|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
4-297 |
3.68e-124 |
|
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: 356.90 E-value: 3.68e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNANIQV 83
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEATLDAIADLVEEAEEELGAPATVGIGTPGSISPRTGLVKNANSTW 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 84 INGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHITLPg 163
Cdd:cd24066 82 LNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNPLP- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 164 YTEQEDGPSVSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATIVNVVD 243
Cdd:cd24066 161 WPDEDELPGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVINILD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446481236 244 PGVIVIGGGLSNVELLITDLNAEVAPLVFTDQFTTPIVKAQHGDSSGMRGAAWL 297
Cdd:cd24066 241 PDVIVLGGGLSNIDELYTEGPAALARYVFSDEVETPIVKNKHGDSSGVRGAAWL 294
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
4-297 |
2.99e-108 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 316.97 E-value: 2.99e-108
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNANIQV 83
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNANSTW 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 84 INGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHITLPG 163
Cdd:PRK09557 83 LNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGHNPLPW 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 164 YTEQE--DGPSVSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATIVNV 241
Cdd:PRK09557 163 MDEDElrYRNEVPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAHVINI 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 446481236 242 VDPGVIVIGGGLSNVELLITDLNAEVAPLVFTDQFTTPIVKAQHGDSSGMRGAAWL 297
Cdd:PRK09557 243 LDPDVIVLGGGMSNVDRLYPTLPALLKQYVFGGECETPVRKALHGDSSGVRGAAWL 298
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
1-297 |
1.19e-92 |
|
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: 277.19 E-value: 1.19e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 1 MHYlGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNAN 80
Cdd:cd24057 1 MYY-GFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAFLAAIAELVAEADARFGVKGPVGIGIPGVIDPEDGTLITAN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 81 IQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHIT 160
Cdd:cd24057 80 IPAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 161 LPGY--TEQEDGPSVSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATI 238
Cdd:cd24057 160 LPADalLLGYDLPVLRCGCGQTGCLETYLSGRGLERLYAHLYGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLANI 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 239 VNVVDPGVIVIGGGLSNVELLITDLNAEVAPLVFtDQFTTP-IVKAQHGDSSGMRGAAWL 297
Cdd:cd24057 240 LTALDPDVVVLGGGLSNFPALIAELPAALPAHLL-SGARTPrIVPARHGDAGGVRGAAFL 298
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-300 |
1.00e-89 |
|
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: 269.84 E-value: 1.00e-89
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 1 MHYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKS-TYQQFVSCVVALIEQIRRDVQRPMLT----GIALPGSISPLTGL 75
Cdd:COG1940 5 GYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGaGPEAVLEAIAELIEELLAEAGISRGRilgiGIGVPGPVDPETGV 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 76 IKNA-NIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAA 154
Cdd:COG1940 85 VLNApNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAG 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 155 ECGHITLpgyteQEDGPsvSCYCGKHNCVESFVSGSGFSERYQQMTG-NLLTSAAIVTLAQRGDACAMQQVARFRQQLAR 233
Cdd:COG1940 165 EIGHMPV-----DPDGP--LCGCGNRGCLETYASGPALLRRARELGGaEKLTAEELFAAARAGDPLALEVLDEAARYLGI 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446481236 234 TLATIVNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLVFTD-QFTTPIVKAQHGDSSGMRGAAWLAMR 300
Cdd:COG1940 238 GLANLINLLDPEVIVLGGGVSAAgDLLLEPIREALAKYALPPaREDPRIVPASLGDDAGLLGAAALALE 306
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
3-297 |
1.08e-77 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 239.12 E-value: 1.08e-77
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNANIQ 82
Cdd:PRK13310 2 YYGFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 83 VINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHITLP 162
Cdd:PRK13310 82 AASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHMRLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 163 -------GyteqEDGPSVSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTL 235
Cdd:PRK13310 162 vdaltllG----WDAPLRRCGCGQKGCIENYLSGRGFEWLYQHYYGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAICL 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446481236 236 ATIVNVVDPGVIVIGGGLSNVELLITDLNAEVAPLVFTDQFTTPIVKAQHGDSSGMRGAAWL 297
Cdd:PRK13310 238 GNILTIVDPHLVVLGGGLSNFDAIYEQLPKRLPRHLLPVARVPRIEKARHGDAGGVRGAAFL 299
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
4-298 |
6.28e-71 |
|
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: 221.44 E-value: 6.28e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQ-FVSCVVALIEQIRRDVQRPMLTGIALPGSISP-LTGLIKNANI 81
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEEtLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPkYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 82 QViNGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHITL 161
