|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-321 |
1.06e-88 |
|
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: 267.92 E-value: 1.06e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 1 MKKVAIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSVKLLNPEIEiqGIGIGAPNA-NY 79
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRIL--GIGIGVPGPvDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 80 YAGTIEYAANLAFKGVVPLVKLLK--LKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLV 157
Cdd:COG1940 81 ETGVVLNAPNLPGWRGVPLAELLEerLGLP----VFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 158 YGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLVKynatdslladksfNELDSKMIFDAAERGDKV 237
Cdd:COG1940 157 RGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGGA-------------EKLTAEELFAAARAGDPL 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 238 ANEVFEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPgDAAIVGASA 317
Cdd:COG1940 224 ALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGD-DAGLLGAAA 302
|
....
gi 1774967535 318 LVYQ 321
Cdd:COG1940 303 LALE 306
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
5-318 |
2.10e-66 |
|
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: 210.49 E-value: 2.10e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINsvkllnpEIEIQGIGIGAP---NANyyA 81
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKE-------KYDIEGIGISSAgqvDPK--T 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 82 GTIEYA-ANL-AFKGVvPLVKLLKLKF--PelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLV 157
Cdd:cd24068 73 GEVIYAtDNLpGWTGT-NLKEELEERFglP----VAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLY 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 158 YGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLVKynatdslladksfNELDSKMIFDAAERGDKV 237
Cdd:cd24068 148 RGANGSAGELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGE-------------PGIDGREIFDLADAGDPL 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 238 ANEVFEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKpGDAAIVGASA 317
Cdd:cd24068 215 AKEVVEEFAEDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLG-NDAGLLGAAY 293
|
.
gi 1774967535 318 L 318
Cdd:cd24068 294 L 294
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
5-318 |
3.31e-66 |
|
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: 210.29 E-value: 3.31e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTrtdgdvDRYVDDLSSAIHELINSvklLNPEIEIQGIGIGAPN-ANYYAGT 83
Cdd:cd24061 1 TIGVDIGGTKIAAGVVDEEGEILATERVPT------PPTADGIVDAIVEAVEE---LREGHDVSAVGVAAAGfVDADRAT 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEYAANLAFKGVvPLVKLLK--LKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDD 161
Cdd:cd24061 72 VLFAPNIAWRNE-PLKDLLEarIGLP----VVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAF 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 162 GFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAfellvKYNATDS------LLADKSFNELDSKMIFDAAERGD 235
Cdd:cd24061 147 GIAGEFGHIRVVPDGLLCGCGSRGCWEQYASGRALVRYA-----KEAANATpegaavLLADGSVDGITGKHISEAARAGD 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 236 KVANEVFEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTS-FKNKIQILPSQLKPgDAAIVG 314
Cdd:cd24061 222 PVALDALRELARWLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFERWLPGRgWRPIPRLRTAQLGN-DAGLIG 300
|
....
gi 1774967535 315 ASAL 318
Cdd:cd24061 301 AADL 304
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
4-318 |
1.78e-64 |
|
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: 205.99 E-value: 1.78e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 4 VAIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINsvKLLNPEIEIQGIGIGAPN-ANYYAG 82
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLLE--ELGYSKEDLIGIGVGVPGpVDVETG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 83 TIEYAANLAFKGVvPLVKLLKLKFPELKAISmtNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDG 162
Cdd:cd24062 79 TVEVAVNLGWKNF-PLKDKLEALTGIPVVID--NDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 163 FAGECGHTTLIP-GGRLCGCGALGHFEAYCSAPGMKRTAFELLVKYNATDSLLADKSFNELDSKMIFDAAERGDKVANEV 241
Cdd:cd24062 156 AAGEIGHITVNPeGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1774967535 242 FEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKpGDAAIVGASAL 318
Cdd:cd24062 236 VDTVARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLG-NDAGVIGAAWL 311
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
5-321 |
1.03e-62 |
|
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: 201.25 E-value: 1.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSVKLlnPEIEIQGIGIGAPN-ANYYAGT 83
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPD--SPLGILGIGVGVPGlVDSEDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEYAANLAFKGVvPLVKLLKLKFPELKAISmtNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGF 163
Cdd:cd24076 81 VLLAPNLGWRDV-PLRDLLEEALGVPVFVD--NEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGF 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 164 AGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFEllvkynatdsllADKSFNELDSKMIFDAAERGDKVANEVFE 243
Cdd:cd24076 158 AGEIGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGR------------LGAGGEPLSLAELVEAARAGDPAALAALE 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774967535 244 QTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPgDAAIVGASALVYQ 321
Cdd:cd24076 226 EVGEYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGE-DAAALGAAALAID 302
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-318 |
1.18e-61 |
|
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: 196.15 E-value: 1.18e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSVKLLNpeiEIQGIGIGAPNA-NYYAGTI 84
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGVRE---RILGIGIGVPGPvDPETGIV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 85 EYAANLAFKGVVPLVKLL--KLKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDG 162
Cdd:cd23763 78 LFAPNLPWWKNVPLRELLeeRLGLP----VVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 163 FAGECGHTTlipggrlcgcgalghfeaycsapgmkrtafellvkynatdslladksfneldskmifdaaergdkvaneVF 242
Cdd:cd23763 154 AAGEIGHIT---------------------------------------------------------------------VL 164
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774967535 243 EQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPgDAAIVGASAL 318
