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Conserved domains on  [gi|1059433484|ref|NP_001317354|]
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N-acetyl-D-glucosamine kinase isoform 2 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
1-271 3.62e-163

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or 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. Members in this family are mainly from metazoa.


:

Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 455.89  E-value: 3.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   1 MVNRAKRKAGVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGGVVLISGTGSNC 80
Cdd:cd24078    49 MVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNC 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGYVKQAMFHYFQVPDRLGILTHLYRDFDKC 160
Cdd:cd24078   129 QLINPDGSTAGCGGWGHMLGDEGSAYWIAHRAIKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKS 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 161 RFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTqgr 240
Cdd:cd24078   209 KIAGFCKKLAEGAAEGDPLCRHLFREAGEELARHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGLK--- 285
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1059433484 241 eiQAQNFFSSFTLMKLRHSSALGGASLGARH 271
Cdd:cd24078   286 --QRSDKIKKLSLVRLKESSALGAARLGAKE 314
 
Name Accession Description Interval E-value
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
1-271 3.62e-163

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or 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. Members in this family are mainly from metazoa.


Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 455.89  E-value: 3.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   1 MVNRAKRKAGVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGGVVLISGTGSNC 80
Cdd:cd24078    49 MVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNC 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGYVKQAMFHYFQVPDRLGILTHLYRDFDKC 160
Cdd:cd24078   129 QLINPDGSTAGCGGWGHMLGDEGSAYWIAHRAIKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKS 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 161 RFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTqgr 240
Cdd:cd24078   209 KIAGFCKKLAEGAAEGDPLCRHLFREAGEELARHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGLK--- 285
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1059433484 241 eiQAQNFFSSFTLMKLRHSSALGGASLGARH 271
Cdd:cd24078   286 --QRSDKIKKLSLVRLKESSALGAARLGAKE 314
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
2-274 8.39e-43

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 148.49  E-value: 8.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   2 VNRAKRKAGvdPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYlsESYLITTDAAGSIATATPDG-GVVLISGTGSNC 80
Cdd:COG2971    51 LEEALAAAG--DPADIEAVGFGLAGAGTPEDAEALEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAphdiGYVKQAMFHYFQVPDRLGILTHLYRD-FDK 159
Cdd:COG2971   127 AGRDGDGRTARVGGWGYLLGDEGSGAWLGREALRAALRALDGRGPP----TALTEAVLAEFGLDDPEELIAWVYRGpAPP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 160 CRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPvlfqgkiglPILCVGSVWKSWELLKEGFLLALTQG 239
Cdd:COG2971   203 ADLASLAPLVFEAAEAGDPVARAILEEAADELAELARALLERGAL---------PVVLAGGVAAAQPLLREALRARLAAG 273
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1059433484 240 ReiqaqnffssFTLMKLRHSSALGGASLGARHIGH 274
Cdd:COG2971   274 G----------AEIVPPAGDPVDGALLLALRLLGA 298
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
55-230 1.26e-05

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 45.81  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  55 TDAAGSIATAT-PDGGVVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLeaAPHdigyv 133
Cdd:pfam01869  94 ADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELDGL--APK----- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 134 kqamfhyfqvpdrlgilTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIdpvlfqGKIGL 213
Cdd:pfam01869 166 -----------------TTLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRL------GFVPD 222
                         170
                  ....*....|....*..
gi 1059433484 214 PILCVGSVWKSWELLKE 230
Cdd:pfam01869 223 EVVLTGGVAKNAGLVKA 239
 
Name Accession Description Interval E-value
ASKHA_NBD_NAGK_meta cd24078
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ...
1-271 3.62e-163

nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or 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. Members in this family are mainly from metazoa.


