|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-312 |
2.81e-94 |
|
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: 281.40 E-value: 2.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 1 MKYYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNG 80
Cdd:COG1940 4 AGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPETG 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 81 IISYSNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTA-NGHNASSYilitlgtgigggA------------VI 146
Cdd:COG1940 84 VVLNAPNLPgWRGVPLAELLEERLGLPVFVENDANAAALAEAWFgAGRGADNV------------VyltlgtgigggiVI 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 147 NSKIYRGFNGVGIEPGHMTLINGGERCTCGKHGCWETYGSVTALINqtklkmtdnpdslMHKISGKFGEVNGRVAFEAAK 226
Cdd:COG1940 152 NGKLLRGANGNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLR-------------RARELGGAEKLTAEELFAAAR 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 227 AGDRAGLEVVEKYTEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGII 306
Cdd:COG1940 219 AGDPLALEVLDEAARYLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLL 298
|
....*.
gi 1052835205 307 GAALSA 312
Cdd:COG1940 299 GAAALA 304
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
3-309 |
5.64e-76 |
|
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: 235.26 E-value: 5.64e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGE-YTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:cd24062 81 EVAVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEmWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTLI-NGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLMHKISGKFGEVNGRVAFEAAKAGDRAGLEVVEKYT 240
Cdd:cd24062 161 GHITVNpEGGAPCNCGKTGCLETVASATGIVRIAREELEEGKGSSALRILALGGELTAKDVFEAAKAGDELALAVVDTVA 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 241 EYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAA 309
Cdd:cd24062 241 RYLGLALANLANTLNPEKIVIGGGVSAAGEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAA 309
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
5-312 |
1.66e-72 |
|
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: 226.08 E-value: 1.66e-72
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTlnTRPIEAIMLDMTKLCKTLLDKsqmdiNKIEAVGIGCPGTVDNKNGIISY 84
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPT--PPTADGIVDAIVEAVEELREG-----HDVSAVGVAAAGFVDADRATVLF 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYT-ANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPGH 163
Cdd:cd24061 75 APNIAWRNEPLKDLLEARIGLPVVIENDANAAAWAEYRfGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGH 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 164 MTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLMHKIS-GKFGEVNGRVAFEAAKAGDRAGLEVVEKYTEY 242
Cdd:cd24061 155 IRVVPDGLLCGCGSRGCWEQYASGRALVRYAKEAANATPEGAAVLLAdGSVDGITGKHISEAARAGDPVALDALRELARW 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052835205 243 VADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNK-YRPKTKIEIASLNNDAGIIGAALSA 312
Cdd:cd24061 235 LGAGLASLAALLDPELFVIGGGVSDAGDLLLDPIREAFERWLPGRgWRPIPRLRTAQLGNDAGLIGAADLA 305
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-310 |
5.92e-71 |
|
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: 221.66 E-value: 5.92e-71
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSqmdinKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24068 1 KILGIDIGGTKIKYGLVDADGEILEKDSVPTPASKGGDAILERLLEIIAELKEKY-----DIEGIGISSAGQVDPKTGEV 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSN-NIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTA-NGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGI 159
Cdd:cd24068 76 IYATdNLPgWTGTNLKEELEERFGLPVAVENDVNCAALAEKWLgAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAG 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 160 EPGHMTLINGGERCTCGKHGCWETYGSVTALInqtklkmtdnpdslmHKISGKFGE--VNGRVAFEAAKAGDRAGLEVVE 237
Cdd:cd24068 156 ELGHMVVDPGGRPCCCGGKGCLEQYASGTALV---------------RRVAEALGEpgIDGREIFDLADAGDPLAKEVVE 220
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052835205 238 KYTEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAAL 310
Cdd:cd24068 221 EFAEDLATGLANLVHIFDPEVIVIGGGISAQGELFLEELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAY 293
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
5-309 |
1.39e-63 |
|
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: 203.11 E-value: 1.39e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQmdinkIEAVGIGCPGTVDNKNGIISY 84
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENGKEDVINRIAETVNELIEEME-----LLGIGIGSPGSIDRENGIVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTANGHNASSYILITLGTGIGGGAVI-NSKIYRGFNGVGIEPG 162
Cdd:cd24064 77 SPNFPdWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVIcHGQLLTGYDGIAAELG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 163 HMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLmhkiSGKFGEVNGRVAFEAAKAGDRAGLEVVEKYTEY 242
Cdd:cd24064 157 HVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRYPDSL----AGESEKINAKHVFDAARKNDPLATMVFRRVVDA 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052835205 243 VADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAA 309
Cdd:cd24064 233 LAIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVEDAGILGAA 299
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
5-309 |
2.03e-62 |
|
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: 200.51 E-value: 2.03e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRpiEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGIISY 84
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTP--ETIVDAIASAVDSFIQHIAKVGHEIVAIGIGAPGPVNRQRGTVYF 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEY-TANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPGH 163
Cdd:TIGR00744 79 AVNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYkKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGH 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 164 MTLI-NGGERCTCGKHGCWETYGSVTALINQTKLKMT--DNPDSLMHKISGKfgEVNGRVAFEAAKAGDRAGLEVVEKYT 240
Cdd:TIGR00744 159 IRMVpDGRLLCNCGKQGCIETYASATGLVRYAKRANAkpERAEVLLALGDGD--GISAKHVFVAARQGDPVAVDSYREVA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 241 EYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAA 309
Cdd:TIGR00744 237 RWAGAGLADLASLFNPSAIVLGGGLSDAGDLLLDPIRKSYKRWLFGGARQVADIIAAQLGNDAGLVGAA 305
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
5-310 |
2.74e-58 |
|
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: 189.08 E-value: 2.74e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKtGKIIAKDSVPTLNTrPIEAIMLDMTKLCKTLldksQMDINKIEAVGIGCPGTVDNKNGIISY 84
Cdd:cd24065 3 IGLDLGGTKIAAGVVDG-GRILSRLVVPTPRE-GGEAVLDALARAVEAL----QAEAPGVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEY---TANGHNASSYILITLGTGIGGgaVINSKIYRGFNGVGIE 160
Cdd:cd24065 77 APNIPgLTDFPIRRGLAERLGLPVVLENDANAAALAEHhygAARGTESSVYVTISTGIGGGL--VLGGRVLRGRHGQAGE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 161 PGHMTLINGGERCTCGKHGCWETYGSVTALINQTklkmtdnpdslmhkiSGKFG-EVNGRVAFEAAKAGDRAGLEVVEKY 239
Cdd:cd24065 155 IGHTTVLPGGPMCGCGLVGCLEALASGRALARDA---------------SFAYGrPMSTAELFELAQQGEPKALRIVEQA 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052835205 240 TEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEinEFNKYRPKTKIEIASLNNDAGIIGAAL 310