Cdd:cd23763 165 EEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGD-DAGLLGAAAL 239
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
5-318 |
1.46e-60 |
|
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: 195.79 E-value: 1.46e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTD-GDVDryvddlssAIHELINSVKLLNPEIEIQGIGIGAPNA-NYYAG 82
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTIDTKVEnGKED--------VINRIAETVNELIEEMELLGIGIGSPGSiDRENG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 83 TIEYAANLAFKGVVPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDG 162
Cdd:cd24064 73 IVRFSPNFPDWRNFPLVPLIEERTG--IKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDG 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 163 FAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLVKYNatDSLLADKsfNELDSKMIFDAAERGDKVANEVF 242
Cdd:cd24064 151 IAAELGHVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRYP--DSLAGES--EKINAKHVFDAARKNDPLATMVF 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1774967535 243 EQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPgDAAIVGASAL 318
Cdd:cd24064 227 RRVVDALAIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVE-DAGILGAASI 301
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
6-325 |
4.08e-60 |
|
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily of proteins. The three members of the seed alignment for this model all have experimental evidence for activity as glucokinase, but the set of related proteins is crowded with paralogs of different or unknown function. Proteins scoring above the trusted_cutoff will show strong similarity to at least one known glucokinase and may be designated as putative glucokinases. However, definitive identification of glucokinases should be done only with extreme caution. [Unknown function, General]
Pssm-ID: 273246 [Multi-domain] Cd Length: 318 Bit Score: 195.12 E-value: 4.08e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVdrYVDDLSSAIHELINSVKllNPEIEIQGIGIGAPN-ANYYAGTI 84
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPET--IVDAIASAVDSFIQHIA--KVGHEIVAIGIGAPGpVNRQRGTV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 85 EYAANLAFKGVVplvklLKLKFPELKAIS--MTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDG 162
Cdd:TIGR00744 77 YFAVNLDWKQEP-----LKEKVEARVGLPvvVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 163 FAGECGHTTLIPGGRL-CGCGALGHFEAYCSAPGMKRTAFELLVKYNATDSLLADKSFNELDSKMIFDAAERGDKVANEV 241
Cdd:TIGR00744 152 VGAEIGHIRMVPDGRLlCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDGISAKHVFVAARQGDPVAVDS 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 242 FEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKpGDAAIVGASALVYQ 321
Cdd:TIGR00744 232 YREVARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLG-NDAGLVGAADLART 310
|
....
gi 1774967535 322 ELNK 325
Cdd:TIGR00744 311 YIIE 314
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
5-323 |
1.40e-57 |
|
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: 188.18 E-value: 1.40e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELInsvKLLNPEIEIQGIGIGAPNA-NYYAGT 83
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLL---EKENIKSKILGIGIGAPGPlDVEKGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEYAANlaFKGV--VPLVKLLKLKFpELKAIsMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDD 161
Cdd:cd24059 80 ILNPPN--FPGWenIPLVELLEEKF-GIPVY-LDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVD 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 162 GFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLvkYNATDslladksfnelDSKMIFDAAERGDKVANEV 241
Cdd:cd24059 156 GYAGEIGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSAL--GSGRS-----------FQLDIVEALQKGDPIADEV 222
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 242 FEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKpGDAAIVGASALVYQ 321
Cdd:cd24059 223 IEEAAKYLGIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLG-EDAPLLGAAALVLN 301
|
..
gi 1774967535 322 EL 323
Cdd:cd24059 302 KY 303
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
4-318 |
2.45e-56 |
|
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: 184.85 E-value: 2.45e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 4 VAIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSvkllNPEIEIQGIGIG-APNANYYAG 82
Cdd:cd24063 1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLSK----AGKDSIEGIGVSsAGPLDLRKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 83 TIEYAANLAFKgVVPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDG 162
Cdd:cd24063 77 TIVNSPNIKGK-EIPLVEPLKEEFN--IPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 163 FAGECGHTTLIPGGRL-CGCGALGHFEAYCSAPGMKRTAFELLVKYNATDSL-LADKSFNELDSKMIFDAAERGDKVANE 240
Cdd:cd24063 154 NAAEVGHLVVDTESGLkCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLkLRNPGGEGITAKEVFSAARKGDPLALK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1774967535 241 VFEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSfkNKIQILPSQLKpGDAAIVGASAL 318
Cdd:cd24063 234 IIEKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKNPAIS--KGPEIVLSELG-DDVGLIGALAL 308
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
4-323 |
1.42e-50 |
|
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: 170.04 E-value: 1.42e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 4 VAIGVDIGGTNTAIGVVDELGNVVAKGNIsTRTDGDVDRYVDDLSSAIHELINSVKLLNPEIeiQGIGIGAPNA-NYYAG 82
Cdd:cd24073 2 YVVGVKLTEDRITAVLTDLRGNVLASHTL-PLDSGDPEAVAEAIAEAVAELLAQAGLSPDRL--LGIGVGLPGLvDAETG 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 83 TIEYAANLAFKGVvPLVKLL--KLKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGD 160
Cdd:cd24073 79 ICRWSPLLGWRDV-PLAELLeeRLGLP----VYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGA 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 161 DGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLVKYNATDslLADksfneldskmIFDAAERGDKVANE 240
Cdd:cd24073 154 HGGAGEIGHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLRGEPLT--IED----------LLAAARAGDPAARA 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 241 VFEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPGDAAiVGASALVY 320
Cdd:cd24073 222 ILRRAGRALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWA-RGAAALAL 300
|
...
