|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
2-281 |
3.57e-113 |
|
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: 327.99 E-value: 3.57e-113
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 2 TIATIDIGGTGIKFASLTPDGKILDKTSIPTPEN-LEDLLAWLDQRLSEQDY--SGIAMSVPGAVNQETGVIDGFSAVPY 78
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDsLEEFLDYIKKIIKRYDEeiDGIAISAPGVIDPETGIIYGGGALPY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 79 IHGFSWYEALSSY-QIPVHLENDANCVGLSELLAHP--ELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMTTLA 155
Cdd:cd24152 81 LKGFNLKEELEERcNLPVSIENDAKCAALAELWLGSlkGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLLTDD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 156 PAEKLNNWSQLASTGNMVRYVIEKSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDPDVISLGGSIS 235
Cdd:cd24152 161 DDKDLLFFSGLASMFGLVKRYNKAKGLEPLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGGGIS 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1893910534 236 QNPDFIQGVKEAVEDFVETYEEYTVAPVIQACTYHADANLYGALVN 281
Cdd:cd24152 241 EQPLFIEDLKKEVNEILANRPGSIPKPEIKACKFGNDANLLGALYN 286
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-284 |
3.32e-74 |
|
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: 229.40 E-value: 3.32e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 1 MTIATIDIGGTGIKFASLTPDGKILDKTSIPTPEN------LEDLLAWLDQRLSE-----QDYSGIAMSVPGAVNQETGV 69
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGagpeavLEAIAELIEELLAEagisrGRILGIGIGVPGPVDPETGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 70 IDGFSAVPYIHGFSWYEALSS-YQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGG 146
Cdd:COG1940 85 VLNAPNLPGWRGVPLAELLEErLGLPVFVENDANAAALAEAWfgAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 147 EFGYMTTLAPAEKLNN-----WSQLASTGNMVRYVIEKSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQY 221
Cdd:COG1940 165 EIGHMPVDPDGPLCGCgnrgcLETYASGPALLRRARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYLGIGLANLIN 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1893910534 222 LIDPDVISLGGSISQNPD-FIQGVKEAVEDFVetYEEYTVAPVIQACTYHADANLYGALVNWLQ 284
Cdd:COG1940 245 LLDPEVIVLGGGVSAAGDlLLEPIREALAKYA--LPPAREDPRIVPASLGDDAGLLGAAALALE 306
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-281 |
1.28e-69 |
|
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: 217.43 E-value: 1.28e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 3 IATIDIGGTGIKFASLTPDGKILDKTSIPTPEN------LEDLLAWLDQRLSEQDYSGIAMSVPGAVNQETGVIDGFSA- 75
Cdd:cd24068 2 ILGIDIGGTKIKYGLVDADGEILEKDSVPTPASkggdaiLERLLEIIAELKEKYDIEGIGISSAGQVDPKTGEVIYATDn 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 76 VPYIHGFSWYEALSS-YQIPVHLENDANCVGLSE--LLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMT 152
Cdd:cd24068 82 LPGWTGTNLKEELEErFGLPVAVENDVNCAALAEkwLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMV 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 153 TLAPAE-----KLNNWSQLASTGNMVRYVIEKSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDPDV 227
Cdd:cd24068 162 VDPGGRpcccgGKGCLEQYASGTALVRRVAEALGEPGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEV 241
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 228 ISLGGSIS-QNPDFIQGVKEAVEDfvETYEEYTVAPVIQACTYHADANLYGALVN 281
Cdd:cd24068 242 IVIGGGISaQGELFLEELREELRK--LLMPPLLDATKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
6-278 |
5.02e-48 |
|
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: 159.94 E-value: 5.02e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP--ENLEDLLAWLDQRLSE--------QDYSGIAMSVPGAVNQETGVIDGFSA 75
Cdd:cd23763 3 IDIGGTKIRAALVDLDGEILARERVPTPaeEGPEAVLDRIAELIEEllaeagvrERILGIGIGVPGPVDPETGIVLFAPN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 76 VPYIHGFSWYEALSS-YQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMT 152
Cdd:cd23763 83 LPWWKNVPLRELLEErLGLPVVVENDANAAALGEAWfgAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGHIT 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 153 tlapaeklnnwsqlastgnmvryVIEKSGqtdwdgrkiyqeaeagnalcqeaiermnRNLAQGLLNIQYLIDPDVISLGG 232
Cdd:cd23763 163 -----------------------VLEEAA----------------------------RYLGIGLANLINLLNPELIVLGG 191
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1893910534 233 SISQNPDFIQG-VKEAVEDFVetYEEYTVAPVIQACTYHADANLYGA 278
Cdd:cd23763 192 GVAEAGDLLLEpIREAVRRRA--LPPLRRRVRIVPSELGDDAGLLGA 236
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
6-284 |
1.04e-41 |
|
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: 145.18 E-value: 1.04e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP-----ENLEDLLAWLDQRLSEQDYS--GIAMSVPGAVNQETGVIDgFSAVPY 78
