|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
15-270 |
1.23e-67 |
|
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: 213.22 E-value: 1.23e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGES---------NVVTDIVRVARILSNEALPIGIGIPGQVNCATGQVSN 85
Cdd:COG1940 8 IGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGpeavleaiaELIEELLAEAGISRGRILGIGIGVPGPVDPETGVVLN 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 86 VVNL-DIETLELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDGNA----TVVFLNFGTGLAAGLVRGGQAEHGYSGS 160
Cdd:COG1940 88 APNLpGWRGVPLAELLEERLGLPVFVENDANAAALA-----EAWFGAGrgadNVVYLTLGTGIGGGIVINGKLLRGANGN 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 161 IGEIGHLPIDPNGFECPCGQRGCLETVASGGAVAKLW----PSANPPMPDLIRKARQGDGHANDVLTMVAHAMGDTIQIV 236
Cdd:COG1940 163 AGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRArelgGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANL 242
|
250 260 270
....*....|....*....|....*....|....
gi 1537797675 237 AQAYDPQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:COG1940 243 INLLDPEVIVLGGGVSAAGDLLLEPIREALAKYA 276
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
15-269 |
8.00e-47 |
|
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: 159.26 E-value: 8.00e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPS--HSGESNVVTDIVRVARILSNEALP--IGIGIPGQVNCATGQV-SNVVNL 89
Cdd:cd24068 3 LGIDIGGTKIKYGLVDADGEILEKDSVPTpaSKGGDAILERLLEIIAELKEKYDIegIGISSAGQVDPKTGEViYATDNL 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 90 -DIETLELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDGNA----TVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEI 164
Cdd:cd24068 83 pGWTGTNLKEELEERFGLPVAVENDVNCAALA-----EKWLGAAkgldDFLCLTLGTGIGGAIILDGRLYRGANGSAGEL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 165 GHLPIDPNGFECPCGQRGCLETVASGGAVAKLWPSANPPMP----DLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQAY 240
Cdd:cd24068 158 GHMVVDPGGRPCCCGGKGCLEQYASGTALVRRVAEALGEPGidgrEIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIF 237
|
250 260
....*....|....*....|....*....
gi 1537797675 241 DPQRIIIGGGMAKTGDALIEVIQAELSRR 269
Cdd:cd24068 238 DPEVIVIGGGISAQGELFLEELREELRKL 266
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
15-270 |
1.14e-46 |
|
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: 159.27 E-value: 1.14e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGESnvVTDIVRVARILSNEA-----------LPIGIGIPGQVNCATGQV 83
Cdd:cd24076 4 IGVELGVDYITVVVTDLAGEVLWRREVPLPASDD--PDEVLAQLAALIREAlaaapdsplgiLGIGVGVPGLVDSEDGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 84 SNVVNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFVEqVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGE 163
Cdd:cd24076 82 LLAPNLGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGA-GRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 164 IGHLPIDPNGFECPCGQRGCLETVASGGAV---AKLWPSANPPM--PDLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQ 238
Cdd:cd24076 161 IGHMTVDPDGPPCSCGNRGCWETYASERALlraAGRLGAGGEPLslAELVEAARAGDPAALAALEEVGEYLGIGLANLVN 240
|
250 260 270
....*....|....*....|....*....|..
gi 1537797675 239 AYDPQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:cd24076 241 TFNPELVVLGGALAPLGPWLLPPLRAEVARRA 272
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
15-272 |
1.46e-45 |
|
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: 155.96 E-value: 1.46e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPS---------HSGESNVVTDIVRVArilsNEALPIGIGIPGQVNCATGQVSN 85
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTptttteetlVDAIAFFVDSAQRKF----GELIAVGIGSPGLISPKYGYITN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 86 VVNLDIETLELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDGNA----TVVFLNFGTGLAAGLVRGGQAEHGYSGSI 161
Cdd:pfam00480 77 TPNIGWDNFDLVEKLEERFNVPVFFENDANAAALA-----EAVFGASkdvqNVIYVTVGTGVGGGVISNGKLFTGRNGVA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 162 GEIGHLPIDPNGFECPCGQRGCLETVASGGAVAKLWPSANPPMP--DLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQA 239
Cdd:pfam00480 152 GEIGHIQLDPNGPKCGCGNHGCLETIASGRALEKRYQQKGEDLEgkDIIVLAEQGDEVAEEAVERLARYLAKAIANLINL 231
|
250 260 270
....*....|....*....|....*....|...
