|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
1-303 |
0e+00 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 551.13 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAANV 80
Cdd:PRK13310 1 MYYGFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIRL 160
Cdd:PRK13310 81 PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHMRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 161 PVDALEVVGRDFPLLRCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNI 240
Cdd:PRK13310 161 PVDALTLLGWDAPLRRCGCGQKGCIENYLSGRGFEWLYQHYYGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAICLGNI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1460644637 241 LTIVDPDLLVLGGGLSNFTAISEGLAQRLPRHLLPVARVPRIERARHGDAGGMRGAAFLHLTH 303
Cdd:PRK13310 241 LTIVDPHLVVLGGGLSNFDAIYEQLPKRLPRHLLPVARVPRIEKARHGDAGGVRGAAFLHLTD 303
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
1-299 |
2.68e-159 |
|
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: 445.91 E-value: 2.68e-159
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAANV 80
Cdd:cd24057 1 MYYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAFLAAIAELVAEADARFGVKGPVGIGIPGVIDPEDGTLITANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIRL 160
Cdd:cd24057 81 PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 161 PVDALeVVGRDFPLLRCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNI 240
Cdd:cd24057 161 PADAL-LLGYDLPVLRCGCGQTGCLETYLSGRGLERLYAHLYGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLANI 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644637 241 LTIVDPDLLVLGGGLSNFTAISEGLAQRLPRHLLPVARVPRIERARHGDAGGMRGAAFL 299
Cdd:cd24057 240 LTALDPDVVVLGGGLSNFPALIAELPAALPAHLLSGARTPRIVPARHGDAGGVRGAAFL 298
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
1-244 |
4.47e-101 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 296.56 E-value: 4.47e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAANV 80
Cdd:PRK13311 1 MYYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVFTANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIRL 160
Cdd:PRK13311 81 PSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 161 PVDALEVVGRDFPLLRCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNI 240
Cdd:PRK13311 161 PVDALDILGADIPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAHYAAGEPKAVAHVERFMDVLAVCLGNL 240
|
....
gi 1460644637 241 LTIV 244
Cdd:PRK13311 241 LTML 244
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
4-299 |
3.32e-70 |
|
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: 219.38 E-value: 3.32e-70
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDQQGSVGIGIPG--MPETadGTLYAANVP 81
Cdd:cd24066 3 GIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEATLDAIADLVEEAEEELGAPATVGIGTPGsiSPRT--GLVKNANST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 82 AASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHirLP 161
Cdd:cd24066 81 WLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGH--NP 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 162 VDALEVVGRDFPLlrCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNIL 241
Cdd:cd24066 159 LPWPDEDELPGPP--CYCGKRGCVETFLSGPALERDYARLTGKTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVI 236
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1460644637 242 TIVDPDLLVLGGGLSNFTAISEGLAQRLPRHLL-PVARVPrIERARHGDAGGMRGAAFL 299
Cdd:cd24066 237 NILDPDVIVLGGGLSNIDELYTEGPAALARYVFsDEVETP-IVKNKHGDSSGVRGAAWL 294
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
1-299 |
6.97e-69 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 216.04 E-value: 6.97e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAANV 80
Cdd:PRK09557 1 MRIGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNANS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIRL 160
Cdd:PRK09557 81 TWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGHNPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 161 P-VDALEVVGRDfpLLRCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGN 239
