|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
4-316 |
1.67e-142 |
|
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: 404.36 E-value: 1.67e-142
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 4 KIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTV 83
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 84 IGAYNLNWKTLqLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGE 163
Cdd:cd24062 81 EVAVNLGWKNF-PLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 164 LGHITVDFDEPFACTCGKKGCLETVASATGIVNLSRRYADQYAGDAKLKqMIDDGQDVTAKDVFDLAKEGDDLALIVYRH 243
Cdd:cd24062 160 IGHITVNPEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALR-ILALGGELTAKDVFEAAKAGDELALAVVDT 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556614290 244 FSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASL 316
Cdd:cd24062 239 VARYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-319 |
2.26e-99 |
|
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: 294.88 E-value: 2.26e-99
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 1 MSKKIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEA 80
Cdd:COG1940 3 DAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPET 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 81 GTVIGAYNL-NWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTlgtgvgggviaagNLIRGVKG 159
Cdd:COG1940 83 GVVLNAPNLpGWRGVPL-AELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTlgtgigggivingKLLRGANG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 160 AGGELGHITVDFDEPfACTCGKKGCLETVASATGIVnlsRRYADQYAGDaklkqmiddgqDVTAKDVFDLAKEGDDLALI 239
Cdd:COG1940 162 NAGEIGHMPVDPDGP-LCGCGNRGCLETYASGPALL---RRARELGGAE-----------KLTAEELFAAARAGDPLALE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 240 VYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASLVLK 319
Cdd:COG1940 227 VLDEAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAALALE 306
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
6-317 |
7.65e-91 |
|
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: 273.70 E-value: 7.65e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDD-GSHIVPDIIDSIKQRFDThglTKDDFLGVGMGSPGVVDSEAGTVI 84
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPEtIVDAIASAVDSFIQHIAK---VGHEIVAIGIGAPGPVNRQRGTVY 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 85 GAYNLNWKTlQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGEL 164
Cdd:TIGR00744 78 FAVNLDWKQ-EPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 165 GHITVDFDEPFACTCGKKGCLETVASATGIVNLSRRYADQYAGDAKLKQMIDDGQdVTAKDVFDLAKEGDDLALIVYRHF 244
Cdd:TIGR00744 157 GHIRMVPDGRLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDGDG-ISAKHVFVAARQGDPVAVDSYREV 235
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556614290 245 SEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASLV 317
Cdd:TIGR00744 236 ARWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAADLA 308
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
4-316 |
2.18e-75 |
|
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: 233.22 E-value: 2.18e-75
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 4 KIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIvPDIIDSIKQRFdthgLTKDDFLGVGMGSPGVVDSEAGTV 83
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAI-LERLLEIIAEL----KEKYDIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 84 IGAY-NL-NWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAG 161
Cdd:cd24068 76 IYATdNLpGWTGTNL-KEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 162 GELGHITVDFDEpFACTCGKKGCLETVASATGIVnlsrRYADQYAGDAKLkqmiddgqdvTAKDVFDLAKEGDDLALIVY 241
Cdd:cd24068 155 GELGHMVVDPGG-RPCCCGGKGCLEQYASGTALV----RRVAEALGEPGI----------DGREIFDLADAGDPLAKEVV 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556614290 242 RHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASL 316
Cdd:cd24068 220 EEFAEDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
5-318 |
9.41e-65 |
|
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: 206.26 E-value: 9.41e-65
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTVI 84
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVVL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 85 GAYNLNWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGEL 164
Cdd:cd24076 83 LAPNLGWRDVPL-RDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 165 GHITVDFDEPfACTCGKKGCLETVASATGIVnlsrryadqyagdAKLKQMIDDGQDVTAKDVFDLAKEGDDLALIVYRHF 244
Cdd:cd24076 162 GHMTVDPDGP-PCSCGNRGCWETYASERALL-------------RAAGRLGAGGEPLSLAELVEAARAGDPAALAALEEV 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556614290 245 SEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASLVL 318
Cdd:cd24076 228 GEYLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALAI 301
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
5-316 |
1.71e-61 |
|
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: 197.72 E-value: 1.71e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDthgltKDDFLGVGMGSPGVVDSEAGTVI 84
Cdd:cd24064 1 VIGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELIE-----EMELLGIGIGSPGSIDRENGIVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 85 GAYNL-NWKTLQLVkDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGE 163