Cdd:pfam00480 3 IDIGGTKIAAALFDEEGEILARERVPTPtttteETLVDAIAFFVDSAQRKFGEliAVGIGSPGLISPKYGYIT-NTPNIG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 79 IHGFSWYEALSS-YQIPVHLENDANCVGLSE--LLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMTtLA 155
Cdd:pfam00480 82 WDNFDLVEKLEErFNVPVFFENDANAAALAEavFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQ-LD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 156 PAEKLNN------WSQLAStGNMVRYVIEKSGQtDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDPDVIS 229
Cdd:pfam00480 161 PNGPKCGcgnhgcLETIAS-GRALEKRYQQKGE-DLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINLFDPQAIV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 230 LGGSISQNPDFIQGVKEAVEDFVETYEEYTVAPVIQAcTYHADANLYGALVNWLQ 284
Cdd:pfam00480 239 LGGGVSNADGLLEAIRSLVKKYLNGYLPVPPVIIVAA-SLGDNAGALGAAALAKQ 292
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
3-278 |
1.78e-38 |
|
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: 137.42 E-value: 1.78e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 3 IATIDIGGTGIKFASLTPDGKILDKTSIPTPEN------LEDLLAWLDQRLSEQDYS-----GIAMSVPGAVNQETGVID 71
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLeggeniITDIAESIQQLLEELGYSkedliGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 72 GfsAVP-YIHGFSWYEALS-SYQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGE 147
Cdd:cd24062 82 V--AVNlGWKNFPLKDKLEaLTGIPVVIDNDANAAALGEMWkgAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 148 FGYMtTLAPAE-------KLNNWSQLASTGNMVRYVIEKSGQT-------------DWDGRKIYQEAEAGNALCQEAIER 207
Cdd:cd24062 160 IGHI-TVNPEGgapcncgKTGCLETVASATGIVRIAREELEEGkgssalrilalggELTAKDVFEAAKAGDELALAVVDT 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1893910534 208 MNRNLAQGLLNIQYLIDPDVISLGGSISQNPDF-IQGVKEAVEDFveTYEEYTVAPVIQACTYHADANLYGA 278
Cdd:cd24062 239 VARYLGLALANLANTLNPEKIVIGGGVSAAGEFlLSPVKEYFDRF--TFPRVRQDTEIVLATLGNDAGVIGA 308
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
6-252 |
1.28e-37 |
|
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: 134.64 E-value: 1.28e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP--------ENLEDLLAWLDQRLSEQDYSGIAMsvPGAVNQETGVIDGFSAVp 77
Cdd:cd24066 4 IDLGGTKIEGIALDRAGRELLRRRVPTPrgdyeatlDAIADLVEEAEEELGAPATVGIGT--PGSISPRTGLVKNANST- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 78 YIHGFSWYEALSS-YQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMTTL 154
Cdd:cd24066 81 WLNGKPLKADLEArLGRPVRIENDANCFALSEATdgAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNPLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 155 APAEKLNNW-----------SQLASTGNMVRYVIEKSGQTdWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLI 223
Cdd:cd24066 161 WPDEDELPGppcycgkrgcvETFLSGPALERDYARLTGKT-LSAEEIVALARAGDAAAVATLDRFLDRLGRALANVINIL 239
|
250 260
....*....|....*....|....*....
gi 1893910534 224 DPDVISLGGSISQNPDFIQGVKEAVEDFV 252
Cdd:cd24066 240 DPDVIVLGGGLSNIDELYTEGPAALARYV 268
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
6-278 |
6.30e-36 |
|
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: 130.14 E-value: 6.30e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTpDGKILDKTSIPTP----ENLEDLLAWLDQRLsEQDYSG---IAMSVPGAVNQETGVIDGFSAVPY 78
Cdd:cd24065 5 LDLGGTKIAAGVVD-GGRILSRLVVPTPreggEAVLDALARAVEAL-QAEAPGveaVGLGVPGPLDFRRGRVRFAPNIPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 79 IHGFSWYEALS-SYQIPVHLENDANCVGLSE--LLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMT--- 152
Cdd:cd24065 83 LTDFPIRRGLAeRLGLPVVLENDANAAALAEhhYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTTvlp 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 153 --TLAPAEKLNNWSQLASTGNMVR---YVIeksgQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDPDV 227
Cdd:cd24065 163 ggPMCGCGLVGCLEALASGRALARdasFAY----GRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQKALDPEV 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1893910534 228 ISLGGSISQN-PDFIQGVKEAVEDFVETYEeytvAPVIQACTYHADANLYGA 278
Cdd:cd24065 239 FVLGGGVAQVgDYYLLPVQEAARRYTEGWH----APPLRLAHLGTDAGVIGA 286
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
6-278 |
1.15e-34 |
|
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: 127.08 E-value: 1.15e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP---ENLEDLLAWLDQRLSEQ-DYSGIAMSVPGAVNQETGVIdgfSAVPYIhg 81
Cdd:cd24061 4 VDIGGTKIAAGVVDEEGEILATERVPTPptaDGIVDAIVEAVEELREGhDVSAVGVAAAGFVDADRATV---LFAPNI-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 82 fSW-YEALSSY-----QIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMTT 153
