|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
4-315 |
2.27e-163 |
|
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: 457.52 E-value: 2.27e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 4 KIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTV 83
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 84 VGAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGE 163
Cdd:cd24062 81 EVAVNLGWKNF-PLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 164 VGHVTVDP-NGFDCTCGKRGCLETVSSATGVVRVARHLSEEFAGDSELKqAIDDGQDVSSKDVFEFAEKGDHFALMVVDR 242
Cdd:cd24062 160 IGHITVNPeGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALR-ILALGGELTAKDVFEAAKAGDELALAVVDT 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488285125 243 VCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24062 239 VARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-318 |
1.32e-108 |
|
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: 318.38 E-value: 1.32e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 1 MDKKIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEK 80
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 81 GTVVGAYNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGC 160
Cdd:COG1940 83 GVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 161 AGEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEefagdselkqaiddGQDVSSKDVFEFAEKGDHFALMVV 240
Cdd:COG1940 163 AGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGG--------------AEKLTAEELFAAARAGDPLALEVL 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488285125 241 DRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLALQ 318
Cdd:COG1940 229 DEAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
6-323 |
1.88e-92 |
|
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: 277.94 E-value: 1.88e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDGVVQQKWSIETNilEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVVG 85
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTD--TTPETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 86 AYNLNWTTvQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVG 165
Cdd:TIGR00744 79 AVNLDWKQ-EPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 166 HVTVDPNG-FDCTCGKRGCLETVSSATGVVRVARHLSEEFAGDSELKQAIDDGQdVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:TIGR00744 158 HIRMVPDGrLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDG-ISAKHVFVAARQGDPVAVDSYREVA 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLALQFSKEK 323
Cdd:TIGR00744 237 RWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAADLARTYIIEP 315
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
4-315 |
7.79e-86 |
|
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: 259.80 E-value: 7.79e-86
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 4 KIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHridlyNMKKEDFVGIGMGTPGSVDIEKGTV 83
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAE-----LKEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 84 VGAY-NL-NWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCA 161
Cdd:cd24068 76 IYATdNLpGWTGT-NLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 162 GEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEEfagdselkqaiddgQDVSSKDVFEFAEKGDHFALMVVD 241
Cdd:cd24068 155 GELGHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGE--------------PGIDGREIFDLADAGDPLAKEVVE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488285125 242 RVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24068 221 EFAEDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
5-318 |
1.35e-76 |
|
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: 236.69 E-value: 1.35e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24076 83 LAPNLGWRDV-PLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARhlseefagdselkQAIDDGQDVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:cd24076 162 GHMTVDPDGPPCSCGNRGCWETYASERALLRAAG-------------RLGAGGEPLSLAELVEAARAGDPAALAALEEVG 228
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLALQ 318
Cdd:cd24076 229 EYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALAID 302
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
5-315 |
1.09e-70 |
|
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: 221.60 E-value: 1.09e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDlynmkKEDFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELIE-----EMELLGIGIGSPGSIDRENGIVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNL-NWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGE 163
Cdd:cd24064 76 FSPNFpDWRNF-PLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 164 VGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEEFAgdSELKQAIDdgqDVSSKDVFEFAEKGDHFALMVVDRV 243
Cdd:cd24064 155 LGHVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRYP--DSLAGESE---KINAKHVFDAARKNDPLATMVFRRV 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488285125 244 CFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24064 230 VDALAIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAASI 301
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-315 |
3.57e-67 |
|
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: 210.40 E-value: 3.57e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNmKKEDFVGIGMGTPGSVDIEKGTVVG 85
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAG-VRERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 86 AYNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTgvgggivaagELLHGVAGCAGEVG 165
Cdd:cd23763 80 APNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTgigggiiidgKLYRGANGAAGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 166 HVTvdpngfdctcgkrgcletvssatgvvrvarhlseefagdselkqaiddgqdvsskdvfefaekgdhfalmVVDRVCF 245
Cdd:cd23763 160 HIT----------------------------------------------------------------------VLEEAAR 169
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 246 YLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd23763 170 YLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAAL 239
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
6-318 |
3.23e-66 |
|
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: 209.89 E-value: 3.23e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDGVVQQKWSIETNiledGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVVG 85
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTP----TTTTEETLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 86 AYNLNWTTvQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVG 165
Cdd:pfam00480 77 TPNIGWDN-FDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 166 HVTVDPNGFDCTCGKRGCLETVSSATGVVRVARhlseefagdselkqaiDDGQDVSSKDVFEFAEKGDHFALMVVDRVCF 245
Cdd:pfam00480 156 HIQLDPNGPKCGCGNHGCLETIASGRALEKRYQ----------------QKGEDLEGKDIIVLAEQGDEVAEEAVERLAR 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488285125 246 YLGLATGNLGNTLNPDSVVIGGGVSAAGEFL---RSRVEKY-FQEFTFPQVRnstkIKLAELGNEAGVIGAASLALQ 318
Cdd:pfam00480 220 YLAKAIANLINLFDPQAIVLGGGVSNADGLLeaiRSLVKKYlNGYLPVPPVI----IVAASLGDNAGALGAAALAKQ 292
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
4-317 |
7.06e-64 |
|
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and similar proteins; This subfamily includes a group of uncharacterized proteins similar to N-acetylglucosamine kinase (Tm1224; EC 2.7.1.59) from Thermotoga maritima, which belongs to kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Tm1224 lacks the cysteine-rich zinc-binding motif, which presents in other family members.
