|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
1-301 |
0e+00 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 631.68 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANS 80
Cdd:PRK09557 1 MRIGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIPGSISPYTGLVKNANS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPL 160
Cdd:PRK09557 81 TWLNGQPLDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWGHNPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 161 PWMDEDELRYREEVPCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVV 240
Cdd:PRK09557 161 PWMDEDELRYRNEVPCYCGKQGCIETFISGTGFATDYRRLSGKALKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAHVI 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699304 241 NILDPDVIVLGGGMSNVDRLYQTVPQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWLWPQ 301
Cdd:PRK09557 241 NILDPDVIVLGGGMSNVDRLYPTLPALLKQYVFGGECETPVRKALHGDSSGVRGAAWLWPK 301
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
2-298 |
0e+00 |
|
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: 510.98 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 2 RIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANST 81
Cdd:cd24066 1 RIGIDLGGTKIEGIALDRAGRELLRRRVPTPRGDYEATLDAIADLVEEAEEELGAPATVGIGTPGSISPRTGLVKNANST 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 82 WLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPLP 161
Cdd:cd24066 81 WLNGKPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGANGIAGEWGHNPLP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 162 WMDEDElryREEVPCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVVN 241
Cdd:cd24066 161 WPDEDE---LPGPPCYCGKRGCVETFLSGPALERDYARLTGKTLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVIN 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699304 242 ILDPDVIVLGGGMSNVDRLYQTVPQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWL 298
Cdd:cd24066 238 ILDPDVIVLGGGLSNIDELYTEGPAALARYVFSDEVETPIVKNKHGDSSGVRGAAWL 294
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
3-301 |
2.57e-122 |
|
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: 352.03 E-value: 2.57e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTI-ETIATLVDMAEQATGQRGTVGMGIPGSISP-YTGVVKNANS 80
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEETLvDAIAFFVDSAQRKFGELIAVGIGSPGLISPkYGYITNTPNI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TWLNgQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPL 160
Cdd:pfam00480 81 GWDN-FDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGHIQL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 161 PwmdedelryREEVPCYCGKQGCIETFISGTGFATDYRRlSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVV 240
Cdd:pfam00480 160 D---------PNGPKCGCGNHGCLETIASGRALEKRYQQ-KGEDLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIANLI 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 241 NILDPDVIVLGGGMSNVDRLYQTVPQLIKQFVFGGECETPVR--KAKHGDSSGVRGAAWLWPQ 301
Cdd:pfam00480 230 NLFDPQAIVLGGGVSNADGLLEAIRSLVKKYLNGYLPVPPVIivAASLGDNAGALGAAALAKQ 292
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
1-298 |
5.49e-102 |
|
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: 300.30 E-value: 5.49e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANS 80
Cdd:cd24057 1 MYYGFDIGGTKIEFAVFDEALQLVWTKRVPTPTDDYAAFLAAIAELVAEADARFGVKGPVGIGIPGVIDPEDGTLITANI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPL 160
Cdd:cd24057 81 PAAKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 161 P---WMDEDELryrEEVPCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLA 237
Cdd:cd24057 161 PadaLLLGYDL---PVLRCGCGQTGCLETYLSGRGLERLYAHLYGEELDAPEIIAAWAAGDPQAVAHVDRWLDLLAGCLA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699304 238 HVVNILDPDVIVLGGGMSNVDRLYQTVPQLIKQFVFGGeCETP-VRKAKHGDSSGVRGAAWL 298
Cdd:cd24057 238 NILTALDPDVVVLGGGLSNFPALIAELPAALPAHLLSG-ARTPrIVPARHGDAGGVRGAAFL 298
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
1-301 |
7.81e-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: 279.86 E-value: 7.81e-94
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTP-RDDYRQTIETIATLVDMAEQATGQRG----TVGMGIPGSISPYTGVV 75
Cdd:COG1940 6 YVIGIDIGGTKIKAALVDLDGEVLARERIPTPaGAGPEAVLEAIAELIEELLAEAGISRgrilGIGIGVPGPVDPETGVV 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 76 KNANST-WLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGE 154
Cdd:COG1940 86 LNAPNLpGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANGNAGE 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 155 WGHNPLPwmdedelryREEVPCYCGKQGCIETFISGTGFATDYRRLSG-HALKGSEIIRLVEESDPVAELALRRYELRLA 233
Cdd:COG1940 166 IGHMPVD---------PDGPLCGCGNRGCLETYASGPALLRRARELGGaEKLTAEELFAAARAGDPLALEVLDEAARYLG 236