Cdd:cd24061 79 -AWrNEPLKDLleariGLPVVIENDANAAAWAEYRfgAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 154 -----LAPAEKLNNWSQLASTGNMVRYVIEK------------SGQTDW--DGRKIYQEAEAGNALCQEAIERMNRNLAQ 214
Cdd:cd24061 158 vpdglLCGCGSRGCWEQYASGRALVRYAKEAanatpegaavllADGSVDgiTGKHISEAARAGDPVALDALRELARWLGA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 215 GLLNIQYLIDPDVISLGGSISQNPDFIQG-VKEAVEDFVETYEEYTVAPVIQACTYHaDANLYGA 278
Cdd:cd24061 238 GLASLAALLDPELFVIGGGVSDAGDLLLDpIREAFERWLPGRGWRPIPRLRTAQLGN-DAGLIGA 301
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
6-248 |
5.79e-34 |
|
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called GlcNAc kinase, catalyzes the phosphorylation of N-acetyl-D-glucosamine (GlcNAc) derived from cell-wall degradation, yielding GlcNAc-6-P. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466907 [Multi-domain] Cd Length: 298 Bit Score: 125.04 E-value: 5.79e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP--------ENLEDLLAWLDQRLSEQdySGIAMSVPGAVNQETGVIdgFSA-V 76
Cdd:cd24057 5 FDIGGTKIEFAVFDEALQLVWTKRVPTPtddyaaflAAIAELVAEADARFGVK--GPVGIGIPGVIDPEDGTL--ITAnI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 77 PYIHGFSWYEALS-SYQIPVHLENDANCVGLSEllAHPEL----ENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYM 151
Cdd:cd24057 81 PAAKGRPLRADLSaRLGRPVRIDNDANCFALSE--AWDGAgrgyPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 152 TtlAPAEKLNNWSQLA-------STGNMVRYViekSG-----------QTDWDGRKIYQEAEAGNALCQEAIERMNRNLA 213
Cdd:cd24057 159 P--LPADALLLGYDLPvlrcgcgQTGCLETYL---SGrglerlyahlyGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLA 233
|
250 260 270
....*....|....*....|....*....|....*
gi 1893910534 214 QGLLNIQYLIDPDVISLGGSISQNPDFIQGVKEAV 248
Cdd:cd24057 234 GCLANILTALDPDVVVLGGGLSNFPALIAELPAAL 268
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
6-249 |
6.30e-31 |
|
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: 117.28 E-value: 6.30e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP------ENLEDLLAWLDQRLSEQDYS-----GIAMSVPGAVNQETGVID--- 71
Cdd:cd24076 6 VELGVDYITVVVTDLAGEVLWRREVPLPasddpdEVLAQLAALIREALAAAPDSplgilGIGVGVPGLVDSEDGVVLlap 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 72 --GFSAVPYIHGFSwyealSSYQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGE 147
Cdd:cd24076 86 nlGWRDVPLRDLLE-----EALGVPVFVDNEANAAALAEKRfgAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 148 FGYMtTLAPAEKLNN------WSQLASTGNMVRYVIEKSGQTDW-DGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQ 220
Cdd:cd24076 161 IGHM-TVDPDGPPCScgnrgcWETYASERALLRAAGRLGAGGEPlSLAELVEAARAGDPAALAALEEVGEYLGIGLANLV 239
|
250 260 270
....*....|....*....|....*....|
gi 1893910534 221 YLIDPDVISLGGSISQ-NPDFIQGVKEAVE 249
Cdd:cd24076 240 NTFNPELVVLGGALAPlGPWLLPPLRAEVA 269
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-278 |
2.05e-30 |
|
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: 116.15 E-value: 2.05e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 4 ATIDIGGTGIKFASLTPDGKILDKTSIPT---PENLEDLLA-WLDQRLSEQDYSG-----IAMSVPGAVNQETGVIDGFS 74
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTdttPETIVDAIAsAVDSFIQHIAKVGheivaIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 75 AVpYIHGFSWYEALSSY-QIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYM 151
Cdd:TIGR00744 81 NL-DWKQEPLKEKVEARvGLPVVVENDANAAALGEYKkgAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 152 TTLAPAEKLNN------WSQLASTGNMVRYV------------IEKSGQTD-WDGRKIYQEAEAGNALCQEAIERMNRNL 212
Cdd:TIGR00744 160 RMVPDGRLLCNcgkqgcIETYASATGLVRYAkranakperaevLLALGDGDgISAKHVFVAARQGDPVAVDSYREVARWA 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1893910534 213 AQGLLNIQYLIDPDVISLGGSISQNPDFIqgvkeaVEDFVETYEEYTVAPVIQACTYHA-----DANLYGA 278
Cdd:TIGR00744 240 GAGLADLASLFNPSAIVLGGGLSDAGDLL------LDPIRKSYKRWLFGGARQVADIIAaqlgnDAGLVGA 304
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
6-249 |
5.29e-30 |
|
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: 114.61 E-value: 5.29e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP--ENLEDLLAWLDQ---RLSEQDY-----SGIAMSVPGAVNQETGVIdgfSA 75
Cdd:cd24059 6 VEIGRDLLSAVLCDLSGNILAREKYPLDekENPEEVLEKLYElidRLLEKENikskiLGIGIGAPGPLDVEKGII---LN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 76 VPYIHGFSWY---EALSS-YQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFG 149
Cdd:cd24059 83 PPNFPGWENIplvELLEEkFGIPVYLDNDANAAALAEKWygKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 150 YMTTLAPAEKLNNWSQ-----LASTGNMVRYVIEKSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLID 224
Cdd:cd24059 163 HTSIDINGPRCSCGNRgclelYASIPAIEKKARSALGSGRSFQLDIVEALQKGDPIADEVIEEAAKYLGIGLVNLINLLN 242
|
250 260
....*....|....*....|....*.