Cdd:PRK09557 161 PwMDEDELRYRN--EVPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAH 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644637 240 ILTIVDPDLLVLGGGLSNFTAISEGLAQRLPRHLL-PVARVPrIERARHGDAGGMRGAAFL 299
Cdd:PRK09557 239 VINILDPDVIVLGGGMSNVDRLYPTLPALLKQYVFgGECETP-VRKALHGDSSGVRGAAWL 298
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-299 |
4.79e-64 |
|
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: 203.98 E-value: 4.79e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKS-SYEDFLQAVEALVREADERFDQQGS----VGIGIPGMPETADGT- 74
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGaGPEAVLEAIAELIEELLAEAGISRGrilgIGIGVPGPVDPETGVv 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 75 LYAANVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMglilgtgvgggLVLNGKSITGHSYITGE 154
Cdd:COG1940 86 LNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVyltlgtgigggIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 155 FGHIRLPVDAlevvgrdfplLRCGCGQLGCIENYLSGRGFA-WLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLL 233
Cdd:COG1940 166 IGHMPVDPDG----------PLCGCGNRGCLETYASGPALLrRARELGGAEKLTAEELFAAARAGDPLALEVLDEAARYL 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644637 234 AVCLGNILTIVDPDLLVLGGGLSN-FTAISEGLAQRLPRHLLPVARV-PRIERARHGDAGGMRGAAFL 299
Cdd:COG1940 236 GIGLANLINLLDPEVIVLGGGVSAaGDLLLEPIREALAKYALPPAREdPRIVPASLGDDAGLLGAAAL 303
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
3-299 |
1.97e-56 |
|
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: 184.08 E-value: 1.97e-56
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 3 YGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFL-QAVEALVREADERFDQQGSVGIGIPGMpeTADGTLYAANVP 81
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEETLvDAIAFFVDSAQRKFGELIAVGIGSPGL--ISPKYGYITNTP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 82 AASGR--PLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIR 159
Cdd:pfam00480 79 NIGWDnfDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 160 LpvdalevvgrDFPLLRCGCGQLGCIENYLSGRGFAWLYEhfyQQP--LSSPEIVAQWQQHDPRAQAHVERYLDLLAVCL 237
Cdd:pfam00480 159 L----------DPNGPKCGCGNHGCLETIASGRALEKRYQ---QKGedLEGKDIIVLAEQGDEVAEEAVERLARYLAKAI 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644637 238 GNILTIVDPDLLVLGGGLSNFTAISEGLAQRLPRHLLPVARVP--RIERARHGDAGGMRGAAFL 299
Cdd:pfam00480 226 ANLINLFDPQAIVLGGGVSNADGLLEAIRSLVKKYLNGYLPVPpvIIVAASLGDNAGALGAAAL 289
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
1-299 |
3.56e-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: 160.03 E-value: 3.56e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSY-EDFLQAVEALVREADERFDQQGsVGIGIPGMPETADGT-LYA- 77
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGgDAILERLLEIIAELKEKYDIEG-IGISSAGQVDPKTGEvIYAt 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 78 ANVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAW-------DDeftqypLVMglilgtgvggglvlngksIT---- 146
Cdd:cd24068 80 DNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWlgaakglDD------FLC------------------LTlgtg 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 147 -------------GHSYITGEFGHIRLpvdalevvgrDFPLLRCGCGQLGCIENYLSGRGFAWLY-EHFYQQPLSSPEIV 212
Cdd:cd24068 136 iggaiildgrlyrGANGSAGELGHMVV----------DPGGRPCCCGGKGCLEQYASGTALVRRVaEALGEPGIDGREIF 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 213 AQWQQHDPRAQAHVERYLDLLAVCLGNILTIVDPDLLVLGGGLSN-----FTAISEGLAQRLPRHLLpvaRVPRIERARH 287
Cdd:cd24068 206 DLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEVIVIGGGISAqgelfLEELREELRKLLMPPLL---DATKIEPAKL 282
|
330
....*....|..
gi 1460644637 288 GDAGGMRGAAFL 299
Cdd:cd24068 283 GNDAGLLGAAYL 294
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-297 |
3.73e-41 |
|
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: 144.39 E-value: 3.73e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQwEKRVATPKSSYEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADG-TLYAANVPA 82
Cdd:cd24065 4 GLDLGGTKIAAGVVDGGRILS-RLVVPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGrVRFAPNIPG 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 83 ASGRPLRTDLSARLGRDVRLDNDANCFALSE-----AWDDEFTQYPLVmglilGTGVGGGLVLNGKSITGHSYITGEFGH 157