gi 1774967535 321 QEL 323
Cdd:cd24073 301 QEF 303
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
6-321 |
1.01e-46 |
|
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: 159.43 E-value: 1.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRTDgdvdRYVDDLSSAIHELINSvkLLNPEIEIQGIGIGAP---NANYyaG 82
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTT----TTEETLVDAIAFFVDS--AQRKFGELIAVGIGSPgliSPKY--G 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 83 TIEYAANLAFKGVvPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDG 162
Cdd:pfam00480 73 YITNTPNIGWDNF-DLVEKLEERFN--VPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 163 FAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRtafellvkynatdslLADKSFNELDSKMIFDAAERGDKVANEVF 242
Cdd:pfam00480 150 VAGEIGHIQLDPNGPKCGCGNHGCLETIASGRALEK---------------RYQQKGEDLEGKDIIVLAEQGDEVAEEAV 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 243 EQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAgDYIFKPAKESMEKHLLTSFKNK-IQILPSQLkpGD-AAIVGASALVY 320
Cdd:pfam00480 215 ERLARYLAKAIANLINLFDPQAIVLGGGVSNA-DGLLEAIRSLVKKYLNGYLPVPpVIIVAASL--GDnAGALGAAALAK 291
|
.
gi 1774967535 321 Q 321
Cdd:pfam00480 292 Q 292
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
5-323 |
2.01e-46 |
|
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: 159.37 E-value: 2.01e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSVKLLNpeiEIQGIGIGAPNA-NYYAGT 83
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLIKNKHVEK---KLLGIGIAVSGLvDSKKGI 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEYAANLAFKGVvPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGF 163
Cdd:cd24071 80 VIRSTILGWENV-ELKKILKEKFK--IPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 164 AGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLVKYNATDsllaDKSFNELDSKMIFDAAERGDKVANEVFE 243
Cdd:cd24071 157 AGEIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSL----LKELEDFEIEKVREAAEEGDSVATELFK 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 244 QTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPgDAAIVGASALVYQEL 323
Cdd:cd24071 233 KAGEYLGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGE-DAWVLGAALLVIDHL 311
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
6-315 |
4.14e-40 |
|
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: 142.08 E-value: 4.14e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDelGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSVkllnPEIEIQGIGIGAPnANYYAGTIE 85
Cdd:cd24065 3 IGLDLGGTKIAAGVVD--GGRILSRLVVPTPREGGEAVLDALARAVEALQAEA----PGVEAVGLGVPGP-LDFRRGRVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 86 YAANLafKGV--VPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGF 163
Cdd:cd24065 76 FAPNI--PGLtdFPIRRGLAERLG--LPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 164 AGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRtafellvkynatdslLADKSFN-ELDSKMIFDAAERGDKVANEVF 242
Cdd:cd24065 152 AGEIGHTTVLPGGPMCGCGLVGCLEALASGRALAR---------------DASFAYGrPMSTAELFELAQQGEPKALRIV 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1774967535 243 EQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHlLTSFkNKIQILPSQLKPgDAAIVGA 315
Cdd:cd24065 217 EQAAAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRY-TEGW-HAPPLRLAHLGT-DAGVIGA 286
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
9-318 |
8.68e-33 |
|
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: 122.68 E-value: 8.68e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 9 DIGGTNTAIGVVDELGNVVAKGNISTRTDgDVDRYVDDLSSAIHELINSVKllnpeieiqGIGIGAPNA-NYYAGTIEY- 86
Cdd:cd24152 6 DIGGTFIKYALVDENGNIIKKGKIPTPKD-SLEEFLDYIKKIIKRYDEEID---------GIAISAPGViDPETGIIYGg 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 87 AANLAFKGVvPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGFAGE 166
Cdd:cd24152 76 GALPYLKGF-NLKEELEERCN--LPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 167 CGHTTLIPGGRlcgcgalGHFEAYCSApgmkrTAFELLVKYNATDSLladksfNELDSKMIFDAAERGDKVANEVFEQTG 246
Cdd:cd24152 153 FSYLLTDDDDK-------DLLFFSGLA-----SMFGLVKRYNKAKGL------EPLDGEEIFEKYAKGDEAAKKILDEYI 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1774967535 247 KWLGQGFADTAHHLSPEAIFLFGGPTAAgDYIFKPAKESMEKHLLTSFKN--KIQILPSQLKpGDAAIVGASAL 318
Cdd:cd24152 215 RNLAKLIYNIQYILDPEVIVIGGGISEQ-PLFIEDLKKEVNEILANRPGSipKPEIKACKFG-NDANLLGALYN 286
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
5-325 |
9.42e-33 |
|
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: 123.25 E-value: 9.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNIsTRTDGDVDRYVDDLSSAIHELINSvkllNPEI--EIQGIGIGAPN-ANYYA 81
Cdd:cd24075 3 ILAVRLGRHDLTLGLYDLSGELLAEHTV-PLTALNQEALLSQLIEEIAQFLKS----HRRKtqRLIAISITLPGlINPKT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 82 GTIEYAANLAFKGVvPLVKLLKLKFPELKAISmtNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDD 161
Cdd:cd24075 78 GVVHYMPHIQVKSW-PIVEELEQRFNVPCFIG--NDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 162 GFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLvKYNATDSLladkSFNELDSKMIFDAAERGDKVANEV 241
Cdd:cd24075 155 GNAGEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLL-KQGYASQL----TLQDCTIKDICQAALNGDQLAQDV 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 242 FEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSFKNKIQILPSQLKPGDAaiVGASALVYQ 321
Cdd:cd24075 230 IKRAGRYLGKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDHNSA--IGAFALVKR 307
|
....