Cdd:cd24065 220 AAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLLPVQEAAR--RYTEGWHAPPLRLAHLGTDAGVIGAAL 288
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
5-310 |
9.71e-58 |
|
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family corresponds to a group of proteins including sugar kinases, transcriptional repressors, and yet uncharacterized open reading frames. ROK family sugar kinases phosphorylate a range of structurally distinct hexoses including the key carbon source D-glucose, various glucose epimers, and several acetylated hexosamines. The sugar kinases include N-acetyl-D-glucosamine kinase (NAGK; EC 2.7.1.59), polyphosphate glucokinase (PPGK; EC 2.7.1.63/EC 2.7.1.2), glucokinase (GLK; EC 2.7.1.2), fructokinase (FRK; EC 2.7.1.4), hexokinase (HK; EC 2.7.1.1), D-allose kinase (AlsK; EC 2.7.1.55), bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE; EC 3.2.1.183/EC 2.7.1.60), N-acetylmannosamine kinase (NanK; EC 2.7.1.60), beta-glucoside kinase (BglK; EC 2.7.1.85), and N-acetylglucosamine kinase (EC 2.7.1.59). The family also contains the repressor proteins, such as N-acetylglucosamine repressor (NagC), xylose repressor (XylR), cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and protein Mlc. ROK kinases harbor a conserved N-terminal ATP binding motif of sequence DxGxT, while ROK repressors possess a N-terminal extension that contains a canonical helix-turn-helix DNA binding motif. The ROK family proteins belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily of phosphotransferases, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466849 [Multi-domain] Cd Length: 239 Bit Score: 185.74 E-value: 9.71e-58
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMdINKIEAVGIGCPGTVDNKNGIISY 84
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEGPEAVLDRIAELIEELLAEAGV-RERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTA-NGHNASSYilitlgtgigggA------------VINSKI 150
Cdd:cd23763 80 APNLPwWKNVPLRELLEERLGLPVVVENDANAAALGEAWFgAGRGVRNF------------VyitlgtgigggiIIDGKL 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 151 YRGFNGVGIEPGHMTlinggerctcgkhgcwetygsvtalinqtklkmtdnpdslmhkisgkfgevngrvafeaakagdr 230
Cdd:cd23763 148 YRGANGAAGEIGHIT----------------------------------------------------------------- 162
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 231 agleVVEKYTEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAAL 310
Cdd:cd23763 163 ----VLEEAARYLGIGLANLINLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAA 238
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
3-312 |
9.36e-55 |
|
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: 180.45 E-value: 9.36e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24076 2 AVIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGVV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYT-ANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:cd24076 82 LLAPNLGWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRfGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEI 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLMHKIsgkfgevngrvaFEAAKAGDRAGLEVVEKYTE 241
Cdd:cd24076 162 GHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAGGEPLSLAEL------------VEAARAGDPAALAALEEVGE 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052835205 242 YVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAALSA 312
Cdd:cd24076 230 YLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAAALA 300
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
5-312 |
2.15e-54 |
|
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: 179.07 E-value: 2.15e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAimldMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGIISY 84
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEET----LVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEY-TANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPGH 163
Cdd:pfam00480 77 TPNIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAvFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 164 MTLINGGERCTCGKHGCWETYGSVTALINQTKLKmtdnpdslMHKISGKfgEVngrvaFEAAKAGDRAGLEVVEKYTEYV 243
Cdd:pfam00480 157 IQLDPNGPKCGCGNHGCLETIASGRALEKRYQQK--------GEDLEGK--DI-----IVLAEQGDEVAEEAVERLARYL 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1052835205 244 ADGITSVINIFEPEILVIGGGISkEGEYLLNPIRKFVE--INEFNKyRPKTKIEIASLNNDAGIIGAALSA 312
Cdd:pfam00480 222 AKAIANLINLFDPQAIVLGGGVS-NADGLLEAIRSLVKkyLNGYLP-VPPVIIVAASLGDNAGALGAAALA 290
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
3-309 |
2.16e-54 |
|
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: 179.32 E-value: 2.16e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMDiNKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24059 2 YVIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEEVLEKLYELIDRLLEKENIK-SKILGIGIGAPGPLDVEKGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGE-YTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIE 160
Cdd:cd24059 81 LNPPNFPgWENIPLVELLEEKFGIPVYLDNDANAAALAEkWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 161 PGHMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLMHKIsgkfgevngrvafEAAKAGDRAGLEVVEKYT 240
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGSGRSFQLDIV-------------EALQKGDPIADEVIEEAA 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 241 EYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAA 309
Cdd:cd24059 228 KYLGIGLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAA 296
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
3-311 |
1.08e-51 |
|
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: 172.52 E-value: 1.08e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMDinKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24063 1 YYVAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTGDPGTVSEQVLGLIETLLSKAGKD--SIEGIGVSSAGPLDLRKGTI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEY---TANGHNASSYilITLGTGIGGGAVINSKIYRGFNGVGI 159
Cdd:cd24063 79 VNSPNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHlfgAGRGTSNLVY--ITISTGIGGGVIVDGRLLLGKNGNAA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 160 EPGHMTL-INGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLMHKISGKFGE-VNGRVAFEAAKAGDRAGLEVVE 237
Cdd:cd24063 157 EVGHLVVdTESGLKCGCGGYGHWEAFASGRGIPRFAREWAEGFSSRTSLKLRNPGGEgITAKEVFSAARKGDPLALKIIE 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052835205 238 KYTEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEinEFNKYRPKTKIEIASLNNDAGIIGAALS 311
Cdd:cd24063 237 KLARYNGRGIANVINAYDPELIVIGGSVFNNNKDILDPLIEYLE--KNPAISKGPEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
3-310 |
5.64e-51 |
|
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: 170.93 E-value: 5.64e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQmDINKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24071 2 YIIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEKVIELIAENIKKLIKNKH-VEKKLLGIGIAVSGLVDSKKGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEY---TANGHnaSSYILITLGTGIGGGAVINSKIYRG-FNGVG 158