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 234 KSLAHVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVFGGECE-TPVRKAKHGDSSGVRGAAWLWPQ 301
Cdd:COG1940 237 IGLANLINLLDPEVIVLGGGVSAAgDLLLEPIREALAKYALPPAREdPRIVPASLGDDAGLLGAAALALE 306
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
1-298 |
2.92e-93 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 278.41 E-value: 2.92e-93
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANS 80
Cdd:PRK13310 1 MYYGFDIGGTKIELGVFNEKLELQWEERVPTPRDSYDAFLDAVCELVAEADQRFGCKGSVGIGIPGMPETEDGTLYAANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPL 160
Cdd:PRK13310 81 PAASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHMRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 161 PW-----MDEDELRYReevpCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKS 235
Cdd:PRK13310 161 PVdaltlLGWDAPLRR----CGCGQKGCIENYLSGRGFEWLYQHYYGEPLQAPEIIALYYQGDEQAVAHVERYLDLLAIC 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 236 LAHVVNILDPDVIVLGGGMSNVDRLYQTVPQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWL 298
Cdd:PRK13310 237 LGNILTIVDPHLVVLGGGLSNFDAIYEQLPKRLPRHLLPVARVPRIEKARHGDAGGVRGAAFL 299
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
3-298 |
3.80e-51 |
|
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: 168.41 E-value: 3.80e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRD-DYRQTIETIATLVDMAEQATGQRGT---VGMGIPGSISPYTGVVKNA 78
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEeGPEAVLDRIAELIEELLAEAGVRERilgIGIGVPGPVDPETGIVLFA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 -NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGH 157
Cdd:cd23763 81 pNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGH 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 nplpwmdedelryreevpcycgkqgcietfisgtgfatdyrrlsghalkgseiIRLVEEsdpVAELalrryelrLAKSLA 237
Cdd:cd23763 161 -----------------------------------------------------ITVLEE---AARY--------LGIGLA 176
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 238 HVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVF-GGECETPVRKAKHGDSSGVRGAAWL 298
Cdd:cd23763 177 NLINLLNPELIVLGGGVAEAgDLLLEPIREAVRRRALpPLRRRVRIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
3-296 |
8.24e-51 |
|
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: 169.43 E-value: 8.24e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKtevIALG--DAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNA-N 79
Cdd:cd24065 3 IGLDLGGTK---IAAGvvDGGRILSRLVVPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGRVRFApN 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 80 STWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGH-- 157
Cdd:cd24065 80 IPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIGHtt 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 -NPLPWMdedelryreevpCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSL 236
Cdd:cd24065 160 vLPGGPM------------CGCGLVGCLEALASGRALARDASFAYGRPMSTAELFELAQQGEPKALRIVEQAAAHLGIGL 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699304 237 AHVVNILDPDVIVLGGGMS-NVDRLYQTVPQLIKQFVfGGECETPVRKAKHGDSSGVRGAA 296
Cdd:cd24065 228 ANLQKALDPEVFVLGGGVAqVGDYYLLPVQEAARRYT-EGWHAPPLRLAHLGTDAGVIGAA 287
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
1-243 |
1.07e-50 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 167.90 E-value: 1.07e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNANS 80
Cdd:PRK13311 1 MYYGFDMGGTKIELGVFDENLQRIWHKRVPTPREDYPQLLQILRDLTEEADTYCGVQGSVGIGIPGLPNADDGTVFTANV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPL 160
Cdd:PRK13311 81 PSAMGQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRL 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 161 PWMDEDELRYR-EEVPCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHV 239
Cdd:PRK13311 161 PVDALDILGADiPRVPCGCGHRGCIENYISGRGFEWMYSHFYQHTLPATDIIAHYAAGEPKAVAHVERFMDVLAVCLGNL 240
|
....
gi 1447699304 240 VNIL 243
Cdd:PRK13311 241 LTML 244
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
3-298 |
3.72e-49 |
|
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: 165.04 E-value: 3.72e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKtevIALG---DAGEQLYRHRLPTPRDDYR-----QTIETIATLVDmAEQATGqrgtVGMGIPGSISPYTGV 74
Cdd:cd24068 3 LGIDIGGTK---IKYGlvdADGEILEKDSVPTPASKGGdaileRLLEIIAELKE-KYDIEG----IGISSAGQVDPKTGE 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 75 VKNANSTWLN--GQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTA 152
Cdd:cd24068 75 VIYATDNLPGwtGTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 153 GEWGHNPLpwmdedelrYREEVPCYCGKQGCIETFISGTGFATDYRRLSG-HALKGSEIIRLVEESDPVAELALRRYELR 231
Cdd:cd24068 155 GELGHMVV---------DPGGRPCCCGGKGCLEQYASGTALVRRVAEALGePGIDGREIFDLADAGDPLAKEVVEEFAED 225