gi 1774967535 322 ELNK 325
Cdd:cd24075 308 ALLE 311
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
5-318 |
3.86e-29 |
|
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: 113.67 E-value: 3.86e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAK------GNISTRTDGDVDRYVDDLSSAIHelinsvklLNPEIEIQGIGIGApNAN 78
Cdd:cd24060 2 ALAVDLGGTNLRVAIVSMKGEIVKKytqpnpKTYEERIDLILQMCVEAASEAVK--------LNCRILGVGISTGG-RVN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 79 YYAGTIEYAANLaFKG--VVPLVKLL--KLKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNG 154
Cdd:cd24060 73 PREGIVLHSTKL-IQEwsSVDLRTPIsdALHLP----VWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNH 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 155 DLVYGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELlvkyNATDSLLAD----KSFNELDSKMIFDA 230
Cdd:cd24060 148 ELIHGSSFCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKL----HDEDLLLVEgmsvTNDEEVTAKHLIQA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 231 AERGDKVANEVFEQTGKWLGQGFADTAHHLSPEAIFLfGGPTAagDYIFKPAKESMEKHLLTSFKNkIQILPSQLKpgDA 310
Cdd:cd24060 224 AKLGNAKAQKILRTAGTALGLGIVNILHTLNPSLVIL-SGVLA--SHYENIVKDVIAQRALPSVQN-VDVVVSDLV--DP 297
|
....*...
gi 1774967535 311 AIVGASAL 318
Cdd:cd24060 298 ALLGAASM 305
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
8-255 |
2.17e-28 |
|
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: 110.84 E-value: 2.17e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 8 VDIGGTNTAIGVVDElGNVVAKGNISTRTDGDVDRYVDDLSSaiheLINSVKLLNPEIEIQGIGIGAPNANYYAGtieyA 87
Cdd:cd24069 3 IDIGGTKIAAALIGN-GQIIDRRQIPTPRSGTPEALADALAS----LLADYQGQFDRVAVASTGIIRDGVLTALN----P 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 88 ANLAFKGVVPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGFAGEC 167
Cdd:cd24069 74 KNLGGLSGFPLADALQQLLG--VPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 168 GHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLVKYnatdslladksfneLDSKMIFDAAERGDKVANEVFEQTGK 247
Cdd:cd24069 152 GHTLADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEP--------------VDAKDVFERARSGDEEAARLIDRAAR 217
|
....*...
gi 1774967535 248 WLGQGFAD 255
Cdd:cd24069 218 ALADLIAD 225
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
5-321 |
8.33e-28 |
|
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: 109.55 E-value: 8.33e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDgDVDRYVDDLSSAIHELINSVkllnPEIE--IQGIGI---GAPNANy 79
Cdd:cd24077 3 SIGIDLGYNYISLMLTYLDGEIISSKQIKLLDI-SFENILEILKSIIQELISQA----PKTPygLVGIGIgihGIVDEN- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 80 yagTIEYAANLAFKGVvPLVKLL--KLKFPelkaISMTNDANAAAIGEMIYggAVGMKNFVMYTLGTGVGSGIVVNGDLV 157
Cdd:cd24077 77 ---EIIFTPYYDLEDI-DLKEKLeeKFNVP----VYLENEANLSALAERTF--SEDYDNLISISIHSGIGAGIIINNQLY 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 158 YGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSapgmkrtafE--LLVKYNATdslladKSFNELDSKMIFDAAERGD 235
Cdd:cd24077 147 RGYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYAS---------EkaLLKELSEK------KGLETLTFDDLIQLYNEGD 211
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 236 KVANEVFEQTGKWLGQGFADTAHHLSPEAIFLfggptaaGDYIFKPAKESMEK---HLLTSFKNKIQILPSQLkPGDAAI 312
Cdd:cd24077 212 PEALELIDQFIKYLAIGINNIINTFNPEIIII-------NSSLINEIPELLEKikeQLSSSFNKYVEILISTL-GKNATL 283
|
....*....
gi 1774967535 313 VGASALVYQ 321
Cdd:cd24077 284 LGGAAVAIK 292
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
5-270 |
6.91e-27 |
|
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: 107.32 E-value: 6.91e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDgdvDRyvDDLSSAIHELINSVKLLNPEIEIQGIGI-GAPNANyyAGT 83
Cdd:cd24057 2 YYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTD---DY--AAFLAAIAELVAEADARFGVKGPVGIGIpGVIDPE--DGT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IeYAANL-AFKGVvPLVKLL--KLKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGD 160
Cdd:cd24057 75 L-ITANIpAAKGR-PLRADLsaRLGRP----VRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGR 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 161 DGFAGECGHTTLiPGGRL----------CGCGALGHFEAYCSAPGMKRtafellvkynatdsLLADKSFNELDSKMIFDA 230
Cdd:cd24057 149 SGIAGEWGHGPL-PADALllgydlpvlrCGCGQTGCLETYLSGRGLER--------------LYAHLYGEELDAPEIIAA 213
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1774967535 231 AERGDKVANEVFEQTGKWLGQGFADTAHHLSPEAIFLFGG 270
Cdd:cd24057 214 WAAGDPQAVAHVDRWLDLLAGCLANILTALDPDVVVLGGG 253
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-321 |
1.31e-26 |
|
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: 106.48 E-value: 1.31e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 3 KVAIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINsvkllNPEIEIQGIGIGAPNA-NYYA 81
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVEVLADLIREYIE-----EAGLKPAAIVIGVPGTvDKDR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 82 GTIEYAANLAFKGVVPLVKLL--KLKFPelkaISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYG 159
Cdd:cd24070 76 RTVISTPNIPGLDGVNLADILenKLGIP----VILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 160 DDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSapGMKrtafelLVKynatdslLADKSFNELDSKMIFDAAERGDKVAN 239
Cdd:cd24070 152 KNGVAGELGHIPVYGNGKPCGCGNTGCLETYAS--GRA------LEE-------IAEEHYPDTPILDIFVDHGDEPELDE 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 240 EVfeqtgKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLTSF-KNKIQILPSQLKPgDAAIVGASAL 318
Cdd:cd24070 217 FV-----EDLALAIATEINILDPDAVILGGGVIDMKGFPRETLEEYIRKHLRKPYpADNLKIIYAELGP-EAGVIGAAIY 290
|
...