Cdd:cd24064 76 FSPNFpDWRNFPLV-PLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 164 LGHITVDFDEPFaCTCGKKGCLETVASATGIVNLSR----RYADQYAGDAKlkqmiddgqDVTAKDVFDLAKEGDDLALI 239
Cdd:cd24064 155 LGHVIVEPNGPI-CGCGNRGCVEAFASATAIIRYAResrkRYPDSLAGESE---------KINAKHVFDAARKNDPLATM 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556614290 240 VYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASL 316
Cdd:cd24064 225 VFRRVVDALAIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAASI 301
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
6-318 |
5.16e-60 |
|
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. It is highly specific for glucose. Glucokinases are found in invertebrates and microorganisms. They belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466911 [Multi-domain] Cd Length: 306 Bit Score: 194.11 E-value: 5.16e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKTNIldDGSHIVPDIIDSIKQRFDTHgltkdDFLGVGMGSPGVVDSEAGTVIG 85
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTPP--TADGIVDAIVEAVEELREGH-----DVSAVGVAAAGFVDADRATVLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 86 AYNLNWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELG 165
Cdd:cd24061 75 APNIAWRNEPL-KDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFG 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 166 HITVDFDEpFACTCGKKGCLETVASATGIVNLSRRYADQYAGDAKLKQMIDDGQDVTAKDVFDLAKEGDDLALIVYRHFS 245
Cdd:cd24061 154 HIRVVPDG-LLCGCGSRGCWEQYASGRALVRYAKEAANATPEGAAVLLADGSVDGITGKHISEAARAGDPVALDALRELA 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556614290 246 EYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAEN-SFPQIKESTQIVLATRGNDAGVLGAASLVL 318
Cdd:cd24061 233 RWLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFERWlPGRGWRPIPRLRTAQLGNDAGLIGAADLAR 306
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
6-319 |
6.66e-59 |
|
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: 191.01 E-value: 6.66e-59
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKTNIlDDGSHIVPDIIDSIKQRFDTHGltkDDFLGVGMGSPGVVDSEAGTVIG 85
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPT-TTTEETLVDAIAFFVDSAQRKF---GELIAVGIGSPGLISPKYGYITN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 86 AYNLNWKTLQLVKDqFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELG 165
Cdd:pfam00480 77 TPNIGWDNFDLVEK-LEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 166 HITVDFDEPfACTCGKKGCLETVASATGIVnlsRRYADQyagdaklkqmiddGQDVTAKDVFDLAKEGDDLALIVYRHFS 245
Cdd:pfam00480 156 HIQLDPNGP-KCGCGNHGCLETIASGRALE---KRYQQK-------------GEDLEGKDIIVLAEQGDEVAEEAVERLA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556614290 246 EYLGVACANIAAVLNPAYIVLGGGVSAAgEFLLDGVRKVFAENSFPQIKES-TQIVLATRGNDAGVLGAASLVLK 319
Cdd:pfam00480 219 RYLAKAIANLINLFDPQAIVLGGGVSNA-DGLLEAIRSLVKKYLNGYLPVPpVIIVAASLGDNAGALGAAALAKQ 292
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-316 |
1.07e-57 |
|
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: 185.74 E-value: 1.07e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLtKDDFLGVGMGSPGVVDSEAGTVIG 85
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGV-RERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 86 AYNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMtlgtgvgggviaagN------------- 152
Cdd:cd23763 80 APNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYI--------------Tlgtgigggiiidg 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 153 -LIRGVKGAGGELGHITvdfdepfactcgkkgcletvasatgivnlsrryadqyagdaklkqmiddgqdvtakdvfdlak 231
Cdd:cd23763 146 kLYRGANGAAGEIGHIT--------------------------------------------------------------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 232 egddlaliVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVL 311
Cdd:cd23763 163 --------VLEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLL 234
|
....*
gi 556614290 312 GAASL 316
Cdd:cd23763 235 GAAAL 239
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
6-318 |
7.05e-57 |
|
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: 185.83 E-value: 7.05e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKTNiLDDGSHIVPDIIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTVIG 85
Cdd:cd24073 4 VGVKLTEDRITAVLTDLRGNVLASHTLPLD-SGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 86 AYNLNWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELG 165
Cdd:cd24073 83 SPLLGWRDVPL-AELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 166 HITVDFDEPfACTCGKKGCLETVASATGIVnlsrryadqyagdAKLKQMIDDGQDVTAKDVFDLAKEGDDLALIVYRHFS 245
Cdd:cd24073 162 HTTVDPDGP-PCRCGKRGCLEAYASDPAIL-------------RQAREAGLRGEPLTIEDLLAAARAGDPAARAILRRAG 227
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556614290 246 EYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASLVL 318
Cdd:cd24073 228 RALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGAAALAL 300
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
5-319 |
8.56e-57 |
|
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: 185.95 E-value: 8.56e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLTKDdFLGVGMGSPGVVDSEAGTVI 84