Cdd:cd24071 81 IRSTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELwkgKGKGY--SNFICVTVGAGIGSSLVIDGKLYTGnFGGAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 159 iEPGHMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLM-HKISGKFGEVngrvaFEAAKAGDRAGLEVVE 237
Cdd:cd24071 159 -EIGHMTIQPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSLLkELEDFEIEKV-----REAAEEGDSVATELFK 232
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052835205 238 KYTEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAAL 310
Cdd:cd24071 233 KAGEYLGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAAL 305
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
3-309 |
1.02e-49 |
|
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: 167.34 E-value: 1.02e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPtLNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24073 2 YVVGVKLTEDRITAVLTDLRGNVLASHTLP-LDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGE-YTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:cd24073 81 RWSPLLGWRDVPLAELLEERLGLPVYVENDVNALALAEhWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTLINGGERCTCGKHGCWETYGSVTALINQtklkmtdnpdslMHKISGKFGEVNGRVAFEAAKAGDRAGLEVVEKYTE 241
Cdd:cd24073 161 GHTTVDPDGPPCRCGKRGCLEAYASDPAILRQ------------AREAGLRGEPLTIEDLLAAARAGDPAARAILRRAGR 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1052835205 242 YVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAA 309
Cdd:cd24073 229 ALGLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGLASDLELVIHPWGDEAWARGAA 296
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
3-308 |
9.05e-42 |
|
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: 146.17 E-value: 9.05e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlntrPIEAIMLDMTKLCKtLLDKSQMdinKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPT----PKDSLEEFLDYIKK-IIKRYDE---EIDGIAISAPGVIDPETGII 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTA----NGHNAssyilitlgtgigggAVI----------- 146
Cdd:cd24152 73 YGGGALPyLKGFNLKEELEERCNLPVSIENDAKCAALAELWLgslkGIKNG---------------AVIvlgtgiggaii 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 147 -NSKIYRGFNGVGIEPGHMTLINGGErctcgKHGCWETYGSVTALINQTKLKMTDNPdslmhkisgkfgeVNGRVAFEAA 225
Cdd:cd24152 138 iDGKLYRGSHFFAGEFSYLLTDDDDK-----DLLFFSGLASMFGLVKRYNKAKGLEP-------------LDGEEIFEKY 199
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 226 KAGDRAGLEVVEKYTEYVADGITSVINIFEPEILVIGGGISKEgEYLLNPIRKFVE--INEFNKYRPKTKIEIASLNNDA 303
Cdd:cd24152 200 AKGDEAAKKILDEYIRNLAKLIYNIQYILDPEVIVIGGGISEQ-PLFIEDLKKEVNeiLANRPGSIPKPEIKACKFGNDA 278
|
....*
gi 1052835205 304 GIIGA 308
Cdd:cd24152 279 NLLGA 283
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
2-312 |
4.40e-40 |
|
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: 141.92 E-value: 4.40e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 2 KYYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLDKSQMdinKIEAVGIGCPGTVD-NKNG 80
Cdd:cd24070 1 KYVLGIDIGGTNIRIGLVDEDGKLLDFEKVPSKDLLRAGDPVEVLADLIREYIEEAGL---KPAAIVIGVPGTVDkDRRT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 81 IISySNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTANGHNASSyilitlgtgigggAV-------------- 145
Cdd:cd24070 78 VIS-TPNIPgLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEG-------------VVlgfyigtgignail 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 146 INSKIYRGFNGVGIEPGHMTLINGGERCTCGKHGCWETYGSVTALinqTKLKMTDNPDSLMHKIsgkfgevngrvaFEAA 225
Cdd:cd24070 144 INGKPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRAL---EEIAEEHYPDTPILDI------------FVDH 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 226 KAGdraglEVVEKYTEYVADGITSVINIFEPEILVIGGGISK-EG---EYLLNPIRKFVEinefnKYRPKTKIEI--ASL 299
Cdd:cd24070 209 GDE-----PELDEFVEDLALAIATEINILDPDAVILGGGVIDmKGfprETLEEYIRKHLR-----KPYPADNLKIiyAEL 278
|
330
....*....|...
gi 1052835205 300 NNDAGIIGAALSA 312
Cdd:cd24070 279 GPEAGVIGAAIYA 291
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
3-310 |
6.51e-40 |
|
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: 141.52 E-value: 6.51e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNgiI 82
Cdd:cd24077 2 YSIGIDLGYNYISLMLTYLDGEIISSKQIKL-LDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVDENE--I 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYTANgHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPG 162
Cdd:cd24077 79 IFTPYYDLEDIDLKEKLEEKFNVPVYLENEANLSALAERTFS-EDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEIG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 163 HMTLINGGERCTCGKHGCWETYGSVTALINQ-TKLKMTDNPDslmhkisgkFGEVNgrvafEAAKAGDRAGLEVVEKYTE 241
Cdd:cd24077 158 HMIIVPNGKPCPCGNKGCLEQYASEKALLKElSEKKGLETLT---------FDDLI-----QLYNEGDPEALELIDQFIK 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 242 YVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVeINEFNKYRpktKIEIASLNNDAGIIGAAL 310
Cdd:cd24077 224 YLAIGINNIINTFNPEIIIINSSLINEIPELLEKIKEQL-SSSFNKYV---EILISTLGKNATLLGGAA 288
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
5-310 |
1.37e-38 |
|
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: 138.11 E-value: 1.37e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLN---TRPIEAImldmtklcKTLLDKSQMDINKIEAVGIGCPGTVDNKNGI 81
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRVPTPRgdyEATLDAI--------ADLVEEAEEELGAPATVGIGTPGSISPRTGL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 82 ISYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYTAN-GHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIE 160
Cdd:cd24066 74 VKNANSTWLNGKPLKADLEARLGRPVRIENDANCFALSEATDGaGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGE 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 161 PGHMTLI------NGGERCTCGKHGCWETYGSVTALINQTKlkmtdnpdslmhKISGKfgEVNGRVAFEAAKAGDRAGLE 234
Cdd:cd24066 154 WGHNPLPwpdedeLPGPPCYCGKRGCVETFLSGPALERDYA------------RLTGK--TLSAEEIVALARAGDAAAVA 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 235 VVEKYTEYVADGITSVINIFEPEILVIGGGISK-EGEYLLNP--IRKFVEINEFNkyrpkTKIEIASLNNDAGIIGAAL 310
Cdd:cd24066 220 TLDRFLDRLGRALANVINILDPDVIVLGGGLSNiDELYTEGPaaLARYVFSDEVE-----TPIVKNKHGDSSGVRGAAW 293
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
4-310 |
1.07e-37 |
|
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: 135.82 E-value: 1.07e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 4 YIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlntrPIEAIMLDMTKLCkTLLDKSQMDINKIEAVGIGCPGTVDNKNGIIs 83
Cdd:cd24057 2 YYGFDIGGTKIEFAVFDEALQLVWTKRVPT----PTDDYAAFLAAIA-ELVAEADARFGVKGPVGIGIPGVIDPEDGTL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 84 YSNNIP-MKNVPMRKFMEKQLNISVNLENDANAAALGEYTAN-GHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:cd24057 76 ITANIPaAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGaGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEW 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHM----TLINGGE-----RCTCGKHGCWETYGSVTALINqtklkmtdnpdsLMHKISGKfgevnGRVAFE---AAKAGD 229
Cdd:cd24057 156 GHGplpaDALLLGYdlpvlRCGCGQTGCLETYLSGRGLER------------LYAHLYGE-----ELDAPEiiaAWAAGD 218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 230 RAGLEVVEKYTEYVADGITSVINIFEPEILVIGGGISKEGEyLLNPIRKFVEINEFNKYRPKtKIEIASLNNDAGIIGAA 309
Cdd:cd24057 219 PQAVAHVDRWLDLLAGCLANILTALDPDVVVLGGGLSNFPA-LIAELPAALPAHLLSGARTP-RIVPARHGDAGGVRGAA 296
|
.