Cdd:cd24065 83 LTDFPIRRGLAERLGLPVVLENDANAAALAEhhygaARGTESSVYVTI-----STGIGGGLVLGGRVLRGRHGQAGEIGH 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 158 IRL----PVdalevvgrdfpllrCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLL 233
Cdd:cd24065 158 TTVlpggPM--------------CGCGLVGCLEALASGRALARDASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHL 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1460644637 234 AVCLGNILTIVDPDLLVLGGglsnftaiseGLAQRLPRHLLPVARV----------PRIERARHGDAGGMRGAA 297
Cdd:cd24065 224 GIGLANLQKALDPEVFVLGG----------GVAQVGDYYLLPVQEAarrytegwhaPPLRLAHLGTDAGVIGAA 287
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
4-297 |
3.51e-35 |
|
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: 128.84 E-value: 3.51e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATPKS-SYEDFLQAVEALVREADERFDQQGS----VGIGIPGMPETADGT-LYA 77
Cdd:cd24076 5 GVELGVDYITVVVTDLAGEVLWRREVPLPASdDPDEVLAQLAALIREALAAAPDSPLgilgIGVGVPGLVDSEDGVvLLA 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 78 ANVpAASGRPLRTDLSARLGRDVRLDNDANCFALSEAW---DDEFTQYPLVmglilgtgvggglvlngkSIT-------- 146
Cdd:cd24076 85 PNL-GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRfgaGRGVSDLVYL------------------SAGvgigagii 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 147 -------GHSYITGEFGHIRLPVDalevvGRdfpllRCGCGQLGCIENYLSGRGFAWLYEH--FYQQPLSSPEIVAQWQQ 217
Cdd:cd24076 146 ldgelyrGASGFAGEIGHMTVDPD-----GP-----PCSCGNRGCWETYASERALLRAAGRlgAGGEPLSLAELVEAARA 215
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 218 HDPRAQAHVERYLDLLAVCLGNILTIVDPDLLVLGGGLSNFTA-ISEGLAQRLPRHLLPVARVP-RIERARHGDAGGMRG 295
Cdd:cd24076 216 GDPAALAALEEVGEYLGIGLANLVNTFNPELVVLGGALAPLGPwLLPPLRAEVARRALPAPARDvRIVVSRLGEDAAALG 295
|
..
gi 1460644637 296 AA 297
Cdd:cd24076 296 AA 297
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
4-297 |
3.22e-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: 126.31 E-value: 3.22e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATPKSSyEDFLQAVEALVREADERFDQqGSVGIGIPGMPETADGTLYAANVPAA 83
Cdd:cd24061 3 GVDIGGTKIAAGVVDEEGEILATERVPTPPTA-DGIVDAIVEAVEELREGHDV-SAVGVAAAGFVDADRATVLFAPNIAW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 84 SGRPLRTDLSARLGRDVRLDNDANCFALSE-AWDDEFTQYPLVMGLILGTGVGgGLVLNGKSITGHSYITGEFGHIRLPV 162
Cdd:cd24061 81 RNEPLKDLLEARIGLPVVIENDANAAAWAEyRFGAGRGTDDMVMITVGTGLGG-GIVIGGKLLRGAFGIAGEFGHIRVVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 163 DAlevvgrdfplLRCGCGQLGCIENYLSGR---------------GFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVE 227
Cdd:cd24061 160 DG----------LLCGCGSRGCWEQYASGRalvryakeaanatpeGAAVLLADGSVDGITGKHISEAARAGDPVALDALR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644637 228 RYLDLLAVCLGNILTIVDPDLLVLGGGLSN-----FTAISEGLAQRLP-RHLLPvarVPRIERARHGDAGGMRGAA 297
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVSDagdllLDPIREAFERWLPgRGWRP---IPRLRTAQLGNDAGLIGAA 302
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-299 |
5.40e-33 |
|
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: 121.42 E-value: 5.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATPKS-SYEDFLQAVEALVREADERFDQQG---SVGIGIPGMPETADGT-LYAA 78
Cdd:cd23763 2 GIDIGGTKIRAALVDLDGEILARERVPTPAEeGPEAVLDRIAELIEELLAEAGVRErilGIGIGVPGPVDPETGIvLFAP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 79 NVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYP-LVMglilgtgvggglvlngksIT----------- 146
Cdd:cd23763 82 NLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRnFVY------------------ITlgtgigggiii 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 147 ------GHSYITGEFGHIRLpvdalevvgrdfpllrcgcgqlgcienylsgrgfawlyehfyqqplsspeivaqwqqhdp 220
Cdd:cd23763 144 dgklyrGANGAAGEIGHITV------------------------------------------------------------ 163
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 221 raqahVERYLDLLAVCLGNILTIVDPDLLVLGGGLSN-----FTAISEGLAQRLprhLLPVARVPRIERARHGDAGGMRG 295
Cdd:cd23763 164 -----LEEAARYLGIGLANLINLLNPELIVLGGGVAEagdllLEPIREAVRRRA---LPPLRRRVRIVPSELGDDAGLLG 235
|
....