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLIKNKHVEKK-LLGIGIAVSGLVDSKKGIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 85 GAYNLNWKTLQLVKDqFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGEL 164
Cdd:cd24071 82 RSTILGWENVELKKI-LKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 165 GHITVDFDEPfACTCGKKGCLETVASATGIVNLSRRYADQYagdakLKQMIDDGQDVTAKDVFDLAKEGDDLALIVYRHF 244
Cdd:cd24071 161 GHMTIQPDGR-KCYCGQKGCLEAYASFEALVNEIKELTESY-----PLSLLKELEDFEIEKVREAAEEGDSVATELFKKA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 556614290 245 SEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASLVLK 319
Cdd:cd24071 235 GEYLGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALLVID 309
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
4-318 |
1.74e-52 |
|
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: 174.70 E-value: 1.74e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 4 KIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIkQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTV 83
Cdd:cd24059 2 YVIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELI-DRLLEKENIKSKILGIGIGAPGPLDVEKGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 84 IGAYNL-NWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGG 162
Cdd:cd24059 81 LNPPNFpGWENIPL-VELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 163 ELGHITVDFDEPFaCTCGKKGCLETVASATGIVnlsrRYAdqyagDAKLKQMIDDGQdvtakDVFDLAKEGDDLALIVYR 242
Cdd:cd24059 160 EIGHTSIDINGPR-CSCGNRGCLELYASIPAIE----KKA-----RSALGSGRSFQL-----DIVEALQKGDPIADEVIE 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556614290 243 HFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKESTQIVLATRGNDAGVLGAASLVL 318
Cdd:cd24059 225 EAAKYLGIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAAALVL 300
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
5-316 |
1.79e-50 |
|
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: 169.44 E-value: 1.79e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDthGLTKDDFLGVGMGSPGVVDSEAGTVI 84
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLS--KAGKDSIEGIGVSSAGPLDLRKGTIV 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 85 GAYNLNWKTLQLVKDQFEAaLGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGEL 164
Cdd:cd24063 80 NSPNIKGKEIPLVEPLKEE-FNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 165 GHITVDFDEPFACTCGKKGCLETVASATGIVNLSRRYADQYAGDAKLKQMIDDGQDVTAKDVFDLAKEGDDLALIVYRHF 244
Cdd:cd24063 159 GHLVVDTESGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLKLRNPGGEGITAKEVFSAARKGDPLALKIIEKL 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 556614290 245 SEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENsfPQIKESTQIVLATRGNDAGVLGAASL 316
Cdd:cd24063 239 ARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLEKN--PAISKGPEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-316 |
4.23e-48 |
|
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: 162.88 E-value: 4.23e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 4 KIIGIDLGGTSVKLAILTtEGEIQEKWSIKTNilDDGSHIVPDIIDSIKQRFDTHgltKDDFLGVGMGSPGVVDSEAGTV 83
Cdd:cd24065 1 STIGLDLGGTKIAAGVVD-GGRILSRLVVPTP--REGGEAVLDALARAVEALQAE---APGVEAVGLGVPGPLDFRRGRV 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 84 IGAYNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGE 163
Cdd:cd24065 75 RFAPNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 164 LGHITVDFDEPfACTCGKKGCLETVASATGIvnlsrryadqyAGDAKLKQmiddGQDVTAKDVFDLAKEGDDLALIVYRH 243
Cdd:cd24065 155 IGHTTVLPGGP-MCGCGLVGCLEALASGRAL-----------ARDASFAY----GRPMSTAELFELAQQGEPKALRIVEQ 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 556614290 244 FSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAEnsFPQIKESTQIVLATRGNDAGVLGAASL 316
Cdd:cd24065 219 AAAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAARR--YTEGWHAPPLRLAHLGTDAGVIGAALA 289
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
4-316 |
6.16e-47 |
|
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: 159.66 E-value: 6.16e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 4 KIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDdgshiVPDIIDSIKQRFDTHgltKDDFLGVGMGSPGVVDSEAGTV 83
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDS-----LEEFLDYIKKIIKRY---DEEIDGIAISAPGVIDPETGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 84 IGA------YNLNWKTLqlvkdqFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGV 157
Cdd:cd24152 73 YGGgalpylKGFNLKEE------LEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGS 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 158 KGAGGELGHITVDFDEPFactcgkkgcLETVASATGIVNLSRRYADqyagdaklkqmIDDGQDVTAKDVFDLAKEGDDLA 237
Cdd:cd24152 147 HFFAGEFSYLLTDDDDKD---------LLFFSGLASMFGLVKRYNK-----------AKGLEPLDGEEIFEKYAKGDEAA 206
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 238 LIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAgEFLLDGVRKVFAE--NSFPQIKESTQIVLATRGNDAGVLGAAS 315
Cdd:cd24152 207 KKILDEYIRNLAKLIYNIQYILDPEVIVIGGGISEQ-PLFIEDLKKEVNEilANRPGSIPKPEIKACKFGNDANLLGALY 285
|
.
gi 556614290 316 L 316
Cdd:cd24152 286 N 286
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
8-316 |
1.09e-41 |
|
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.