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1447699304 232 LAKSLAHVVNILDPDVIVLGGGMSN-----VDRLYQTVPQLIKQFVFGGeceTPVRKAKHGDSSGVRGAAWL 298
Cdd:cd24068 226 LATGLANLVHIFDPEVIVIGGGISAqgelfLEELREELRKLLMPPLLDA---TKIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
3-298 |
4.83e-44 |
|
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: 152.44 E-value: 4.83e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTI-----ETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKN 77
Cdd:cd24062 3 VGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENIitdiaESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTVEV 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 78 ANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGH 157
Cdd:cd24062 83 AVNLGWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEIGH 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 NPlpwMDEDELRyreevPCYCGKQGCIETFISGTGFATDYRRLS--------------GHALKGSEIIRLVEESDPVAEL 223
Cdd:cd24062 163 IT---VNPEGGA-----PCNCGKTGCLETVASATGIVRIAREELeegkgssalrilalGGELTAKDVFEAAKAGDELALA 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699304 224 ALRRYELRLAKSLAHVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVFGGECE-TPVRKAKHGDSSGVRGAAWL 298
Cdd:cd24062 235 VVDTVARYLGLALANLANTLNPEKIVIGGGVSAAgEFLLSPVKEYFDRFTFPRVRQdTEIVLATLGNDAGVIGAAWL 311
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
3-296 |
2.60e-43 |
|
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: 150.20 E-value: 2.60e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDyRQTIETIATLVDMAeQATGQRGTVGMGIPGSISPYTGVVKNANSTW 82
Cdd:cd24061 2 IGVDIGGTKIAAGVVDEEGEILATERVPTPPTA-DGIVDAIVEAVEEL-REGHDVSAVGVAAAGFVDADRATVLFAPNIA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 83 LNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHnplpw 162
Cdd:cd24061 80 WRNEPLKDLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGH----- 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 163 mdedeLRY-REEVPCYCGKQGCIETFISGT---------------GFATDYRRLSGHALKGSEIIRLVEESDPVAELALR 226
Cdd:cd24061 155 -----IRVvPDGLLCGCGSRGCWEQYASGRalvryakeaanatpeGAAVLLADGSVDGITGKHISEAARAGDPVALDALR 229
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 227 RYELRLAKSLAHVVNILDPDVIVLGGGMS-NVDRLYQTVPQLIKQFVFGGE--CETPVRKAKHGDSSGVRGAA 296
Cdd:cd24061 230 ELARWLGAGLASLAALLDPELFVIGGGVSdAGDLLLDPIREAFERWLPGRGwrPIPRLRTAQLGNDAGLIGAA 302
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
3-296 |
2.78e-41 |
|
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: 145.02 E-value: 2.78e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTP-RDDYRQTIETIATLVDMAEQATGQRGT----VGMGIPGSISPYTGVVKN 77
Cdd:cd24076 4 IGVELGVDYITVVVTDLAGEVLWRREVPLPaSDDPDEVLAQLAALIREALAAAPDSPLgilgIGVGVPGLVDSEDGVVLL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 78 A-NSTWlNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWG 156
Cdd:cd24076 84 ApNLGW-RDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASGFAGEIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 157 HNPLpwmDEDELryreevPCYCGKQGCIETFISGTGFATDYRRLS--GHALKGSEIIRLVEESDPVAELALRRYELRLAK 234
Cdd:cd24076 163 HMTV---DPDGP------PCSCGNRGCWETYASERALLRAAGRLGagGEPLSLAELVEAARAGDPAALAALEEVGEYLGI 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699304 235 SLAHVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVF-GGECETPVRKAKHGDSSGVRGAA 296
Cdd:cd24076 234 GLANLVNTFNPELVVLGGALAPLgPWLLPPLRAEVARRALpAPARDVRIVVSRLGEDAAALGAA 297
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
1-298 |
1.55e-40 |
|
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: 142.32 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMA-EQATGqrgtVGMGIPGSISPYTGVVKNAN 79
Cdd:cd24152 1 KYLVFDIGGTFIKYALVDENGNIIKKGKIPTPKDSLEEFLDYIKKIIKRYdEEIDG----IAISAPGVIDPETGIIYGGG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 80 S-TWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHN 158
Cdd:cd24152 77 AlPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYL 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 159 PLpwmdEDELRYREEVPCYCgkqgcietfiSGTGFATDYRRLSGH-ALKGSEIIRLVEESDPVAELALRRYELRLAKSLA 237
Cdd:cd24152 157 LT----DDDDKDLLFFSGLA----------SMFGLVKRYNKAKGLePLDGEEIFEKYAKGDEAAKKILDEYIRNLAKLIY 222
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699304 238 HVVNILDPDVIVLGGGMSNVDRLYQTVPQLIKQFV---FGGECETPVRKAKHGDSSGVRGAAWL 298
Cdd:cd24152 223 NIQYILDPEVIVIGGGISEQPLFIEDLKKEVNEILanrPGSIPKPEIKACKFGNDANLLGALYN 286
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
3-296 |
1.55e-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: 142.69 E-value: 1.55e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTprDDYRQTIETIATLVDMAEQATGQRGT----VGMGIPGSISPYTGVVKNA 78