gi 1774967535 319 VYQ 321
Cdd:cd24070 291 AFD 293
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
6-292 |
1.50e-25 |
|
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: 103.65 E-value: 1.50e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRYVDDLSSAIHELINSVK--LLNPEIEIQGIgigapnANYYAGT 83
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEFEYRVITLETPEALIDEIIDCIDRLLKLWKdrVKGIALAIQGL------VDSHKGV 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEYAANLAFKGVvPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGF 163
Cdd:cd24072 78 SLWSPGAPWRNI-EIKYLLEERYG--IPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 164 AGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTAFELLvKYNATDSLLADKSFNELdskmiFDAAERGDKVANEVFE 243
Cdd:cd24072 155 SGEIGHTKVNPDGARCDCGRRGCLETVASNSALKRNARVTL-KLGPVSADPEKLTMEQL-----IEALEEGEPIATQIFD 228
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1774967535 244 QTGKWLGQGFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHLLT 292
Cdd:cd24072 229 RAANAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAIAENPFS 277
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
6-318 |
3.10e-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: 102.67 E-value: 3.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGdvdrYvddlsSAIHELINS-VKLLNPEIEIQG-IGIGAPnanyyaGT 83
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRGD----Y-----EATLDAIADlVEEAEEELGAPAtVGIGTP------GS 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEyaanlAFKGVV-----------PLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVV 152
Cdd:cd24066 67 IS-----PRTGLVknanstwlngkPLKADLEARLG--RPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVV 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 153 NGDLVYGDDGFAGECGHTTLIPG------GRLCGCGALGHFEAYCSAPGMKRTAFELLVKYnatdslladksfneLDSKM 226
Cdd:cd24066 140 NGRVLTGANGIAGEWGHNPLPWPdedelpGPPCYCGKRGCVETFLSGPALERDYARLTGKT--------------LSAEE 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 227 IFDAAERGDKVANEVFEQTGKWLGQGFADTAHHLSPEAIFLFGGPTAAgDYIFKPAKESMEKHLLTSFKNkIQILPSQLk 306
Cdd:cd24066 206 IVALARAGDAAAVATLDRFLDRLGRALANVINILDPDVIVLGGGLSNI-DELYTEGPAALARYVFSDEVE-TPIVKNKH- 282
|
330
....*....|...
gi 1774967535 307 pGDAAIV-GASAL 318
Cdd:cd24066 283 -GDSSGVrGAAWL 294
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
1-255 |
1.01e-20 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 90.36 E-value: 1.01e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 1 MKKVAIgvDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDRyvddLSSAIHELINSVKLLNPEIEIQGIGI------GA 74
Cdd:PRK05082 1 MTTLAI--DIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEA----LRQALSALVSPLQAQADRVAVASTGIindgilTA 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 75 PNAnyyagtieyaANLAFKGVVPLVKLLKlkfpEL--KAISMTNDANAAAIGEMiYGGAVGMKNFVMYTLGTGVGSGIVV 152
Cdd:PRK05082 75 LNP----------HNLGGLLHFPLVQTLE----QLtdLPTIALNDAQAAAWAEY-QALPDDIRNMVFITVSTGVGGGIVL 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 153 NGDLVYGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKRTafellvkynatdsllADKSFNELDSKMIFDAAE 232
Cdd:PRK05082 140 NGKLLTGPGGLAGHIGHTLADPHGPVCGCGRRGCVEAIASGRAIAAA---------------AQGWLAGCDAKTIFERAG 204
|
250 260
....*....|....*....|...
gi 1774967535 233 RGDKVANEVFEQTGKWLGQGFAD 255
Cdd:PRK05082 205 QGDEQAQALINRSAQAIARLIAD 227
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
116-323 |
8.32e-18 |
|
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: 82.36 E-value: 8.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 116 NDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPG 195
Cdd:cd24074 110 HDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPA 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 196 MKRTAFELLVKYNATDSLLADKSFNEldskmIFDAAERGDKVANEVFEQTGKWLGQGFADTAHHLSPEAIfLFGGPTAAG 275
Cdd:cd24074 190 ILEQANQLLEQSPDSMLHGQPISIES-----LCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKI-LIGSPLNNA 263
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1774967535 276 DYIFKPA-KESMEKHLLTSFKNKIQILPSQLKpgDAAIVGASALVYQEL 323
Cdd:cd24074 264 AEILFPAlSQSIRQQSLPAYSQHLQIESTKFY--NDGTMPGAALIKDAL 310
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
1-198 |
6.43e-17 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 79.64 E-value: 6.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 1 MKKVAIGVDIGGTNTAIGVVDELGNVVAKGNISTRtdgdvDRYVDDLSSAIHELINSvKLLNPEIEIQGIGIGAPnanyy 80
Cdd:PRK09698 2 QKNVVLGIDMGGTHIRFCLVDAEGEILHCEKKRTA-----EVIAPDLVSGLGEMIDE-YLRRFNARCHGIVMGFP----- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 81 agtieyaanlafkGVVPLVKLLKLKFPELKAiSMTNDANAAAIGEMIYGGAVGMK---NFVM----------------YT 141
Cdd:PRK09698 71 -------------ALVSKDRRTVISTPNLPL-TALDLYDLADKLENTLNCPVFFSrdvNLQLlwdvkennltqqlvlgAY 136
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 1774967535 142 LGTGVGSGIVVNGDLVYGDDGFAGECGHTTLIPGGRLCGCGALGHFEAYCSAPGMKR 198
Cdd:PRK09698 137 LGTGMGFAVWMNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRR 193
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
7-318 |
3.64e-16 |
|
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: 77.20 E-value: 3.64e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 7 GVDIGGTNTAIGVVDELGNVVAKGNISTRTdgdVDRYVDDLSSAIHELinsvkllnpEIEIQGIGIGA-------PNANY 79
Cdd:cd24067 3 GIEAGGTKFVCAVGTGDGNIIERTEFPTTT---PEETLQAVIDFFREQ---------EEPIDAIGIASfgpidlnPTSPT 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 80 YaGTIEYAANLAFKGvVPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVVNGDLVYG 159
Cdd:cd24067 71 Y-GYITTTPKPGWRN-FDILGALKRAFP--VPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHG 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 160 ----------------DDGFAGECghttliPGGRLCgcgalghFEAYCSAPGMKRtafellvKYNATDSLLADksfneld 223
Cdd:cd24067 147 llhpemghirvprhpdDDGFPGVC------PFHGDC-------LEGLASGPAIAA-------RWGIPAEELPD------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 224 skmifdaaergdkvANEVFEQTGKWLGQGFADTAHHLSPEAIFLfGGPTAAGDYIFKPAKESMEKHL-----LTSFKNKI 298
Cdd:cd24067 200 --------------DHPAWDLEAYYLAQACANLTLTLSPERIVL-GGGVMQRPGLFPRIREKFRKLLngyleVPRLLPDI 264
|
330 340
....*....|....*....|..