Pssm-ID: 466910 [Multi-domain] Cd Length: 305 Bit Score: 146.41 E-value: 1.09e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 8 IDLGGTSVKLAILTTEGEIQEKWSIKTnilddgSHIVPDIIDSIKQRF--DTHGLTKDD--FLGVGMGSPGVVDSEAGTV 83
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPN------PKTYEERIDLILQMCveAASEAVKLNcrILGVGISTGGRVNPREGIV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 84 IGAYNL--NWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAG 161
Cdd:cd24060 79 LHSTKLiqEWSSVDL-RTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 162 GELGHITVDFDEPfACTCGKKGCLETVASATGIVNLSRRYADqyAGDAKLKQM-IDDGQDVTAKDVFDLAKEGDDLALIV 240
Cdd:cd24060 158 AELGHIVVSLDGP-DCMCGSHGCVEAYASGMALQREAKKLHD--EDLLLVEGMsVTNDEEVTAKHLIQAAKLGNAKAQKI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556614290 241 YRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEfllDGVRKVFAENSFPQIKESTQIVLATRgnDAGVLGAASL 316
Cdd:cd24060 235 LRTAGTALGLGIVNILHTLNPSLVILSGVLASHYE---NIVKDVIAQRALPSVQNVDVVVSDLV--DPALLGAASM 305
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-317 |
5.38e-38 |
|
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: 136.52 E-value: 5.38e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 3 KKIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLTKDdflGVGMGSPGVVDSEAGT 82
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVEVLADLIREYIEEAGLKPA---AIVIGVPGTVDKDRRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 83 VIGAYNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVV-----------FMTLGTgvgggviaag 151
Cdd:cd24070 78 VISTPNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLgfyigtgignaILINGK---------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 152 nLIRGVKGAGGELGHITV-DFDEPfaCTCGKKGCLETVASATGIVNLSRRYadqyagdaklkqmiddGQDVTAKDVFDLA 230
Cdd:cd24070 148 -PLRGKNGVAGELGHIPVyGNGKP--CGCGNTGCLETYASGRALEEIAEEH----------------YPDTPILDIFVDH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 231 KEGDDLalivyRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENS-FPQIKESTQIVLATRGNDAG 309
Cdd:cd24070 209 GDEPEL-----DEFVEDLALAIATEINILDPDAVILGGGVIDMKGFPRETLEEYIRKHLrKPYPADNLKIIYAELGPEAG 283
|
....*...
gi 556614290 310 VLGAASLV 317
Cdd:cd24070 284 VIGAAIYA 291
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
5-316 |
5.71e-38 |
|
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: 136.59 E-value: 5.71e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGEIQEKWSIKTNIlDDGSHIVPDI---IDSIKQRFDTHGltkddflGVGMGSPGVVDSEAG 81
Cdd:cd24057 2 YYGFDIGGTKIEFAVFDEALQLVWTKRVPTPT-DDYAAFLAAIaelVAEADARFGVKG-------PVGIGIPGVIDPEDG 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 82 TVIGAyNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAG 161
Cdd:cd24057 74 TLITA-NIPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIA 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 162 GELGHITV-------DFDEP-FACTCGKKGCLETVASATGIVNLSRRYAdqyagdaklkqmiddGQDVTAKDVFDLAKEG 233
Cdd:cd24057 153 GEWGHGPLpadalllGYDLPvLRCGCGQTGCLETYLSGRGLERLYAHLY---------------GEELDAPEIIAAWAAG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 234 DDLALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEfLLDGVRKVFAENSFPQIKeSTQIVLATRGNDAGVLGA 313
Cdd:cd24057 218 DPQAVAHVDRWLDLLAGCLANILTALDPDVVVLGGGLSNFPA-LIAELPAALPAHLLSGAR-TPRIVPARHGDAGGVRGA 295
|
...
gi 556614290 314 ASL 316
Cdd:cd24057 296 AFL 298
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
6-316 |
2.01e-33 |
|
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: 124.62 E-value: 2.01e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKT------NILDDGSHIVPDIIDSIKQRFDthgltkddflgVGMGSPGVVDSE 79
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTprgdyeATLDAIADLVEEAEEELGAPAT-----------VGIGTPGSISPR 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 80 AGTVIGAyNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKG 159
Cdd:cd24066 71 TGLVKNA-NSTWLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 160 AGGELGHITVDFDEPF-----ACTCGKKGCLETVASATGivnLSRRYADQYagdaklkqmiddGQDVTAKDVFDLAKEGD 234
Cdd:cd24066 150 IAGEWGHNPLPWPDEDelpgpPCYCGKRGCVETFLSGPA---LERDYARLT------------GKTLSAEEIVALARAGD 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 235 DLALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAgEFLLDGVRKVFAENSFPQIKEsTQIVLATRGNDAGVLGAA 314
Cdd:cd24066 215 AAAVATLDRFLDRLGRALANVINILDPDVIVLGGGLSNI-DELYTEGPAALARYVFSDEVE-TPIVKNKHGDSSGVRGAA 292
|
..