gi 1537797675 240 YDPQRIIIGGGMAKTgDALIEVIQAELSRRAEG 272
Cdd:pfam00480 232 FDPQAIVLGGGVSNA-DGLLEAIRSLVKKYLNG 263
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
15-269 |
6.46e-44 |
|
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: 152.12 E-value: 6.46e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGESNVVTDIVRVARILS-NEALP-IGIGIPGQVNCATGQVSNVVNLDIE 92
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTPPTADGIVDAIVEAVEELReGHDVSaVGVAAAGFVDADRATVLFAPNIAWR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 93 TLELGERVSAIMHAPVHVENDVNAAAVGAAEFvEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHLPIDPN 172
Cdd:cd24061 82 NEPLKDLLEARIGLPVVIENDANAAAWAEYRF-GAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRVVPD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 173 GFECPCGQRGCLETVASGGAVAKLWPSANPPMP------------------DLIRKARQGDGHANDVLTMVAHAMGDTIQ 234
Cdd:cd24061 161 GLLCGCGSRGCWEQYASGRALVRYAKEAANATPegaavlladgsvdgitgkHISEAARAGDPVALDALRELARWLGAGLA 240
|
250 260 270
....*....|....*....|....*....|....*
gi 1537797675 235 IVAQAYDPQRIIIGGGMAKTGDALIEVIQAELSRR 269
Cdd:cd24061 241 SLAALLDPELFVIGGGVSDAGDLLLDPIREAFERW 275
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
15-268 |
9.54e-43 |
|
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: 149.28 E-value: 9.54e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPS-HSGESNVVT-------DIVRVARIlSNEALPIGIGIPGQVNCATGQVSNV 86
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTdTTPETIVDAiasavdsFIQHIAKV-GHEIVAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 87 VNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFVEQvDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGH 166
Cdd:TIGR00744 80 VNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAG-KGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 167 LPIDPNG-FECPCGQRGCLETVASGGAVAKLWPSANPPMP-----------------DLIRKARQGDGHANDVLTMVAHA 228
Cdd:TIGR00744 159 IRMVPDGrLLCNCGKQGCIETYASATGLVRYAKRANAKPEraevllalgdgdgisakHVFVAARQGDPVAVDSYREVARW 238
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1537797675 229 MGDTIQIVAQAYDPQRIIIGGGMAKTGDALIEVIQAELSR 268
Cdd:TIGR00744 239 AGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKR 278
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
15-263 |
8.73e-42 |
|
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: 146.67 E-value: 8.73e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSH--SGESNVVTDIVRVARILSNEALP-------IGIGIPGQVNCATGQVSN 85
Cdd:cd24062 3 VGIDVGGTTIKMAFLTQEGEIVQKWEIPTNklEGGENIITDIAESIQQLLEELGYskedligIGVGVPGPVDVETGTVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 86 VVNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAeFVEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIG 165
Cdd:cd24062 83 AVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEM-WKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 166 HLPIDP-NGFECPCGQRGCLETVASGGAVA-----KLWPSANPPMPDLIRK------------ARQGDGHANDVLTMVAH 227
Cdd:cd24062 162 HITVNPeGGAPCNCGKTGCLETVASATGIVriareELEEGKGSSALRILALggeltakdvfeaAKAGDELALAVVDTVAR 241
|
250 260 270
....*....|....*....|....*....|....*.
gi 1537797675 228 AMGDTIQIVAQAYDPQRIIIGGGMAKTGDALIEVIQ 263
Cdd:cd24062 242 YLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVK 277
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
15-270 |
7.99e-41 |
|
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: 143.85 E-value: 7.99e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMP--SHSGE------SNVVTDIVRVARILSNEALPIGIGIPGQVNCATGQVSNV 86
Cdd:cd24073 4 VGVKLTEDRITAVLTDLRGNVLASHTLPldSGDPEavaeaiAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRWS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 87 VNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFVE--QVDGNATVVFlnfGTGLAAGLVRGGQAEHGYSGSIGEI 164
Cdd:cd24073 84 PLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAgrGLDNFAVVTI---GRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 165 GHLPIDPNGFECPCGQRGCLETVASGGAVAKLWPSANPP-----MPDLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQA 239
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLRgepltIEDLLAAARAGDPAARAILRRAGRALGLALANLVNL 240
|
250 260 270
....*....|....*....|....*....|.
gi 1537797675 240 YDPQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:cd24073 241 LDPELIIISGEGVRAGDLLFEPMREALRAHV 271
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
15-277 |
4.38e-40 |
|
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: 141.57 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPS----HSGESNVVTDIVRVARILSNEALPIGIGIPGQVNCATGQV--SNVVN 88
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTprgdYEATLDAIADLVEEAEEELGAPATVGIGTPGSISPRTGLVknANSTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 89 LDIETLElgERVSAIMHAPVHVENDVNAAAVGaaefvEQVDG---NATVVF-LNFGTGLAAGLVRGGQAEHGYSGSIGEI 164
Cdd:cd24066 82 LNGKPLK--ADLEARLGRPVRIENDANCFALS-----EATDGagaGAGVVFgVILGTGVGGGIVVNGRVLTGANGIAGEW 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 165 GHLPIDP------NGFECPCGQRGCLETVASGGAVAKLWPSANP---PMPDLIRKARQGDGHANDVL----TMVAHAMGD 231
Cdd:cd24066 155 GHNPLPWpdedelPGPPCYCGKRGCVETFLSGPALERDYARLTGktlSAEEIVALARAGDAAAVATLdrflDRLGRALAN 234
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1537797675 232 TIQIVaqayDPQRIIIGGGMAKTgDALIEVIQAELSRRAEGCRFLT 277
Cdd:cd24066 235 VINIL----DPDVIVLGGGLSNI-DELYTEGPAALARYVFSDEVET 275
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
15-272 |
8.23e-38 |
|
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: 135.53 E-value: 8.23e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIE-GVLLDATDRVIDVCRMPSHSGEsNVVTDIVRVARILSNEA---LPIGIGIPGQVNCATGQVSNVVNL- 89
Cdd:cd24065 3 IGLDLGGTKIAaGVVDGGRILSRLVVPTPREGGE-AVLDALARAVEALQAEApgvEAVGLGVPGPLDFRRGRVRFAPNIp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 90 DIETLELGERVSAIMHAPVHVENDVNAAAV-----GAAEfveqvdGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEI 164
Cdd:cd24065 82 GLTDFPIRRGLAERLGLPVVLENDANAAALaehhyGAAR------GTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEI 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 165 GHLPIDPNGFECPCGQRGCLETVASGGAVAKLWPSA-NPPM--PDLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQAYD 241
Cdd:cd24065 156 GHTTVLPGGPMCGCGLVGCLEALASGRALARDASFAyGRPMstAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALD 235
|
250 260 270
....*....|....*....|....*....|.