gi 1460644637 296 AAFL 299
Cdd:cd23763 236 AAAL 239
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-299 |
9.26e-31 |
|
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: 117.69 E-value: 9.26e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATPKSS---YEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAANV 80
Cdd:TIGR00744 2 GVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPetiVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAVN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIRL 160
Cdd:TIGR00744 82 LDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHIRM 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 161 PVDalevvGRdfplLRCGCGQLGCIENYLSGRGFAWLYEHFYQQP--------------LSSPEIVAQWQQHDPRAQAHV 226
Cdd:TIGR00744 162 VPD-----GR----LLCNCGKQGCIETYASATGLVRYAKRANAKPeraevllalgdgdgISAKHVFVAARQGDPVAVDSY 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 227 ERYLDLLAVCLGNILTIVDPDLLVLGGGLSNftaisEGLAQRLP-----RHLL--PVARVPRIERARHGDAGGMRGAAFL 299
Cdd:TIGR00744 233 REVARWAGAGLADLASLFNPSAIVLGGGLSD-----AGDLLLDPirksyKRWLfgGARQVADIIAAQLGNDAGLVGAADL 307
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
4-297 |
4.81e-28 |
|
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: 109.56 E-value: 4.81e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVAT-PKSSYEDFLQAVEALVREADERFDQQ-GSVGIGIPGM-PETADGTLYAANV 80
Cdd:cd24070 5 GIDIGGTNIRIGLVDEDGKLLDFEKVPSkDLLRAGDPVEVLADLIREYIEEAGLKpAAIVIGVPGTvDKDRRTVISTPNI 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIrl 160
Cdd:cd24070 85 PGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI-- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 161 PVDALEvvgrdfplLRCGCGQLGCIENYLSGRGFAWLYEHFYqQPLSSPEIVAqwqqhDPRAQAHVERYLDLLAVCLGNI 240
Cdd:cd24070 163 PVYGNG--------KPCGCGNTGCLETYASGRALEEIAEEHY-PDTPILDIFV-----DHGDEPELDEFVEDLALAIATE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1460644637 241 LTIVDPDLLVLGGGLSNFTAIS-EGLAQRLPRHL---LPVARVpRIERARHGDAGGMRGAA 297
Cdd:cd24070 229 INILDPDAVILGGGVIDMKGFPrETLEEYIRKHLrkpYPADNL-KIIYAELGPEAGVIGAA 288
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
2-299 |
4.41e-26 |
|
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: 104.68 E-value: 4.41e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 2 YYGFDIGGSKIALGVFNQERRLQWEKRVATPKSS-----YEDFLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLY 76
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEggeniITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 77 AANVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFG 156
Cdd:cd24062 82 VAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 157 HIrlPVDALEvvGRdfpllRCGCGQLGCIENYLSGRGFAWLY------------EHFY--QQPLSSPEIVAQWQQHDPRA 222
Cdd:cd24062 162 HI--TVNPEG--GA-----PCNCGKTGCLETVASATGIVRIAreeleegkgssaLRILalGGELTAKDVFEAAKAGDELA 232
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 223 QAHVERYLDLLAVCLGNILTIVDPDLLVLGGGLSnftAISEGLAQRL----PRHLLP-VARVPRIERARHGDAGGMRGAA 297
Cdd:cd24062 233 LAVVDTVARYLGLALANLANTLNPEKIVIGGGVS---AAGEFLLSPVkeyfDRFTFPrVRQDTEIVLATLGNDAGVIGAA 309
|
..