Pssm-ID: 466909 [Multi-domain] Cd Length: 305 Bit Score: 203.97 E-value: 7.06e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 4 KIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNmKKEDFVGIGMGTPGSVDIEKGTV 83
Cdd:cd24059 2 YVIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKEN-IKSKILGIGIGAPGPLDVEKGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 84 VGAYNL-NWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAG 162
Cdd:cd24059 81 LNPPNFpGWENI-PLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 163 EVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARhlseefagdSELKQAIDDgqdvsSKDVFEFAEKGDHFALMVVDR 242
Cdd:cd24059 160 EIGHTSIDINGPRCSCGNRGCLELYASIPAIEKKAR---------SALGSGRSF-----QLDIVEALQKGDPIADEVIEE 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488285125 243 VCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLAL 317
Cdd:cd24059 226 AAKYLGIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAAALVL 300
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
6-317 |
1.95e-62 |
|
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: 200.66 E-value: 1.95e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDG-KHIVPSIIESIRHRidlynmkkEDFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGiVDAIVEAVEELREG--------HDVSAVGVAAAGFVDADRATVL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24061 74 FAPNIAWRNE-PLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEEFAGDSELKQAIDDGQDVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:cd24061 153 GHIRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATPEGAAVLLADGSVDGITGKHISEAARAGDPVALDALRELA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAAGE-FLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLAL 317
Cdd:cd24061 233 RWLGAGLASLAALLDPELFVIGGGVSDAGDlLLDPIREAFERWLPGRGWRPIPRLRTAQLGNDAGLIGAADLAR 306
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
5-315 |
4.82e-60 |
|
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: 194.48 E-value: 4.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRhrIDLYNMKKEDFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIE--TLLSKAGKDSIEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24063 80 NSPNIKGKEI-PLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPN-GFDCTCGKRGCLETVSSATGVVRVARHLSEEFAGDSELKQAIDDGQDVSSKDVFEFAEKGDHFALMVVDRV 243
Cdd:cd24063 159 GHLVVDTEsGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488285125 244 CFYLGLATGNLGNTLNPDSVVIGGGV-SAAGEFLRSRVEKYFQEFTFpqvRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24063 239 ARYNGRGIANVINAYDPELIVIGGSVfNNNKDILDPLIEYLEKNPAI---SKGPEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
5-318 |
1.29e-55 |
|
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Listeria monocytogenes Lmo0178 protein, which is a predicted transcription repressor belonging to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466921 [Multi-domain] Cd Length: 312 Bit Score: 183.26 E-value: 1.29e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKKEdFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLIKNKHVEKK-LLGIGIAVSGLVDSKKGIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24071 82 RSTILGWENV-ELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEefagdSELKQAIDDGQDVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:cd24071 161 GHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTE-----SYPLSLLKELEDFEIEKVREAAEEGDSVATELFKKAG 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLALQ 318
Cdd:cd24071 236 EYLGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVID 309
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-315 |
1.96e-55 |
|
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: 181.76 E-value: 1.96e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 4 KIIGIDLGGTTIKFAILTtDGVVQQKwSIETNILEDGKHIVPSIIESIRhriDLynmkKEDFVG---IGMGTPGSVDIEK 80
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSR-LVVPTPREGGEAVLDALARAVE---AL----QAEAPGveaVGLGVPGPLDFRR 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 81 GTVVGAYNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGC 160
Cdd:cd24065 72 GRVRFAPNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQ 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 161 AGEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSeefagdselkqaiddGQDVSSKDVFEFAEKGDHFALMVV 240