Cdd:pfam00480 81 GW-DNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 162 PGyteqeDGPsvSCYCGKHNCVESFVSGSGFSERYQQmTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATIVNV 241
Cdd:pfam00480 160 DP-----NGP--KCGCGNHGCLETIASGRALEKRYQQ-KGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLINL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 242 VDPGVIVIGGGLSNVELLITDLNAEVAPLVFtDQFTTP---IVKAQHGDSSGMRGAAWLA 298
Cdd:pfam00480 232 FDPQAIVLGGGVSNADGLLEAIRSLVKKYLN-GYLPVPpviIVAASLGDNAGALGAAALA 290
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
2-297 |
1.63e-67 |
|
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: 212.80 E-value: 1.63e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVscVVALIEQIRRDVQRPMLTGIAL--PGSISPLTGLIK-- 77
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAI--LERLLEIIAELKEKYDIEGIGIssAGQVDPKTGEVIya 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NANIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECG 157
Cdd:cd24068 79 TDNLPGWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 158 HITLpgyteqeDGPSVSCYCGKHNCVESFVSGSGFSERYQQMTG-NLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLA 236
Cdd:cd24068 159 HMVV-------DPGGRPCCCGGKGCLEQYASGTALVRRVAEALGePGIDGREIFDLADAGDPLAKEVVEEFAEDLATGLA 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446481236 237 TIVNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLVFTDQF-TTPIVKAQHGDSSGMRGAAWL 297
Cdd:cd24068 232 NLVHIFDPEVIVIGGGISAQgELFLEELREELRKLLMPPLLdATKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
4-297 |
9.42e-49 |
|
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: 162.63 E-value: 9.42e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKS-TYQQFVSCVVALIEQIRRD---VQRPMLTGIALPGSISPLTGLIKNA 79
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEeGPEAVLDRIAELIEELLAEagvRERILGIGIGVPGPVDPETGIVLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 80 -NIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGH 158
Cdd:cd23763 81 pNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 159 ITLpgyteqedgpsvscycgkhncvesfvsgsgfseryqqmtgnlltsaaivtlaqrgdacaMQQVARFrqqLARTLATI 238
Cdd:cd23763 161 ITV-----------------------------------------------------------LEEAARY---LGIGLANL 178
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446481236 239 VNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLVFTDQF-TTPIVKAQHGDSSGMRGAAWL 297
Cdd:cd23763 179 INLLNPELIVLGGGVAEAgDLLLEPIREAVRRRALPPLRrRVRIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
4-298 |
4.35e-45 |
|
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: 155.20 E-value: 4.35e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTyQQFVSCVVALIEQIRRdvQRPMLT-GIALPGSISPLTGLIKNA-NI 81
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTPPTA-DGIVDAIVEAVEELRE--GHDVSAvGVAAAGFVDADRATVLFApNI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 82 QViNGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHITL 161
Cdd:cd24061 79 AW-RNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRV 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 162 pgyteQEDGpsVSCYCGKHNCVESFVSGS---------------GFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVAR 226
Cdd:cd24061 158 -----VPDG--LLCGCGSRGCWEQYASGRalvryakeaanatpeGAAVLLADGSVDGITGKHISEAARAGDPVALDALRE 230
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446481236 227 FRQQLARTLATIVNVVDPGVIVIGGGLSNVELLITDLNAEV--APLVFTDQFTTP-IVKAQHGDSSGMRGAAWLA 298
Cdd:cd24061 231 LARWLGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAfeRWLPGRGWRPIPrLRTAQLGNDAGLIGAADLA 305
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
3-297 |
4.54e-45 |
|
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: 154.65 E-value: 4.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVqrpmlTGIA--LPGSISPLTGLIKN-A 79
Cdd:cd24152 2 YLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLEEFLDYIKKIIKRYDEEI-----DGIAisAPGVIDPETGIIYGgG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 80 NIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHI 159
Cdd:cd24152 77 ALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 160 TLPGYTEQEDGPSVSCycgkhncvesfvSGSGFSERYQQMTG-NLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATI 238
Cdd:cd24152 157 LTDDDDKDLLFFSGLA------------SMFGLVKRYNKAKGlEPLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIYNI 224
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446481236 239 VNVVDPGVIVIGGGLSNVELLITDLNAEVA---PLVFTDQFTTPIVKAQHGDSSGMRGAAWL 297
Cdd:cd24152 225 QYILDPEVIVIGGGISEQPLFIEDLKKEVNeilANRPGSIPKPEIKACKFGNDANLLGALYN 286
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
2-301 |
1.85e-44 |
|
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: 153.49 E-value: 1.85e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPT-----QKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLI 76
Cdd:cd24076 2 AVIGVELGVDYITVVVTDLAGEVLWRREVPLpasddPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 77 KNA-NIQVINgHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDY-DVVFgITLGTGCGGGIAIKQRPFIGAWGNAA 154
Cdd:cd24076 82 LLApNLGWRD-VPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVsDLVY-LSAGVGIGAGIILDGELYRGASGFAG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 155 ECGHITLpgyteQEDGPSvsCYCGKHNCVESFVSGSGFSERYQQM--TGNLLTSAAIVTLAQRGDACAMQQVARFRQQLA 232