gi 1537797675 242 PQRIIIGGGMAKTGDALIEVIQAELSRRAEG 272
Cdd:cd24065 236 PEVFVLGGGVAQVGDYYLLPVQEAARRYTEG 266
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
15-270 |
5.59e-37 |
|
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: 132.20 E-value: 5.59e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMP--SHSGESNVVTDIVRVARILSNEA------LPIGIGIPGQVNCATGQVSNV 86
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPtpAEEGPEAVLDRIAELIEELLAEAgvreriLGIGIGVPGPVDPETGIVLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 87 VNLDIET-LELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDGNA----TVVFLNFGTGLAAGLVRGGQAEHGYSGSI 161
Cdd:cd23763 81 PNLPWWKnVPLRELLEERLGLPVVVENDANAAALG-----EAWFGAGrgvrNFVYITLGTGIGGGIIIDGKLYRGANGAA 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 162 GEIGHLPidpngfecpcgqrgcletvasggavaklwpsanppmpdlirkarqgdghandVLTMVAHAMGDTIQIVAQAYD 241
Cdd:cd23763 156 GEIGHIT----------------------------------------------------VLEEAARYLGIGLANLINLLN 183
|
250 260
....*....|....*....|....*....
gi 1537797675 242 PQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:cd23763 184 PELIVLGGGVAEAGDLLLEPIREAVRRRA 212
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
15-269 |
8.32e-35 |
|
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: 128.09 E-value: 8.32e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGES---------NVVTDIVRVARILSNeALPIGIGIPGQVNCATGQVSN 85
Cdd:cd24059 4 IGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENpeevleklyELIDRLLEKENIKSK-ILGIGIGAPGPLDVEKGIILN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 86 VVNL-DIETLELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDGNAT----VVFLNFGTGLAAGLVRGGQAEHGYSGS 160
Cdd:cd24059 83 PPNFpGWENIPLVELLEEKFGIPVYLDNDANAAALA-----EKWYGKGKnydnFIYILADEGIGAGIIINGKLYRGVDGY 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 161 IGEIGHLPIDPNGFECPCGQRGCLETVASGGAVAKLWPSA--NPPM--PDLIRKARQGDGHANDVLTMVAHAMGDTIQIV 236
Cdd:cd24059 158 AGEIGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSAlgSGRSfqLDIVEALQKGDPIADEVIEEAAKYLGIGLVNL 237
|
250 260 270
....*....|....*....|....*....|...
gi 1537797675 237 AQAYDPQRIIIGGGMAKTGDALIEVIQAELSRR 269
Cdd:cd24059 238 INLLNPEAIIIGGELIYLGERYLEPIEKEVNSR 270
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
15-265 |
1.39e-33 |
|
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: 124.92 E-value: 1.39e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPS--HSGESNVVTDIVRVARILSN--EALPIGIGIPGQVNCATGQVSNVVNL- 89
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTkvENGKEDVINRIAETVNELIEemELLGIGIGSPGSIDRENGIVRFSPNFp 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 90 DIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFvEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHLPI 169
Cdd:cd24064 82 DWRNFPLVPLIEERTGIKVFLENDANAFALGEWWF-GNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 170 DPNGFECPCGQRGCLETVASGGAVAKL-------WPSANPPMPD------LIRKARQGDGHANDVLTMVAHAMGDTIQIV 236
Cdd:cd24064 161 EPNGPICGCGNRGCVEAFASATAIIRYaresrkrYPDSLAGESEkinakhVFDAARKNDPLATMVFRRVVDALAIAIGGF 240
|
250 260
....*....|....*....|....*....