gi 1774967535 299 Q--ILPSQLKPgDAAIVGASAL 318
Cdd:cd24067 265 DeyIVPPALGN-DAGILGALAL 285
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
7-318 |
2.34e-15 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 75.02 E-value: 2.34e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 7 GVDIGGTNTAIGVVDELGNVVAkgniSTRTDGDVDRYvDDLSSAIHELINSVkllNPEIEIQG-IGIGAPNANYYAGTIE 85
Cdd:PRK13310 4 GFDIGGTKIELGVFNEKLELQW----EERVPTPRDSY-DAFLDAVCELVAEA---DQRFGCKGsVGIGIPGMPETEDGTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 86 YAANLAFKGVVPLVKLLKLKFPelKAISMTNDANAAAIGEMiYGGAVGMKNFVM-YTLGTGVGSGIVVNGDLVYGDDGFA 164
Cdd:PRK13310 76 YAANVPAASGKPLRADLSARLG--RDVRLDNDANCFALSEA-WDDEFTQYPLVMgLILGTGVGGGLVFNGKPISGRSYIT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 165 GECGHTTL-----------IPGGRlCGCGALGHFEAYCSAPGmkrtaFELlvkynatdsLLADKSFNELDSKMIFDAAER 233
Cdd:PRK13310 153 GEFGHMRLpvdaltllgwdAPLRR-CGCGQKGCIENYLSGRG-----FEW---------LYQHYYGEPLQAPEIIALYYQ 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 234 GDKVANEVFEQTGKWLGQGFADTAHHLSPEAIFLfGGPTAAGDYIFKPAKESMEKHLLTSFK-NKIQilpsQLKPGDAAI 312
Cdd:PRK13310 218 GDEQAVAHVERYLDLLAICLGNILTIVDPHLVVL-GGGLSNFDAIYEQLPKRLPRHLLPVARvPRIE----KARHGDAGG 292
|
....*..
gi 1774967535 313 V-GASAL 318
Cdd:PRK13310 293 VrGAAFL 299
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
6-270 |
4.77e-14 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 71.21 E-value: 4.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNIST-RTDgdvdrYVDDLSsAIHELINSVKLlnpEIEIQG-IGIGAPnanyyaGT 83
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTpRDD-----YQQTIE-AIATLVDMAEQ---ATGQRGtVGVGIP------GS 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 84 IEyaanlAFKGVV-----------PLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMYTLGTGVGSGIVV 152
Cdd:PRK09557 68 IS-----PYTGLVknanstwlngqPLDKDLSARLN--REVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAI 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 153 NGDLVYGDDGFAGECGHTTL---------IPGGRLCGCGALGHFEAYCSAPGMKRTAFELlvkynatdslladkSFNELD 223
Cdd:PRK09557 141 NGRVHIGGNGIAGEWGHNPLpwmdedelrYRNEVPCYCGKQGCIETFISGTGFATDYRRL--------------SGKALK 206
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1774967535 224 SKMIFDAAERGDKVANEVFEQTGKWLGQGFADTAHHLSPEAIFLFGG 270
Cdd:PRK09557 207 GSEIIRLVEEGDPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGGG 253
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
7-197 |
1.21e-09 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 58.12 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 7 GVDIGGTNTAIGVVDElgnvvakgNISTRTDGDVDRYVDDLSSAIHELINSVKLLNPEIEIQG-IGIGAPN-ANYYAGTI 84
Cdd:PRK13311 4 GFDMGGTKIELGVFDE--------NLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGsVGIGIPGlPNADDGTV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 85 eYAANLAFKGVVPL-VKLLKLKFPELKaisMTNDANAAAIGEM------IYGGAVGMknfvmyTLGTGVGSGIVVNGDLV 157
Cdd:PRK13311 76 -FTANVPSAMGQPLqADLSRLIQREVR---IDNDANCFALSEAwdpefrTYPTVLGL------ILGTGVGGGLIVNGSIV 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1774967535 158 YGDDGFAGECGHTTL------IPGGRL----CGCGALGHFEAYCSAPGMK 197
Cdd:PRK13311 146 SGRNHITGEFGHFRLpvdaldILGADIprvpCGCGHRGCIENYISGRGFE 195
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
7-157 |
4.25e-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: 56.04 E-value: 4.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 7 GVDIGGTNTAIGVVDElgnvvAKGNISTrtdgdvDRYV---------DDLSSAIHELinsVKLLNPEIEIqGIGIGAPNA 77
Cdd:cd24058 3 GIDIGGSGIKGAIVDT-----DTGELLS------ERIRiptpqpatpEAVADVVAEL---VAHFPWFGPV-GVGFPGVVR 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 78 NyyaGTIEYAANL--AFKGVvPLVKLLKLKFPelKAISMTNDANAAAIGEMIYGGAVGMKNFVMY-TLGTGVGSGIVVNG 154
Cdd:cd24058 68 R---GVVRTAANLdkSWIGF-DAAKLLSKRLG--RPVRVLNDADAAGLAEMKGGAGKGEKGVVLVlTLGTGIGSALFVDG 141
|
...