Cdd:cd24065 152 AGEIGHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAY---------------GRPMSTAELFELAQQGEPKALRIV 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488285125 241 DRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTfpQVRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24065 217 EQAAAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARRYT--EGWHAPPLRLAHLGTDAGVIGAALA 289
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
8-318 |
1.46e-54 |
|
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: 180.06 E-value: 1.46e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 8 IDLGGTTIKFAILTTDGVvqqkwsietnileDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVVGAY 87
Cdd:cd24073 18 TDLRGNVLASHTLPLDSG-------------DPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRWSP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 88 NLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVGHV 167
Cdd:cd24073 85 LLGWRDV-PLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHT 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 168 TVDPNGFDCTCGKRGCLETVSSATGVVRVARhlseefagdselkQAIDDGQDVSSKDVFEFAEKGDHFALMVVDRVCFYL 247
Cdd:cd24073 164 TVDPDGPPCRCGKRGCLEAYASDPAILRQAR-------------EAGLRGEPLTIEDLLAAARAGDPAARAILRRAGRAL 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 488285125 248 GLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNSTKIKLAELGNEAGVIGAASLALQ 318
Cdd:cd24073 231 GLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGAAALALQ 301
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
4-315 |
2.09e-46 |
|
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: 158.50 E-value: 2.09e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 4 KIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEdgkhiVPSIIESIRHRIDLYnmkKEDFVGIGMGTPGSVDIEKGTV 83
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDS-----LEEFLDYIKKIIKRY---DEEIDGIAISAPGVIDPETGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 84 VGAYNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGE 163
Cdd:cd24152 73 YGGGALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGE 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 164 VGHVTVDPNGFDCTCGKRGCletvsSATGVVRVARHLSeefagdselkqaidDGQDVSSKDVFEFAEKGDHFALMVVDRV 243
Cdd:cd24152 153 FSYLLTDDDDKDLLFFSGLA-----SMFGLVKRYNKAK--------------GLEPLDGEEIFEKYAKGDEAAKKILDEY 213
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488285125 244 CFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLrSRVEKYFQEFT--FPQVRNSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24152 214 IRNLAKLIYNIQYILDPEVIVIGGGISEQPLFI-EDLKKEVNEILanRPGSIPKPEIKACKFGNDANLLGALYN 286
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-316 |
4.28e-46 |
|
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: 157.71 E-value: 4.28e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 3 KKIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKkedFVGIGMGTPGSVDIEKGT 82
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVEVLADLIREYIEEAGLK---PAAIVIGVPGTVDKDRRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 83 VVGAYNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAG 162
Cdd:cd24070 78 VISTPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 163 EVGHVTVDPNGFDCTCGKRGCLETVSSAtgvvRVARHLSEEFagdselkqaiddGQDVSSKDVFEfaekgDHFALMVVDR 242
Cdd:cd24070 158 ELGHIPVYGNGKPCGCGNTGCLETYASG----RALEEIAEEH------------YPDTPILDIFV-----DHGDEPELDE 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488285125 243 VCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFT-FPQVRNSTKIKLAELGNEAGVIGAASLA 316
Cdd:cd24070 217 FVEDLALAIATEINILDPDAVILGGGVIDMKGFPRETLEEYIRKHLrKPYPADNLKIIYAELGPEAGVIGAAIYA 291
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
8-315 |
5.46e-44 |
|
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: 152.57 E-value: 5.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 8 IDLGGTTIKFAILTTDGVVQQKWSIETniledgkhivPSIIESirhRID-LYNMKKE----------DFVGIGMGTPGSV 76
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPN----------PKTYEE---RIDlILQMCVEaaseavklncRILGVGISTGGRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 77 DIEKGTVVGAYNL--NWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELL 154
Cdd:cd24060 72 NPREGIVLHSTKLiqEWSSV-DLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELI 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 155 HGVAGCAGEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEE----FAGdselkQAIDDGQDVSSKDVFEFAE 230
Cdd:cd24060 151 HGSSFCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAKKLHDEdlllVEG-----MSVTNDEEVTAKHLIQAAK 225
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 231 KGDHFALMVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEflrSRVEKYFQEFTFPQVRNsTKIKLAELgNEAGVI 310