Pssm-ID: 466928 [Multi-domain]  Cd Length: 314  Bit Score: 455.89  E-value: 3.62e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   1 MVNRAKRKAGVDPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYLSESYLITTDAAGSIATATPDGGVVLISGTGSNC 80
Cdd:cd24078    49 MVQEAKKKAGLDPDTPLKSLGLSLSGAEQEEAQEELIEGLRSRYPNLSESYYVTSDTVGAIATAFENGGIVLISGTGSNC 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAPHDIGYVKQAMFHYFQVPDRLGILTHLYRDFDKC 160
Cdd:cd24078   129 QLINPDGSTAGCGGWGHMLGDEGSAYWIAHRAIKAVFDAEDNFEPPPHDISYVKKAMFEYFKIEDRLDLLPHLYTNFDKS 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 161 RFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTqgr 240
Cdd:cd24078   209 KIAGFCKKLAEGAAEGDPLCRHLFREAGEELARHVLAVLPKIDKALLEGEGGLPIVCVGSVWKSWDLLKEGFLEGLK--- 285
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1059433484 241 eiQAQNFFSSFTLMKLRHSSALGGASLGARH 271
Cdd:cd24078   286 --QRSDKIKKLSLVRLKESSALGAARLGAKE 314
ASKHA_NBD_eukNAGK-like cd24007
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ...
1-267 1.19e-55

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: 181.73  E-value: 1.19e-55
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   1 MVNRAKRKAGvdPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPylSESYLITTDAAGSIATATPDG-GVVLISGTGSN 79
Cdd:cd24007    48 AVREALSQAG--SLGEIDAICLGLAGIDSEEDRERLRSALKELFL--SGRIIIVNDAEIALAAALGGGpGIVVIAGTGSV 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  80 CRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEaaPHDIgyVKQAMFHYFQVPDRLGILTHLYR-DFD 158
Cdd:cd24007   124 AYGRNGDGEEARVGGWGHLLGDEGSGYWIGRRALRAALRALDGRG--PKTP--LLDAILKFLGLDSIEELITAIYRsSDR 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 159 KCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLpeidpVLFQGKIGLPILCVGSVWKSWELLKEGFLLALTQ 238
Cdd:cd24007   200 KKEIASLAPLVFEAAEEGDPVAQAILKEAAEELAKLVVALA-----KLLLLGEKLPLALSGGVFKNNYYLAEFLEELLKK 274
                         250       260
                  ....*....|....*....|....*....
gi 1059433484 239 greiqaqnFFSSFTLMKLRHSSALGGASL 267
Cdd:cd24007   275 --------KKPNAKVVEPKGSPVVGALLL 295
BadF COG2971
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ...
2-274 8.39e-43

BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];


Pssm-ID: 442210 [Multi-domain]  Cd Length: 298  Bit Score: 148.49  E-value: 8.39e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   2 VNRAKRKAGvdPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPYlsESYLITTDAAGSIATATPDG-GVVLISGTGSNC 80
Cdd:COG2971    51 LEEALAAAG--DPADIEAVGFGLAGAGTPEDAEALEAALRELFPF--ARVVVVNDALAALAGALGGEdGIVVIAGTGSIA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  81 RLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEAAphdiGYVKQAMFHYFQVPDRLGILTHLYRD-FDK 159
Cdd:COG2971   127 AGRDGDGRTARVGGWGYLLGDEGSGAWLGREALRAALRALDGRGPP----TALTEAVLAEFGLDDPEELIAWVYRGpAPP 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 160 CRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPvlfqgkiglPILCVGSVWKSWELLKEGFLLALTQG 239
Cdd:COG2971   203 ADLASLAPLVFEAAEAGDPVARAILEEAADELAELARALLERGAL---------PVVLAGGVAAAQPLLREALRARLAAG 273
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1059433484 240 ReiqaqnffssFTLMKLRHSSALGGASLGARHIGH 274
Cdd:COG2971   274 G----------AEIVPPAGDPVDGALLLALRLLGA 298
ASKHA_NBD_MurK-like cd24084
nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid ...
26-267 2.93e-31

nucleotide-binding domain (NBD) of Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK) and similar proteins; The family includes a group of uncharacterized proteins similar to Clostridium acetobutylicum N-acetylmuramic acid/N-acetylglucosamine kinase (MurK; EC 2.7.1.-/EC 2.7.1.59), also known MurNAc/GlcNAc kinase, or murein sugar kinase. It 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. Neither the non-N-acetylated forms of the cell wall sugars, i.e., glucosamine and/or muramic acid, nor epimeric hexoses or 1,6-anhydro-MurNAc are substrates for the enzyme. MurK may have a role in the rescue of the murein sugars GlcNAc and MurNAc released from muropeptides during cell wall turnover in C.acetobutylicum.