gi 1893910534 225 PDVISLGGSISQNPD-FIQGVKEAVE 249
Cdd:cd24059 243 PEAIIIGGELIYLGErYLEPIEKEVN 268
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
3-232 |
1.38e-25 |
|
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: 103.13 E-value: 1.38e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 3 IATIDIGGTGIKFASLTPDGKILDKTSIPT-----PENLEDLLA-WLDQRLSEQDYS----GIAMSVPGAVNQETG-VID 71
Cdd:cd24071 3 IIGVKIEEGYLVLALTDLKGKILEKTRIPFdhetdPEKVIELIAeNIKKLIKNKHVEkkllGIGIAVSGLVDSKKGiVIR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 72 ----GFSAVPY---IHgfswyealSSYQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRH 142
Cdd:cd24071 83 stilGWENVELkkiLK--------EKFKIPVFIDNDVNSFALAELWkgKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNF 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 143 GLGGEFGYMTTLAPAEKLNNWSQ-----LASTGNMVRYVIEKSGQ---------TDWDGRKIYQEAEAGNALCQEAIERM 208
Cdd:cd24071 155 GGAGEIGHMTIQPDGRKCYCGQKgcleaYASFEALVNEIKELTESyplsllkelEDFEIEKVREAAEEGDSVATELFKKA 234
|
250 260
....*....|....*....|....
gi 1893910534 209 NRNLAQGLLNIQYLIDPDVISLGG 232
Cdd:cd24071 235 GEYLGIGIKNLINIFNPEAIIIGG 258
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
6-283 |
2.14e-25 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 102.41 E-value: 2.14e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTP--------ENLEDLLAWLDQRLSEQDYSGIAmsVPGAVNQETGVIDGFSAVp 77
Cdd:PRK09557 5 IDLGGTKIEVIALDDAGEELFRKRLPTPrddyqqtiEAIATLVDMAEQATGQRGTVGVG--IPGSISPYTGLVKNANST- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 78 YIHGFSWYEALSSY-QIPVHLENDANCVGLSEllahpELENAAC-------VVIGTGIGGAMIINGRLHRGRHGLGGEFG 149
Cdd:PRK09557 82 WLNGQPLDKDLSARlNREVRLANDANCLAVSE-----AVDGAAAgkqtvfaVIIGTGCGAGVAINGRVHIGGNGIAGEWG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 150 -----YMTtlapAEKLNNWSQ--------------LASTGnMVRYVIEKSGQTDwDGRKIYQEAEAGNALCQEAIERMNR 210
Cdd:PRK09557 157 hnplpWMD----EDELRYRNEvpcycgkqgcietfISGTG-FATDYRRLSGKAL-KGSEIIRLVEEGDPVAELAFRRYED 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893910534 211 NLAQGLLNIQYLIDPDVISLGGSISQNPDFIQGVKEAVEDFVETYEEYTvaPVIQACtYHADANLYGALvnWL 283
Cdd:PRK09557 231 RLAKSLAHVINILDPDVIVLGGGMSNVDRLYPTLPALLKQYVFGGECET--PVRKAL-HGDSSGVRGAA--WL 298
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
5-278 |
7.93e-25 |
|
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: 7.93e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 5 TIDIGGTGIKFASLTPDGKILDKTSIPTP----ENLEDLLAWLDQRLSEQDYS------GIAMSVPGAVNQETgVIdgFS 74
Cdd:cd24077 5 GIDLGYNYISLMLTYLDGEIISSKQIKLLdisfENILEILKSIIQELISQAPKtpyglvGIGIGIHGIVDENE-II--FT 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 75 avPYIH--GFSWYEALSS-YQIPVHLENDANCVGLSELLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYM 151
Cdd:cd24077 82 --PYYDleDIDLKEKLEEkFNVPVYLENEANLSALAERTFSEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIGHM 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 152 tTLAPAEKLNN------WSQLASTGNMVRYVIEKSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDP 225
Cdd:cd24077 160 -IIVPNGKPCPcgnkgcLEQYASEKALLKELSEKKGLETLTFDDLIQLYNEGDPEALELIDQFIKYLAIGINNIINTFNP 238
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1893910534 226 DVISLGGS-ISQNPDFIQGVKEAVEDFVETYEEytvapvIQACTYHADANLYGA 278
Cdd:cd24077 239 EIIIINSSlINEIPELLEKIKEQLSSSFNKYVE------ILISTLGKNATLLGG 286
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
6-278 |
1.09e-24 |
|
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: 100.65 E-value: 1.09e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPT--PENLEDLLAWLDQRLSE----QDYSGIAMSVPGAVNQETGVIDGFSAVPYI 79
Cdd:cd24064 4 IDLGGTDTKIGIVDENGDILKKKTIDTkvENGKEDVINRIAETVNElieeMELLGIGIGSPGSIDRENGIVRFSPNFPDW 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 80 HGFSWYEALSS-YQIPVHLENDANCVGLSE--LLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYMTTLAP 156
Cdd:cd24064 84 RNFPLVPLIEErTGIKVFLENDANAFALGEwwFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHVIVEPN 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 157 AEKLNNWSQ-----LASTGNMVRYVIE---------KSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYL 222
Cdd:cd24064 164 GPICGCGNRgcveaFASATAIIRYAREsrkrypdslAGESEKINAKHVFDAARKNDPLATMVFRRVVDALAIAIGGFVHI 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1893910534 223 IDPDVISLGGSISQNPDFI-QGVKEAVED-----FVETYEeytvapvIQACTYHADANLYGA 278