gi 1460644637 298 FL 299
Cdd:cd24062 310 WL 311
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
1-299 |
1.08e-24 |
|
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: 100.34 E-value: 1.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 1 MYYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDqqgsvGIGI--PGMPETADGTLY-A 77
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLEEFLDYIKKIIKRYDEEID-----GIAIsaPGVIDPETGIIYgG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 78 ANVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGH 157
Cdd:cd24152 76 GALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSY 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 158 IrlpvdalevVGRDFPLLRCGCGqlgcieNYLSGRGFAWLYEHFYQQPLSSPEIVAQW-QQHDPRAQAHVERYLDLLAVC 236
Cdd:cd24152 156 L---------LTDDDDKDLLFFS------GLASMFGLVKRYNKAKGLEPLDGEEIFEKyAKGDEAAKKILDEYIRNLAKL 220
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1460644637 237 LGNILTIVDPDLLVLGGGLSNFTAISEGL---AQRLPRHLLPVARVPRIERARHGDAGGMRGAAFL 299
Cdd:cd24152 221 IYNIQYILDPEVIVIGGGISEQPLFIEDLkkeVNEILANRPGSIPKPEIKACKFGNDANLLGALYN 286
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
4-256 |
9.34e-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: 98.34 E-value: 9.34e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATP-KSSYEDFLQAVEALVREADERFDQQGsVGIGIPGMPETADG-TLYAANVP 81
Cdd:cd24064 3 GIDLGGTDTKIGIVDENGDILKKKTIDTKvENGKEDVINRIAETVNELIEEMELLG-IGIGSPGSIDRENGiVRFSPNFP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 82 AASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIrlp 161
Cdd:cd24064 82 DWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHV--- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 162 vdaleVVGRDFPLlrCGCGQLGCIENYLSGRGFAWLYEHFYQ----------QPLSSPEIVAQWQQHDPRAQAHVERYLD 231
Cdd:cd24064 159 -----IVEPNGPI--CGCGNRGCVEAFASATAIIRYARESRKrypdslagesEKINAKHVFDAARKNDPLATMVFRRVVD 231
|
250 260
....*....|....*....|....*
gi 1460644637 232 LLAVCLGNILTIVDPDLLVLGGGLS 256
Cdd:cd24064 232 ALAIAIGGFVHIFNPEIIIIGGGIS 256
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
6-299 |
3.44e-21 |
|
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: 90.81 E-value: 3.44e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 6 DIGGSKIALGVFNQERRLQwEKRVATPKS-SYEDFLQAVEALVREADERFDQqgsVGIGIPGMpeTADGTLYAAN---VP 81
Cdd:cd24069 4 DIGGTKIAAALIGNGQIID-RRQIPTPRSgTPEALADALASLLADYQGQFDR---VAVASTGI--IRDGVLTALNpknLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 82 AASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHirlp 161
Cdd:cd24069 78 GLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGH---- 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 162 vdalevVGRDFPLLRCGCGQLGCIENYLSGRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNIL 241
Cdd:cd24069 154 ------TLADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEPVDAKDVFERARSGDEEAARLIDRAARALADLIADLK 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 242 TIVDPDLLVLGGGLsnftAISEGLAQRLPRHL--LPVARVPRIERARHGDAGGMRGAAFL 299
Cdd:cd24069 228 ATLDLDCVVIGGSV----GLAEGFLERVEQYLadEPAIFRVSLEPARLGQDAGLLGAALL 283
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
2-299 |
2.60e-19 |
|
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: 86.24 E-value: 2.60e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 2 YYGFDIGGSKIALGVFNQERRLQWEKRVATPKSSYED-FLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAANV 80
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGtVSEQVLGLIETLLSKAGKDSIEGIGVSSAGPLDLRKGTIVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 81 PAASGR--PLRTDLSARLGRDVRLDNDANCFALSEAWddeftqyplvmglilgtgvggglVLNGKSITGHSYIT------ 152
Cdd:cd24063 82 PNIKGKeiPLVEPLKEEFNIPVALLNDAVAAALGEHL-----------------------FGAGRGTSNLVYITistgig 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 153 -----------------GEFGHIrlpvdaleVVGRDFPLlRCGCGQLGCIENYLSGRG----FAWLYEHFYQQPL----- 206