Pssm-ID: 466934 [Multi-domain]  Cd Length: 302  Bit Score: 118.23  E-value: 2.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  26 GGDQEDAGRILIEELRDRFPYLSesYLITTDAAGSIATATPDG-GVVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGS 104
Cdd:cd24084    74 GASHQGAKETLKDILTELGPDAK--IEVVNDAEIALAAGLEGKpGIVLISGTGSICYGRNTDGETARAGGWGHLLGDEGS 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 105 AYWIAHQAVKIVFDSIDNleAAPHDIGYvkQAMFHYFQVPDRLGILTHLYR-DFDKCRFAGFCRKIAEGAQQGDPLSRYI 183
Cdd:cd24084   152 GYWIAMQALGAVLQAFDG--RGPKTILT--ELLLEELKLSSPRELIDFIYSsDADKKEIASLARLVDEAADQGDEVAKEI 227
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 184 FRKAGEMLGRHIVAVLPEidpvLFQGKIGLPILCVGSVWKSWELLKEGFL-LALTQGREIQAQnffssftlmKLRHSSAL 262
Cdd:cd24084   228 LEEAARELARLAIAVAQK----LLMKPKDFVVILGGSVLENCCVLRSKLSaLILTKYPNAIVG---------LLKHDAAY 294

                  ....*
gi 1059433484 263 GGASL 267
Cdd:cd24084   295 GAVKL 299
ASKHA_NBD_DdNAGK-like cd24081
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ...
5-230 1.15e-21

nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; The family includes a group of uncharacterized proteins similar to Dictyostelium discoideum N-acetyl-D-glucosamine kinase (NAGK). NAGK (EC 2.7.1.59), also called N-acetylglucosamine kinase, or GlcNAc kinase, converts N-acetylglucosamine (GlcNAc), a major component of complex carbohydrates, into GlcNAc 6-phosphate. It also has ManNAc kinase activity.


Pssm-ID: 466931 [Multi-domain]  Cd Length: 311  Bit Score: 92.38  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   5 AKRKAGVdPLVPLRSLGLSLSGGDQEDAGRILIEELRDRFPyLSESYLITTDAAGSIATATpDG---GVVLISGTGSNCR 81
Cdd:cd24081    57 ALKQAGV-PRSAVRAVCLGISGVDRPADAERVRSWLRELFP-ENVKVFVFNDAVAALASGT-AGklhGCVLIAGTGTIAY 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  82 LINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDnleaaphdiGYVKQAMFHYfQVPDRLG------ILTHLYR 155
Cdd:cd24081   134 GFNEDGKRARAGGWGPLLGDRGSGHAIGSQALTAVMRAED---------GRGPPTSLTG-AILKKLGlsspddLIGWAYD 203
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1059433484 156 DFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLFQGKIGLPILCVGSVWK---SWELLKE 230
Cdd:cd24081   204 DTSWARVAALVPLVKACAAAGDAVALGILEDAAEELALSVKAVVRKLGLRGTDGSESFPLVLVGGVLErngGLDLFKE 281
ASKHA_NBD_KdgK-like cd24083
nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase ...
23-232 2.60e-19

nucleotide-binding domain (NBD) of Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK) and similar proteins; The family includes a group of uncharacterized proteins similar to Thermoplasma acidophilum 2-dehydro-3-deoxygluconokinase (KdgK; EC 2.7.1.45), also called 2-keto-3-deoxy-D-gluconate kinase, or KDG kinase. It catalyzes the phosphorylation of 2-keto-3-deoxygluconate (KDG) to produce 2-keto-3-deoxy-6-phosphogluconate (KDPG). It is specific for KDG.