Cdd:cd24070 4 LGIDIGGTNIRIGLVDEDGKLLDFEKVPS--KDLLRAGDPVEVLADLIREYIEEAGLkpaaIVIGVPGTVDKDRRTVIST 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 -NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGH 157
Cdd:cd24070 82 pNIPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGH 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 NPLpwmdedelrYREEVPCYCGKQGCIETFISGTGFAtdyrRLSGHALKGSEIIRLVEesDPVAELALRRYELRLAKSLA 237
Cdd:cd24070 162 IPV---------YGNGKPCGCGNTGCLETYASGRALE----EIAEEHYPDTPILDIFV--DHGDEPELDEFVEDLALAIA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1447699304 238 HVVNILDPDVIVLGGGMSNV-----DRLYQTVPQLIKQFVFGGECEtpVRKAKHGDSSGVRGAA 296
Cdd:cd24070 227 TEINILDPDAVILGGGVIDMkgfprETLEEYIRKHLRKPYPADNLK--IIYAELGPEAGVIGAA 288
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
3-298 |
2.42e-40 |
|
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: 142.73 E-value: 2.42e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIeTIATLVDMAEQATGQRG----TVGMGIPGSISPYTGVVKNA 78
Cdd:TIGR00744 1 IGVDIGGTTIKLGVVDEEGNILSKWKVPTDTTPETIVD-AIASAVDSFIQHIAKVGheivAIGIGAPGPVNRQRGTVYFA 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHN 158
Cdd:TIGR00744 80 VNLDWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLGGGIIINGEIRHGHNGVGAEIGHI 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 159 PlpwMDEDelryrEEVPCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVE--------------ESDPVAELA 224
Cdd:TIGR00744 160 R---MVPD-----GRLLCNCGKQGCIETYASATGLVRYAKRANAKPERAEVLLALGDgdgisakhvfvaarQGDPVAVDS 231
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699304 225 LRRYELRLAKSLAHVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVFGGECE-TPVRKAKHGDSSGVRGAAWL 298
Cdd:TIGR00744 232 YREVARWAGAGLADLASLFNPSAIVLGGGLSDAgDLLLDPIRKSYKRWLFGGARQvADIIAAQLGNDAGLVGAADL 307
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
20-296 |
2.20e-38 |
|
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: 137.30 E-value: 2.20e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 20 AGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRGT----VGMGIPGSISPYTGVVKNA-NSTWlNGQPFDKDLSA 94
Cdd:cd24073 21 RGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPDrllgIGVGLPGLVDAETGICRWSpLLGW-RDVPLAELLEE 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 95 RLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPlpwMDEDELryreev 174
Cdd:cd24073 100 RLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIGHTT---VDPDGP------ 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 175 PCYCGKQGCIETFISGTGFATDYR--RLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVVNILDPDVIVLGG 252
Cdd:cd24073 171 PCRCGKRGCLEAYASDPAILRQAReaGLRGEPLTIEDLLAAARAGDPAARAILRRAGRALGLALANLVNLLDPELIIISG 250
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1447699304 253 -GMSNVDRLYQTVPQLIKQFVFGGEC-ETPVRKAKHGDSSGVRGAA 296
Cdd:cd24073 251 eGVRAGDLLFEPMREALRAHVFPGLAsDLELVIHPWGDEAWARGAA 296
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
3-298 |
2.42e-33 |
|
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: 123.99 E-value: 2.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRD-DYRQTIETIATLVDMAEQATGQRGTVGMGIpGSISPY---TGVVKNA 78
Cdd:cd24063 3 VAVDIGGTWIRAGLVDEDGRILLKIRQPTPKTgDPGTVSEQVLGLIETLLSKAGKDSIEGIGV-SSAGPLdlrKGTIVNS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHN 158
Cdd:cd24063 82 PNIKGKEIPLVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 159 plpWMDEDelryrEEVPCYCGKQGCIETFISGTGFATDYR-RLSGHALKGSEIIRLVEES--------------DPVAEL 223
Cdd:cd24063 162 ---VVDTE-----SGLKCGCGGYGHWEAFASGRGIPRFAReWAEGFSSRTSLKLRNPGGEgitakevfsaarkgDPLALK 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1447699304 224 ALRRYELRLAKSLAHVVNILDPDVIVLGGGM--SNVDRLYQTVPQLIKQFVFGGECEtpVRKAKHGDSSGVRGAAWL 298
Cdd:cd24063 234 IIEKLARYNGRGIANVINAYDPELIVIGGSVfnNNKDILDPLIEYLEKNPAISKGPE--IVLSELGDDVGLIGALAL 308
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
3-296 |
1.08e-29 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 114.31 E-value: 1.08e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQR-GTVGMGIPGSISPYTGVV---KNA 78
Cdd:PRK09698 7 LGIDMGGTHIRFCLVDAEGEILHCEKKRTAEVIAPDLVSGLGEMIDEYLRRFNARcHGIVMGFPALVSKDRRTVistPNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGaQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHn 158
Cdd:PRK09698 87 PLTALDLYDLADKLENTLNCPVFFSRDVNLQLLWDVKENNLTQ-QLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGH- 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 159 pLPWMDEDElryreevPCYCGKQGCIETFIsgtgfatdyrrlSGHALKgseiiRLVEESDPVA-----------ELALRR 227
Cdd:PRK09698 165 -IPLGDMTQ-------HCGCGNPGCLETNC------------SGMALR-----RWYEQQPRDYplsdlfvhagdHPFIQS 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 228 YELRLAKSLAHVVNILDPDVIVLGGG-MSNVDRLYQTVPQLIKQFVFG---GEcETPVRKAKHGDSSGVRGAA 296