Cdd:cd24063 139 ggvivdgrlllgkngnaAEVGHL--------VVDTESGL-KCGCGGYGHWEAFASGRGiprfAREWAEGFSSRTSlklrn 209
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 207 ------SSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNILTIVDPDLLVLGGGL-SNFTAISEGLAQRLPRHlLPVARV 279
Cdd:cd24063 210 pggegiTAKEVFSAARKGDPLALKIIEKLARYNGRGIANVINAYDPELIVIGGSVfNNNKDILDPLIEYLEKN-PAISKG 288
|
330 340
....*....|....*....|
gi 1460644637 280 PRIERARHGDAGGMRGAAFL 299
Cdd:cd24063 289 PEIVLSELGDDVGLIGALAL 308
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-299 |
7.81e-17 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 78.87 E-value: 7.81e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFLQAVEALVREADERFDQQ-GSVGIGIPGMPETADGTLYAA-NVP 81
Cdd:PRK09698 8 GIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIDEYLRRFNARcHGIVMGFPALVSKDRRTVISTpNLP 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 82 AASGR--PLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQyPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIr 159
Cdd:PRK09698 88 LTALDlyDLADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQ-QLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGHI- 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 160 lPVDALEvvgrdfplLRCGCGQLGCIENYLSGRGF-AWLYEHFYQQPLSspEIVAQWQQHdPRAQAhverYLDLLAVCLG 238
Cdd:PRK09698 166 -PLGDMT--------QHCGCGNPGCLETNCSGMALrRWYEQQPRDYPLS--DLFVHAGDH-PFIQS----LLENLARAIA 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1460644637 239 NILTIVDPDLLVLGGGLSNFTAIS-EGLAQRLPRHL---LPVARVpRIERARHGDAGGMRGAAFL 299
Cdd:PRK09698 230 TSINLFDPDAIILGGGVMDMPAFPrETLIAMIQKYLrkpLPYEVV-RFIYASSSDFNGAQGAAIL 293
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
41-297 |
8.84e-16 |
|
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: 76.05 E-value: 8.84e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 41 QAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAA------NVPaasgrpLRTDLSARLGRDVRLDNDANCFALSEA 114
Cdd:cd24073 46 EAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGICRWSpllgwrDVP------LAELLEERLGLPVYVENDVNALALAEH 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 115 W------DDEFTqyplvmglilgtgvggglvlngkSIT-----------------GHSYITGEFGHIrlPVDALevvGRd 171
Cdd:cd24073 120 WfgagrgLDNFA-----------------------VVTigrgigcglvvdgrlyrGAHGGAGEIGHT--TVDPD---GP- 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 172 fpllRCGCGQLGCIENYLSGRGF--AWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGNILTIVDPDLL 249
Cdd:cd24073 171 ----PCRCGKRGCLEAYASDPAIlrQAREAGLRGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELI 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 1460644637 250 VLGG-GLSNFTAISEGLAQRLPRHLLP-VARVPRIERARHGDAGGMRGAA 297
Cdd:cd24073 247 IISGeGVRAGDLLFEPMREALRAHVFPgLASDLELVIHPWGDEAWARGAA 296
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
12-273 |
2.65e-15 |
|
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: 74.76 E-value: 2.65e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 12 IALGVFNQERRLQWEKRVATPkSSYEDFLQAVEALVREA-DERFDQQGSVGIGIPGMPETADGT-LYAanvPAASGR--P 87
Cdd:cd24072 15 AQVGNACGELLGEFEYRVITL-ETPEALIDEIIDCIDRLlKLWKDRVKGIALAIQGLVDSHKGVsLWS---PGAPWRniE 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 88 LRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVLNGKSITGHSYITGEFGHIRLPVDAlev 167
Cdd:cd24072 91 IKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGSGEIGHTKVNPDG--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 168 vgrdfplLRCGCGQLGCIENYLS-------GRGFAWLYEHFYQQP-LSSPEIVAQWQQHDPRAQAHVERYLDLLAVCLGN 239
Cdd:cd24072 168 -------ARCDCGRRGCLETVASnsalkrnARVTLKLGPVSADPEkLTMEQLIEALEEGEPIATQIFDRAANAIGRSLAN 240
|
250 260 270
....*....|....*....|....*....|....*....