Cdd:cd24064 244 FNPEIIIIGGGISRAGSFLlDPIREKTKKyvmlsFQDTYS-------IELSNLVEDAGILGA 298
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
1-280 |
5.22e-24 |
|
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: 98.39 E-value: 5.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 1 MTIATIDIGGTGIKFASLTPDGKILD--KTSIPTPENLEDLLAWLDQRLSEQ------DYSGIAMSVPGAVNQETGVIdg 72
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDfeKVPSKDLLRAGDPVEVLADLIREYieeaglKPAAIVIGVPGTVDKDRRTV-- 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 73 FSAvPYIHGFSWYEALSS----YQIPVHLENDANCVGLSELLAHpELENAACVV---IGTGIGGAMIINGRLHRGRHGLG 145
Cdd:cd24070 79 IST-PNIPGLDGVNLADIlenkLGIPVILERDVNLLLLYDMRAG-NLDDEGVVLgfyIGTGIGNAILINGKPLRGKNGVA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 146 GEFGYMTTLAPAEKLNNWSQ-----LASTGNMVRYVIEKSGQTDwdgrkIYQEAEAGNAlcQEAIERMNRNLAQGLLNIQ 220
Cdd:cd24070 157 GELGHIPVYGNGKPCGCGNTgcletYASGRALEEIAEEHYPDTP-----ILDIFVDHGD--EPELDEFVEDLALAIATEI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1893910534 221 YLIDPDVISLGGSISQNPDFIQgvkeavEDFVETYEEYTVAPV------IQACTYHADANLYGALV 280
Cdd:cd24070 230 NILDPDAVILGGGVIDMKGFPR------ETLEEYIRKHLRKPYpadnlkIIYAELGPEAGVIGAAI 289
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
2-279 |
2.58e-23 |
|
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: 97.02 E-value: 2.58e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 2 TIATIDIGGTGIKFASLTPDGKILDKTSIPTPEN---------LEDLLAWLDQRLSEQDYSGIAMSVPGAVNQETGVIDG 72
Cdd:cd24063 1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTgdpgtvseqVLGLIETLLSKAGKDSIEGIGVSSAGPLDLRKGTIVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 73 -----FSAVPYIhgfswyEALSS-YQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGL 144
Cdd:cd24063 81 spnikGKEIPLV------EPLKEeFNIPVALLNDAVAAALGEHLfgAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGN 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 145 GGEFGYMTTLAPAEKL------NNWSQLASTGNMVRYVIEKSGQTDWDGRK--------------IYQEAEAGNALCQEA 204
Cdd:cd24063 155 AAEVGHLVVDTESGLKcgcggyGHWEAFASGRGIPRFAREWAEGFSSRTSLklrnpggegitakeVFSAARKGDPLALKI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 205 IERMNRNLAQGLLNIQYLIDPDVISLGGSISQNPDFIqgVKEAVEDFVETYEEYTvAPVIQACTYHADANLYGAL 279
Cdd:cd24063 235 IEKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDI--LDPLIEYLEKNPAISK-GPEIVLSELGDDVGLIGAL 306
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
7-241 |
2.81e-23 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 96.60 E-value: 2.81e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 7 DIGGTGIKFASLTPDGKILDKTSIPTP--------ENLEDLLAWLDQRLSEQDYSGIAmsVPGAVNQETGVIDgFSAVPY 78
Cdd:PRK13310 6 DIGGTKIELGVFNEKLELQWEERVPTPrdsydaflDAVCELVAEADQRFGCKGSVGIG--IPGMPETEDGTLY-AANVPA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 79 IHGFSWYEALSS-YQIPVHLENDANCVGLSELLaHPELENAACV---VIGTGIGGAMIINGRLHRGRHGLGGEFGYMTTL 154
Cdd:PRK13310 83 ASGKPLRADLSArLGRDVRLDNDANCFALSEAW-DDEFTQYPLVmglILGTGVGGGLVFNGKPISGRSYITGEFGHMRLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 155 APAEKLNNW-SQLASTGNMVRYVIEK--SGQT-DWDGRKIYQEA----------EAGNALCQEAIERMNRNLAQGLLNIQ 220
Cdd:PRK13310 162 VDALTLLGWdAPLRRCGCGQKGCIENylSGRGfEWLYQHYYGEPlqapeiialyYQGDEQAVAHVERYLDLLAICLGNIL 241
|
250 260
....*....|....*....|.
gi 1893910534 221 YLIDPDVISLGGSISqNPDFI 241
Cdd:PRK13310 242 TIVDPHLVVLGGGLS-NFDAI 261
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
6-279 |
2.12e-22 |
|
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: 93.89 E-value: 2.12e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKfASLTPDGKILDKTSIPTP-----ENLEDLLAWLDQRLSEQ-DYSGIAMsvpgavnqeTGVID--GFSA-- 75
Cdd:cd24069 3 IDIGGTKIA-AALIGNGQIIDRRQIPTPrsgtpEALADALASLLADYQGQfDRVAVAS---------TGIIRdgVLTAln 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 76 ---VPYIHGFSWYEALSS-YQIPVHLENDANCVGLSE--LLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFG 149
Cdd:cd24069 73 pknLGGLSGFPLADALQQlLGVPVVLLNDAQAAAWGEyqAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 150 YMTT-LAPAE----KLNNWSQLAStGNMVRYVIEKSGQTDWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLID 224
Cdd:cd24069 153 HTLAdPPGPVcgcgRRGCVEAIAS-GTAIAAAASEILGEPVDAKDVFERARSGDEEAARLIDRAARALADLIADLKATLD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 225 PDVISLGGSISQNPDFIQGVKEAVEDFVETYEeytvaPVIQACTYHADANLYGAL 279