Cdd:PRK09698 220 LLENLARAIATSINLFDPDAIILGGGvMDMPAFPRETLIAMIQKYLRKplpYE-VVRFIYASSSDFNGAQGAA 291
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
3-296 |
1.98e-29 |
|
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: 113.75 E-value: 1.98e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDD-YRQTIETIATLVDMAEQATGQRGtVGMGIPGSISPYTGVVKNANS- 80
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIDTKVENgKEDVINRIAETVNELIEEMELLG-IGIGSPGSIDRENGIVRFSPNf 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 -TWLNgQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGH-- 157
Cdd:cd24064 81 pDWRN-FPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAELGHvi 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 ----NPLpwmdedelryreevpCYCGKQGCIETFISGTG---FATDYRRLSGHALKGS-------EIIRLVEESDPVAEL 223
Cdd:cd24064 160 vepnGPI---------------CGCGNRGCVEAFASATAiirYARESRKRYPDSLAGEsekinakHVFDAARKNDPLATM 224
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699304 224 ALRRYELRLAKSLAHVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVFGGECET-PVRKAKHGDSSGVRGAA 296
Cdd:cd24064 225 VFRRVVDALAIAIGGFVHIFNPEIIIIGGGISRAgSFLLDPIREKTKKYVMLSFQDTySIELSNLVEDAGILGAA 299
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
5-298 |
1.63e-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: 102.75 E-value: 1.63e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 5 IDLGGTKTEViALGDAGEQLYRHRLPTPRDDYRQTIetIATLVDMAEQATGQRGTVGMGIPGSISpyTGVVK--NANSTW 82
Cdd:cd24069 3 IDIGGTKIAA-ALIGNGQIIDRRQIPTPRSGTPEAL--ADALASLLADYQGQFDRVAVASTGIIR--DGVLTalNPKNLG 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 83 -LNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHNPlp 161
Cdd:cd24069 78 gLSGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTL-- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 162 wMDEDELRyreevpCYCGKQGCIETFISGTGFATDYRRLSGHALKGSEIIRLVEESDPVAELALRRYELRLAKSLAHVVN 241
Cdd:cd24069 156 -ADPPGPV------CGCGRRGCVEAIASGTAIAAAASEILGEPVDAKDVFERARSGDEEAARLIDRAARALADLIADLKA 228
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699304 242 ILDPDVIVLGGGMSN----VDRLYQTVPQLIKQFvfggecETPVRKAKHGDSSGVRGAAWL 298
Cdd:cd24069 229 TLDLDCVVIGGSVGLaegfLERVEQYLADEPAIF------RVSLEPARLGQDAGLLGAALL 283
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
5-270 |
2.22e-25 |
|
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.
Pssm-ID: 466910 [Multi-domain] Cd Length: 305 Bit Score: 102.88 E-value: 2.22e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 5 IDLGGTKTEVIALGDAGEQLYRHRLPTPRDdYRQTIETIATLVDMAEQATGQRG--TVGMGIP--GSISPYTGVVknANS 80
Cdd:cd24060 5 VDLGGTNLRVAIVSMKGEIVKKYTQPNPKT-YEERIDLILQMCVEAASEAVKLNcrILGVGIStgGRVNPREGIV--LHS 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TWL----NGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWG 156
Cdd:cd24060 82 TKLiqewSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHGSSFCAAELG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 157 HNPLPwMDEDElryreevpCYCGKQGCIETFISGTGFATDYRRL--------SGHALKGSEII---RLVEES---DPVAE 222
Cdd:cd24060 162 HIVVS-LDGPD--------CMCGSHGCVEAYASGMALQREAKKLhdedlllvEGMSVTNDEEVtakHLIQAAklgNAKAQ 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1447699304 223 LALRRYELRLAKSLAHVVNILDPDVIVLGGGMSNvdrLYQT-VPQLIKQ 270
Cdd:cd24060 233 KILRTAGTALGLGIVNILHTLNPSLVILSGVLAS---HYENiVKDVIAQ 278
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
3-252 |
2.33e-24 |
|
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as a repressor of the nagEBACD operon involved in the uptake and degradation of the amino sugars, N-acetyl-D-glucosamine (GlcNAc) and glucosamine (GlcN). It acts both as an activator and a repressor for the transcription of the glmSU operon, encoding proteins necessary for the synthesis of GlcN (glmS) and the formation of UDP-GlcNAc (glmU). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466925 [Multi-domain] Cd Length: 315 Bit Score: 100.13 E-value: 2.33e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYR----QTIETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNA 78
Cdd:cd24075 4 LAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEallsQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVHYM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWGHn 158
Cdd:cd24075 84 PHIQVKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEIGH- 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 159 plpwMDEDELRYReevpCYCGKQGCIETFISG------------TGFATdyrRLSGHALKGSEIIRLVEESDPVAELALR 226
Cdd:cd24075 163 ----IQIEPLGER----CHCGNFGCLETVASNaaieqrvkkllkQGYAS---QLTLQDCTIKDICQAALNGDQLAQDVIK 231
|
250 260
....*....|....*....|....*.