gi 1537797675 237 AQAYDPQRIIIGGGMAKTGDALIEVIQAE 265
Cdd:cd24064 241 VHIFNPEIIIIGGGISRAGSFLLDPIREK 269
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
16-269 |
2.11e-29 |
|
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: 113.48 E-value: 2.11e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 16 GIDIGGTKIEGVLLDATDRVIDVCRMPSHSGESN----VVTDIVRVARILSNEALPIGIGIPGQVNCATGQV--SNVVNL 89
Cdd:cd24057 4 GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAaflaAIAELVAEADARFGVKGPVGIGIPGVIDPEDGTLitANIPAA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 90 DIETLelGERVSAIMHAPVHVENDVNAAAVGAAEFvEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHLPI 169
Cdd:cd24057 84 KGRPL--RADLSARLGRPVRIDNDANCFALSEAWD-GAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 170 ---------DPNGFECPCGQRGCLETVASGGAVAKLWP---SANPPMPDLIRKARQGDGHANDV----LTMVAHAMGDTI 233
Cdd:cd24057 161 padalllgyDLPVLRCGCGQTGCLETYLSGRGLERLYAhlyGEELDAPEIIAAWAAGDPQAVAHvdrwLDLLAGCLANIL 240
|
250 260 270
....*....|....*....|....*....|....*.
gi 1537797675 234 QIVaqayDPQRIIIGGGMAKTgDALIEVIQAELSRR 269
Cdd:cd24057 241 TAL----DPDVVVLGGGLSNF-PALIAELPAALPAH 271
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
48-270 |
2.19e-29 |
|
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: 114.00 E-value: 2.19e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 48 SNVVTDIVRVARILSNEALPIGIGIPGQVNCATGQVSNVVNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAEF-VE 126
Cdd:cd24075 45 IEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVHYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFgAS 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 127 QVDGNATVVFLNFGTGlaAGLVRGGQAEHGYSGSIGEIGHLPIDPNGFECPCGQRGCLETVASG-------------GAV 193
Cdd:cd24075 125 KDCKDSILVRIHHGIG--AGIIIDGKLFLGQNGNAGEIGHIQIEPLGERCHCGNFGCLETVASNaaieqrvkkllkqGYA 202
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1537797675 194 AKLwPSANPPMPDLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQAYDPQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:cd24075 203 SQL-TLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQA 278
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
15-270 |
3.31e-29 |
|
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: 113.53 E-value: 3.31e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMP-SHSGESNVVTD-IVRVARILSNEA------LPIGIGIPGQVNCATGQVSNV 86
Cdd:cd24071 4 IGVKIEEGYLVLALTDLKGKILEKTRIPfDHETDPEKVIElIAENIKKLIKNKhvekklLGIGIAVSGLVDSKKGIVIRS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 87 VNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFVEQVDGNATVVfLNFGTGLAAGLVRGGQAEHGYSGSIGEIGH 166
Cdd:cd24071 84 TILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFIC-VTVGAGIGSSLVIDGKLYTGNFGGAGEIGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 167 LPIDPNGFECPCGQRGCLETVASGGAVA------------KLWPSANPPMPDLIRK-ARQGDGHANDVLTMVAHAMGDTI 233
Cdd:cd24071 163 MTIQPDGRKCYCGQKGCLEAYASFEALVneikeltesyplSLLKELEDFEIEKVREaAEEGDSVATELFKKAGEYLGIGI 242
|
250 260 270
....*....|....*....|....*....|....*..
gi 1537797675 234 QIVAQAYDPQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:cd24071 243 KNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENF 279
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
15-260 |
5.44e-29 |
|
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: 112.82 E-value: 5.44e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPS-HSGESNVVTDIV--RVARILSNEALP----IGIGIPGQVNCATGQVSNVV 87
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTpKTGDPGTVSEQVlgLIETLLSKAGKDsiegIGVSSAGPLDLRKGTIVNSP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 88 NLDIETLELGERVSAIMHAPVHVENDVNAAAVGAaEFVEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHL 167
Cdd:cd24063 83 NIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGE-HLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 168 PIDPN-GFECPCGQRGCLETVASGGAVAKL---WPSANPPMP---------------DLIRKARQGDGHANDVLTMVAHA 228
Cdd:cd24063 162 VVDTEsGLKCGCGGYGHWEAFASGRGIPRFareWAEGFSSRTslklrnpggegitakEVFSAARKGDPLALKIIEKLARY 241
|
250 260 270
....*....|....*....|....*....|..