Cdd:cd24076 160 EIGHMTV-----DPDGPP--CSCGNRGCWETYASERALLRAAGRLgaGGEPLSLAELVEAARAGDPAALAALEEVGEYLG 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446481236 233 RTLATIVNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLVF-TDQFTTPIVKAQHGDSSGMRGAAWLAMRN 301
Cdd:cd24076 233 IGLANLVNTFNPELVVLGGALAPLgPWLLPPLRAEVARRALpAPARDVRIVVSRLGEDAAALGAAALAIDH 303
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
4-295 |
8.43e-42 |
|
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: 145.94 E-value: 8.43e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDahGWEI-RRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNA-NI 81
Cdd:cd24065 3 IGLDLGGTKIAAGVVD--GGRIlSRLVVPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGRVRFApNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 82 QVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHIT- 160
Cdd:cd24065 81 PGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHTTv 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 161 LPGyteqedGPsvSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATIVN 240
Cdd:cd24065 161 LPG------GP--MCGCGLVGCLEALASGRALARDASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGLANLQK 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446481236 241 VVDPGVIVIGGGLSNVELLITDLNAEVAPLVFTDQFTTPIVKAQHGDSSGMRGAA 295
Cdd:cd24065 233 ALDPEVFVLGGGVAQVGDYYLLPVQEAARRYTEGWHAPPLRLAHLGTDAGVIGAA 287
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
4-298 |
1.51e-38 |
|
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: 138.49 E-value: 1.51e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKS---TYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNAN 80
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTpetIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYFAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 81 IQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHIT 160
Cdd:TIGR00744 81 NLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHIR 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 161 LpgyteQEDGpSVSCYCGKHNCVESFVSGSG---FSERY-----------QQMTGNLLTSAAIVTLAQRGDACAMQQVAR 226
Cdd:TIGR00744 161 M-----VPDG-RLLCNCGKQGCIETYASATGlvrYAKRAnakperaevllALGDGDGISAKHVFVAARQGDPVAVDSYRE 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446481236 227 FRQQLARTLATIVNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLVFT-DQFTTPIVKAQHGDSSGMRGAAWLA 298
Cdd:TIGR00744 235 VARWAGAGLADLASLFNPSAIVLGGGLSDAgDLLLDPIRKSYKRWLFGgARQVADIIAAQLGNDAGLVGAADLA 308
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
3-297 |
9.63e-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: 135.88 E-value: 9.63e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKST-----YQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIK 77
Cdd:cd24062 2 IVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEggeniITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NANIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECG 157
Cdd:cd24062 82 VAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 158 HITLpgytEQEDGpsVSCYCGKHNCVESFVSGSGF---------------SERYQQMTGNlLTSAAIVTLAQRGDACAMQ 222
Cdd:cd24062 162 HITV----NPEGG--APCNCGKTGCLETVASATGIvriareeleegkgssALRILALGGE-LTAKDVFEAAKAGDELALA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446481236 223 QVARFRQQLARTLATIVNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLVF-TDQFTTPIVKAQHGDSSGMRGAAWL 297
Cdd:cd24062 235 VVDTVARYLGLALANLANTLNPEKIVIGGGVSAAgEFLLSPVKEYFDRFTFpRVRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-298 |
1.56e-37 |
|
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: 134.98 E-value: 1.56e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQ-FVSCVVALIEQ-IRRDVQRPMLTGIALPGSISP-LTGLIKNA 79
Cdd:cd24070 3 VLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGdPVEVLADLIREyIEEAGLKPAAIVIGVPGTVDKdRRTVISTP 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 80 NIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHI 159
Cdd:cd24070 83 NIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHI 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 160 TLPGYTEQedgpsvsCYCGKHNCVESFVSGSGFsERYQQMTGNlltSAAIVTLAQR-GDAcamQQVARFRQQLARTLATI 238
Cdd:cd24070 163 PVYGNGKP-------CGCGNTGCLETYASGRAL-EEIAEEHYP---DTPILDIFVDhGDE---PELDEFVEDLALAIATE 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446481236 239 VNVVDPGVIVIGGGLSNV-----ELLITDLNaEVAPLVFTDQfTTPIVKAQHGDSSGMRGAAWLA 298
Cdd:cd24070 229 INILDPDAVILGGGVIDMkgfprETLEEYIR-KHLRKPYPAD-NLKIIYAELGPEAGVIGAAIYA 291
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
3-242 |
1.39e-36 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 131.69 E-value: 1.39e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPMLTGIALPGSISPLTGLIKNANIQ 82
Cdd:PRK13311 2 YYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVFTANVP 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 83 VINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHITLP 162
Cdd:PRK13311 82 SAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRLP 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 163 GYTEQ---EDGPSVSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATIV 239
Cdd:PRK13311 162 VDALDilgADIPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAHYAAGEPKAVAHVERFMDVLAVCLGNLL 241
|
...