Pssm-ID: 466933 [Multi-domain]  Cd Length: 284  Bit Score: 85.52  E-value: 2.60e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  23 SLSGGDQEDAGRILIEELRDRFPylsESYLITTDAAGSIATATPDG-GVVLISGTGSNCrLINPDGSESGCGGWGHMMGD 101
Cdd:cd24083    68 GLAGIGDSYEATIMGEEIIRSGL---KKFDIYNDGEAAYYSGNGDDdGIVFAPGTGSVG-YIKDEGRVNRIGGWGWSLGD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 102 EGSAYWIAHQAVKIVFDSIDNLEaaphDIGYVKQAMFHYFQVPDRLGILTHLYRdFDKCRFAGFCRKIAEGAQQGDPLSR 181
Cdd:cd24083   144 EGSAFWIAKQAIEAAMREMDGRE----EWTSLVVEVEKEFKLSLRELVINISYE-GIKRLVASLAKLVSQLAEKGDPVAL 218
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1059433484 182 YIFRKAGEMLGRHIVAVLPEIDPvlfQGKIGLpilcVGSVWKSWELLKEGF 232
Cdd:cd24083   219 AIFDEAASEIKKIINAHRLNFGP---PIRVSL----VGGVMQSGPIYLEKF 262
ASKHA_NBD_StHK-like cd24080
nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and ...
51-236 5.12e-18

nucleotide-binding domain (NBD) of Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK) and similar proteins; The family includes a group of uncharacterized proteins similar to Sulfurisphaera tokodaii ATP-dependent hexokinase (StHK). Hexokinase (EC 2.7.1.1) catalyzes the phosphorylation of glucose to glucose 6-phosphate by using ATP as a phosphoryl donor. StHK is a novel hexokinase that can phosphorylate not only glucose but also GlcNAc, glucosamine, and mannose. It differs from other known hexokinases and glucokinases in that its activity is strongly inhibited by ADP. It is distinct in its broad substrate specificity from the GlcNAc kinases, which are specific for GlcNAc.


Pssm-ID: 466930 [Multi-domain]  Cd Length: 291  Bit Score: 82.09  E-value: 5.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  51 YLITTDAAGSIATATPDG-GVVLISGTGSNCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLEaaPHD 129
Cdd:cd24080    91 VIVQHDGEIALIAETRGSpGVMVIAGTGSIVEGYDGRGRVVRVGGWGWLLGDEGSGYWIGREALRALLRMLDGRE--NKT 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 130 IGYVKqaMFHYFQVPDRLGILTHLYRDFDKC-RFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLfq 208
Cdd:cd24080   169 ILAEK--VLKTLNVEDFDELVEWIYSSLCPVdLIASLAKAVDEAAEEGDTVARDILKRAAEELASAAVALARKIGPVK-- 244
                         170       180
                  ....*....|....*....|....*...
gi 1059433484 209 gkiglpILCVGSVWKSwELLKEGFLLAL 236
Cdd:cd24080   245 ------VYLKGGMFNS-KIFHKFFTRYL 265
ASKHA_NBD_GspK-like cd24082
nucleotide-binding domain (NBD) of Vibrio cholerae glucosamine kinase GspK and similar ...
2-207 9.03e-15