gi 1537797675 229 MGDTIQIVAQAYDPQRIIIGGGMAKTGDALIE 260
Cdd:cd24063 242 NGRGIANVINAYDPELIVIGGSVFNNNKDILD 273
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
15-290 |
4.77e-27 |
|
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: 107.25 E-value: 4.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSH--SGESNVVTDIVRVARILSNEA----LPIGIGIPGQVNCATGQVSNVVN 88
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLDFEKVPSKdlLRAGDPVEVLADLIREYIEEAglkpAAIVIGVPGTVDKDRRTVISTPN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 89 LD-IETLELGERVSAIMHAPVHVENDVNAAAVGAAEFVEqVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHL 167
Cdd:cd24070 84 IPgLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGN-LDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 168 PIDPNGFECPCGQRGCLETVASGGAVAKLWPSANPPMPDLIRKARQGDghANDVLTMVaHAMGDTIQIVAQAYDPQRIII 247
Cdd:cd24070 163 PVYGNGKPCGCGNTGCLETYASGRALEEIAEEHYPDTPILDIFVDHGD--EPELDEFV-EDLALAIATEINILDPDAVIL 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1537797675 248 GGG-MAKTG---DALIEVIQAELSRR--AEGCRFL-TTLDIASNIRIAAM 290
Cdd:cd24070 240 GGGvIDMKGfprETLEEYIRKHLRKPypADNLKIIyAELGPEAGVIGAAI 289
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
68-270 |
7.77e-27 |
|
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: 107.40 E-value: 7.77e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 68 IGIGIPGQVNCATGQVSNVVNLDIETLELGERVSAIMHAPVHVENDVNAAAV-----GAAEfveqvdGNATVVFLNFGTG 142
Cdd:cd24074 66 IAITLPGIIDPESGIVHRLPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLaerffGAAK------GAKNIIQIVIDDD 139
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 143 LAAGLVRGGQAEHGYSGSIGEIGHLPIDPNGFECPCGQRGCLETVASGGAVAKLWPSANPPMPD------------LIRK 210
Cdd:cd24074 140 IGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQSPDsmlhgqpisiesLCQA 219
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 211 ARQGDGHANDVLTMVAHAMGDTIQIVAQAYDPQRIIIGGGMAKTGDALIEVIQAELSRRA 270
Cdd:cd24074 220 ALAGDPLAQDIIIQVGRHLGRILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQS 279
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
17-250 |
7.40e-25 |
|
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: 101.21 E-value: 7.40e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 17 IDIGGTKIEGVLLDaTDRVIDVCRMPSHSgeSNVVTDIVRVARIL----SNEALPIGIGIPGQVNcaTGQVSNVVNLDIE 92
Cdd:cd24069 3 IDIGGTKIAAALIG-NGQIIDRRQIPTPR--SGTPEALADALASLladyQGQFDRVAVASTGIIR--DGVLTALNPKNLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 93 TLE---LGERVSAIMHAPVHVENDVNAAAVGaaEFV-EQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHLP 168
Cdd:cd24069 78 GLSgfpLADALQQLLGVPVVLLNDAQAAAWG--EYQaGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 169 IDPNGFECPCGQRGCLETVASGGAVAKLWPSA-NPPM--PDLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQAYDPQRI 245
Cdd:cd24069 156 ADPPGPVCGCGRRGCVEAIASGTAIAAAASEIlGEPVdaKDVFERARSGDEEAARLIDRAARALADLIADLKATLDLDCV 235
|
....*
gi 1537797675 246 IIGGG 250
Cdd:cd24069 236 VIGGS 240
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
15-251 |
8.02e-25 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 101.26 E-value: 8.02e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGES----NVVTDIVRVARILSNEALPIGIGIPGQVNCATGQVSNVVNLD 90
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYqqtiEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNANSTW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 91 IETLELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDG---NATVVF-LNFGTGLAAGLVRGGQAEHGYSGSIGEIGH 166
Cdd:PRK09557 83 LNGQPLDKDLSARLNREVRLANDANCLAVS-----EAVDGaaaGKQTVFaVIIGTGCGAGVAINGRVHIGGNGIAGEWGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 167 LPI---------DPNGFECPCGQRGCLETVASG-GAVAKLWPSANPPMP--DLIRKARQGDGHANDVLTMVAHAMGDTIQ 234
Cdd:PRK09557 158 NPLpwmdedelrYRNEVPCYCGKQGCIETFISGtGFATDYRRLSGKALKgsEIIRLVEEGDPVAELAFRRYEDRLAKSLA 237
|
250
....*....|....*..
gi 1537797675 235 IVAQAYDPQRIIIGGGM 251
Cdd:PRK09557 238 HVINILDPDVIVLGGGM 254
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
15-267 |
1.10e-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: 100.69 E-value: 1.10e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVL--LDATdrVIDVCRMP-SHSGESNVVTDIVRVARILSNEALP-------IGIGIPGQVNcaTGQVS 84
Cdd:cd24077 4 IGIDLGYNYISLMLtyLDGE--IISSKQIKlLDISFENILEILKSIIQELISQAPKtpyglvgIGIGIHGIVD--ENEII 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 85 NVVNLDIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFVEQVDgnaTVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEI 164
Cdd:cd24077 80 FTPYYDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFSEDYD---NLISISIHSGIGAGIIINNQLYRGYNGFAGEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 165 GHLPIDPNGFECPCGQRGCLETVASGGAV----AKLWPSANPPMPDLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQAY 240
Cdd:cd24077 157 GHMIIVPNGKPCPCGNKGCLEQYASEKALlkelSEKKGLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNIINTF 236
|
250 260
....*....|....*....|....*..