Cdd:cd24069 232 LDCVVIGGSVGLAEGFLERVEQYLADEPAIFR-----VSLEPARLGQDAGLLGAA 281
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
1-288 |
4.61e-22 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 93.05 E-value: 4.61e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 1 MTIATIDIGGTGIKFASLTPDGKILDKTSIPTP-----ENLEDLLAWLDQRLSEQ-DYSGIAmsvpgavnqETGVID--G 72
Cdd:PRK05082 1 MTTLAIDIGGTKIAAALVGEDGQIRQRRQIPTPasqtpEALRQALSALVSPLQAQaDRVAVA---------STGIINdgI 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 73 FSAV-PYIHG----FSWYEALSSY-QIPVHLENDANCVGLSELLAHP-ELENAACVVIGTGIGGAMIINGRLHRGRHGLG 145
Cdd:PRK05082 72 LTALnPHNLGgllhFPLVQTLEQLtDLPTIALNDAQAAAWAEYQALPdDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLA 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 146 GEFGYmtTLA-PAEKLNNWSQ------LAStGNmvryVIEKSGQTDWDG---RKIYQEAEAGNALCQEAIERMNRNLAQG 215
Cdd:PRK05082 152 GHIGH--TLAdPHGPVCGCGRrgcveaIAS-GR----AIAAAAQGWLAGcdaKTIFERAGQGDEQAQALINRSAQAIARL 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893910534 216 LLNIQYLIDPDVISLGGSISQNPDFIQGVKEAVEDFVETYEeytvaPVIQACTYHADANLYGALVnWLQEENQ 288
Cdd:PRK05082 225 IADLKATLDCQCVVLGGSVGLAEGYLELVQAYLAQEPAIYH-----VPLLAAHYRHDAGLLGAAL-WAQGEKL 291
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
6-249 |
7.13e-21 |
|
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: 90.17 E-value: 7.13e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTPENLEDLLAWLDQRLSEQDYS---------GIAMSVPGAVNQETGV------- 69
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPNPKTYEERIDLILQMCVEAASEavklncrilGVGISTGGRVNPREGIvlhstkl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 70 IDGFSAVPYIHGFSwyealSSYQIPVHLENDANCVGLSEL-LAHPE-LENAACVVIGTGIGGAMIINGRLHRGRHGLGGE 147
Cdd:cd24060 85 IQEWSSVDLRTPIS-----DALHLPVWVDNDGNCAALAERkFGHGKgVENFVTVITGTGIGGGIILNHELIHGSSFCAAE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 148 FG---------------------YMTTLA---PAEKLNNWSQLastgnMVRYVIEKSGQTdWDGRKIYQEAEAGNALCQE 203
Cdd:cd24060 160 LGhivvsldgpdcmcgshgcveaYASGMAlqrEAKKLHDEDLL-----LVEGMSVTNDEE-VTAKHLIQAAKLGNAKAQK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1893910534 204 AIERMNRNLAQGLLNIQYLIDPDVISLGGSISqnPDFIQGVKEAVE 249
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGVLA--SHYENIVKDVIA 277
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
21-252 |
3.44e-20 |
|
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: 87.99 E-value: 3.44e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 21 DGKILDKTSIP----TPENLEDLLAWLDQRLSEQ------DYSGIAMSVPGAVNQETGVIDgfsavpYIHGFSWY----- 85
Cdd:cd24073 21 RGNVLASHTLPldsgDPEAVAEAIAEAVAELLAQaglspdRLLGIGVGLPGLVDAETGICR------WSPLLGWRdvpla 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 86 ----EALSsyqIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGYmTTLAPAEK 159
Cdd:cd24073 95 elleERLG---LPVYVENDVNALALAEHWfgAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGH-TTVDPDGP 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 160 LNNWSQ------LASTGNMVRYVIEKSGQ---TDWDgrKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDPDVISL 230
Cdd:cd24073 171 PCRCGKrgcleaYASDPAILRQAREAGLRgepLTIE--DLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELIII 248
|
250 260
....*....|....*....|...
gi 1893910534 231 GGS-ISQNPDFIQGVKEAVEDFV 252
Cdd:cd24073 249 SGEgVRAGDLLFEPMREALRAHV 271
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
3-241 |
1.28e-18 |
|
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: 84.00 E-value: 1.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 3 IATIDIGGTGIKFASLTPDGKILDKTS-----IPTPENLEDLL--AWLDQRL-SEQDYSGIAMSVPGAVNQETGVidgfs 74
Cdd:cd24072 3 VLGIVVSPNSLRAQVGNACGELLGEFEyrvitLETPEALIDEIidCIDRLLKlWKDRVKGIALAIQGLVDSHKGV----- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 75 aVPYIHGFSW------YEALSSYQIPVHLENDANCVGLSELLaHPEL---ENAACVVIGTGIGGAMIINGRLHRGRHGLG 145
Cdd:cd24072 78 -SLWSPGAPWrnieikYLLEERYGIPVFVENDCNMLALAEKW-QGELrqsRDFCVINLDYGIGSAIVIDNKLYIGASSGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 146 GEFGYM-----------------TTLAPAEKL-NNWSQLastgnmvryviEKSGQTDWDGRKI-----YQEAEAGNALCQ 202
Cdd:cd24072 156 GEIGHTkvnpdgarcdcgrrgclETVASNSALkRNARVT-----------LKLGPVSADPEKLtmeqlIEALEEGEPIAT 224
|
250 260 270
....*....|....*....|....*....|....*....