gi 1460644637 240 ILTIVDPDLLVLGGGLSNF-----TAISEGLAQRLPRHL 273
Cdd:cd24072 241 ILNLLNPEQVLLYGRGCRAgdlllPAIRRAIAENPFSQH 279
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
6-299 |
5.70e-15 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 73.41 E-value: 5.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 6 DIGGSKIALGVFNQERRLQWEKRVATPKSSYEDFL-QAVEALVREADERFDQQGSVGIGIpgmpeTADGTLYAANvPAAS 84
Cdd:PRK05082 7 DIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALrQALSALVSPLQAQADRVAVASTGI-----INDGILTALN-PHNL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 85 GR----PLRTDLSARLGRDVRLDNDANcfalSEAWDdEFTQYPLVMGLIL----GTGVGGGLVLNGKSITGHSYITGEFG 156
Cdd:PRK05082 81 GGllhfPLVQTLEQLTDLPTIALNDAQ----AAAWA-EYQALPDDIRNMVfitvSTGVGGGIVLNGKLLTGPGGLAGHIG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 157 HIrlpvdaleVVGRDFPllRCGCGQLGCIENYLSGRGFA-----WLyehfyqQPLSSPEIVAQWQQHDPRAQAHVERYLD 231
Cdd:PRK05082 156 HT--------LADPHGP--VCGCGRRGCVEAIASGRAIAaaaqgWL------AGCDAKTIFERAGQGDEQAQALINRSAQ 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 232 LLAVCLGNILTIVDPDLLVLGGGLsnftAISEGLAQRLPRHL--LPVARVPRIERARHGDAGGMRGAAFL 299
Cdd:PRK05082 220 AIARLIADLKATLDCQCVVLGGSV----GLAEGYLELVQAYLaqEPAIYHVPLLAAHYRHDAGLLGAALW 285
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
4-303 |
5.20e-14 |
|
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: 71.08 E-value: 5.20e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQERRLQweKRVATPKSSYEDFLQAVEALVREADERFDQQG------SVGIGIPGMPETADGT-LY 76
Cdd:cd24059 5 GVEIGRDLLSAVLCDLSGNIL--AREKYPLDEKENPEEVLEKLYELIDRLLEKENikskilGIGIGAPGPLDVEKGIiLN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 77 AANVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAW------DDEFTqYPLVMGLILGTGvggglVLNGKSITGHSY 150
Cdd:cd24059 83 PPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWygkgknYDNFI-YILADEGIGAGI-----IINGKLYRGVDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 151 ITGEFGHIRLPVDalevvGRdfpllRCGCGQLGCIENYLS-GRGFAWLYEHFYQQPLSSPEIVAQWQQHDPRAQAHVERY 229
Cdd:cd24059 157 YAGEIGHTSIDIN-----GP-----RCSCGNRGCLELYASiPAIEKKARSALGSGRSFQLDIVEALQKGDPIADEVIEEA 226
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1460644637 230 LDLLAVCLGNILTIVDPDLLVLGGG---LSNFtaISEGLAQRLPRHLLPV-ARVPRIERARHGDAGGMRGAAFLHLTH 303
Cdd:cd24059 227 AKYLGIGLVNLINLLNPEAIIIGGEliyLGER--YLEPIEKEVNSRLFGRnAREVRILKSSLGEDAPLLGAAALVLNK 302
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
6-257 |
1.62e-12 |
|
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: 66.67 E-value: 1.62e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 6 DIGGSKIALGVFNQERRLQWEKRVATPKSsYED----FLQAVEALVREADERFDQQGSVGIGIPGMPETADGTLYAAN-- 79
Cdd:cd24060 6 DLGGTNLRVAIVSMKGEIVKKYTQPNPKT-YEEridlILQMCVEAASEAVKLNCRILGVGISTGGRVNPREGIVLHSTkl 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 80 VPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAW------DDEFtqyplvMGLILGTGVGGGLVLNGKSITGHSYITG 153
Cdd:cd24060 85 IQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKfghgkgVENF------VTVITGTGIGGGIILNHELIHGSSFCAA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 154 EFGHIRLPVDALEvvgrdfpllrCGCGQLGCIENYLSGRGFAWLYEHFYQQPL---------SSPEIVAQ-----WQQHD 219
Cdd:cd24060 159 ELGHIVVSLDGPD----------CMCGSHGCVEAYASGMALQREAKKLHDEDLllvegmsvtNDEEVTAKhliqaAKLGN 228
|
250 260 270
....*....|....*....|....*....|....*...