gi 556614290 315 SL 316
Cdd:cd24066 293 WL 294
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
47-317 |
1.19e-32 |
|
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: 122.86 E-value: 1.19e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 47 IIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTVIGAYNLNWKTLQLVkDQFEAALGLPFFIDNDANVAALGEQWVG 126
Cdd:cd24075 44 LIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVHYMPHIQVKSWPIV-EELEQRFNVPCFIGNDIRSLALAEHYFG 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 127 AGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELGHITVdfdEPFA--CTCGKKGCLETVASATGIVNlsrryadq 204
Cdd:cd24075 123 ASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGHIQI---EPLGerCHCGNFGCLETVASNAAIEQ-------- 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 205 yagdaKLKQMIDDG-------QDVTAKDVFDLAKEGDDLALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFL 277
Cdd:cd24075 192 -----RVKKLLKQGyasqltlQDCTIKDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGEITQADKVL 266
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 556614290 278 LDGVRKVFAENSFPQIKESTQIVLATRGNDAgVLGAASLV 317
Cdd:cd24075 267 LPVIKKCIQSQALPDFRQELKIVASQLDHNS-AIGAFALV 305
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
5-319 |
9.22e-32 |
|
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: 120.60 E-value: 9.22e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGE-------IQEKWSIKTNILDdgshIVPDIIDSIKQRfdthglTKDDFLGVGMGSPGVVD 77
Cdd:cd24072 3 VLGIVVSPNSLRAQVGNACGEllgefeyRVITLETPEALID----EIIDCIDRLLKL------WKDRVKGIALAIQGLVD 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 78 SEAGTVIGAYNLNWKTLQlVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGV 157
Cdd:cd24072 73 SHKGVSLWSPGAPWRNIE-IKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 158 KGAGGELGHITVDFDePFACTCGKKGCLETVASATGIvnlsRRYADQYagdAKLKQMIDDGQDVTAKDVFDLAKEGDDLA 237
Cdd:cd24072 152 SSGSGEIGHTKVNPD-GARCDCGRRGCLETVASNSAL----KRNARVT---LKLGPVSADPEKLTMEQLIEALEEGEPIA 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 238 LIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSFPQIKEST-QIVLATRGN-DAGVLGAAS 315
Cdd:cd24072 224 TQIFDRAANAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAIAENPFSQHATQIgFGQLSTEQGcAQQALGLVY 303
|
....
gi 556614290 316 LVLK 319
Cdd:cd24072 304 LYIE 307
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
8-316 |
4.01e-27 |
|
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: 107.37 E-value: 4.01e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 8 IDLGGTSVKLAILTtEGEIQEKWSIKTNILDDGSHIVpDIIDSIKQRFdthgltKDDFLGVGMGSPGVVDSEAGTVIGAY 87
Cdd:cd24069 3 IDIGGTKIAAALIG-NGQIIDRRQIPTPRSGTPEALA-DALASLLADY------QGQFDRVAVASTGIIRDGVLTALNPK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 88 NL-NWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELGH 166
Cdd:cd24069 75 NLgGLSGFPL-ADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 167 ITVDFDEPfACTCGKKGCLETVASATGIVnlsrRYADQYagdaklkqmidDGQDVTAKDVFDLAKEGDDLALIVYRHFSE 246
Cdd:cd24069 154 TLADPPGP-VCGCGRRGCVEAIASGTAIA----AAASEI-----------LGEPVDAKDVFERARSGDEEAARLIDRAAR 217
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 247 YLGVACANIAAVLNPAYIVLGGGVSAAGEFlLDGVRkvFAENSFPQIKESTqIVLATRGNDAGVLGAASL 316
Cdd:cd24069 218 ALADLIADLKATLDLDCVVIGGSVGLAEGF-LERVE--QYLADEPAIFRVS-LEPARLGQDAGLLGAALL 283
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
47-319 |
1.51e-26 |
|
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: 106.63 E-value: 1.51e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 47 IIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTV--IGAYNL-NWKtlqlVKDQFEAALGLPFFIDNDANVAALGEQ 123
Cdd:cd24074 45 LLESISEFFSRHQKKLERLTAIAITLPGIIDPESGIVhrLPFYDIkNLP----LGEALEQHTGLPVYVQHDISAWTLAER 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 124 WVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELGHITVDfDEPFACTCGKKGCLETVASATGIVNLSRRYAD 203
Cdd:cd24074 121 FFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHTQID-PYGKRCYCGNHGCLETVASIPAILEQANQLLE 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 204 QYAGDAKLkqmiddGQDVTAKDVFDLAKEGDDLALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRK 283
Cdd:cd24074 200 QSPDSMLH------GQPISIESLCQAALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNNAAEILFPALSQ 273
|
250 260 270
....*....|....*....|....*....|....*.