gi 1052835205 310 L 310
Cdd:cd24057 297 F 297
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
3-310 |
3.64e-35 |
|
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: 129.41 E-value: 3.64e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPtLNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGII 82
Cdd:cd24075 2 HILAVRLGRHDLTLGLYDLSGELLAEHTVP-LTALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 83 SYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGE-YTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:cd24075 81 HYMPHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEhYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTLINGGERCTCGKHGCWETYGSVTALINQ----------TKLKMTDnpdSLMHKIsgkfgevngrvaFEAAKAGDRA 231
Cdd:cd24075 161 GHIQIEPLGERCHCGNFGCLETVASNAAIEQRvkkllkqgyaSQLTLQD---CTIKDI------------CQAALNGDQL 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 232 GLEVVEKYTEYVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAAL 310
Cdd:cd24075 226 AQDVIKRAGRYLGKVIAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDHNSAIGAFAL 304
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
5-278 |
4.65e-31 |
|
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: 118.29 E-value: 4.65e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMldmTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGIISY 84
Cdd:cd24072 4 LGIVVSPNSLRAQVGNACGELLGEFEYRVITLETPEALI---DEIIDCIDRLLKLWKDRVKGIALAIQGLVDSHKGVSLW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 85 SNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEyTANGHNASS--YILITLGTGIGGGAVINSKIYRGFNGVGIEPG 162
Cdd:cd24072 81 SPGAPWRNIEIKYLLEERYGIPVFVENDCNMLALAE-KWQGELRQSrdFCVINLDYGIGSAIVIDNKLYIGASSGSGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 163 HMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLmhkisgKFGEVNGRVAFEAAKAGDRAGLEVVEKYTEY 242
Cdd:cd24072 160 HTKVNPDGARCDCGRRGCLETVASNSALKRNARVTLKLGPVSA------DPEKLTMEQLIEALEEGEPIATQIFDRAANA 233
|
250 260 270
....*....|....*....|....*....|....*.
gi 1052835205 243 VADGITSVINIFEPEILVIGGGISKEGEYLLNPIRK 278
Cdd:cd24072 234 IGRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRR 269
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
2-314 |
1.44e-30 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 117.01 E-value: 1.44e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 2 KYYIGIDLGGTNIAAGIVDKTGKIIAKDSVPT---LNTRPIEAIMlDMtkLCKTLLDKSQmdinKIEAVGIGCPGTVDNK 78
Cdd:PRK09698 4 NVVLGIDMGGTHIRFCLVDAEGEILHCEKKRTaevIAPDLVSGLG-EM--IDEYLRRFNA----RCHGIVMGFPALVSKD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 79 NGIISYSNNIPMK---NVPMRKFMEKQLNISVNLENDAN--------------AAALGEYTANGHNASSYilitlgtgig 141
Cdd:PRK09698 77 RRTVISTPNLPLTaldLYDLADKLENTLNCPVFFSRDVNlqllwdvkennltqQLVLGAYLGTGMGFAVW---------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 142 ggavINSKIYRGFNGVGIEPGHMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNP--DSLMHKISGKFgevngr 219
Cdd:PRK09698 147 ----MNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLETNCSGMALRRWYEQQPRDYPlsDLFVHAGDHPF------ 216
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 220 vafeaakagdraglevVEKYTEYVADGITSVINIFEPEILVIGGG-ISKEG---EYLLNPIRKFVEinefnkyRPKT--- 292
Cdd:PRK09698 217 ----------------IQSLLENLARAIATSINLFDPDAIILGGGvMDMPAfprETLIAMIQKYLR-------KPLPyev 273
|
330 340
....*....|....*....|...
gi 1052835205 293 -KIEIASLNNDAGIIGAALSANR 314
Cdd:PRK09698 274 vRFIYASSSDFNGAQGAAILAHQ 296
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
7-309 |
1.87e-27 |
|
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: 108.66 E-value: 1.87e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 7 IDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRpiEAIMLDMTKLCKTLLdKSQMDIN-KIEAVGIGCPGTVDNKNGIISYS 85
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPNPKTY--EERIDLILQMCVEAA-SEAVKLNcRILGVGISTGGRVNPREGIVLHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 86 NNI--PMKNVPMRKFMEKQLNISVNLENDANAAALGEYT-ANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPG 162
Cdd:cd24060 82 TKLiqEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKfGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 163 HMTLINGGERCTCGKHGCWETYGSVTALINQTKlKMTDNpDSLM--HKISGKFGEVNGRVAFEAAKAGDRAGLEVVEKYT 240
Cdd:cd24060 162 HIVVSLDGPDCMCGSHGCVEAYASGMALQREAK-KLHDE-DLLLveGMSVTNDEEVTAKHLIQAAKLGNAKAQKILRTAG 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 241 EYVADGITSVINIFEPEILVIGGGISKEGEyllNPIRKFVEINEFNKYRpKTKIEIASLnNDAGIIGAA 309
Cdd:cd24060 240 TALGLGIVNILHTLNPSLVILSGVLASHYE---NIVKDVIAQRALPSVQ-NVDVVVSDL-VDPALLGAA 303
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
7-310 |
3.06e-25 |
|
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466919 [Multi-domain] Cd Length: 283 Bit Score: 101.98 E-value: 3.06e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 7 IDLGGTNIAAGIVDKtGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLldksqmdINKIEAVGIGCPGTVDNknGIISYSN 86
Cdd:cd24069 3 IDIGGTKIAAALIGN-GQIIDRRQIPTPRSGTPEALADALASLLADY-------QGQFDRVAVASTGIIRD--GVLTALN 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 87 --NIPMKNV-PMRKFMEKQLNISVNLENDANAAALGEYTA-NGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPG 162
Cdd:cd24069 73 pkNLGGLSGfPLADALQQLLGVPVVLLNDAQAAAWGEYQAgDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 163 HMTLINGGERCTCGKHGCWETYGSVTALINQtklkmtdnpdslMHKISGKfgEVNGRVAFEAAKAGDRAGLEVVEKYTEY 242
Cdd:cd24069 153 HTLADPPGPVCGCGRRGCVEAIASGTAIAAA------------ASEILGE--PVDAKDVFERARSGDEEAARLIDRAARA 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052835205 243 VADGITSVINIFEPEILVIGGGISkegeylLNPirKFVEINEF------NKYRPktKIEIASLNNDAGIIGAAL 310
Cdd:cd24069 219 LADLIADLKATLDLDCVVIGGSVG------LAE--GFLERVEQyladepAIFRV--SLEPARLGQDAGLLGAAL 282