gi 1774967535 155 DLV 157
Cdd:cd24058 142 HLV 144
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
6-312 |
2.85e-07 |
|
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: 51.15 E-value: 2.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAK---GNISTRTDGdVDRYVDDLSSAIHELINSVKLLNpeiEIQGIGIGApnanyyAG 82
Cdd:cd24007 2 LGVDGGGTKTRAVLADEDGKILGRgkgGPSNPASVG-IEEAKENLKEAVREALSQAGSLG---EIDAICLGL------AG 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 83 tieyAANLAFKGVvpLVKLLKLKFPELKaISMTNDANAAAIGemiyggavgmknfvmytlGTGVGSGIVV---NGDLVYG 159
Cdd:cd24007 72 ----IDSEEDRER--LRSALKELFLSGR-IIIVNDAEIALAA------------------ALGGGPGIVViagTGSVAYG 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 160 DDGfagecghttlipGGRLCGCGALGH-FEAYCSAPGMKRTAFELLVKYN---ATDSLLADKSFNELD------------ 223
Cdd:cd24007 127 RNG------------DGEEARVGGWGHlLGDEGSGYWIGRRALRAALRALdgrGPKTPLLDAILKFLGldsieelitaiy 194
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 224 ------------SKMIFDAAERGDKVANEVFEQTGKWLGQGFADTAHHL---SPEAIFLFGGPTAAGDYIFKpakesMEK 288
Cdd:cd24007 195 rssdrkkeiaslAPLVFEAAEEGDPVAQAILKEAAEELAKLVVALAKLLllgEKLPLALSGGVFKNNYYLAE-----FLE 269
|
330 340
....*....|....*....|....
gi 1774967535 289 HLLTSFKNKIQILPSQLKPGDAAI 312
Cdd:cd24007 270 ELLKKKKPNAKVVEPKGSPVVGAL 293
|
|
| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
6-270 |
6.81e-06 |
|
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: 46.75 E-value: 6.81e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKG-----NISTrtdgDVDRYVDDLSSAIHELINSVKLLNPEIEIQGIGIGApnanyy 80
Cdd:cd24082 3 IGIDGGGTKCRARLADADGTVLGEAtggpaNLSS----DLDQAWASILAAIKQALAQAGLDAAALSDLHAGLGL------ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 81 AGTieyaanlafkGVVPLVKLLKLKFPELKAISMTNDANAAAIGemiyggAVGMKNFVMYTLGTGVGSGIVVNGD----- 155
Cdd:cd24082 73 AGA----------NVPEARAAFLAALPPFASLVVVSDAHIACLG------AHGGEDGAIIILGTGSVGAALDGGEvrqvg 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 156 ---LVYGDDGfagecghttlipGGRLCGCGALGH-FEAY-CSAPGmkrTAF--ELLVKYNATDSLLAD-------KSFNE 221
Cdd:cd24082 137 gwgFPLGDEG------------SGAWLGLRALRHtLLALdGLAPS---SPLtrAVLARFGGDPAEIVAwantatpADFAA 201
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1774967535 222 LdSKMIFDAAERGDKVANEVFEQTGKWLGQgFADTAHHLSPEAIFLFGG 270
Cdd:cd24082 202 L-APLVFEAAEQGDPVALAILQEAAAYIER-LLRALGAQGALPLCLLGG 248
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
6-315 |
9.65e-06 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 46.41 E-value: 9.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKG-----NISTRtdgDVDRYVDDLSSAIHELINSvklLNPEIEIQGIGIGAPNanyy 80
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLGRGraggaNPQSV---GLEEALASLREALEEALAA---AGDPADIEAVGFGLAG---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 81 AGTIEYAANLAfkgvvplvKLLKLKFPElKAISMTNDANAAAIGEmiYGGAVGMknfVMYtLGTG-VGSGIVVNGDLVY- 158
Cdd:COG2971 74 AGTPEDAEALE--------AALRELFPF-ARVVVVNDALAALAGA--LGGEDGI---VVI-AGTGsIAAGRDGDGRTARv 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 159 -------GDDGFAGECGHTTL----------IPGGRLcgcgaLGHFEAYCSAPGMkRTAFELLVKYNATDSLLAdkSFne 221
Cdd:COG2971 139 ggwgyllGDEGSGAWLGREALraalraldgrGPPTAL-----TEAVLAEFGLDDP-EELIAWVYRGPAPPADLA--SL-- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 222 ldSKMIFDAAERGDKVANEVFEQTGKWLGQgFADTAHHLSPEAIFLFGGPTAAGDYIFKPAKESMEKHlltsfknKIQIL 301
Cdd:COG2971 209 --APLVFEAAEAGDPVARAILEEAADELAE-LARALLERGALPVVLAGGVAAAQPLLREALRARLAAG-------GAEIV 278
|
330
....*....|....
