlvltlgtgig 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 137 -AItlgtglgggiisngeIVHGHNGSGAEIGHFRAdfdqrfkcncgRSGCIETVASAtGVVnlinfyypkltfrssilel 215
Cdd:cd24058 135 sAL---------------FVDGHLVPNTELGHLEI-----------RGKDAEERASL-GVR------------------- 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 216 iKENKVTAKAvfdaakagdqfcifITEKVANYIGYLCSIIsvtsNPKYIVLGGGMSTagpilienikteYHNLTFAPAQF 295
Cdd:cd24058 169 -AREDLGWKR--------------WAKRVNKYLQYLERLF----NPDLFIIGGGNSK------------KADKFLPLLDV 217
|
250
....*....|....*....
gi 586307212 296 ETEIVQAKLGNDAGITGAA 314
Cdd:cd24058 218 KTPVVPAVLRNDAGIVGAA 236
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
5-269 |
1.24e-07 |
|
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: 52.23 E-value: 1.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 5 ILAADVGGTTCKLGIFTPELEQL-HKWSIHTDTSDstgytllkgiYDSFVEKVNE--NNYNFSNVLGVGIGVPGPVDfek 81
Cdd:cd24008 1 ILVGDIGGTNARLALADAGDGSGdLLFVRKYPSAD----------FASLEDALAAflAELGAPRPKAACIAVAGPVD--- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 82 gtvNGAVNLY-WPEKVNVREIFEQFVDCPVYVDND--AN---IAALGEK-----HKGAGEGADDV-----------VAIt 139
Cdd:cd24008 68 ---GGRVRLTnLDWSIDAAELRKALGIGRVRLLNDfeAAaygLPALGPEdllvlYGGGGPLPGGPravlgpgtglgVAL- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 140 lgtglgggiisngeIVHGHNGS----GAEIGH----FRADFDQRFKCNC----GRSGCIETVASATGVVNLINFYYPKLT 207
Cdd:cd24008 144 --------------LVPDGDGGyvvlPSEGGHadfaPVTEEEAELLEFLrkrfGRSVSYEDVLSGPGLENIYEFLAKLDG 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586307212 208 frssilelIKENKVTAKAVFDAAKAGDQFCIFITEKVANYIGYLCSIISVTSNPKY-IVLGGG 269
Cdd:cd24008 210 --------AEPPDLTAEEIAEAALAGDPLAREALDLFARILGRFAGNLALSFLATGgVYLAGG 264
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
3-284 |
4.36e-06 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 47.57 E-value: 4.36e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 3 KIILAADVGGTTCKLGIFTPELEQLHK-----WSIHTDTSDSTGYTLLKGIydsfvEKVNENNYNFSNVLGVGIGVPGpV 77
Cdd:COG2971 1 PYILGVDGGGTKTRAVLVDADGEVLGRgraggANPQSVGLEEALASLREAL-----EEALAAAGDPADIEAVGFGLAG-A 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 78 DFEKgtvngavnlywpEKVNVREIFEQ-FVDCPVYVDNDANIAALGekhkgAGEGADDVVAitlgtglgggiiSNGEIVH 156
Cdd:COG2971 75 GTPE------------DAEALEAALRElFPFARVVVVNDALAALAG-----ALGGEDGIVViag-------tgSIAAGRD 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 157 GHN---------------GSGAEIGH------FRAdFDQRfkcncGRSGCI-ETVASATGVVN---LINFYYPKLTFRSS 211
Cdd:COG2971 131 GDGrtarvggwgyllgdeGSGAWLGRealraaLRA-LDGR-----GPPTALtEAVLAEFGLDDpeeLIAWVYRGPAPPAD 204
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 586307212 212 ILELikenkvtAKAVFDAAKAGDQFCIFITEKVANYIGYLCSIISVTSNPKyIVLGGGMSTAGPILIENIKTE 284
Cdd:COG2971 205 LASL-------APLVFEAAEAGDPVARAILEEAADELAELARALLERGALP-VVLAGGVAAAQPLLREALRAR 269
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
5-304 |
9.19e-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: 37.28 E-value: 9.19e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 5 ILAADVGGTTCKLGIFTPELEQLHK-----WSIHTDTSDSTGYTLLKGIydsfvEKVNENNYNFSNVLGVGIGVPGpvdf 79
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRgkggpSNPASVGIEEAKENLKEAV-----REALSQAGSLGEIDAICLGLAG---- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 80 ekgtvngavnlYWPEKVnvREIFEQFVD-----CPVYVDNDANIAalgekHKGAGEGADDVVAITLGTGLGGGIISNGEI 154
Cdd:cd24007 72 -----------IDSEED--RERLRSALKelflsGRIIIVNDAEIA-----LAAALGGGPGIVVIAGTGSVAYGRNGDGEE 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 155 VH----GH----NGSGAEIGH-----FRADFDQRFKcncgRSGCIETVASATGVVN---LINFYYPKLTFRSSILELike 218
Cdd:cd24007 134 ARvggwGHllgdEGSGYWIGRralraALRALDGRGP----KTPLLDAILKFLGLDSieeLITAIYRSSDRKKEIASL--- 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 586307212 219 nkvtAKAVFDAAKAGDQFCIFITEKVANY----IGYLCSIISVTSNPKyIVLGGGMSTAGPIL----IENIKTEYHNLTF 290
Cdd:cd24007 207 ----APLVFEAAEEGDPVAQAILKEAAEElaklVVALAKLLLLGEKLP-LALSGGVFKNNYYLaeflEELLKKKKPNAKV 281
|
330
....*....|....
gi 586307212 291 APAQFETEIVQAKL 304
Cdd:cd24007 282 VEPKGSPVVGALLL 295
|
|
| |