gi 1447699304 227 RYELRLAKSLAHVVNILDPDVIVLGG 252
Cdd:cd24075 232 RAGRYLGKVIAILINLLNPQKIIIAG 257
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
3-296 |
2.61e-24 |
|
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: 99.97 E-value: 2.61e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEViALGDA-GEQLYRHRLPTPRDDYR-QTIETIATLVD-MAEQATGQR--GTVGMGIPGSISPYTGVVKN 77
Cdd:cd24059 4 IGVEIGRDLLSA-VLCDLsGNILAREKYPLDEKENPeEVLEKLYELIDrLLEKENIKSkiLGIGIGAPGPLDVEKGIILN 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 78 ANSTWLNGQ-PFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEWG 156
Cdd:cd24059 83 PPNFPGWENiPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGEIG 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 157 HNPLpwmdedelrYREEVPCYCGKQGCIETFISGTGFATDYRRLSGHAL-KGSEIIRLVEESDPVAELALRRYELRLAKS 235
Cdd:cd24059 163 HTSI---------DINGPRCSCGNRGCLELYASIPAIEKKARSALGSGRsFQLDIVEALQKGDPIADEVIEEAAKYLGIG 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 236 LAHVVNILDPDVIVLGGGMSNV-DRLYQTVPQLIKQFVFG-GECETPVRKAKHGDSSGVRGAA 296
Cdd:cd24059 234 LVNLINLLNPEAIIIGGELIYLgERYLEPIEKEVNSRLFGrNAREVRILKSSLGEDAPLLGAA 296
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
1-270 |
5.93e-24 |
|
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies protein, acts as a transcriptional repressor that regulates the expression of proteins that are part of the phosphotransferase system for sugar uptake. It regulates the expression of malT. Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466924 [Multi-domain] Cd Length: 322 Bit Score: 99.31 E-value: 5.93e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 1 MRIGidlGGTKTevIALGD-AGEQLYRHRLPTPRDDYRQTIETIATLVD---MAEQATGQRGT-VGMGIPGSISPYTGVV 75
Cdd:cd24074 7 IRIG---RGYIT--LALRDlNGRLLAEERYPLPAKDNDPFLDRLLESISeffSRHQKKLERLTaIAITLPGIIDPESGIV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 76 KNANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEW 155
Cdd:cd24074 82 HRLPFYDIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGEL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 156 GHNPLPwmdedelryREEVPCYCGKQGCIETFISGTGFATDYR----RLSGHALKGSEI-IR----LVEESDPVAELALR 226
Cdd:cd24074 162 GHTQID---------PYGKRCYCGNHGCLETVASIPAILEQANqlleQSPDSMLHGQPIsIEslcqAALAGDPLAQDIII 232
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1447699304 227 RYELRLAKSLAHVVNILDPDVIVLGGGMSNVDR-LYQTVPQLIKQ 270
Cdd:cd24074 233 QVGRHLGRILAILVNLFNPEKILIGSPLNNAAEiLFPALSQSIRQ 277
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
60-298 |
9.42e-24 |
|
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: 98.51 E-value: 9.42e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 60 VGMGIPGSISPYTGVVKNanSTWLNGQ--PFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAG 137
Cdd:cd24071 65 IGIAVSGLVDSKKGIVIR--STILGWEnvELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSS 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 138 VAFNGRAHIGGNGTAGEWGHNPLpwmdedelrYREEVPCYCGKQGCIETFISGTGFATDYRRLSGHALKG---------- 207
Cdd:cd24071 143 LVIDGKLYTGNFGGAGEIGHMTI---------QPDGRKCYCGQKGCLEAYASFEALVNEIKELTESYPLSllkeledfei 213
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 208 SEIIRLVEESDPVAELALRRYELRLAKSLAHVVNILDPDVIVLGG-GMSNVDRLYQTVPQLIKQFVFG-GECETPVRKAK 285
Cdd:cd24071 214 EKVREAAEEGDSVATELFKKAGEYLGIGIKNLINIFNPEAIIIGGeGLEFKDYFLPKIIEIAKENFFGkAGRNVIILVDS 293
|
250
....*....|...
gi 1447699304 286 HGDSSGVRGAAWL 298
Cdd:cd24071 294 LGEDAWVLGAALL 306
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
60-281 |
1.12e-23 |
|
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: 98.26 E-value: 1.12e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 60 VGMGIPGSISPYTGVVKNANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVA 139
Cdd:cd24072 63 IALAIQGLVDSHKGVSLWSPGAPWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIV 142
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 140 FNGRAHIGGNGTAGEWGHNPlpwMDEDELRyreevpCYCGKQGCIETFISGTGFATDYR---RLSGHALKGSEI-----I 211
Cdd:cd24072 143 IDNKLYIGASSGSGEIGHTK---VNPDGAR------CDCGRRGCLETVASNSALKRNARvtlKLGPVSADPEKLtmeqlI 213
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699304 212 RLVEESDPVAELALRRYELRLAKSLAHVVNILDPDVIVL-GGGMSNVDRLYQTVPQLIKQFVFGGECETPV 281
Cdd:cd24072 214 EALEEGEPIATQIFDRAANAIGRSLANILNLLNPEQVLLyGRGCRAGDLLLPAIRRAIAENPFSQHATQIG 284
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
3-271 |
5.45e-21 |
|
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: 90.68 E-value: 5.45e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLV-DMAEQATGQR-GTVGMGIpgSISpytGVVKNANS 80
Cdd:cd24077 4 IGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIqELISQAPKTPyGLVGIGI--GIH---GIVDENEI 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 81 TW-----LNGQPFDKDLSARLQREVRLANDANCLAVSEAVdgAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTAGEW 155
Cdd:cd24077 79 IFtpyydLEDIDLKEKLEEKFNVPVYLENEANLSALAERT--FSEDYDNLISISIHSGIGAGIIINNQLYRGYNGFAGEI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 156 GHNPLpwmdedelrYREEVPCYCGKQGCIETFISGTGFATDYRRLSG-HALKGSEIIRLVEESDPVAELALRRYELRLAK 234
Cdd:cd24077 157 GHMII---------VPNGKPCPCGNKGCLEQYASEKALLKELSEKKGlETLTFDDLIQLYNEGDPEALELIDQFIKYLAI 227
|
250 260 270
....*....|....*....|....*....|....*..