Cdd:cd24060 226 LGNAKAQKILRTAGTALGLGIVNILHTLNPSLVILSGVLASHYE---NIVKDVIAQRALPSVQN-VDVVVSDL-VDPALL 300
|
....*
gi 488285125 311 GAASL 315
Cdd:cd24060 301 GAASM 305
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
5-315 |
6.24e-44 |
|
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: 152.39 E-value: 6.24e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKWSIETNIlEDGKHIVPSIIESIrHRIDLYNMKKEDfvgIGMGTPGSVDIEKGTVV 84
Cdd:cd24057 2 YYGFDIGGTKIEFAVFDEALQLVWTKRVPTPT-DDYAAFLAAIAELV-AEADARFGVKGP---VGIGIPGVIDPEDGTLI 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAyNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24057 77 TA-NIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GH----VTVDPNGFD-----CTCGKRGCLETVSSATGVVRVARHLSeefagdselkqaiddGQDVSSKDVFEFAEKGDHF 235
Cdd:cd24057 156 GHgplpADALLLGYDlpvlrCGCGQTGCLETYLSGRGLERLYAHLY---------------GEELDAPEIIAAWAAGDPQ 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 236 ALMVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRsRVEKYFQEFTFPQVRnSTKIKLAELGNEAGVIGAASL 315
Cdd:cd24057 221 AVAHVDRWLDLLAGCLANILTALDPDVVVLGGGLSNFPALIA-ELPAALPAHLLSGAR-TPRIVPARHGDAGGVRGAAFL 298
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
6-315 |
1.71e-42 |
|
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; Escherichia coli FRK (EC 2.7.1.4), also called D-fructose kinase, manno(fructo)kinase, or MAK, catalyzes the phosphorylation of fructose to fructose-6-phosphate. It has also low level glucokinase activity in vitro. It is not able to phosphorylate D-ribose, D-mannitol, D-sorbitol, inositol, and L-threonine. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466916 [Multi-domain] Cd Length: 294 Bit Score: 148.51 E-value: 1.71e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDGVVQQKWSIETniLEDGKHivpSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVVG 85
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPT--PRGDYE---ATLDAIADLVEEAEEELGAPATVGIGTPGSISPRTGLVKN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 86 AyNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVG 165
Cdd:cd24066 77 A-NSTWLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 166 HVTVDP------NGFDCTCGKRGCLETVSSATGVVRVARHLSeefagdselkqaiddGQDVSSKDVFEFAEKGDHFALMV 239
Cdd:cd24066 156 HNPLPWpdedelPGPPCYCGKRGCVETFLSGPALERDYARLT---------------GKTLSAEEIVALARAGDAAAVAT 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488285125 240 VDRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAgEFLRSRVEKYFQEFTF-PQVRnsTKIKLAELGNEAGVIGAASL 315
Cdd:cd24066 221 LDRFLDRLGRALANVINILDPDVIVLGGGLSNI-DELYTEGPAALARYVFsDEVE--TPIVKNKHGDSSGVRGAAWL 294
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
38-315 |
2.40e-40 |
|
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: 143.28 E-value: 2.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 38 EDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVVgaYN-LNWTTVQPVKEQIESALGIPFALDNDAN 116
Cdd:cd24075 35 LNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVH--YMpHIQVKSWPIVEELEQRFNVPCFIGNDIR 112
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 117 VAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRV 196
Cdd:cd24075 113 SLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGHIQIEPLGERCHCGNFGCLETVASNAAIEQR 192
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 197 ARHLSEefAG-DSELkqaidDGQDVSSKDVFEFAEKGDHFALMVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEF 275
Cdd:cd24075 193 VKKLLK--QGyASQL-----TLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGEITQADKV 265
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 488285125 276 LRSRVEKYFQEFTFPQVRNSTKIKLAELgNEAGVIGAASL 315
Cdd:cd24075 266 LLPVIKKCIQSQALPDFRQELKIVASQL-DHNSAIGAFAL 304
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
8-315 |
3.45e-40 |
|
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: 142.04 E-value: 3.45e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 8 IDLGGTTIKFAILTtDGVVQQKWSIETNILEDGKhivpSIIESIRHRIDLYnmkKEDFVGIGMGTPGSVDIEKGTVVGAY 87
Cdd:cd24069 3 IDIGGTKIAAALIG-NGQIIDRRQIPTPRSGTPE----ALADALASLLADY---QGQFDRVAVASTGIIRDGVLTALNPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 88 NLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVGHV 167
Cdd:cd24069 75 NLGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 168 TVDPNGFDCTCGKRGCLETVSSATGVVRVARHLseefagdselkqaidDGQDVSSKDVFEFAEKGDHFALMVVDRVCFYL 247
Cdd:cd24069 155 LADPPGPVCGCGRRGCVEAIASGTAIAAAASEI---------------LGEPVDAKDVFERARSGDEEAARLIDRAARAL 219