gi 1537797675 241 DPQRIIIGGGMAKTGDALIEVIQAELS 267
Cdd:cd24077 237 NPEIIIINSSLINEIPELLEKIKEQLS 263
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
16-269 |
5.90e-23 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 96.21 E-value: 5.90e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 16 GIDIGGTKIE-GVL-----LDATDRVidvcRMPSHSGES--NVVTDIVRVARILSNEALPIGIGIPGQVNCATGQV--SN 85
Cdd:PRK13310 4 GFDIGGTKIElGVFnekleLQWEERV----PTPRDSYDAflDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLyaAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 86 VVNLDIETLElgERVSAIMHAPVHVENDVNAAAVGAAeFVEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIG 165
Cdd:PRK13310 80 VPAASGKPLR--ADLSARLGRDVRLDNDANCFALSEA-WDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 166 H--LPID---------PNgFECPCGQRGCLETVASGGAVAKLWP---SANPPMPDLIRKARQGD----GHANDVLTMVAH 227
Cdd:PRK13310 157 HmrLPVDaltllgwdaPL-RRCGCGQKGCIENYLSGRGFEWLYQhyyGEPLQAPEIIALYYQGDeqavAHVERYLDLLAI 235
|
250 260 270 280
....*....|....*....|....*....|....*....|..
gi 1537797675 228 AMGDTIQIVaqayDPQRIIIGGGMAKtgdalIEVIQAELSRR 269
Cdd:PRK13310 236 CLGNILTIV----DPHLVVLGGGLSN-----FDAIYEQLPKR 268
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
68-285 |
6.00e-23 |
|
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: 96.33 E-value: 6.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 68 IGIGIPGQVNCATGQVSNVVNL---DIETLELGERVSAImhaPVHVENDVNAAAVgaaefVEQVDGNAT----VVFLNFG 140
Cdd:cd24072 63 IALAIQGLVDSHKGVSLWSPGApwrNIEIKYLLEERYGI---PVFVENDCNMLAL-----AEKWQGELRqsrdFCVINLD 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 141 TGLAAGLVRGGQAEHGYSGSIGEIGHLPIDPNGFECPCGQRGCLETVASGGAVAKLW--------PSANPP---MPDLIR 209
Cdd:cd24072 135 YGIGSAIVIDNKLYIGASSGSGEIGHTKVNPDGARCDCGRRGCLETVASNSALKRNArvtlklgpVSADPEkltMEQLIE 214
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1537797675 210 KARQGDGHANDVLTMVAHAMGDTIQIVAQAYDPQRIIIGGGMAKTGDALIEVIqaelsRRAegCRFLTTLDIASNI 285
Cdd:cd24072 215 ALEEGEPIATQIFDRAANAIGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAI-----RRA--IAENPFSQHATQI 283
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
15-250 |
1.39e-21 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 92.35 E-value: 1.39e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGESN-VVTDIVRVAR--ILSNEALP--IGIGIPGQVNCATGQVSNVVNL 89
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPdLVSGLGEMIDeyLRRFNARChgIVMGFPALVSKDRRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 90 DIETLE---LGERVSAIMHAPVHVENDVNAAAV-GAAEFveQVDGNaTVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIG 165
Cdd:PRK09698 87 PLTALDlydLADKLENTLNCPVFFSRDVNLQLLwDVKEN--NLTQQ-LVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELG 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 166 HLPIDPNGFECPCGQRGCLETVASGGAVaKLWPSANPP---MPDLIRKArqGDGHA-NDVLTMVAHAMGDTIQIvaqaYD 241
Cdd:PRK09698 164 HIPLGDMTQHCGCGNPGCLETNCSGMAL-RRWYEQQPRdypLSDLFVHA--GDHPFiQSLLENLARAIATSINL----FD 236
|
....*....
gi 1537797675 242 PQRIIIGGG 250
Cdd:PRK09698 237 PDAIILGGG 245
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
14-250 |
5.87e-21 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 90.36 E-value: 5.87e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 14 CVGIDIGGTKIEGVLLDATDRVIDVCRMPS-HSGESNVVTD-IVRVARILSNEALPIGIGipgqvncATGQVSNVVNLDI 91
Cdd:PRK05082 3 TLAIDIGGTKIAAALVGEDGQIRQRRQIPTpASQTPEALRQaLSALVSPLQAQADRVAVA-------STGIINDGILTAL 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 92 ETLELG--------ERVSAIMHAPVHVENDVNAAAvgAAEFVEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGE 163
Cdd:PRK05082 76 NPHNLGgllhfplvQTLEQLTDLPTIALNDAQAAA--WAEYQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGH 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 164 IGHLPIDPNGFECPCGQRGCLETVASG---GAVAKLWpsANPPMPDLI-RKARQGDGHANDVLTMVAHAMGDTIQIVAQA 239
Cdd:PRK05082 154 IGHTLADPHGPVCGCGRRGCVEAIASGraiAAAAQGW--LAGCDAKTIfERAGQGDEQAQALINRSAQAIARLIADLKAT 231
|
250
....*....|.