gi 1447699304 235 SLAHVVNILDPDVIVLGGgmsnvdRLYQTVPQLIKQF 271
Cdd:cd24077 228 GINNIINTFNPEIIIINS------SLINEIPELLEKI 258
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
4-299 |
7.94e-20 |
|
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: 86.08 E-value: 7.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 4 GIDLGGT--KTEVIALGDAGEQLYRHRLPTPRDDY-RQTIETIATLVdmaeQATGQRGTVGMGIPGSISpyTGVVK---N 77
Cdd:cd24058 3 GIDIGGSgiKGAIVDTDTGELLSERIRIPTPQPATpEAVADVVAELV----AHFPWFGPVGVGFPGVVR--RGVVRtaaN 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 78 ANSTWLnGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAG-AQTVFAVIIGTGCGAGVAFNGRA--HIggngtagE 154
Cdd:cd24058 77 LDKSWI-GFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGeKGVVLVLTLGTGIGSALFVDGHLvpNT-------E 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 155 WGHNPlpwMDEDElryreevpcycgkqgcietfisgtgfATDYRRLSGHALKgseiirlveesdpvaELALRRYELRLAK 234
Cdd:cd24058 149 LGHLE---IRGKD--------------------------AEERASLGVRARE---------------DLGWKRWAKRVNK 184
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1447699304 235 SLAHVVNILDPDVIVLGGGMSnvdrlyqtvpQLIKQFVFGGECETPVRKAKHGDSSGVRGAAWLW 299
Cdd:cd24058 185 YLQYLERLFNPDLFIIGGGNS----------KKADKFLPLLDVKTPVVPAVLRNDAGIVGAALLA 239
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
5-302 |
3.47e-15 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 74.18 E-value: 3.47e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 5 IDLGGTKTEVIALGDAGEQLYRHRLPTPR----DDYRQTIETIAT-LVDMAEQ-ATGQRGTVGMGIPGSISPytgvvknA 78
Cdd:PRK05082 6 IDIGGTKIAAALVGEDGQIRQRRQIPTPAsqtpEALRQALSALVSpLQAQADRvAVASTGIINDGILTALNP-------H 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 79 NSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFaVIIGTGCGAGVAFNGRAHIGGNGTAGEWGH- 157
Cdd:PRK05082 79 NLGGLLHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDIRNMVF-ITVSTGVGGGIVLNGKLLTGPGGLAGHIGHt 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 -----NPLpwmdedelryreevpCYCGKQGCIETFISGTGFATDYRRLSGhALKGSEIIRLVEESDPVAELALRRYELRL 232
Cdd:PRK05082 158 ladphGPV---------------CGCGRRGCVEAIASGRAIAAAAQGWLA-GCDAKTIFERAGQGDEQAQALINRSAQAI 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 233 AKSLAHVVNILDPDVIVLGGGMSNVDRLYQTVPQLIKQfvFGGECETPVRKAKHGDSSGVRGAAWlWPQE 302
Cdd:PRK05082 222 ARLIADLKATLDCQCVVLGGSVGLAEGYLELVQAYLAQ--EPAIYHVPLLAAHYRHDAGLLGAAL-WAQG 288
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
4-298 |
5.50e-12 |
|
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: 64.87 E-value: 5.50e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 4 GIDLGGTKTeVIALGDAGEQLY-RHRLPT--PRddyrqtiETIATLVDMAEQATGQRGTVGMGIPGSI-----SPYTGVV 75
Cdd:cd24067 3 GIEAGGTKF-VCAVGTGDGNIIeRTEFPTttPE-------ETLQAVIDFFREQEEPIDAIGIASFGPIdlnptSPTYGYI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 76 KNANSTWLNGQPFDKDLSARLQREVRLANDANCLAVSEAVDGAAAGAQTVFAVIIGTGCGAGVAFNGRAHIGGNGTagEW 155
Cdd:cd24067 75 TTTPKPGWRNFDILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP--EM 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 156 GHNPLPwMDEDELRYrEEVPCYCGkqGCIETFISGTGFAtdyRRLSghaLKGSEIirlvEESDPVAELAlRRYelrLAKS 235
Cdd:cd24067 153 GHIRVP-RHPDDDGF-PGVCPFHG--DCLEGLASGPAIA---ARWG---IPAEEL----PDDHPAWDLE-AYY---LAQA 214
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1447699304 236 LAHVVNILDPDVIVLGGGMSN----VDRLYQTVPQLIKQFVFGGECETPVRK----AKHGDSSGVRGAAWL 298
Cdd:cd24067 215 CANLTLTLSPERIVLGGGVMQrpglFPRIREKFRKLLNGYLEVPRLLPDIDEyivpPALGNDAGILGALAL 285
|
|
| ASKHA_NBD_GLK |
cd24008 |
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7. ... |
2-298 |
1.43e-10 |
|
nucleotide-binding domain (NBD) of glucokinase (GLK) and similar proteins; Glucokinase (EC 2.7.1.2), also called glucose kinase, acts as an ATP-dependent kinase that phosphorylates glucose using ATP as a donor to give glucose-6-phosphate and ADP. Glucokinases are mainly found in invertebrates and microorganisms and highly specific for glucose. Glucokinases belong to the ASKHA (Acetate and Sugar Kinases/Hsc70/Actin) superfamily, all members of which share a common characteristic five-stranded beta sheet occurring in both the N- and C-terminal domains.