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 488285125 248 GLATGNLGNTLNPDSVVIGGGVSAAGEFLrSRVEKYFQEF-TFPQVrnstKIKLAELGNEAGVIGAASL 315
Cdd:cd24069 220 ADLIADLKATLDLDCVVIGGSVGLAEGFL-ERVEQYLADEpAIFRV----SLEPARLGQDAGLLGAALL 283
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
5-307 |
8.08e-40 |
|
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: 141.78 E-value: 8.08e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKwsiETNILEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24072 3 VLGIVVSPNSLRAQVGNACGELLGE---FEYRVITLETPEALIDEIIDCIDRLLKLWKDRVKGIALAIQGLVDSHKGVSL 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24072 80 WSPGAPWRNI-EIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEI 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSEEFAGDSelkqaidDGQDVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:cd24072 159 GHTKVNPDGARCDCGRRGCLETVASNSALKRNARVTLKLGPVSA-------DPEKLTMEQLIEALEEGEPIATQIFDRAA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTFPQVRNST-KIKLAELGNEA 307
Cdd:cd24072 232 NAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAIAENPFSQHATQIgFGQLSTEQGCA 295
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
6-318 |
1.43e-33 |
|
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: 124.96 E-value: 1.43e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDG-VVQQKWsiETNILEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVV 84
Cdd:cd24077 4 IGIDLGYNYISLMLTYLDGeIISSKQ--IKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENEIIFT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNwttVQPVKEQIESALGIPFALDNDANVAALGERwkGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:cd24077 82 PYYDLE---DIDLKEKLEEKFNVPVYLENEANLSALAER--TFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPNGFDCTCGKRGCLETVSSatgvvrvARHLSEEFagdSELKQAiddgQDVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:cd24077 157 GHMIIVPNGKPCPCGNKGCLEQYAS-------EKALLKEL---SEKKGL----ETLTFDDLIQLYNEGDPEALELIDQFI 222
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAA-GEFLrSRVEKYFQEFTfpqvRNSTKIKLAELGNEAGVIGAASLALQ 318
Cdd:cd24077 223 KYLAIGINNIINTFNPEIIIINSSLINEiPELL-EKIKEQLSSSF----NKYVEILISTLGKNATLLGGAAVAIK 292
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
1-318 |
5.38e-32 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 120.86 E-value: 5.38e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 1 MDKKIIGIDLGGTTIKFAILTTDGVVQQKWSIETNILEDGKHIVpSIIESIRHRIDLYNMKKEdfvGIGMGTPGSVDIEK 80
Cdd:PRK09698 2 QKNVVLGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVS-GLGEMIDEYLRRFNARCH---GIVMGFPALVSKDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 81 GTVVGAYNLNWTT--VQPVKEQIESALGIPFALDNDANVAALgerWKgAGENN--PDVIF-ITLGTGVGGGIVAAGELLH 155
Cdd:PRK09698 78 RTVISTPNLPLTAldLYDLADKLENTLNCPVFFSRDVNLQLL---WD-VKENNltQQLVLgAYLGTGMGFAVWMNGAPWT 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 156 GVAGCAGEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVArhlsEEFAGDSELKQAiddgqdvsskdvfeFAEKGDHF 235
Cdd:PRK09698 154 GAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWY----EQQPRDYPLSDL--------------FVHAGDHP 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 236 AL-MVVDRVCFYlgLATGNlgNTLNPDSVVIGGGVSAAGEFLRSRVEKYFQEFTF-PQVRNSTKIKLAELGNEAGVIGAA 313
Cdd:PRK09698 216 FIqSLLENLARA--IATSI--NLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRkPLPYEVVRFIYASSSDFNGAQGAA 291
|
....*
gi 488285125 314 SLALQ 318
Cdd:PRK09698 292 ILAHQ 296
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
46-318 |
6.57e-29 |
|
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: 113.18 E-value: 6.57e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 46 SIIESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEKGTVV--GAYNL-NWttvqPVKEQIESALGIPFALDNDANVAALGE 122
Cdd:cd24074 44 RLLESISEFFSRHQKKLERLTAIAITLPGIIDPESGIVHrlPFYDIkNL----PLGEALEQHTGLPVYVQHDISAWTLAE 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 123 RWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVGHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARHLSE 202
Cdd:cd24074 120 RFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 203 EFaGDSELKQaiddgQDVSSKDVFEFAEKGDHFALMVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLRSRVEK 282
Cdd:cd24074 200 QS-PDSMLHG-----QPISIESLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNNAAEILFPALSQ 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 488285125 283 YFQEFTFPQVRNSTKIKLAELgNEAGVIGAASLALQ 318
Cdd:cd24074 274 SIRQQSLPAYSQHLQIESTKF-YNDGTMPGAALIKD 308