gi 1893910534 203 EAIERMNRNLAQGLLNIQYLIDPDVISLGGSISQNPDFI 241
Cdd:cd24072 225 QIFDRAANAIGRSLANILNLLNPEQVLLYGRGCRAGDLL 263
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
3-280 |
1.46e-18 |
|
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: 83.36 E-value: 1.46e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 3 IATIDIGGTGIKFASLTPDGKILDKTSIPT--P-ENLEDLLAWLDQRLSEQDYSGIAMSVPGAVNQET---GVID----- 71
Cdd:cd24067 1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPTttPeETLQAVIDFFREQEEPIDAIGIASFGPIDLNPTSptyGYITttpkp 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 72 GFSAVPYIHGFSWYealssYQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHrgrHGLG-GEF 148
Cdd:cd24067 81 GWRNFDILGALKRA-----FPVPVGFDTDVNAAALAEYRwgAAKGLDSLAYITVGTGIGVGLVVNGKPV---HGLLhPEM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 149 GYM-TTLAPAEKLNN---------WSQLASTGNMV-RYviEKSGQTDWDGRKIYqEAEAgnalcqeaiermnRNLAQGLL 217
Cdd:cd24067 153 GHIrVPRHPDDDGFPgvcpfhgdcLEGLASGPAIAaRW--GIPAEELPDDHPAW-DLEA-------------YYLAQACA 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1893910534 218 NIQYLIDPDVISLGGSISQNPDFIQGVKEAVEDFVETY----------EEYTVAPviqacTYHADANLYGALV 280
Cdd:cd24067 217 NLTLTLSPERIVLGGGVMQRPGLFPRIREKFRKLLNGYlevprllpdiDEYIVPP-----ALGNDAGILGALA 284
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
3-255 |
1.07e-14 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 72.71 E-value: 1.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 3 IATIDIGGTGIKFASLTPDGKILDKTSIPT-----PENLEDLLAWLDQRLSEQDY--SGIAMSVPGAVNQETGVIdgfSA 75
Cdd:PRK09698 6 VLGIDMGGTHIRFCLVDAEGEILHCEKKRTaeviaPDLVSGLGEMIDEYLRRFNArcHGIVMGFPALVSKDRRTV---IS 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 76 VPYIHGFSW-----YEALSSY-QIPVHLENDANCVGLSELLAHpELEN--AACVVIGTGIGGAMIINGRLHRGRHGLGGE 147
Cdd:PRK09698 83 TPNLPLTALdlydlADKLENTlNCPVFFSRDVNLQLLWDVKEN-NLTQqlVLGAYLGTGMGFAVWMNGAPWTGAHGVAGE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 148 FGYMttlapaeKLNNWSQLASTGNMVRYVIEKSGQTDwdgRKIYQEAEAGNALCQ--------EAIERMNRNLAQGLLNI 219
Cdd:PRK09698 162 LGHI-------PLGDMTQHCGCGNPGCLETNCSGMAL---RRWYEQQPRDYPLSDlfvhagdhPFIQSLLENLARAIATS 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1893910534 220 QYLIDPDVISLGGSISQNPDFiqgVKEAVEDFVETY 255
Cdd:PRK09698 232 INLFDPDAIILGGGVMDMPAF---PRETLIAMIQKY 264
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
7-150 |
7.95e-14 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 69.67 E-value: 7.95e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 7 DIGGTGIKFASLTPDGKILDKTSIPTP-ENLEDLLAWLDQRLSEQD-YSGIAMSV----PGAVNQETGVIdgFSA-VPYI 79
Cdd:PRK13311 6 DMGGTKIELGVFDENLQRIWHKRVPTPrEDYPQLLQILRDLTEEADtYCGVQGSVgigiPGLPNADDGTV--FTAnVPSA 83
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 80 HGFSWYEALSSY-QIPVHLENDANCVGLSELLaHPELENAACV---VIGTGIGGAMIINGRLHRGRHGLGGEFGY 150
Cdd:PRK13311 84 MGQPLQADLSRLiQREVRIDNDANCFALSEAW-DPEFRTYPTVlglILGTGVGGGLIVNGSIVSGRNHITGEFGH 157
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
22-251 |
7.17e-13 |
|
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: 67.39 E-value: 7.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 22 GKILDKTSIP----TPENLEDLL-----AWLDQ-RLSEQDYSGIAMSVPGAVNQETGVIdgfSAVPYIHGFSW--YEALS 89
Cdd:cd24075 22 GELLAEHTVPltalNQEALLSQLieeiaQFLKShRRKTQRLIAISITLPGLINPKTGVV---HYMPHIQVKSWpiVEELE 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 90 S-YQIPVHLENDANCVGLSE--LLAHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEFGY--MTTLAPAEKLNNWS 164
Cdd:cd24075 99 QrFNVPCFIGNDIRSLALAEhyFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGHiqIEPLGERCHCGNFG 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 165 QL------ASTGNMVRYVIEKSGQT-----DWDGRKIYQEAEAGNALCQEAIERMNRNLAQGLLNIQYLIDPDVISLGGS 233
Cdd:cd24075 179 CLetvasnAAIEQRVKKLLKQGYASqltlqDCTIKDICQAALNGDQLAQDVIKRAGRYLGKVIAILINLLNPQKIIIAGE 258
|
250 260
....*....|....*....|....