gi 1460644637 220 PRAQAHVERYLDLLAVCLGNILTIVDPDLLVLGGGLSN 257
Cdd:cd24060 229 AKAQKILRTAGTALGLGIVNILHTLNPSLVILSGVLAS 266
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
60-253 |
4.71e-12 |
|
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: 65.38 E-value: 4.71e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 60 VGIGIPGMPETADGTLYAANVPAASGRPLRTDLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLV 139
Cdd:cd24071 65 IGIAVSGLVDSKKGIVIRSTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLV 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 140 LNGKSITGHSYITGEFGHIRLPVDalevvGRdfpllRCGCGQLGCIENYLSGRGFA-WLYEHFYQQPLS--------SPE 210
Cdd:cd24071 145 IDGKLYTGNFGGAGEIGHMTIQPD-----GR-----KCYCGQKGCLEAYASFEALVnEIKELTESYPLSllkeledfEIE 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 1460644637 211 IVAQW-QQHDPRAQAHVERYLDLLAVCLGNILTIVDPDLLVLGG 253
Cdd:cd24071 215 KVREAaEEGDSVATELFKKAGEYLGIGIKNLINIFNPEAIIIGG 258
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
26-257 |
5.12e-10 |
|
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: 59.09 E-value: 5.12e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 26 EKRVATPKSSYEDFLQAVEALVREADERFDQQG----SVGIGIPGMPETaDGTLYAANVpAASGRPLRTDLSARLGRDVR 101
Cdd:cd24077 27 SKQIKLLDISFENILEILKSIIQELISQAPKTPyglvGIGIGIHGIVDE-NEIIFTPYY-DLEDIDLKEKLEEKFNVPVY 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 102 LDNDANCFALSEawddeFTQYP----LVmglilgtgvggglvlngkSITGHSYIT-----------------GEFGH-IR 159
Cdd:cd24077 105 LENEANLSALAE-----RTFSEdydnLI------------------SISIHSGIGagiiinnqlyrgyngfaGEIGHmII 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 160 LPVdalevvGRdfpllRCGCGQLGCIENYLSGRGfawLYEHFYQQ----PLSSPEIVAQWQQHDPRAQAHVERYLDLLAV 235
Cdd:cd24077 162 VPN------GK-----PCPCGNKGCLEQYASEKA---LLKELSEKkgleTLTFDDLIQLYNEGDPEALELIDQFIKYLAI 227
|
250 260
....*....|....*....|..
gi 1460644637 236 CLGNILTIVDPDLLVLGGGLSN 257
Cdd:cd24077 228 GINNIINTFNPEIIIINSSLIN 249
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
4-114 |
2.16e-09 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 56.81 E-value: 2.16e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 4 GFDIGGSKIALGVFNQER-RLQWEK-RVATPK-SSYEDFLQAVEALVREaderFDQQGSVGIGIPGMpeTADG-TLYAAN 79
Cdd:cd24058 3 GIDIGGSGIKGAIVDTDTgELLSERiRIPTPQpATPEAVADVVAELVAH----FPWFGPVGVGFPGV--VRRGvVRTAAN 76
|
90 100 110
....*....|....*....|....*....|....*.
gi 1460644637 80 V-PAASGRPLRTDLSARLGRDVRLDNDANCFALSEA 114
Cdd:cd24058 77 LdKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEM 112
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
6-299 |
5.25e-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: 56.46 E-value: 5.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 6 DIGGSKIALGVFN---QERRLQWEKRVATpkSSYEDFLQAVEALVREADERfdQQGSVGIGIPGmPeTADGTLYAANVP- 81
Cdd:cd24008 5 DIGGTNARLALADagdGSGDLLFVRKYPS--ADFASLEDALAAFLAELGAP--RPKAACIAVAG-P-VDGGRVRLTNLDw 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 82 AASGRplrtDLSARLGRD-VRLDND--ANCFALSEAWDDEFTQYplvmglilgTGVGGGLVLNGKSIT------GHSYIT 152
Cdd:cd24008 79 SIDAA----ELRKALGIGrVRLLNDfeAAAYGLPALGPEDLLVL---------YGGGGPLPGGPRAVLgpgtglGVALLV 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 153 -----------GEFGHIRL-PVDALEvvgrdFPLLRCGCGQLG---CIENYLSGRGFAWLYEHFYQ------QPLSSPEI 211
Cdd:cd24008 146 pdgdggyvvlpSEGGHADFaPVTEEE-----AELLEFLRKRFGrsvSYEDVLSGPGLENIYEFLAKldgaepPDLTAEEI 220
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1460644637 212 VAQWQQHDPRAQAHVERYLDLLAVCLGNI-LTIVDPDLLVLGGGL--SNFTAISEGLAQRL----PRHLLPVARVPrIER 284
Cdd:cd24008 221 AEAALAGDPLAREALDLFARILGRFAGNLaLSFLATGGVYLAGGIapKNLDLLDSSAFREAfldkGRMSDLLEDIP-VYL 299
|
330
....*....|....*
gi 1460644637 285 ARHGDAgGMRGAAFL 299
Cdd:cd24008 300 VTNEDL-GLLGAAAY 313
|
|
| |