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
8-316 |
6.12e-27 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 107.31 E-value: 6.12e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 8 IDLGGTTIKFAILTTDGVVQQKWSIET---NILEDGKHIVPSIIESIRHRIDlynmkkedFVGIGmgTPGSVDIEKGTVV 84
Cdd:PRK05082 6 IDIGGTKIAAALVGEDGQIRQRRQIPTpasQTPEALRQALSALVSPLQAQAD--------RVAVA--STGIINDGILTAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTTVQPVKEQIESALGIPFALDNDANVAALGErWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEV 164
Cdd:PRK05082 76 NPHNLGGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 165 GHVTVDPNGFDCTCGKRGCLETVSSATGVVRVARhlseefagdselkqaiDDGQDVSSKDVFEFAEKGDHFALMVVDRVC 244
Cdd:PRK05082 155 GHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQ----------------GWLAGCDAKTIFERAGQGDEQAQALINRSA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488285125 245 FYLGLATGNLGNTLNPDSVVIGGGVSAAGEFLrSRVEKYFQEftFPQVRNsTKIKLAELGNEAGVIGAASLA 316
Cdd:PRK05082 219 QAIARLIADLKATLDCQCVVLGGSVGLAEGYL-ELVQAYLAQ--EPAIYH-VPLLAAHYRHDAGLLGAALWA 286
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
7-317 |
3.13e-24 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 100.06 E-value: 3.13e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 7 GIDLGGTTIKFAILttDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDlynmkkEDFVG---IGMGTPGSVDIEKGTV 83
Cdd:PRK13310 4 GFDIGGTKIELGVF--NEKLELQWEERVPTPRDSYDAFLDAVCELVAEAD------QRFGCkgsVGIGIPGMPETEDGTL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 84 VGAyNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGE 163
Cdd:PRK13310 76 YAA-NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 164 VGHVTV----------DPNGFDCTCGKRGCLETVSSATGVVRVARHLSeefagdselkqaiddGQDVSSKDVFEFAEKGD 233
Cdd:PRK13310 155 FGHMRLpvdaltllgwDAPLRRCGCGQKGCIENYLSGRGFEWLYQHYY---------------GEPLQAPEIIALYYQGD 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 234 HFALMVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVS---AAGEFLRSRVEKYFQeftfpQVRNSTKIKLAELGNEAGVI 310
Cdd:PRK13310 220 EQAVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLSnfdAIYEQLPKRLPRHLL-----PVARVPRIEKARHGDAGGVR 294
|
....*..
gi 488285125 311 GAASLAL 317
Cdd:PRK13310 295 GAAFLHL 301
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
5-315 |
7.03e-24 |
|
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: 98.77 E-value: 7.03e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDGVVQQKWSIETniledgkhIVPSiiESIRHRIDLYNMKKEDFVGIGMGTPGSVDIEK---- 80
Cdd:cd24067 1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPT--------TTPE--ETLQAVIDFFREQEEPIDAIGIASFGPIDLNPtspt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 81 -GTVVGAYNLNWTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGvag 159
Cdd:cd24067 71 yGYITTTPKPGWRNF-DILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHG--- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 160 cAG--EVGH--VTVDPN--GFDCTC-GKRGCLETVssATGVVRVARhlseefagdseLKQAIDDGQDvsskdvfefaekg 232
Cdd:cd24067 147 -LLhpEMGHirVPRHPDddGFPGVCpFHGDCLEGL--ASGPAIAAR-----------WGIPAEELPD------------- 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 233 DHFalmVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVSaAGEFLRSRVEKYFQEFT--FPQVRNSTK-----IKLAELGN 305
Cdd:cd24067 200 DHP---AWDLEAYYLAQACANLTLTLSPERIVLGGGVM-QRPGLFPRIREKFRKLLngYLEVPRLLPdideyIVPPALGN 275
|
330
....*....|
gi 488285125 306 EAGVIGAASL 315
Cdd:cd24067 276 DAGILGALAL 285
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
6-315 |
3.62e-23 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 97.02 E-value: 3.62e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 6 IGIDLGGTTIKFAILTTDGVVQQKWSIETNiledgKHIVPSIIESIrhrIDLYNMKkEDFVG----IGMGTPGSVDIEKG 81
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTP-----RDDYQQTIEAI---ATLVDMA-EQATGqrgtVGVGIPGSISPYTG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 82 TVVGAyNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCA 161
Cdd:PRK09557 74 LVKNA-NSTWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 162 GEVGH-----VTVD----PNGFDCTCGKRGCLETVSSATGVVRVARHLSeefagdselkqaiddGQDVSSKDVFEFAEKG 232
Cdd:PRK09557 153 GEWGHnplpwMDEDelryRNEVPCYCGKQGCIETFISGTGFATDYRRLS---------------GKALKGSEIIRLVEEG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 233 DHFALMVVDRVCFYLGLATGNLGNTLNPDSVVIGGGVsaageflrSRVEKYFQefTFPQVRNS--------TKIKLAELG 304
Cdd:PRK09557 218 DPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGGGM--------SNVDRLYP--TLPALLKQyvfggeceTPVRKALHG 287
|
330
....*....|.