gi 1537797675 240 YDPQRIIIGGG 250
Cdd:PRK05082 232 LDCQCVVLGGS 242
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
14-268 |
1.06e-20 |
|
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: 89.55 E-value: 1.06e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 14 CVGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGES-NVVTDIVRVARILSNEALPIGIGIPGQVNCATGQVSNV-VNLDI 91
Cdd:cd24152 2 YLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLeEFLDYIKKIIKRYDEEIDGIAISAPGVIDPETGIIYGGgALPYL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 92 ETLELGERVSAIMHAPVHVENDVNAAAVGaaefvEQVDGNA----TVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHL 167
Cdd:cd24152 82 KGFNLKEELEERCNLPVSIENDAKCAALA-----ELWLGSLkgikNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 168 PIDPN-----GFECPCGQRGCLETVASggavAKLWPSANppMPDLIRKARQGDghaNDVLTMVAHAMGD------TIQIV 236
Cdd:cd24152 157 LTDDDdkdllFFSGLASMFGLVKRYNK----AKGLEPLD--GEEIFEKYAKGD---EAAKKILDEYIRNlakliyNIQYI 227
|
250 260 270
....*....|....*....|....*....|..
gi 1537797675 237 aqaYDPQRIIIGGGMAKTgDALIEVIQAELSR 268
Cdd:cd24152 228 ---LDPEVIVIGGGISEQ-PLFIEDLKKEVNE 255
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
17-271 |
2.28e-20 |
|
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: 89.01 E-value: 2.28e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 17 IDIGGTKIEGVLLDATDRVIDVCRMPSHSGESNVVTDIVRVARILSNEA-------LPIGIGIPGQVNCATGQVSNVVNL 89
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEAvklncriLGVGISTGGRVNPREGIVLHSTKL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 90 --DIETLELGERVSAIMHAPVHVENDVNAAAVGAAEFvEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGHL 167
Cdd:cd24060 85 iqEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKF-GHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELGHI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 168 PIDPNGFECPCGQRGCLETVASGGAVA----KLWPSANPPMP-------------DLIRKARQGDGHANDVLTMVAHAMG 230
Cdd:cd24060 164 VVSLDGPDCMCGSHGCVEAYASGMALQreakKLHDEDLLLVEgmsvtndeevtakHLIQAAKLGNAKAQKILRTAGTALG 243
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1537797675 231 DTIQIVAQAYDPQRIIIGGGMAKTGdalIEVIQAELSRRAE 271
Cdd:cd24060 244 LGIVNILHTLNPSLVILSGVLASHY---ENIVKDVIAQRAL 281
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
14-266 |
2.44e-18 |
|
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: 82.23 E-value: 2.44e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 14 CVGIDIGGTKIEGVLLD------ATDRVidvcRMPS-HSGESNVVTDIVR-VARILSNEAlPIGIGIPGQVncATGQVSN 85
Cdd:cd24058 1 ILGIDIGGSGIKGAIVDtdtgelLSERI----RIPTpQPATPEAVADVVAeLVAHFPWFG-PVGVGFPGVV--RRGVVRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 86 VVNLD---IETlELGERVSAIMHAPVHVENDVNAAAVGAAEFVEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYsgsig 162
Cdd:cd24058 74 AANLDkswIGF-DAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVLVLTLGTGIGSALFVDGHLVPNT----- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 163 EIGHLPIDpngfecpcgqRGCLETVASGGAVAKLwpsanppmpDLIRKARQgdGHANDVLtmvahamgdtiQIVAQAYDP 242
Cdd:cd24058 148 ELGHLEIR----------GKDAEERASLGVRARE---------DLGWKRWA--KRVNKYL-----------QYLERLFNP 195
|
250 260
....*....|....*....|....
gi 1537797675 243 QRIIIGGGMAKTGDALIEVIQAEL 266
Cdd:cd24058 196 DLFIIGGGNSKKADKFLPLLDVKT 219
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
15-286 |
2.80e-14 |
|
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: 71.81 E-value: 2.80e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRMPSHSGEsnvvTDIVRVARILSNEALPI-GIGI----PGQVNCATGQVSNVV-- 87
Cdd:cd24067 2 GGIEAGGTKFVCAVGTGDGNIIERTEFPTTTPE----ETLQAVIDFFREQEEPIdAIGIasfgPIDLNPTSPTYGYITtt 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 88 ------NLDIetleLGERVSAImHAPVHVENDVNAAAVGAAEFVEQvDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSi 161
Cdd:cd24067 78 pkpgwrNFDI----LGALKRAF-PVPVGFDTDVNAAALAEYRWGAA-KGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP- 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 162 gEIGH--LPIDPN--GFE--CPcGQRGCLETVASGGAVAKLWpsaNPPMPDLirkarqGDGHanDVLTMVAHAMGDTIQI 235
Cdd:cd24067 151 -EMGHirVPRHPDddGFPgvCP-FHGDCLEGLASGPAIAARW---GIPAEEL------PDDH--PAWDLEAYYLAQACAN 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1537797675 236 VAQAYDPQRIIIGGG-MAKTGdaLIEVIQAELSRRAEGcrFLTTLDIASNIR 286
Cdd:cd24067 218 LTLTLSPERIVLGGGvMQRPG--LFPRIREKFRKLLNG--YLEVPRLLPDID 265
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
16-240 |
3.37e-13 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 68.13 E-value: 3.37e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 16 GIDIGGTKIEGVLLDATDRVIDVCRMPSHSGEsnvVTDIVRVARILSNEAL-------PIGIGIPGQVNCATGQV--SNV 86
Cdd:PRK13311 4 GFDMGGTKIELGVFDENLQRIWHKRVPTPRED---YPQLLQILRDLTEEADtycgvqgSVGIGIPGLPNADDGTVftANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 87 VNLDIETLElgERVSAIMHAPVHVENDVNAAAVGAAeFVEQVDGNATVVFLNFGTGLAAGLVRGGQAEHGYSGSIGEIGH 166
Cdd:PRK13311 81 PSAMGQPLQ--ADLSRLIQREVRIDNDANCFALSEA-WDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 167 --LPIDPNGF--------ECPCGQRGCLETVASGGAVAKLWP---SANPPMPDLIRKARQGD----GHANDVLTMVAHAM 229
Cdd:PRK13311 158 frLPVDALDIlgadiprvPCGCGHRGCIENYISGRGFEWMYShfyQHTLPATDIIAHYAAGEpkavAHVERFMDVLAVCL 237
|
250
....*....|.