gi 446481236 240 NVV 242
Cdd:PRK13311 242 TML 244
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
3-297 |
4.67e-36 |
|
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: 131.69 E-value: 4.67e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQ-QFVSCVVALIEQIRRDVQRPMLTGIALpGSISPL---TGLIKN 78
Cdd:cd24063 2 YVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPgTVSEQVLGLIETLLSKAGKDSIEGIGV-SSAGPLdlrKGTIVN 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 79 ANIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGH 158
Cdd:cd24063 81 SPNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 159 ItlpgYTEQEDGPsvSCYCGKHNCVESFVSGSG-------FSERYQQMT--------GNLLTSAAIVTLAQRGDACAMQQ 223
Cdd:cd24063 161 L----VVDTESGL--KCGCGGYGHWEAFASGRGiprfareWAEGFSSRTslklrnpgGEGITAKEVFSAARKGDPLALKI 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446481236 224 VARFRQQLARTLATIVNVVDPGVIVIGGGLSNVELLItdLNAEVAPLVFTDQFTTP--IVKAQHGDSSGMRGAAWL 297
Cdd:cd24063 235 IEKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDI--LDPLIEYLEKNPAISKGpeIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
2-300 |
7.48e-36 |
|
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: 130.75 E-value: 7.48e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRDVQRPM--LTGI--ALPGSISPLTGLIK 77
Cdd:cd24073 2 YVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPdrLLGIgvGLPGLVDAETGICR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NANIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECG 157
Cdd:cd24073 82 WSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 158 HITLpgyteQEDGPsvSCYCGKHNCVESFVSGSGFSERYQQMTG--NLLTSAAIVTLAQRGDACAMQQVARFRQQLARTL 235
Cdd:cd24073 162 HTTV-----DPDGP--PCRCGKRGCLEAYASDPAILRQAREAGLrgEPLTIEDLLAAARAGDPAARAILRRAGRALGLAL 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446481236 236 ATIVNVVDPGVIVIGG-GLSNVELLITDLNAEVAPLVF-TDQFTTPIVKAQHGDSSGMRGAAWLAMR 300
Cdd:cd24073 235 ANLVNLLDPELIIISGeGVRAGDLLFEPMREALRAHVFpGLASDLELVIHPWGDEAWARGAAALALQ 301
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
4-297 |
1.84e-35 |
|
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: 129.33 E-value: 1.84e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDaHGWEIRRYRCPTQKS-TYQQFVSCVVALIEQIRRDVQRPML--TGIALPGSISPLTglikNAN 80
Cdd:cd24069 1 LAIDIGGTKIAAALIG-NGQIIDRRQIPTPRSgTPEALADALASLLADYQGQFDRVAVasTGIIRDGVLTALN----PKN 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 81 IQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAG-QDYDVVFgITLGTGCGGGIAIKQRPFIGAWGNAAECGHI 159
Cdd:cd24069 76 LGGLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGeGVGNLVF-ITVSTGVGGGLVLNGQLLTGPNGLAGHIGHT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 160 tlpgyteQEDGPSVSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAAIVTLAQRGDACAMQQVARFRQQLARTLATIV 239
Cdd:cd24069 155 -------LADPPGPVCGCGRRGCVEAIASGTAIAAAASEILGEPVDAKDVFERARSGDEEAARLIDRAARALADLIADLK 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446481236 240 NVVDPGVIVIGG--GLSN--VELLITDLNAEVAplvftdQFTTPIVKAQHGDSSGMRGAAWL 297
Cdd:cd24069 228 ATLDLDCVVIGGsvGLAEgfLERVEQYLADEPA------IFRVSLEPARLGQDAGLLGAALL 283
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
4-301 |
4.47e-33 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 123.55 E-value: 4.47e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALI-EQIRRDVQRPMLTGIALPGSIS-PLTGLIKNANI 81
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIdEYLRRFNARCHGIVMGFPALVSkDRRTVISTPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 82 QVI--NGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDyDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHI 159
Cdd:PRK09698 87 PLTalDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQ-QLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGHI 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 160 TLPGYTEQedgpsvsCYCGKHNCVESFVSGSGFSERYQQMTGNlltsAAIVTLAQR-GDACAMQQvarFRQQLARTLATI 238
Cdd:PRK09698 166 PLGDMTQH-------CGCGNPGCLETNCSGMALRRWYEQQPRD----YPLSDLFVHaGDHPFIQS---LLENLARAIATS 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446481236 239 VNVVDPGVIVIGGG-LSNVELLITDLNAEV-----APLVFTDqftTPIVKAQHGDSSGMRGAAWLAMRN 301
Cdd:PRK09698 232 INLFDPDAIILGGGvMDMPAFPRETLIAMIqkylrKPLPYEV---VRFIYASSSDFNGAQGAAILAHQR 297
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
2-299 |
1.06e-31 |
|
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: 120.00 E-value: 1.06e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPT-QKSTYQQFVSCVVALIEQIRR--DVQRPMLT-GIALPGSISPLTGLIK 77
Cdd:cd24059 2 YVIGVEIGRDLLSAVLCDLSGNILAREKYPLdEKENPEEVLEKLYELIDRLLEkeNIKSKILGiGIGAPGPLDVEKGIIL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NA----NIQVINghaLQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNA 153