gi 488285125 305 NEAGVIGAASL 315
Cdd:PRK09557 288 DSSGVRGAAWL 298
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
5-316 |
1.24e-13 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 69.14 E-value: 1.24e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTD--GVVQQKWSIETNILEDGKHIVPSIIESIRHridlynmkKEDFVGIGMGTPGSVdiEKGT 82
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDTDtgELLSERIRIPTPQPATPEAVADVVAELVAH--------FPWFGPVGVGFPGVV--RRGV 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 83 VVGAYNLN--WTTVqPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPD-VIFITLGTGVGGGIVAAGELLHGVag 159
Cdd:cd24058 71 VRTAANLDksWIGF-DAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGvVLVLTLGTGIGSALFVDGHLVPNT-- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 160 cagEVGHVTVDpngfdctcgkRGCLETVSSAtgVVRVARHLSEEfagdselkqaiddgqdvsskdvfEFAEkgdhfalmv 239
Cdd:cd24058 148 ---ELGHLEIR----------GKDAEERASL--GVRAREDLGWK-----------------------RWAK--------- 180
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488285125 240 vdRVCFYLglatGNLGNTLNPDSVVIGGGVSaageflrsrveKYFQEFtFPQVRNSTKIKLAELGNEAGVIGAASLA 316
Cdd:cd24058 181 --RVNKYL----QYLERLFNPDLFIIGGGNS-----------KKADKF-LPLLDVKTPVVPAVLRNDAGIVGAALLA 239
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
7-254 |
2.76e-13 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 68.52 E-value: 2.76e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 7 GIDLGGTTIKFAILttDGVVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKKEDfvgIGMGTPGSVDIEKGTVVGA 86
Cdd:PRK13311 4 GFDMGGTKIELGVF--DENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGS---VGIGIPGLPNADDGTVFTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 87 yNLNWTTVQPVKEQIESALGIPFALDNDANVAALGERWKGAGENNPDVIFITLGTGVGGGIVAAGELLHGVAGCAGEVGH 166
Cdd:PRK13311 79 -NVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 167 VTVDPNGFD----------CTCGKRGCLETVSSATGVVRVARHLSEefagdselkqaiddgQDVSSKDVFEFAEKGDHFA 236
Cdd:PRK13311 158 FRLPVDALDilgadiprvpCGCGHRGCIENYISGRGFEWMYSHFYQ---------------HTLPATDIIAHYAAGEPKA 222
|
250
....*....|....*...
gi 488285125 237 LMVVDRVCFYLGLATGNL 254
Cdd:PRK13311 223 VAHVERFMDVLAVCLGNL 240
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
5-313 |
1.95e-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: 45.68 E-value: 1.95e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILttDGVVQQKWSIETNILEDGKHivPSIIESIRHRIDlyNMKKEDFVGIGMGTPGSVDiekGTVV 84
Cdd:cd24008 1 ILVGDIGGTNARLALA--DAGDGSGDLLFVRKYPSADF--ASLEDALAAFLA--ELGAPRPKAACIAVAGPVD---GGRV 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 85 GAYNLNWTtvqpVK-EQIESALGI-PFALDNDanVAALG-----------ERWKGAGENNPDVIFITL--GTGvgggiva 149
Cdd:cd24008 72 RLTNLDWS----IDaAELRKALGIgRVRLLND--FEAAAyglpalgpedlLVLYGGGGPLPGGPRAVLgpGTG------- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 150 agelLhGVAG-----------CAGEVGHVTVDPNGFD-----CTCGKRG----CLETVSSATGVVRVARHLSEEFAGDSE 209
Cdd:cd24008 139 ----L-GVALlvpdgdggyvvLPSEGGHADFAPVTEEeaellEFLRKRFgrsvSYEDVLSGPGLENIYEFLAKLDGAEPP 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 210 LKQAiddgqdvssKDVFEFAEKGDHFALMVVDRVCFYLGLATGNLG-NTLNPDSVVIGGGVSAA-GEFLRSrvEKYFQEF 287
Cdd:cd24008 214 DLTA---------EEIAEAALAGDPLAREALDLFARILGRFAGNLAlSFLATGGVYLAGGIAPKnLDLLDS--SAFREAF 282
|
330 340 350
....*....|....*....|....*....|
gi 488285125 288 T----FPQVRNSTKIKLAeLGNEAGVIGAA 313