gi 556614290 284 VFAENSFPQIKESTQIVlATRGNDAGVLGAASLVLK 319
Cdd:cd24074 274 SIRQQSLPAYSQHLQIE-STKFYNDGTMPGAALIKD 308
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
1-314 |
1.58e-26 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 106.22 E-value: 1.58e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 1 MSKKIIGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVpDIIDSIKQRFDTHGLTKDdflGVGMGSPGVVDSEA 80
Cdd:PRK09698 2 QKNVVLGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVS-GLGEMIDEYLRRFNARCH---GIVMGFPALVSKDR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 81 GTVIGAYNLNWKTL--QLVKDQFEAALGLPFFIDNDANVAALgeqW-VGAGNNNPNVVFMTLGTGVGGGVIAAGNLI-RG 156
Cdd:PRK09698 78 RTVISTPNLPLTALdlYDLADKLENTLNCPVFFSRDVNLQLL---WdVKENNLTQQLVLGAYLGTGMGFAVWMNGAPwTG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 157 VKGAGGELGHITVdFDEPFACTCGKKGCLETVASATgivNLSRRYADQYaGDAKLKQMIDDgqdvtakdvfdlakEGDDL 236
Cdd:PRK09698 155 AHGVAGELGHIPL-GDMTQHCGCGNPGCLETNCSGM---ALRRWYEQQP-RDYPLSDLFVH--------------AGDHP 215
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556614290 237 ALivyRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFAENSF-PQIKESTQIVLATRGNDAGVLGAA 314
Cdd:PRK09698 216 FI---QSLLENLARAIATSINLFDPDAIILGGGVMDMPAFPRETLIAMIQKYLRkPLPYEVVRFIYASSSDFNGAQGAA 291
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
6-319 |
1.11e-24 |
|
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: 101.08 E-value: 1.11e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEI--QEKWSIKT----NILDDGSHIVPDIIDSIKQRfdTHGLtkddfLGVGMGSPGVVDSE 79
Cdd:cd24077 4 IGIDLGYNYISLMLTYLDGEIisSKQIKLLDisfeNILEILKSIIQELISQAPKT--PYGL-----VGIGIGIHGIVDEN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 80 agTVIGAYNLNWKTLQLvKDQFEAALGLPFFIDNDANVAALGEQ----------------WVGAG--NNNpnvvfmtlgt 141
Cdd:cd24077 77 --EIIFTPYYDLEDIDL-KEKLEEKFNVPVYLENEANLSALAERtfsedydnlisisihsGIGAGiiINN---------- 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 142 gvgggviaagNLIRGVKGAGGELGHITVdFDEPFACTCGKKGCLETVASATGIVNlsrRYADQYAGDaklkqmiddgqDV 221
Cdd:cd24077 144 ----------QLYRGYNGFAGEIGHMII-VPNGKPCPCGNKGCLEQYASEKALLK---ELSEKKGLE-----------TL 198
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 222 TAKDVFDLAKEGDDLALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKVFaeNSFpqIKESTQIVL 301
Cdd:cd24077 199 TFDDLIQLYNEGDPEALELIDQFIKYLAIGINNIINTFNPEIIIINSSLINEIPELLEKIKEQL--SSS--FNKYVEILI 274
|
330
....*....|....*...