Cdd:cd24059 82 NPpnfpGWENIP---LVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYA 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 154 AECGHITLpgyteQEDGPsvSCYCGKHNCVESFVSGSGFSERYQQMTGNLL-TSAAIVTLAQRGDACAMQQVARFRQQLA 232
Cdd:cd24059 159 GEIGHTSI-----DINGP--RCSCGNRGCLELYASIPAIEKKARSALGSGRsFQLDIVEALQKGDPIADEVIEEAAKYLG 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446481236 233 RTLATIVNVVDPGVIVIGGGLSNV-ELLITDLNAEV-APLVFTDQFTTPIVKAQHGDSSGMRGAAWLAM 299
Cdd:cd24059 232 IGLVNLINLLNPEAIIIGGELIYLgERYLEPIEKEVnSRLFGRNAREVRILKSSLGEDAPLLGAAALVL 300
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
4-295 |
2.21e-30 |
|
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: 116.44 E-value: 2.21e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQksTYQQFVScVVALIEQIRRDVQRPM---LTGIALPGSISPLTGLIK-NA 79
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTK--VENGKED-VINRIAETVNELIEEMellGIGIGSPGSIDRENGIVRfSP 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 80 NIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECGHI 159
Cdd:cd24064 79 NFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 160 TLpgyteQEDGPsvSCYCGKHNCVESFVSGSGFS----ERYQQMTGNLLT------SAAIVTLAQRGDACAMQQVARFRQ 229
Cdd:cd24064 159 IV-----EPNGP--ICGCGNRGCVEAFASATAIIryarESRKRYPDSLAGesekinAKHVFDAARKNDPLATMVFRRVVD 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 230 QLARTLATIVNVVDPGVIVIGGGLSNV-ELLITDLNAEVAPLV---FTDQFTtpIVKAQHGDSSGMRGAA 295
Cdd:cd24064 232 ALAIAIGGFVHIFNPEIIIIGGGISRAgSFLLDPIREKTKKYVmlsFQDTYS--IELSNLVEDAGILGAA 299
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
2-301 |
1.66e-29 |
|
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily includes a group of uncharacterized proteins similar to Listeria monocytogenes Lmo0178 protein, which is a predicted transcription repressor belonging to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466921 [Multi-domain] Cd Length: 312 Bit Score: 114.30 E-value: 1.66e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKST-YQQFVSCVVALIEQI---RRDVQRPMLTGIALPGSISPLTGLIK 77
Cdd:cd24071 2 YIIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETdPEKVIELIAENIKKLiknKHVEKKLLGIGIAVSGLVDSKKGIVI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NANIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECG 157
Cdd:cd24071 82 RSTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 158 HITLpgyteQEDGPsvSCYCGKHNCVESFVSGSGFSERYQQMTGNLLTSAA----------IVTLAQRGDACAMQQVARF 227
Cdd:cd24071 162 HMTI-----QPDGR--KCYCGQKGCLEAYASFEALVNEIKELTESYPLSLLkeledfeiekVREAAEEGDSVATELFKKA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 446481236 228 RQQLARTLATIVNVVDPGVIVIGG-GLSNVELLITDLNAEVAPLVFTDQ-FTTPIVKAQHGDSSGMRGAAWLAMRN 301
Cdd:cd24071 235 GEYLGIGIKNLINIFNPEAIIIGGeGLEFKDYFLPKIIEIAKENFFGKAgRNVIILVDSLGEDAWVLGAALLVIDH 310
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
1-298 |
1.91e-29 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 113.47 E-value: 1.91e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 1 MHYLGLDIGGTKIAAVVMDAHGWEIRRYRCPT-QKSTYQQFVSCVVALIEQIRRDVQRpmlTGIAlpgsispLTGLIKNA 79
Cdd:PRK05082 1 MTTLAIDIGGTKIAAALVGEDGQIRQRRQIPTpASQTPEALRQALSALVSPLQAQADR---VAVA-------STGIINDG 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 80 NIQVINGH--------ALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFgITLGTGCGGGIAIKQRPFIGAWG 151
Cdd:PRK05082 71 ILTALNPHnlggllhfPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVF-ITVSTGVGGGIVLNGKLLTGPGG 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 152 NAAECGHiTLPGYTeqedGPsvSCYCGKHNCVESFVSGSGFSERYQQMTGNlLTSAAIVTLAQRGDACAMQQVARFRQQL 231
Cdd:PRK05082 150 LAGHIGH-TLADPH----GP--VCGCGRRGCVEAIASGRAIAAAAQGWLAG-CDAKTIFERAGQGDEQAQALINRSAQAI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446481236 232 ARTLATIVNVVDPGVIVIGG--GLSN--VELLITDLNAEvaPLVftdqFTTPIVKAQHGDSSGMRGAAWLA 298
Cdd:PRK05082 222 ARLIADLKATLDCQCVVLGGsvGLAEgyLELVQAYLAQE--PAI----YHVPLLAAHYRHDAGLLGAALWA 286
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
4-256 |
3.62e-25 |
|
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: 102.49 E-value: 3.62e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKsTYQQFVS-----CVVALIEQIRRDVqRPMLTGIALPGSISPLTGLIKN 78
Cdd:cd24060 3 LAVDLGGTNLRVAIVSMKGEIVKKYTQPNPK-TYEERIDlilqmCVEAASEAVKLNC-RILGVGISTGGRVNPREGIVLH 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 79 AN--IQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAEC 156
Cdd:cd24060 81 STklIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAEL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 157 GHITLpgyteQEDGPsvSCYCGKHNCVESFVSGSGFSERYQ--------QMTGNLLTSAAIVT------LAQRGDACAMQ 222
Cdd:cd24060 161 GHIVV-----SLDGP--DCMCGSHGCVEAYASGMALQREAKklhdedllLVEGMSVTNDEEVTakhliqAAKLGNAKAQK 233
|
250 260 270
....*....|....*....|....*....|....