Cdd:cd24008 283 LdkgrMSDLLEDIPVYLV-TNEDLGLLGAA 311
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
5-318 |
3.55e-05 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 44.87 E-value: 3.55e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDG-VVQQKWSIETNILEDG-KHIVPSIIESIRhRIDLYNMKKEDFVGIGMGTPGSVDIEKgt 82
Cdd:COG2971 3 ILGVDGGGTKTRAVLVDADGeVLGRGRAGGANPQSVGlEEALASLREALE-EALAAAGDPADIEAVGFGLAGAGTPED-- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 83 vvgaynlnwttvqpvKEQIESAL-----GIPFALDNDANVAALGerwkgAGENNPDVIFItLGTgvgggivaagellhGV 157
Cdd:COG2971 80 ---------------AEALEAALrelfpFARVVVVNDALAALAG-----ALGGEDGIVVI-AGT--------------GS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 158 AGCA--GEVGHVTVDPNGF---D----CTCGKRGCLETVSSATGVV---RVARHLSEEFAGDS--ELKQAIDDGQ----D 219
Cdd:COG2971 125 IAAGrdGDGRTARVGGWGYllgDegsgAWLGREALRAALRALDGRGpptALTEAVLAEFGLDDpeELIAWVYRGPappaD 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 220 VSS--KDVFEFAEKGDHFALMVVDRVCFYLGLATGNLGNTlNPDSVVIGGGVSAAGEFLRSRVEKYFQEftfpqvrnsTK 297
Cdd:COG2971 205 LASlaPLVFEAAEAGDPVARAILEEAADELAELARALLER-GALPVVLAGGVAAAQPLLREALRARLAA---------GG 274
|
330 340
....*....|....*....|.
gi 488285125 298 IKLAELGNEAgVIGAASLALQ 318
Cdd:COG2971 275 AEIVPPAGDP-VDGALLLALR 294
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
5-315 |
3.59e-04 |
|
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: 41.52 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 5 IIGIDLGGTTIKFAILTTDG-VVQQKWSIETNILEDGKHIVPSIIESIRHRIDLYNMKKEDFVGIGMGTPGsVDIEKgtv 83
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGkILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAGSLGEIDAICLGLAG-IDSEE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 84 vgaynlnwtTVQPVKEQIESALGI-PFALDNDANVAalgerWKGAGENNPDVIFItLGTGVGGGIVAAGELLHGVAGCag 162
Cdd:cd24007 77 ---------DRERLRSALKELFLSgRIIIVNDAEIA-----LAAALGGGPGIVVI-AGTGSVAYGRNGDGEEARVGGW-- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 163 evGHVTVDP-NGFDctCGKRGCLETVSSATGVV-------RVARHLSEEFAGD--SELKQAIDDGQDVSS--KDVFEFAE 230
Cdd:cd24007 140 --GHLLGDEgSGYW--IGRRALRAALRALDGRGpktplldAILKFLGLDSIEEliTAIYRSSDRKKEIASlaPLVFEAAE 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 231 KGDHFALMVVDRVCFYLGLATGNLGNTLNPDS---VVIGGGVSAAG----EFLRSRVEKYFQEFTFPQVRNStkiklael 303
Cdd:cd24007 216 EGDPVAQAILKEAAEELAKLVVALAKLLLLGEklpLALSGGVFKNNyylaEFLEELLKKKKPNAKVVEPKGS-------- 287
|
330
....*....|..
gi 488285125 304 gneaGVIGAASL 315
Cdd:cd24007 288 ----PVVGALLL 295
|
|
| Glucokinase |
pfam02685 |
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes ... |
185-318 |
7.35e-03 |
|
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes phosphorylate glucose using ATP as a donor to give glucose-6-phosphate and ADP.
Pssm-ID: 397005 Cd Length: 314 Bit Score: 37.54 E-value: 7.35e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488285125 185 ETVSSATGVVRVARHLSEEFAgdseLKQAIDDGQDVSSKdvfefAEKGDHF-ALMVVDRVCFYLGLATGNLGNTLNP-DS 262
Cdd:pfam02685 186 ERVLSGPGLVNLYRALCALDG----ITPELLTPADITAA-----ALAGDDPlAREALELFCAILGSVAGNLALTLGArGG 256
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488285125 263 VVIGGGVS-------AAGEFLRS-----RVEKYFQefTFPqvrnsTKIKLAElgnEAGVIGAASLALQ 318
Cdd:pfam02685 257 VYIAGGIAprileflKASGFRAAfedkgRFSALLR--DIP-----VYVITHP---QPGLLGAAAAARQ 314
|
|
| |