gi 556614290 302 ATRGNDAGVLGAASLVLK 319
Cdd:cd24077 275 STLGKNATLLGGAAVAIK 292
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
5-316 |
4.06e-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: 99.16 E-value: 4.06e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTEGEIQEKWSIKTnilddgshIVPD-IIDSIKQRFDTHgltKDDFLGVGMGSPGVVD----SE 79
Cdd:cd24067 1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPT--------TTPEeTLQAVIDFFREQ---EEPIDAIGIASFGPIDlnptSP 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 80 A-GTVIGAYNLNWKTLQLVkDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGViaagnLIRG-- 156
Cdd:cd24067 70 TyGYITTTPKPGWRNFDIL-GALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGL-----VVNGkp 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 157 VKGAG-GELGHITV----DfDEPFACTC-GKKGCLETVASATGIvnlSRRYadqyagdaklkqmiddgqdvtakdvfdlA 230
Cdd:cd24067 144 VHGLLhPEMGHIRVprhpD-DDGFPGVCpFHGDCLEGLASGPAI---AARW----------------------------G 191
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 231 KEGDDLAL--IVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSaAGEFLLDGVRKVFAE--NSFPQIKESTQ-----IVL 301
Cdd:cd24067 192 IPAEELPDdhPAWDLEAYYLAQACANLTLTLSPERIVLGGGVM-QRPGLFPRIREKFRKllNGYLEVPRLLPdideyIVP 270
|
330
....*....|....*
gi 556614290 302 ATRGNDAGVLGAASL 316
Cdd:cd24067 271 PALGNDAGILGALAL 285
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
7-319 |
5.62e-22 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 93.90 E-value: 5.62e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 7 GIDLGGTSVKLAILTTEGEIQ--EKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLtkddflgVGMGSPGVVDSEAGTVI 84
Cdd:PRK13310 4 GFDIGGTKIELGVFNEKLELQweERVPTPRDSYDAFLDAVCELVAEADQRFGCKGS-------VGIGIPGMPETEDGTLY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 85 GAyNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGEL 164
Cdd:PRK13310 77 AA-NVPAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 165 GHI--TVD------FDEP-FACTCGKKGCLETVASATGIVNLsrrYADQYagdaklkqmiddGQDVTAKDVFDLAKEGDD 235
Cdd:PRK13310 156 GHMrlPVDaltllgWDAPlRRCGCGQKGCIENYLSGRGFEWL---YQHYY------------GEPLQAPEIIALYYQGDE 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 236 LALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAgEFLLDGVRKVFAENSFPQIKeSTQIVLATRGNDAGVLGAAS 315
Cdd:PRK13310 221 QAVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLSNF-DAIYEQLPKRLPRHLLPVAR-VPRIEKARHGDAGGVRGAAF 298
|
....
gi 556614290 316 LVLK 319
Cdd:PRK13310 299 LHLT 302
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
6-316 |
7.23e-18 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 82.38 E-value: 7.23e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 6 IGIDLGGTSVKLAILTTEGEIQEKWSIKTNILDdgshiVPDIIDSIKQRFDTHGLTKDDFLGVGMGSPGVVDSEAGTVIG 85
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTPRDD-----YQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKN 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 86 AyNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNpNVVFMTLGTGVGGGVIAAGNLIR-GVKGAGGEL 164
Cdd:PRK09557 78 A-NSTWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGK-QTVFAVIIGTGCGAGVAINGRVHiGGNGIAGEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 165 GH-----ITVD---FDEPFACTCGKKGCLETVASATGIVnlsRRYadQYAGdaklkqmiddGQDVTAKDVFDLAKEGDDL 236
Cdd:PRK09557 156 GHnplpwMDEDelrYRNEVPCYCGKQGCIETFISGTGFA---TDY--RRLS----------GKALKGSEIIRLVEEGDPV 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 237 ALIVYRHFSEYLGVACANIAAVLNPAYIVLGGGVSAAgEFLLDGVRKVFAENSFPQIKEsTQIVLATRGNDAGVLGAASL 316
Cdd:PRK09557 221 AELAFRRYEDRLAKSLAHVINILDPDVIVLGGGMSNV-DRLYPTLPALLKQYVFGGECE-TPVRKALHGDSSGVRGAAWL 298
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
8-317 |
1.98e-16 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 78.03 E-value: 1.98e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 8 IDLGGTSVKLAILTTEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQrfdthglTKDDFLGVGMGSPGVVDSEAGTVIGAY 87
Cdd:PRK05082 6 IDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSP-------LQAQADRVAVASTGIINDGILTALNPH 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 88 NLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEqWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELGHI 167
Cdd:PRK05082 79 NLGGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 168 TVDFDEPFaCTCGKKGCLETVASATGIvnlsrryadqyAGDAKlkqmiDDGQDVTAKDVFDLAKEGDDLALIVYRHFSEY 247