gi 446481236 223 QVARFRQQLARTLATIVNVVDPGVIVIGGGLSNV 256
Cdd:cd24060 234 ILRTAGTALGLGIVNILHTLNPSLVILSGVLASH 267
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
2-256 |
2.08e-24 |
|
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: 100.46 E-value: 2.08e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQ--IRRDVQRPMLTGIA--LPGSISPLTGLIK 77
Cdd:cd24074 3 QFLSIRIGRGYITLALRDLNGRLLAEERYPLPAKDNDPFLDRLLESISEffSRHQKKLERLTAIAitLPGIIDPESGIVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NANIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGNAAECG 157
Cdd:cd24074 83 RLPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 158 HITLPGYTEQedgpsvsCYCGKHNCVESFVSGSGFSERYQQMTGNL---------LTSAAIVTLAQRGDACAMQQVARFR 228
Cdd:cd24074 163 HTQIDPYGKR-------CYCGNHGCLETVASIPAILEQANQLLEQSpdsmlhgqpISIESLCQAALAGDPLAQDIIIQVG 235
|
250 260
....*....|....*....|....*...
gi 446481236 229 QQLARTLATIVNVVDPGVIVIGGGLSNV 256
Cdd:cd24074 236 RHLGRILAILVNLFNPEKILIGSPLNNA 263
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
2-251 |
9.65e-24 |
|
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: 98.59 E-value: 9.65e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQI----RRDVQRPMLTGIALPGSISPLTGLIK 77
Cdd:cd24075 2 HILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQLIEEIAQFlkshRRKTQRLIAISITLPGLINPKTGVVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 -NANIQViNGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQD-YDVVFgITLGTGCGGGIAIKQRPFIGAWGNAAE 155
Cdd:cd24075 82 yMPHIQV-KSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDcKDSIL-VRIHHGIGAGIIIDGKLFLGQNGNAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 156 CGHITLPGYTEQedgpsvsCYCGKHNCVESFVSGSGFSERYQ---------QMTGNLLTSAAIVTLAQRGDACAMQQVAR 226
Cdd:cd24075 160 IGHIQIEPLGER-------CHCGNFGCLETVASNAAIEQRVKkllkqgyasQLTLQDCTIKDICQAALNGDQLAQDVIKR 232
|
250 260
....*....|....*....|....*
gi 446481236 227 FRQQLARTLATIVNVVDPGVIVIGG 251
Cdd:cd24075 233 AGRYLGKVIAILINLLNPQKIIIAG 257
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
2-255 |
2.81e-19 |
|
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: 86.06 E-value: 2.81e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRRdvQRPM----LTGIALpgSISpltGLIK 77
Cdd:cd24077 2 YSIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELIS--QAPKtpygLVGIGI--GIH---GIVD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 78 NANIQV-----INGHALQADLQQLLGQPVVIANDGNCFALSEACdgAGQDYDVVFGITLGTGCGGGIAIKQRPFIGAWGN 152
Cdd:cd24077 75 ENEIIFtpyydLEDIDLKEKLEEKFNVPVYLENEANLSALAERT--FSEDYDNLISISIHSGIGAGIIINNQLYRGYNGF 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 153 AAECGHITLpgyteQEDGpsVSCYCGKHNCVESFVSGSGFSERYQQMTGN-LLTSAAIVTLAQRGDACAMQQVARFRQQL 231
Cdd:cd24077 153 AGEIGHMII-----VPNG--KPCPCGNKGCLEQYASEKALLKELSEKKGLeTLTFDDLIQLYNEGDPEALELIDQFIKYL 225
|
250 260
....*....|....*....|....
gi 446481236 232 ARTLATIVNVVDPGVIVIGGGLSN 255
Cdd:cd24077 226 AIGINNIINTFNPEIIIINSSLIN 249
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
2-273 |
3.40e-19 |
|
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: 85.93 E-value: 3.40e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 2 HYLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQK-STYQQFVSCVVALIEQIRRDVQRPMLT-GIALPGSISPLTGLIKNA 79
Cdd:cd24072 2 WVLGIVVSPNSLRAQVGNACGELLGEFEYRVITlETPEALIDEIIDCIDRLLKLWKDRVKGiALAIQGLVDSHKGVSLWS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 80 NIQVINGHALQADLQQLLGQPVVIANDGNCFALSEACDG--AGQDYDVVfgITLGTGCGGGIAIKQRPFIGAWGNAAECG 157
Cdd:cd24072 82 PGAPWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGelRQSRDFCV--INLDYGIGSAIVIDNKLYIGASSGSGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 158 HitlpgYTEQEDGpsVSCYCGKHNCVESFVSGSGF---------SERYQQMTGNLLTsAAIVTLAQRGDACAMQQVARFR 228
Cdd:cd24072 160 H-----TKVNPDG--ARCDCGRRGCLETVASNSALkrnarvtlkLGPVSADPEKLTM-EQLIEALEEGEPIATQIFDRAA 231
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 446481236 229 QQLARTLATIVNVVDPG-VIVIGGGLSNVELLITDLNAEVAPLVFT 273
Cdd:cd24072 232 NAIGRSLANILNLLNPEqVLLYGRGCRAGDLLLPAIRRAIAENPFS 277
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
3-297 |
3.80e-17 |