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
4-266 |
1.69e-23 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 97.75 E-value: 1.69e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 4 YIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlntrPIEAIMLDMTKLCkTLLDKSQMDINKIEAVGIGCPGTVDNKNGIIs 83
Cdd:PRK13310 2 YYGFDIGGTKIELGVFNEKLELQWEERVPT----PRDSYDAFLDAVC-ELVAEADQRFGCKGSVGIGIPGMPETEDGTL- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 84 YSNNIPM-KNVPMRKFMEKQLNISVNLENDANAAALGE-YTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:PRK13310 76 YAANVPAaSGKPLRADLSARLGRDVRLDNDANCFALSEaWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEF 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTL------INGGE----RCTCGKHGCWETYGS------VTALINQTKLKMTDnpdslmhkisgkfgevngrvAFEAA 225
Cdd:PRK13310 156 GHMRLpvdaltLLGWDaplrRCGCGQKGCIENYLSgrgfewLYQHYYGEPLQAPE--------------------IIALY 215
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1052835205 226 KAGDRAGLEVVEKYTEYVADGITSVINIFEPEILVIGGGIS 266
Cdd:PRK13310 216 YQGDEQAVAHVERYLDLLAICLGNILTIVDPHLVVLGGGLS 256
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
7-312 |
5.35e-22 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 93.44 E-value: 5.35e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 7 IDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAIMLDMTKLCKTLLdksqmdiNKIEAVGIGCPGTVDNknGIISYSN 86
Cdd:PRK05082 6 IDIGGTKIAAALVGEDGQIRQRRQIPTPASQTPEALRQALSALVSPLQ-------AQADRVAVASTGIIND--GILTALN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 87 niP-----MKNVPMRKFMEKQLNISVNLENDANAAALGEYTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEP 161
Cdd:PRK05082 77 --PhnlggLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHI 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTLINGGERCTCGKHGCWETYGSVTALINQTKlkmtdnpdslmhkisGKFGEVNGRVAFEAAKAGDRAGLEVVEKYTE 241
Cdd:PRK05082 155 GHTLADPHGPVCGCGRRGCVEAIASGRAIAAAAQ---------------GWLAGCDAKTIFERAGQGDEQAQALINRSAQ 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052835205 242 YVADGITSVINIFEPEILVIGGGISKEGEYLlnpirkfVEINEFNKYRPK---TKIEIASLNNDAGIIGAALSA 312
Cdd:PRK05082 220 AIARLIADLKATLDCQCVVLGGSVGLAEGYL-------ELVQAYLAQEPAiyhVPLLAAHYRHDAGLLGAALWA 286
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
5-266 |
9.95e-22 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 92.78 E-value: 9.95e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTlntrP-------IEAImldmtklcKTLLDKSQMDINKIEAVGIGCPGTVDN 77
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPT----PrddyqqtIEAI--------ATLVDMAEQATGQRGTVGVGIPGSISP 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 78 KNGIISYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYTaNGHNASSYILITLGTGIGGGA--VINSKIYRGFN 155
Cdd:PRK09557 71 YTGLVKNANSTWLNGQPLDKDLSARLNREVRLANDANCLAVSEAV-DGAAAGKQTVFAVIIGTGCGAgvAINGRVHIGGN 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 156 GVGIEPGH-----MT----LINGGERCTCGKHGCWETYGSVTALInqtklkmTDnpdslMHKISGKfgEVNGRVAFEAAK 226
Cdd:PRK09557 150 GIAGEWGHnplpwMDedelRYRNEVPCYCGKQGCIETFISGTGFA-------TD-----YRRLSGK--ALKGSEIIRLVE 215
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1052835205 227 AGDRAGLEVVEKYTEYVADGITSVINIFEPEILVIGGGIS 266
Cdd:PRK09557 216 EGDPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGGGMS 255
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
4-310 |
2.07e-21 |
|
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: 92.37 E-value: 2.07e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 4 YIGIDLGGTNIAAGIVDKTGKIIAKDSVPtLNTRPIEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGIIS 83
Cdd:cd24074 4 FLSIRIGRGYITLALRDLNGRLLAEERYP-LPAKDNDPFLDRLLESISEFFSRHQKKLERLTAIAITLPGIIDPESGIVH 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 84 YSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYtANGHNASSYILITLGTGIGGGA-VINS-KIYRGFNGVGIEP 161
Cdd:cd24074 83 RLPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAER-FFGAAKGAKNIIQIVIDDDIGAgVITDgQLLHAGSSRLGEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 162 GHMTLINGGERCTCGKHGCWETYGSVTALINQTKLKMTDNPDSLMHKisgkfGEVNGRVAFEAAKAGDRAGLEVVEKYTE 241
Cdd:cd24074 162 GHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQSPDSMLHG-----QPISIESLCQAALAGDPLAQDIIIQVGR 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 242 YVADGITSVINIFEPEILVIGGGISKEGEYLLNPIRKFVEINEFNKYRPKTKIEIASLNNDAGIIGAAL 310
Cdd:cd24074 237 HLGRILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQSLPAYSQHLQIESTKFYNDGTMPGAAL 305
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
4-310 |
1.01e-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: 81.44 E-value: 1.01e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 4 YIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlnTRPIEAimldMTKLCKTLLDKSqmdiNKIEAVGIGCPGTVD-NKN--- 79
Cdd:cd24067 1 FGGIEAGGTKFVCAVGTGDGNIIERTEFPT--TTPEET----LQAVIDFFREQE----EPIDAIGIASFGPIDlNPTspt 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 80 -GIISYSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGEYTA-NGHNASSYILITLGTGIGGGAVINSKIYRGFngV 157
Cdd:cd24067 71 yGYITTTPKPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWgAAKGLDSLAYITVGTGIGVGLVVNGKPVHGL--L 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 158 GIEPGHMtLIN-----GGERCTCGKHG-CWETYGSVTALINQTKLKMTDNPDSlmHKIsgkfgevngrVAFEAakagdra 231
Cdd:cd24067 149 HPEMGHI-RVPrhpddDGFPGVCPFHGdCLEGLASGPAIAARWGIPAEELPDD--HPA----------WDLEA------- 208
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 232 glevvekytEYVADGITSVINIFEPEILVIGGGISKeGEYLLNPIR-KFVEINefNKY--RPKTKIEI------ASLNND 302
Cdd:cd24067 209 ---------YYLAQACANLTLTLSPERIVLGGGVMQ-RPGLFPRIReKFRKLL--NGYleVPRLLPDIdeyivpPALGND 276
|
....*...