gi 1537797675 230 GDTIQIVAQAY 240
Cdd:PRK13311 238 GNLLTMLGSPF 248
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
15-269 |
1.47e-05 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 45.64 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATDRVIDVCRM----PSHSGESNVVTDIVRVARILSNEALP------IGIGIPGqvncatgqvs 84
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLGRGRAgganPQSVGLEEALASLREALEEALAAAGDpadieaVGFGLAG---------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 85 nvvnldIETLELGERVSAIMH-----APVHVENDVNAAAVGAAEfveqvDGNATVVFLnfGTG-LAAGLVRGGQAE---- 154
Cdd:COG2971 74 ------AGTPEDAEALEAALRelfpfARVVVVNDALAALAGALG-----GEDGIVVIA--GTGsIAAGRDGDGRTArvgg 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 155 HGY------SGS-IG----------EIGHLPIDP------NGFECPCGQRgcletvasggAVAKLWPSANPPM------P 205
Cdd:COG2971 141 WGYllgdegSGAwLGrealraalraLDGRGPPTAlteavlAEFGLDDPEE----------LIAWVYRGPAPPAdlaslaP 210
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1537797675 206 DLIRKARQGDGHANDVLTMVAHAMGDTIQIVAQAyDPQRIIIGGGMAKTGDALIEVIQAELSRR 269
Cdd:COG2971 211 LVFEAAEAGDPVARAILEEAADELAELARALLER-GALPVVLAGGVAAAQPLLREALRARLAAG 273
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
15-270 |
1.82e-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: 1.82e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 15 VGIDIGGTKIEGVLLDATD---RVIDVCRMPSHSGESnvVTDIVRvaRILSNEALP----IGIGIPGQVNcatGQVSNVV 87
Cdd:cd24008 2 LVGDIGGTNARLALADAGDgsgDLLFVRKYPSADFAS--LEDALA--AFLAELGAPrpkaACIAVAGPVD---GGRVRLT 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 88 NLD--IETLELGERVSAimhAPVHVENDVNAAA-----VGAAEFVE-----QVDGNATVVFLNFGTGL-AAGLVRGGQae 154
Cdd:cd24008 75 NLDwsIDAAELRKALGI---GRVRLLNDFEAAAyglpaLGPEDLLVlygggGPLPGGPRAVLGPGTGLgVALLVPDGD-- 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 155 HGYSGSIGEIGHLPIDP-NGFEC--------PCGQRGCLETVASG-------GAVAKLWPSANPPMP--DLIRKARQGDG 216
Cdd:cd24008 150 GGYVVLPSEGGHADFAPvTEEEAelleflrkRFGRSVSYEDVLSGpgleniyEFLAKLDGAEPPDLTaeEIAEAALAGDP 229
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1537797675 217 HANDVLTMVAHAMGDTIQIVAQAYDPQR-IIIGGGMAKtgdALIEVIQAELSRRA 270
Cdd:cd24008 230 LAREALDLFARILGRFAGNLALSFLATGgVYLAGGIAP---KNLDLLDSSAFREA 281
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
14-164 |
4.13e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 38.44 E-value: 4.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 14 CVGIDIGGTKIEGVLLDATDRVIDV-----CRMPSHSGE--SNVVTDIVRVARILSNEALPI---GIGIPGqvncatgqv 83
Cdd:cd24007 1 VLGVDGGGTKTRAVLADEDGKILGRgkggpSNPASVGIEeaKENLKEAVREALSQAGSLGEIdaiCLGLAG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1537797675 84 snvVNLDIETLELGERVSAIMH-APVHVENDVNAAAVGAAEfveqvdGNATVVFLNfGTGlAAGLVRGGQAEHGYSGSIG 162
Cdd:cd24007 72 ---IDSEEDRERLRSALKELFLsGRIIIVNDAEIALAAALG------GGPGIVVIA-GTG-SVAYGRNGDGEEARVGGWG 140
|
..
gi 1537797675 163 EI 164
Cdd:cd24007 141 HL 142
|
|
| |