|
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: 79.90 E-value: 3.80e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTqkSTYQQFVSCVVALIEQIRRDVQRpmlTGIALPGSI-----SPLTGLI- 76
Cdd:cd24067 1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPT--TTPEETLQAVIDFFREQEEPIDA---IGIASFGPIdlnptSPTYGYIt 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 77 -------KNANIqvinghaLQAdLQQLLGQPVVIANDGNCFALSEACDGAGQDYDVVFGITLGTGCGGGIAIKQRPFIGA 149
Cdd:cd24067 76 ttpkpgwRNFDI-------LGA-LKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 150 wgNAAECGHITLPgyTEQEDGPSVSCyCGKH-NCVESFVSGSGFSERYQQMTGNLLTSAAIVTLaqrgdacamqqVARFr 228
Cdd:cd24067 148 --LHPEMGHIRVP--RHPDDDGFPGV-CPFHgDCLEGLASGPAIAARWGIPAEELPDDHPAWDL-----------EAYY- 210
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446481236 229 qqLARTLATIVNVVDPGVIVIGGGLSNVELLITDLNAEVAPL----VFTDQFTTP----IVKAQHGDSSGMRGAAWL 297
Cdd:cd24067 211 --LAQACANLTLTLSPERIVLGGGVMQRPGLFPRIREKFRKLlngyLEVPRLLPDideyIVPPALGNDAGILGALAL 285
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
4-298 |
2.20e-13 |
|
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK (EC 2.7.1.63/EC 2.7.1.2), also called poly(P)/ATP-glucomannokinase (GMK), poly(P) glucokinase, ATP-dependent glucokinase, or polyphosphate--glucose phosphotransferase, catalyzes the phosphorylation of glucose using polyphosphate or ATP as the phosphoryl donor. Polyphosphate, rather than ATP, seems to be the major phosphate donor for the enzyme in Mycobacterium tuberculosis. GTP, UTP and CTP can replace ATP as phosphoryl donor. PPGK belongs to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities. Members of this family lack the cysteine-rich zinc-binding motif, which presents in other ROK families.
Pssm-ID: 466908 [Multi-domain] Cd Length: 239 Bit Score: 68.36 E-value: 2.20e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIR--RYRCPT-QKSTYQQFVSCVVALIEQIRRD--VqrpmltGIALPGSIspLTGLIKN 78
Cdd:cd24058 2 LGIDIGGSGIKGAIVDTDTGELLseRIRIPTpQPATPEAVADVVAELVAHFPWFgpV------GVGFPGVV--RRGVVRT 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 79 A-NI--QVInGHALQADLQQLLGQPVVIANDGNCFALSEACDGAGQDYD-VVFGITLGTGCGGGIAIKQRPFIGawgnaA 154
Cdd:cd24058 74 AaNLdkSWI-GFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKgVVLVLTLGTGIGSALFVDGHLVPN-----T 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 155 ECGHITLPGyteqedgpsvscycgkhncvesfvsgsGFSERYqqmtgnllTSAAIVTLAQRGDacamqqvARFRQQLART 234
Cdd:cd24058 148 ELGHLEIRG---------------------------KDAEER--------ASLGVRAREDLGW-------KRWAKRVNKY 185
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446481236 235 LATIVNVVDPGVIVIGGGLSnvellitdlnAEVAPLVFTDQFTTPIVKAQHGDSSGMRGAAWLA 298
Cdd:cd24058 186 LQYLERLFNPDLFIIGGGNS----------KKADKFLPLLDVKTPVVPAVLRNDAGIVGAALLA 239
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
3-259 |
4.79e-10 |
|
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: 59.54 E-value: 4.79e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWE-----IRRYRCptqkSTYQQFVscvvALIEQIRRDVQRPMLTG--IALPGSISPLTGL 75
Cdd:cd24008 1 ILVGDIGGTNARLALADAGDGSgdllfVRKYPS----ADFASLE----DALAAFLAELGAPRPKAacIAVAGPVDGGRVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 76 IKNANiQVINGHALQadlQQLLGQPVVIAND--GNCFALSEACDGAGQDYD-----------VVFGItlGTGCGGGIAIK 142
Cdd:cd24008 73 LTNLD-WSIDAAELR---KALGIGRVRLLNDfeAAAYGLPALGPEDLLVLYggggplpggprAVLGP--GTGLGVALLVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 143 QRPFiGAWGNAAECGHITLPGYTEQEDgpSVSCYCGKHN----CVESFVSGSGFSERYQQMTG------NLLTSAAIVTL 212
Cdd:cd24008 147 DGDG-GYVVLPSEGGHADFAPVTEEEA--ELLEFLRKRFgrsvSYEDVLSGPGLENIYEFLAKldgaepPDLTAEEIAEA 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 446481236 213 AQRGDACAMQQVARFRQQLARTLATIV-NVVDPGVIVIGGGL--SNVELL 259
Cdd:cd24008 224 ALAGDPLAREALDLFARILGRFAGNLAlSFLATGGVYLAGGIapKNLDLL 273
|
|
| Glk |
COG0837 |
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway ... |
1-253 |
1.10e-05 |
|
Glucokinase [Carbohydrate transport and metabolism]; Glucokinase is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440599 Cd Length: 320 Bit Score: 46.26 E-value: 1.10e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 1 MHYLGLDIGGTKIA-AVVMDAHGW---EIRRYRCptqkstyQQFVScVVALIEQIRRDVQRPMLTG--IALPGSIspLTG 74