gi 1052835205 303 AGIIGAAL 310
Cdd:cd24067 277 AGILGALA 284
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
6-312 |
3.46e-14 |
|
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: 70.68 E-value: 3.46e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 6 GIDLGGTNIAAGIVD-KTGKIIA-KDSVPTLNTRPIEAIMLDMTKLCKTLLDKSqmdinkieAVGIGCPGTVdnKNGIIS 83
Cdd:cd24058 3 GIDIGGSGIKGAIVDtDTGELLSeRIRIPTPQPATPEAVADVVAELVAHFPWFG--------PVGVGFPGVV--RRGVVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 84 YSNNIPMK--NVPMRKFMEKQLNISVNLENDANAAALGE--YTANGHNASSyilitlgtgigggaVINSKIyrgfnGVGI 159
Cdd:cd24058 73 TAANLDKSwiGFDAAKLLSKRLGRPVRVLNDADAAGLAEmkGGAGKGEKGV--------------VLVLTL-----GTGI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 160 epGHMTLINGgerctcgkhgcwetygsvtALINQTKLKMtdnpdslmHKISGKFGEvngrvafEAAKAGDRAGLEV-VEK 238
Cdd:cd24058 134 --GSALFVDG-------------------HLVPNTELGH--------LEIRGKDAE-------ERASLGVRAREDLgWKR 177
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1052835205 239 YTEYVADGITSVINIFEPEILVIGGGISKEGEyllnpirKFVEINEFnkyrpKTKIEIASLNNDAGIIGAALSA 312
Cdd:cd24058 178 WAKRVNKYLQYLERLFNPDLFIIGGGNSKKAD-------KFLPLLDV-----KTPVVPAVLRNDAGIVGAALLA 239
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
4-186 |
6.30e-09 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 55.81 E-value: 6.30e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 4 YIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlntrPIEAIMlDMTKLCKTLLDKSQMDINKIEAVGIGCPGTVDNKNGIIS 83
Cdd:PRK13311 2 YYGFDMGGTKIELGVFDENLQRIWHKRVPT----PREDYP-QLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 84 YSNNIPMKNVPMRKFMEKQLNISVNLENDANAAALGE-YTANGHNASSYILITLGTGIGGGAVINSKIYRGFNGVGIEPG 162
Cdd:PRK13311 77 TANVPSAMGQPLQADLSRLIQREVRIDNDANCFALSEaWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFG 156
|
170 180 190
....*....|....*....|....*....|....
gi 1052835205 163 HMTL------INGGE----RCTCGKHGCWETYGS 186
Cdd:PRK13311 157 HFRLpvdaldILGADiprvPCGCGHRGCIENYIS 190
|
|
| XylB |
COG1070 |
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose ... |
2-69 |
1.26e-07 |
|
Sugar (pentulose or hexulose) kinase [Carbohydrate transport and metabolism]; Sugar (pentulose or hexulose) kinase is part of the Pathway/BioSystem: Non-phosphorylated Entner-Doudoroff pathway
Pssm-ID: 440688 [Multi-domain] Cd Length: 494 Bit Score: 52.53 E-value: 1.26e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052835205 2 KYYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRP--------IEAIMLDMTKLCKTLLDKSQMDINKIEAVGI 69
Cdd:COG1070 1 KYVLGIDIGTTSVKAVLFDADGEVVASASAEYPLSSPhpgwaeqdPEDWWEAVVEAIRELLAKAGVDPEEIAAIGV 76
|
|
| ASKHA_NBD_FGGY_EcLyxK-like |
cd07802 |
nucleotide-binding domain (NBD) of Escherichia coli L-xylulose/3-keto-L-gulonate kinase ... |
3-69 |
3.96e-07 |
|
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: 51.01 E-value: 3.96e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPT--LNTRPIEAIMlDMTKL-------CKTLLDKSQMDINKIEAVGI 69
Cdd:cd07802 1 YLLGIDNGTTNVKAVLFDLDGREIAVASRPTpvISPRPGWAER-DMDELwqataeaIRELLEKSGVDPSDIAGVGV 75
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
2-312 |
4.82e-07 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 50.27 E-value: 4.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 2 KYYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLN--TRPIEAIMLDMTKLCKTLLDKSQmDINKIEAVGIGCPGtVDNKn 79
Cdd:COG2971 1 PYILGVDGGGTKTRAVLVDADGEVLGRGRAGGANpqSVGLEEALASLREALEEALAAAG-DPADIEAVGFGLAG-AGTP- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 80 giisysnnipmknvPMRKFMEKQL-----NISVNLENDANAAALGeytANGHNAssyilitlgtgigGGAVInskiyrGF 154
Cdd:COG2971 78 --------------EDAEALEAALrelfpFARVVVVNDALAALAG---ALGGED-------------GIVVIag---tGS 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 155 NGVGIEPghmtlinGGERCTCGKHGcwetY-----GS-------------------------VTALINQTKLkmtDNPDS 204
Cdd:COG2971 125 IAAGRDG-------DGRTARVGGWG----YllgdeGSgawlgrealraalraldgrgpptalTEAVLAEFGL---DDPEE 190
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 205 LMHKISGKfGEVNGRVA------FEAAKAGDRAGLEVVEKYTEYVADGITSVINiFEPEILVIGGGISKEGEYLLNPIRK 278
Cdd:COG2971 191 LIAWVYRG-PAPPADLAslaplvFEAAEAGDPVARAILEEAADELAELARALLE-RGALPVVLAGGVAAAQPLLREALRA 268
|
330 340 350
....*....|....*....|....*....|....
gi 1052835205 279 FVEinefnkyrpKTKIEIASLNNDAgIIGAALSA 312
Cdd:COG2971 269 RLA---------AGGAEIVPPAGDP-VDGALLLA 292
|
|
| FGGY_N |
pfam00370 |
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease ... |
3-69 |
8.85e-07 |
|
FGGY family of carbohydrate kinases, N-terminal domain; This domain adopts a ribonuclease H-like fold and is structurally related to the C-terminal domain.
Pssm-ID: 395295 [Multi-domain] Cd Length: 245 Bit Score: 49.26 E-value: 8.85e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIE--------AIMLDMTKLCKTLLDKSQMDINKIEAVGI 69
Cdd:pfam00370 1 YYLGIDCGTTSTKAILFNEQGKIIAVAQLENPQITPHPgwaeqdpdEIWQAVAQCIAKTLSQLGISLKQIKGIGI 75
|
|
| ASKHA_NBD_FGGY |
cd00366 |
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is ... |
3-75 |
1.06e-06 |
|
nucleotide-binding domain (NBD) of the FGGY family of carbohydrate kinases; This family is predominantly composed of glycerol kinase (GK) and similar carbohydrate kinases including rhamnulokinase (RhuK), xylulokinase (XK), gluconokinase (GntK), ribulokinase (RBK), and fuculokinase (FK). These enzymes catalyze the transfer of a phosphate group, usually from ATP, to their carbohydrate substrates. The monomer of FGGY proteins contains two large domains, which are separated by a deep cleft that forms the active site. One domain is primarily involved in sugar substrate binding, and the other is mainly responsible for ATP binding. This model includes both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain. Substrate-induced conformational changes and a divalent cation may be required for the catalytic activity. The FGGY family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466787 [Multi-domain] Cd Length: 392 Bit Score: 49.49 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRP--------IEAIMLDMTKLCKTLLDKSQMDINKIEAVGIGC--P 72
Cdd:cd00366 1 YLLGIDIGTTSVKAALFDEDGNLVASASREYPLIYPqpgwaeqdPEDWWQAVVEAIREVLAKAGIDPSDIAAIGISGqmP 80
|
...