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: 72.56  E-value: 9.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484   2 VNRAKRKAGVDPLVPLR-SLGLSLSGGDQEDAGriliEELRDRFPYLSeSYLITTDAAGSIATATpDG--GVVLISGTGS 78
Cdd:cd24082    49 IKQALAQAGLDAAALSDlHAGLGLAGANVPEAR----AAFLAALPPFA-SLVVVSDAHIACLGAH-GGedGAIIILGTGS 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  79 NC-RLINpdGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLeaAPHDIGYvkQAMFHYFQVpDRLGILtHLYRDF 157
Cdd:cd24082   123 VGaALDG--GEVRQVGGWGFPLGDEGSGAWLGLRALRHTLLALDGL--APSSPLT--RAVLARFGG-DPAEIV-AWANTA 194
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1059433484 158 DKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDPVLF 207
Cdd:cd24082   195 TPADFAALAPLVFEAAEQGDPVALAILQEAAAYIERLLRALGAQGALPLC 244
ASKHA_NBD_PG1100-like cd24079
nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine ...
31-221 2.22e-08

nucleotide-binding domain (NBD) of Porphyromonas gingivalis putative N-acetylglucosamine kinase (PG1100) and similar proteins; The family includes a group of uncharacterized proteins similar to Porphyromonas gingivalis putative N-acetylglucosamine kinase (PG1100; EC 2.7.1.59), which may convert GlcNAc to GlcNAc-6-phosphate, a component utilized in UDP-GlcNAc biosynthesis or energy metabolism.


Pssm-ID: 466929 [Multi-domain]  Cd Length: 276  Bit Score: 54.14  E-value: 2.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  31 DAGRILIEE-LRDRFPylSESYLITTDAAGSI-ATATPDGGVVLISGTGSNCRLInpDGSE--SGCGGWGHMMGDEGSAY 106
Cdd:cd24079    70 PERAARIKRlLKKVFP--KAEIEVKSDLLGAArALCGDKKGIVCILGTGSNSCYY--DGEKihDQRPGLGYLLGDEGSGA 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 107 WIAHQAVKivfdsiDNLEA-APHDIgyvKQAMFHYFQVpDRLGILTHLYRDFDKCRF-AGFCRKIAEGAQqgDPLSRYIF 184
Cdd:cd24079   146 YLGKLLLR------DYLYGqLPEEL---RKRFEEQFGL-NKEEILSRVYRSPDPNRYlASLSRFIAEHLE--HPYIRELI 213
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1059433484 185 RKAGEMLGRHIVAVLPEIDPvlfqgkigLPILCVGSV 221
Cdd:cd24079   214 RESFREFFETHVLPYPDYKT--------LPIHFVGSV 242
BcrAD_BadFG pfam01869
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ...
55-230 1.26e-05

BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are two subunits of Benzoyl-CoA reductase, that may be involved in ATP hydrolysis. The family also includes an activase subunit from the enzyme 2-hydroxyglutaryl-CoA dehydratase. The protein Swiss:O66634 contains two copies of this region suggesting that the family may structurally dimerize. This family appears to be related to pfam00370.


Pssm-ID: 396441 [Multi-domain]  Cd Length: 271  Bit Score: 45.81  E-value: 1.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484  55 TDAAGSIATAT-PDGGVVLISGTGSnCRLINPDGSESGCGGWGHMMGDEGSAYWIAHQAVKIVFDSIDNLeaAPHdigyv 133
Cdd:pfam01869  94 ADGAVALAPGTrGEDGVIDIGGTGS-KVIGLDGGKVVRFGGNGQCAGGEGSFLEIAARALGAVVRELDGL--APK----- 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1059433484 134 kqamfhyfqvpdrlgilTHLYRDFDKCRFAGFCRKIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIdpvlfqGKIGL 213
Cdd:pfam01869 166 -----------------TTLNKGAINSTCAVFAEQVVINALSGGETAEDILAGAARSIALRVAALAKRL------GFVPD 222
                         170
                  ....*....|....*..
gi 1059433484 214 PILCVGSVWKSWELLKE 230
Cdd:pfam01869 223 EVVLTGGVAKNAGLVKA 239
ASKHA_ATPase_ROK_CYANR cd24073
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ...
168-204 3.56e-03

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: 38.30  E-value: 3.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1059433484 168 KIAEGAQQGDPLSRYIFRKAGEMLGRHIVAVLPEIDP 204
Cdd:cd24073   207 DLLAAARAGDPAARAILRRAGRALGLALANLVNLLDP 243
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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