Cdd:COG0837 5 TPILVADIGGTNARlALAEGGGGLellEIRRYPS-------ADYAS-LEDALRAYLAELGLPRPRAacLAVAGPV--DGD 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 75 LIKNANIQ-VINGHALQADLQqllGQPVVIANDgncFA--------LSEA-----CDGAGQDYDVVFGITLGTGCGGGIA 140
Cdd:COG0837 75 RVKLTNLPwSISAAALRAALG---LERVLLIND---FEalayalpaLSPDdlvqlGGGEPDPGGPRAVIGPGTGLGVAGL 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 141 IKQ----RPFigawgnAAECGHITLPGYTEQEDgpSVSCYCGK---HNCVESFVSGSGFSERYQQMTGN------LLTSA 207
Cdd:COG0837 149 VPDgggwIVL------PSEGGHVDFAPRDEREL--ELLRYLRRrygHVSAERVLSGPGLVNLYRALAALdgappaPLSPA 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 446481236 208 AIVTLAQRG-DACAMQQVARFRQQLAR--------TLATivnvvdpGVIVIGGGL 253
Cdd:COG0837 221 EITAAALAGsDPLAVEALELFCRILGRvagnlaltLGAR-------GGVYLAGGI 268
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-67 |
1.51e-03 |
|
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli L-xylulose/3-keto-L-gulonate kinase (EcLyxK; EC 2.7.1.-/EC 2.7.1.53), Pasteurella multocida L-xylulose kinase (PmLyX, also known as L-xylulokinase; EC 2.7.1.53), and Brucella abortus erythritol kinase (BaEryA; EC 2.7.1.215). EcLyxK catalyzes the phosphorylation of L-xylulose and 3-keto-L-gulonate. It is involved in L-lyxose utilization via xylulose and may also be involved in the utilization of 2,3-diketo-L-gulonate. PmLyX catalyzes the phosphorylation of L-xylulose only. BaEryA catalyzes the phosphorylation of erythritol to D-erythritol-1-phosphate. Members of this subfamily belong to the FGGY family of carbohydrate kinases, the monomers of which contain two large domains, which are separated by a deep cleft that forms the active site. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466805 [Multi-domain] Cd Length: 444 Bit Score: 39.84 E-value: 1.51e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQF-------------VSCVVALIEQIRRDVQRpmLTGIALPG 67
Cdd:cd07802 2 LLGIDNGTTNVKAVLFDLDGREIAVASRPTPVISPRPGwaerdmdelwqatAEAIRELLEKSGVDPSD--IAGVGVTG 77
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
3-301 |
1.62e-03 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 39.48 E-value: 1.62e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 3 YLGLDIGGTKIAAVVMDAHGWEIRRYRCPT---QKSTYQQFVSCVVALIEQIRRDVQRP-MLTGIALpGsispLTGLIKN 78
Cdd:COG2971 3 ILGVDGGGTKTRAVLVDADGEVLGRGRAGGanpQSVGLEEALASLREALEEALAAAGDPaDIEAVGF-G----LAGAGTP 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 79 ANIQVIngHALQADLqqLLGQPVVIANDGNCfalseACDGAGQDYDVVFGItLGTG-CGGGIAIKQR--------PFIGA 149
Cdd:COG2971 78 EDAEAL--EAALREL--FPFARVVVVNDALA-----ALAGALGGEDGIVVI-AGTGsIAAGRDGDGRtarvggwgYLLGD 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 150 WGNAAECGHITLPGYTEQEDGpsvscyCGKH----NCVESFVSGSGFSERYQQMTGNLLTSAAI-------VTLAQRGDA 218
Cdd:COG2971 148 EGSGAWLGREALRAALRALDG------RGPPtaltEAVLAEFGLDDPEELIAWVYRGPAPPADLaslaplvFEAAEAGDP 221
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 219 CAMQQVARFRQQLARTLATIVNVVDPGVIVIGGGLSNVELLITDLNAEVAplvftdQFTTPIVKAQHgdsSGMRGAAWLA 298
Cdd:COG2971 222 VARAILEEAADELAELARALLERGALPVVLAGGVAAAQPLLREALRARLA------AGGAEIVPPAG---DPVDGALLLA 292
|
...
gi 446481236 299 MRN 301
Cdd:COG2971 293 LRL 295
|
|
| DEDD_Tnp_IS110 |
pfam01548 |
Transposase; Transposase proteins are necessary for efficient DNA transposition. This family ... |
4-86 |
6.46e-03 |
|
Transposase; Transposase proteins are necessary for efficient DNA transposition. This family includes an amino-terminal region of the pilin gene inverting protein (PIVML) and of members of the IS111A/IS1328/IS1533 family of transposases. The C-terminus is represented by family pfam02371.
Pssm-ID: 460249 Cd Length: 155 Bit Score: 36.44 E-value: 6.46e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446481236 4 LGLDIGGTKIAAVVMDAHGWEIRRYRCPTQKSTYQQFVSCVVALIEQIRrdvqrpmlTGIALPGSIS-PLTGLIKNANIQ 82
Cdd:pfam01548 1 VGIDVAKKHHHACVIDPDGKVLLSRRFPNDEEGLRALLAKLLASAGEVL--------VGVEATGHYGaLLVAFLLAAGFQ 72
|
....*.
gi 446481236 83 V--ING 86
Cdd:pfam01548 73 VvyVNP 78
|
|
| |