gi 1052835205 73 GTV 75
Cdd:cd00366 81 GVV 83
|
|
| ASKHA_NBD_FGGY_YgcE-like |
cd07779 |
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; ... |
3-69 |
5.21e-06 |
|
nucleotide-binding domain (NBD) of Escherichia coli sugar kinase YgcE and similar proteins; This subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli sugar kinase YgcE. They 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: 466798 [Multi-domain] Cd Length: 433 Bit Score: 47.51 E-value: 5.21e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSV--PTLNTRP------IEAIMLDMTKLCKTLLDKSQMDINKIEAVGI 69
Cdd:cd07779 1 YILGIDVGTTSTRAIIFDLDGNIVASGYReyPPYYPEPgwveqdPDDWWDALCEALKEAVAKAGVDPEDIAAIGL 75
|
|
| ASKHA_NBD_FGGY_RrXK-like |
cd07804 |
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar ... |
3-69 |
6.01e-06 |
|
nucleotide-binding domain (NBD) of Rhodospirillum rubrum xylulose kinase (RrXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Rhodospirillum rubrum xylulose kinase (RrXK). 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: 466806 [Multi-domain] Cd Length: 451 Bit Score: 47.52 E-value: 6.01e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPT--LNTRP------IEAIMLDMTKLCKTLLDKSQMDINKIEAVGI 69
Cdd:cd07804 1 YLLGIDIGTTGTKGVLVDEDGKVLASASIEHdlLTPKPgwaehdPEVWWGAVCEIIRELLAKAGISPKEIAAIGV 75
|
|
| ASKHA_NBD_FGGY_FK |
cd07773 |
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), ... |
3-38 |
3.65e-05 |
|
nucleotide-binding domain (NBD) of L-fuculokinase (FK) and similar proteins; FK (EC 2.7.1.51), also called L-fuculose kinase, catalyzes the ATP-dependent phosphorylation of L-fuculose to produce L-fuculose-1-phosphate and ADP. It can also phosphorylate, with lower efficiency, D-ribulose, D-xylulose and D-fructose. The presence of Mg2+ or Mn2+ is required for enzymatic activity. FKs 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: 466793 [Multi-domain] Cd Length: 443 Bit Score: 44.89 E-value: 3.65e-05
10 20 30
....*....|....*....|....*....|....*.
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRP 38
Cdd:cd07773 1 YLLGIDIGTTNVKAVLFDEDGRILASASRETPLIHP 36
|
|
| ASKHA_NBD_FGGY_SePSK_AtXK1-like |
cd07783 |
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), ... |
3-69 |
7.95e-05 |
|
nucleotide-binding domain (NBD) of Synechococcus elongatus putative sugar kinase (SePSK), Arabidopsis thaliana xylulose kinase-1 (AtXK-1) and similar proteins; This subfamily corresponds to a group of uncharacterized bacterial proteins with similarity to Synechococcus elongatus putative sugar kinase (also known as SePSK; D-ribulose kinase; D-ribulokinase) and Arabidopsis thaliana xylulose kinase-1 (also known as AtXK-1; D-ribulose kinase; D-ribulokinase; inactive xylulose kinase 1). Both kinases exhibit ATP hydrolysis without substrate and can phosphorylate D-ribulose. They belong to the ribulokinase-like carbohydrate kinases, a subfamily of FGGY family carbohydrate kinases. Ribulokinase-like carbohydrate kinases are responsible for the phosphorylation of sugars such as L-ribulose and D-ribulose. Their monomers 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: 466801 [Multi-domain] Cd Length: 429 Bit Score: 43.75 E-value: 7.95e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSV--PTLNTRPI--EAIMLDMTKLCKTLLDK--SQMDINKIEAVGI 69
Cdd:cd07783 1 LFLGIDLGTSGVRAVVVDEDGTVLASASEpyPTSRPGPGwvEQDPEDWWEALRSLLRElpAELRPRRVVAIAV 73
|
|
| ASKHA_NBD_FGGY_EcXK-like |
cd07808 |
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar ... |
3-69 |
1.44e-04 |
|
nucleotide-binding domain (NBD) of Escherichia coli xylulose kinase (EcXK) and similar proteins; The subfamily contains a group of uncharacterized proteins with similarity to Escherichia coli xylulose kinase (EcXK). XK (EC 2.7.1.17), also called xylulokinase or D-xylulose kinase, catalyze the rate-limiting step in the ATP-dependent phosphorylation of D-xylulose to produce D-xylulose 5-phosphate (X5P), a molecule that may play an important role in the regulation of glucose metabolism and lipogenesis. EcXK, also known as 1-deoxy-D-xylulokinase, can also catalyze the phosphorylation of 1-deoxy-D-xylulose to 1-deoxy-D-xylulose 5-phosphate, with lower efficiency. It can also use D-ribulose, xylitol and D-arabitol, but D-xylulose is preferred over the other substrates. EcXK has a weak substrate-independent Mg-ATP-hydrolyzing activity. 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: 466808 [Multi-domain] Cd Length: 482 Bit Score: 43.30 E-value: 1.44e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDSV--PTLNTRP----------IEAimldMTKLCKTLLDKSQMDINKIEAVGI 69
Cdd:cd07808 1 YLLGIDLGTSSVKAVLVDEDGRVLASASAeyPTSSPKPgwaeqdpedwWQA----TKEALRELLAKAGISPSDIAAIGL 75
|
|
| PRK10331 |
PRK10331 |
L-fuculokinase; Provisional |
1-84 |
2.50e-04 |
|
L-fuculokinase; Provisional
Pssm-ID: 182383 [Multi-domain] Cd Length: 470 Bit Score: 42.32 E-value: 2.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 1 MKYYIGIDLGGTNIAAGIVDKTGKIIAKDSVPTlNTRP-----------IEAIMLDMTKLCKTLLDK-SQMDINKIEAVG 68
Cdd:PRK10331 1 QDVILVLDCGATNVRAIAVDRQGKIVARASTPN-ASDIaaensdwhqwsLDAILQRFADCCRQINSElTECHIRGITVTT 79
|
90 100
....*....|....*....|.
gi 1052835205 69 IGCPGTVDNKNG-----IISY 84
Cdd:PRK10331 80 FGVDGALVDKQGnllypIISW 100
|
|
| Hydant_A_N |
pfam05378 |
Hydantoinase/oxoprolinase N-terminal region; This family is found at the N-terminus of the ... |
5-70 |
2.79e-04 |
|
Hydantoinase/oxoprolinase N-terminal region; This family is found at the N-terminus of the pfam01968 family.