Cdd:PRK05082 158 LADPHGPV-CGCGRRGCVEAIASGRAI-----------AAAAQ-----GWLAGCDAKTIFERAGQGDEQAQALINRSAQA 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 248 LGVACANIAAVLNPAYIVLGGGVSAAgEFLLDGVRKVFAEnsFPQIKEsTQIVLATRGNDAGVLGAASLV 317
Cdd:PRK05082 221 IARLIADLKATLDCQCVVLGGSVGLA-EGYLELVQAYLAQ--EPAIYH-VPLLAAHYRHDAGLLGAALWA 286
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
5-316 |
5.16e-15 |
|
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: 72.99 E-value: 5.16e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILTTE-GE-IQEKWSIKTNilddgSHIVPD-IIDSIKQRFDTHGltkdDFLGVGMGSPGVVdsEAG 81
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDTDtGElLSERIRIPTP-----QPATPEaVADVVAELVAHFP----WFGPVGVGFPGVV--RRG 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 82 TVIGAYNLN--WKTLQLVKdQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIaagnLIRGVKG 159
Cdd:cd24058 70 VVRTAANLDksWIGFDAAK-LLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVLVLTLGTGIGSAL----FVDGHLV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 160 AGGELGHITVDfdepfactcgkKGCLETVASatgivnlsrryadqyAGDAKLKQMIDdgqdvtakdvfdlaKEGDdlali 239
Cdd:cd24058 145 PNTELGHLEIR-----------GKDAEERAS---------------LGVRAREDLGW--------------KRWA----- 179
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 556614290 240 vyRHFSEYLGVacanIAAVLNPAYIVLGGGVSaageflldgvRKvfAENSFPQIKESTQIVLATRGNDAGVLGAASL 316
Cdd:cd24058 180 --KRVNKYLQY----LERLFNPDLFIIGGGNS----------KK--ADKFLPLLDVKTPVVPAVLRNDAGIVGAALL 238
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
7-270 |
1.37e-09 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 57.73 E-value: 1.37e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 7 GIDLGGTSVKLAILttEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRFDTHGLTKDDflgVGMGSPGVVDSEAGTVIGA 86
Cdd:PRK13311 4 GFDMGGTKIELGVF--DENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGS---VGIGIPGLPNADDGTVFTA 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 87 yNLNWKTLQLVKDQFEAALGLPFFIDNDANVAALGEQWVGAGNNNPNVVFMTLGTGVGGGVIAAGNLIRGVKGAGGELGH 166
Cdd:PRK13311 79 -NVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 167 ITVDFDE---------PFACTCGKKGCLETVASATGivnLSRRYADQYAgdaklkqmiddgQDVTAKDVFDLAKEGDDLA 237
Cdd:PRK13311 158 FRLPVDAldilgadipRVPCGCGHRGCIENYISGRG---FEWMYSHFYQ------------HTLPATDIIAHYAAGEPKA 222
|
250 260 270
....*....|....*....|....*....|...
gi 556614290 238 LIVYRHFSEYLGVACANIAAVLNPAYIVLGGGV 270
Cdd:PRK13311 223 VAHVERFMDVLAVCLGNLLTMLGSPFGRGGWGV 255
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
5-314 |
2.74e-09 |
|
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: 57.23 E-value: 2.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 5 IIGIDLGGTSVKLAILT---TEGEIQEKWSIKTNILDDGSHIVPDIIDSIKQRfdthgltkdDFLGVGMGSPGVVDseaG 81
Cdd:cd24008 1 ILVGDIGGTNARLALADagdGSGDLLFVRKYPSADFASLEDALAAFLAELGAP---------RPKAACIAVAGPVD---G 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 82 TVIGAYNLNWktlQLVKDQFEAALGL-PFFIDNDanVAALG-----------EQWVGAGNNNPNvvfmtlgtgvgggvia 149
Cdd:cd24008 69 GRVRLTNLDW---SIDAAELRKALGIgRVRLLND--FEAAAyglpalgpedlLVLYGGGGPLPG---------------- 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 150 agnLIRGVKGAG--------------------GELGHITV----DFDEPFACTCGKKG----CLETVASATGIVNLSRRY 201
Cdd:cd24008 128 ---GPRAVLGPGtglgvallvpdgdggyvvlpSEGGHADFapvtEEEAELLEFLRKRFgrsvSYEDVLSGPGLENIYEFL 204
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 202 ADQYAgdaklkqmiDDGQDVTAKDVFDLAKEGDDLALIVYRHFSEYLGVACANIAAVLNPAY-IVLGGGVSAAGEFLLDg 280
Cdd:cd24008 205 AKLDG---------AEPPDLTAEEIAEAALAGDPLAREALDLFARILGRFAGNLALSFLATGgVYLAGGIAPKNLDLLD- 274
|
330 340 350
....*....|....*....|....*....|....*....
gi 556614290 281 vRKVFAEN-----SFPQIKESTQIVLATRgNDAGVLGAA 314
Cdd:cd24008 275 -SSAFREAfldkgRMSDLLEDIPVYLVTN-EDLGLLGAA 311
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
223-319 |
8.10e-04 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 40.64 E-value: 8.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556614290 223 AKDVFDLAKEGDDLAL-IVYRHFSEYlgVACANIAAVLNPAYIVLGGGVSAAGEFLLDGVRKvfaensfpQIKESTQIVL 301
Cdd:COG2971 209 APLVFEAAEAGDPVARaILEEAADEL--AELARALLERGALPVVLAGGVAAAQPLLREALRA--------RLAAGGAEIV 278
|
90
....*....|....*...
gi 556614290 302 ATRGNdaGVLGAASLVLK 319
Cdd:COG2971 279 PPAGD--PVDGALLLALR 294
|
|
| |