gi 1893910534 234 ISQNPDFIQGV------KEAVEDF 251
Cdd:cd24075 259 ITQADKVLLPVikkciqSQALPDF 282
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
6-137 |
2.67e-11 |
|
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: 62.20 E-value: 2.67e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASL-TPDGKIL-DKTSIPTPENL--EDLLAWLDQRLSEQDYSG-IAMSVPGAVNQetGVIdgFSAvPYIH 80
Cdd:cd24058 4 IDIGGSGIKGAIVdTDTGELLsERIRIPTPQPAtpEAVADVVAELVAHFPWFGpVGVGFPGVVRR--GVV--RTA-ANLD 78
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1893910534 81 ----GFSWYEALSS-YQIPVHLENDANCVGLSEL--LAHPELENAACVV-IGTGIGGAMIINGRL 137
Cdd:cd24058 79 kswiGFDAAKLLSKrLGRPVRVLNDADAAGLAEMkgGAGKGEKGVVLVLtLGTGIGSALFVDGHL 143
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
6-236 |
1.17e-09 |
|
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: 58.09 E-value: 1.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFASLTPDGKILDKTSIPTPENLEDllAWLDQRLSEQDY------------SGIAMSVPGAVNQETGVIDGF 73
Cdd:cd24074 7 IRIGRGYITLALRDLNGRLLAEERYPLPAKDND--PFLDRLLESISEffsrhqkklerlTAIAITLPGIIDPESGIVHRL 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 74 savPY--IHGFSWYEALSS-YQIPVHLENDANCVGLSELL--AHPELENAACVVIGTGIGGAMIINGRLHRGRHGLGGEF 148
Cdd:cd24074 85 ---PFydIKNLPLGEALEQhTGLPVYVQHDISAWTLAERFfgAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 149 GYmTTLAPAEK---------LNNwsqLASTGNM---VRYVIEKSGQTDWDGRKIY-----QEAEAGNALCQEAIERMNRN 211
Cdd:cd24074 162 GH-TQIDPYGKrcycgnhgcLET---VASIPAIleqANQLLEQSPDSMLHGQPISieslcQAALAGDPLAQDIIIQVGRH 237
|
250 260
....*....|....*....|....*
gi 1893910534 212 LAQGLLNIQYLIDPDVISLGGSISQ 236
Cdd:cd24074 238 LGRILAILVNLFNPEKILIGSPLNN 262
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
5-279 |
6.89e-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: 55.69 E-value: 6.89e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 5 TIDIGGTGIKFASLTPD---GKILDKTSIPTPE--NLEDLLAWLDQRLSEQDYSGIAMSVPGAVNQETGVIDG----FSA 75
Cdd:cd24008 3 VGDIGGTNARLALADAGdgsGDLLFVRKYPSADfaSLEDALAAFLAELGAPRPKAACIAVAGPVDGGRVRLTNldwsIDA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 76 vpyihgfswyEALSS--YQIPVHLEND--ANCVGLSELLAH---------PELENAACVVI--GTGIGGAMIINGRlHRG 140
Cdd:cd24008 83 ----------AELRKalGIGRVRLLNDfeAAAYGLPALGPEdllvlygggGPLPGGPRAVLgpGTGLGVALLVPDG-DGG 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 141 RHGLGGEFGYMtTLAPAEKL---------NNWSQLASTGNMV---------RYVIEKSGQTDWD--GRKIYQEAEAGNAL 200
Cdd:cd24008 152 YVVLPSEGGHA-DFAPVTEEeaelleflrKRFGRSVSYEDVLsgpgleniyEFLAKLDGAEPPDltAEEIAEAALAGDPL 230
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 201 CQEAIERMNRNLAQ--GLLNIQYLIDPDVISLGGSISQNPDFIQGvkeavEDFVETYEE-YTVAPVIQAC-TY---HADA 273
Cdd:cd24008 231 AREALDLFARILGRfaGNLALSFLATGGVYLAGGIAPKNLDLLDS-----SAFREAFLDkGRMSDLLEDIpVYlvtNEDL 305
|
....*.
gi 1893910534 274 NLYGAL 279
Cdd:cd24008 306 GLLGAA 311
|
|
| ASKHA_NBD_PanK-II_bac |
cd24085 |
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins ... |
6-171 |
1.31e-03 |
|
nucleotide-binding domain (NBD) of type II pantothenate kinase (PanK-II) and similar proteins mainly from bacteria; PanK (EC 2.7.1.33), also called pantothenic acid kinase, is the first enzyme in the Coenzyme A (CoA) biosynthetic pathway. It catalyzes the phosphorylation of pantothenate (vitamin B5) to form 4'-phosphopantothenate at the expense of a molecule of adenosine triphosphate (ATP), which is the rate-limiting step in CoA biosynthesis. It cannot utilize a phosphoryl donor other than ATP. Three distinct types of PanK have been identified, PanK-I, PanK-II and PanK-III. The model corresponds to a group of PanK-II that is mainly from bacteria.
Pssm-ID: 466935 [Multi-domain] Cd Length: 262 Bit Score: 39.47 E-value: 1.31e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 6 IDIGGTGIKFAsLTPDGKILDKTSIPTpENLEDLLAWLDqRLSEQDYSGIAMsvpgavnqeTGVidGFSAVPyihgfswy 85
Cdd:cd24085 4 IDAGGTLTKIV-LLENNGELKFKAFDS-LKIEALVKFLN-ELGINDIEKIAV---------TGG--GASRLP-------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1893910534 86 EALSSYQIPVHLENDANCVGLSELLAHPeLENA---------ACV---------VIGTGIGGAMIingrlhrgrHGLGGE 147
Cdd:cd24085 62 ENIDGIPIVKVDEFEAIGRGALYLLGEI-LDDAlvvsigtgtSIVlakngtirhVGGTGVGGGTL---------LGLGKL 131
|
170 180
....*....|....*....|....
gi 1893910534 148 FGYMTTLapaEKLNnwsQLASTGN 171
Cdd:cd24085 132 LLGVTDY---DEIT---ELARKGD 149
|
|
| |