Pssm-ID: 398834 [Multi-domain] Cd Length: 176 Bit Score: 41.12 E-value: 2.79e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052835205 5 IGIDLGGTNIAAGIVDKTGKIIAKDSVPTLNTRPIEAImldmTKLCKTLLDKSQMDINKIEAVGIG 70
Cdd:pfam05378 2 IGIDVGGTFTDAVALDEGDGEVAVIKVLTTPDDPVEGI----REALEELLGELGPRTGKVDTVRHG 63
|
|
| ASKHA_NBD_FGGY_SHK |
cd07777 |
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1. ... |
3-69 |
1.41e-03 |
|
nucleotide-binding domain (NBD) of sedoheptulokinase (SHK) and similar proteins; SHK (EC 2.7.1.14), also called heptulokinase, or carbohydrate kinase-like protein (CARKL), is encoded by the carbohydrate kinase-like (CARKL/SHPK) gene. It acts as a modulator of macrophage activation through control of glucose metabolism. SHK catalyzes the ATP-dependent phosphorylation of sedoheptulose to produce sedoheptulose 7-phosphate and ADP. The presence of Mg2+ or Mn2+ might be required for catalytic activity. 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: 466796 [Multi-domain] Cd Length: 436 Bit Score: 39.90 E-value: 1.41e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1052835205 3 YYIGIDLGGTNIAAGIVD-KTGKIIAKDSVPTL----NTRPIEAImLDMTKL---CKTLLDK-SQMDINKIEAVGI 69
Cdd:cd07777 1 NVLGIDIGTTSIKAALLDlESGRILESVSRPTPapisSDDPGRSE-QDPEKIleaVRNLIDElPREYLSDVTGIGI 75
|
|
| ASKHA_NBD_GspK-like |
cd24082 |
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ... |
3-263 |
1.49e-03 |
|
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar proteins; The family includes a group of uncharacterized proteins similar to Vibrio cholerae glucosamine kinase GspK (EC 2.7.1.8), also called GlcN kinase. It acts as ATP-dependent kinase, which is specific for glucosamine. GspK does not show kinase activity with any other sugar.
Pssm-ID: 466932 [Multi-domain] Cd Length: 279 Bit Score: 39.44 E-value: 1.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIA----KDSVPTLN-TRPIEAIMldmtKLCKTLLDKSQMDINKIE--AVGIGCPGTv 75
Cdd:cd24082 1 YFIGIDGGGTKCRARLADADGTVLGeatgGPANLSSDlDQAWASIL----AAIKQALAQAGLDAAALSdlHAGLGLAGA- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 76 dnkngiisysnnipmkNVP-MRKFMEKQLNI--SVNLENDANAAALGeytANGHNAssyilitlgtgiggGAVINskIYR 152
Cdd:cd24082 76 ----------------NVPeARAAFLAALPPfaSLVVVSDAHIACLG---AHGGED--------------GAIII--LGT 120
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 153 GFNGVGIEPGHMTLING-----GERCTcgkhGCW-------------ETYGSVTALINQTKLKMTDNPDSLMHKI----S 210
Cdd:cd24082 121 GSVGAALDGGEVRQVGGwgfplGDEGS----GAWlglralrhtllalDGLAPSSPLTRAVLARFGGDPAEIVAWAntatP 196
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1052835205 211 GKFGEVNGRVaFEAAKAGDRAGLEVVEKYTEYVADGITSVINIFEPEILVIGG 263
Cdd:cd24082 197 ADFAALAPLV-FEAAEQGDPVALAILQEAAAYIERLLRALGAQGALPLCLLGG 248
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
219-310 |
2.16e-03 |
|
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) family; The eukaryotic-type NAGK-like family includes a group of proteins similar to eukaryotic N-acetyl-D-glucosamine kinases, such as Vibrio cholerae glucosamine kinase GspK, Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK), Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK). NAGK (EC 2.7.1.59), also called GlcNAc kinase, converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, from lysosomal degradation or nutritional sources into GlcNAc 6-phosphate. It is involved in the N-glycolylneuraminic acid (Neu5Gc) degradation pathway. NAGK also has ManNAc kinase activity. GspK (EC 2.7.1.8), also called GlcN kinase, acts as ATP-dependent kinase, which is specific for glucosamine. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. KdgK (EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase, catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG. MurK (EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase, catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. The eukaryotic-type N-acetylglucosamine kinase (NAGK) family belongs to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466857 [Multi-domain] Cd Length: 295 Bit Score: 39.21 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1052835205 219 RVAFEAAKAGDRAGLEVVEKYTEYVADGITSVINIF---EPEILVIGGGISKEGEYLLNPIRKFVEinefnkyRPKTKIE 295
Cdd:cd24007 208 PLVFEAAEEGDPVAQAILKEAAEELAKLVVALAKLLllgEKLPLALSGGVFKNNYYLAEFLEELLK-------KKKPNAK 280
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90
....*....|....*
gi 1052835205 296 IASLNNDAgIIGAAL 310
Cdd:cd24007 281 VVEPKGSP-VVGALL 294
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| ASKHA_NBD_FGGY_GntK |
cd07770 |
nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7. ... |
3-71 |
2.42e-03 |
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nucleotide-binding domain (NBD) of gluconate kinase (GntK) and similar proteins; GntK (EC 2.7.1.12), also known as gluconokinase, catalyzes the ATP-dependent phosphorylation of D-gluconate and produce 6-phospho-D-gluconate and ADP. The presence of Mg2+ might be required for catalytic activity. The prototypical member of this subfamily is GntK from Lactobacillus acidophilus. Unlike Escherichia coli GntK, which belongs to the superfamily of P-loop containing nucleoside triphosphate hydrolases, Members of this subfamily are homologous to glycerol kinase, xylulose kinase, and rhamnulokinase from Escherichia coli. They have been classified as members of the FGGY family of carbohydrate kinases, which contain two large domains separated by a deep cleft that forms the active site. This model spans both the N-terminal domain, which adopts a ribonuclease H-like fold, and the structurally related C-terminal domain.
Pssm-ID: 466790 [Multi-domain] Cd Length: 478 Bit Score: 39.46 E-value: 2.42e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1052835205 3 YYIGIDLGGTNIAAGIVDKTGKIIAKDS--VPTLNTRP------IEAIMLDMTKLCKTLLdkSQMDINKIEAVGIGC 71
Cdd:cd07770 1 LILGIDIGTTSTKAVLFDEDGRVVASSSaeYPLIRPEPgwaeqdPEEILEAVLEALKEVL--AKLGGGEVDAIGFSS 75
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