gi 1774967535 302 PSQLKPGDAAIVGA 315
Cdd:COG2971 279 PPAGDPVDGALLLA 292
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
5-270 |
2.38e-05 |
|
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: 45.29 E-value: 2.38e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDGDVDryvdDLSSAIHELINSVKLLNPEIEIqgIGIGAPNANyyaGTI 84
Cdd:cd24008 1 ILVGDIGGTNARLALADAGDGSGDLLFVRKYPSADFA----SLEDALAAFLAELGAPRPKAAC--IAVAGPVDG---GRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 85 EyAANLAFKgvVPLVKLLK-LKFPELKAIsmtND--ANAAAI-------GEMIY--GGAVGMKNFVMYTLGTGVGSGIvv 152
Cdd:cd24008 72 R-LTNLDWS--IDAAELRKaLGIGRVRLL---NDfeAAAYGLpalgpedLLVLYggGGPLPGGPRAVLGPGTGLGVAL-- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 153 ngdLVYGDDG----FAGECGHTTLIPGG----RLCG--CGALGH---FEAYCSAPGMKRTaFELLVKynatdslLADKSF 219
Cdd:cd24008 144 ---LVPDGDGgyvvLPSEGGHADFAPVTeeeaELLEflRKRFGRsvsYEDVLSGPGLENI-YEFLAK-------LDGAEP 212
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1774967535 220 NELDSKMIFDAAERGDKVANEVFEQTGKWLGQGFADTA-HHLSPEAIFLFGG 270
Cdd:cd24008 213 PDLTAEEIAEAALAGDPLAREALDLFARILGRFAGNLAlSFLATGGVYLAGG 264
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
3-74 |
5.31e-05 |
|
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: 44.82 E-value: 5.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 3 KVAIGVDIGGTNTAIGVVDELGNVVAKGNISTRT----DG----DVDRYVDDLSSAIHELINSVKlLNPEiEIQGIGIGA 74
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLssphPGwaeqDPEDWWEAVVEAIRELLAKAG-VDPE-EIAAIGVSG 78
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
6-72 |
1.21e-04 |
|
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: 43.34 E-value: 1.21e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRTDG--------DVDRYVDDLSSAIHELINSVKllnpEIEIQGIGI 72
Cdd:cd07773 3 LGIDIGTTNVKAVLFDEDGRILASASRETPLIHpgpgwaelDPEELWEAVKEAIREAAAQAG----PDPIAAISV 73
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
6-72 |
3.15e-04 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY 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: 466787 [Multi-domain] Cd Length: 392 Bit Score: 42.17 E-value: 3.15e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRT----DG----DVDRYVDDLSSAIHELINSVKlLNPEiEIQGIGI 72
Cdd:cd00366 3 LGIDIGTTSVKAALFDEDGNLVASASREYPLiypqPGwaeqDPEDWWQAVVEAIREVLAKAG-IDPS-DIAAIGI 75
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
6-72 |
5.09e-04 |
|
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: 41.38 E-value: 5.09e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKGNISTRT----DG----DVDRYVDDLSSAIHELINSVKlLNPEiEIQGIGI 72
Cdd:cd07802 3 LGIDNGTTNVKAVLFDLDGREIAVASRPTPVisprPGwaerDMDELWQATAEAIRELLEKSG-VDPS-DIAGVGV 75
|
|
| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
6-72 |
1.27e-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: 40.23 E-value: 1.27e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1774967535 6 IGVDIGGTNTAIGVVDELGNVVAKG----NISTRTDGDVDRYVDDLSSAIHELINSVKLLNPEIEIQGIGI 72
Cdd:cd07770 3 LGIDIGTTSTKAVLFDEDGRVVASSsaeyPLIRPEPGWAEQDPEEILEAVLEALKEVLAKLGGGEVDAIGF 73
|
|
| Pan_kinase |
pfam03309 |
Type III pantothenate kinase; Type III pantothenate kinase catalyzes the phosphorylation of ... |
8-99 |
4.04e-03 |
|
Type III pantothenate kinase; Type III pantothenate kinase catalyzes the phosphorylation of pantothenate (Pan), the first step in the universal pathway of CoA biosynthesis.
Pssm-ID: 460881 [Multi-domain] Cd Length: 205 Bit Score: 37.93 E-value: 4.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 8 VDIGGTNTAIGVVDElGNVVAKGNISTrtdgDVDRYVDDLSSAIHELINsvklLNPEIEIQGIGIG--APNANYyagTIE 85
Cdd:pfam03309 4 IDIGNTNIKWGLFDG-DKLVAHWRIST----DARRTADELGVLLRSLLR----LAGIDPIDGVIISsvVPPLNA---ALE 71
|
90
....*....|....
gi 1774967535 86 YAANLAFKgVVPLV 99
Cdd:pfam03309 72 RACLKYFK-IEPLV 84
|
|
| ASKHA_NBD_benz_CoA_BcrA_BadF |
cd24104 |
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar ... |
5-73 |
7.51e-03 |
|
nucleotide-binding domain (NBD) of benzoyl-CoA reductase subunit A (BcrA/BadF) and similar proteins; Benzoyl-CoA reductase (EC 1.3.7.8), also called benzoyl-CoA reductase (dearomatizing), or 3-hydroxybenzoyl-CoA reductase, catalyzes the anaerobic reduction of benzoyl-CoA and 3-hydroxybenzoyl-CoA to form cyclohexa-1,5-diene-1-carbonyl-CoA and 3-hydroxycyclohexa-1,5-diene-1-carbonyl-CoA, respectively. The enzyme also reduces other benzoyl-CoA analogs with small substituents at the aromatic ring. The model corresponds to subunit A of benzoyl-CoA reductase.
Pssm-ID: 466954 Cd Length: 253 Bit Score: 37.27 E-value: 7.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1774967535 5 AIGVDIGGTNTAIGVVDELGNVVAKGNISTRTDgdvdrYVDDLSSAIHELINSVKLLNPEIE-IQGIGIG 73
Cdd:cd24104 1 AAGVDVGSTQTKAVIIDEDGEIVGRGLTNTGAN-----VVVAAERAFREAIEEAGIKEEEVEyVVGTGYG 65
|
|
| |