Pssm-ID: 466858 [Multi-domain] Cd Length: 313 Bit Score: 61.09 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 2 RIGIDLGGTKTEvIALGDA----GEQLYRHRLPTprDDYRQTIETIATLvdMAEQATGQRGTVGMGIPGSISPytGVVKN 77
Cdd:cd24008 1 ILVGDIGGTNAR-LALADAgdgsGDLLFVRKYPS--ADFASLEDALAAF--LAELGAPRPKAACIAVAGPVDG--GRVRL 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 78 ANSTWlngqPFD-KDLSARL-QREVRLAND--ANCLAVS-------EAVDGAAAGAQTVFAVIIGTGCGAGVAFngrAHI 146
Cdd:cd24008 74 TNLDW----SIDaAELRKALgIGRVRLLNDfeAAAYGLPalgpedlLVLYGGGGPLPGGPRAVLGPGTGLGVAL---LVP 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 147 GGNGT----AGEWGHNPLPWMDEDELRYREEVPCYCGKQGCIETFISGTGFATDYRRLSGHA------LKGSEIIRLVEE 216
Cdd:cd24008 147 DGDGGyvvlPSEGGHADFAPVTEEEAELLEFLRKRFGRSVSYEDVLSGPGLENIYEFLAKLDgaeppdLTAEEIAEAALA 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 217 SDPVAELALRR-YEL--RLAKSLAhvVNILDPDVIVLGGG--MSNVDRLYQtvPQLIKQFVFGGEC-----ETPVRKAKH 286
Cdd:cd24008 227 GDPLAREALDLfARIlgRFAGNLA--LSFLATGGVYLAGGiaPKNLDLLDS--SAFREAFLDKGRMsdlleDIPVYLVTN 302
|
330
....*....|..
gi 1447699304 287 gDSSGVRGAAWL 298
Cdd:cd24008 303 -EDLGLLGAAAY 313
|
|
| BadF |
COG2971 |
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and ... |
3-165 |
1.22e-07 |
|
BadF-type ATPase, related to human N-acetylglucosamine kinase [Carbohydrate transport and metabolism];
Pssm-ID: 442210 [Multi-domain] Cd Length: 298 Bit Score: 52.19 E-value: 1.22e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPT--PRD-DYRQTIETIATLVDMAEQATGQRGT---VGMGIPGSISPY-TGVV 75
Cdd:COG2971 4 LGVDGGGTKTRAVLVDADGEVLGRGRAGGanPQSvGLEEALASLREALEEALAAAGDPADieaVGFGLAGAGTPEdAEAL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 76 KNANStwlngqpfdkdlSARLQREVRLANDANCLAVseavdgAAAGAQTVFAVIIGTG-CGAGVAFNGRAH-IGGngtag 153
Cdd:COG2971 84 EAALR------------ELFPFARVVVVNDALAALA------GALGGEDGIVVIAGTGsIAAGRDGDGRTArVGG----- 140
|
170
....*....|..
gi 1447699304 154 eWGHnplPWMDE 165
Cdd:COG2971 141 -WGY---LLGDE 148
|
|
| ASKHA_NBD_eukNAGK-like |
cd24007 |
nucleotide-binding domain (NBD) of the eukaryotic-type N-acetylglucosamine kinase (NAGK) ... |
3-157 |
9.35e-06 |
|
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: 46.14 E-value: 9.35e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTIETIATLVDMAEQATGQRG------TVGMGIPG-SISPYTGVV 75
Cdd:cd24007 2 LGVDGGGTKTRAVLADEDGKILGRGKGGPSNPASVGIEEAKENLKEAVREALSQAGslgeidAICLGLAGiDSEEDRERL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 76 KNANSTWLNGQPfdkdlsarlqreVRLANDANCLAVseavdgAAAGAQTVFAVIIGTGCGAgVAFNGR---AHIGGngta 152
Cdd:cd24007 82 RSALKELFLSGR------------IIIVNDAEIALA------AALGGGPGIVVIAGTGSVA-YGRNGDgeeARVGG---- 138
|
....*
gi 1447699304 153 geWGH 157
Cdd:cd24007 139 --WGH 141
|
|
| Glucokinase |
pfam02685 |
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes ... |
6-225 |
4.54e-05 |
|
Glucokinase; This is a family of glucokinases or glucose kinases EC:2.7.1.2. These enzymes phosphorylate glucose using ATP as a donor to give glucose-6-phosphate and ADP.
Pssm-ID: 397005 Cd Length: 314 Bit Score: 44.48 E-value: 4.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 6 DLGGTKTE---VIALGDAGEQLYRHRLPTprDDYrqtietiATLVDMAEQATGQRGTVG------MGIPGSISpyTGVVK 76
Cdd:pfam02685 4 DIGGTNARfalVTASGGEPQPLSIRTYAS--ADY-------PSLEEAIQDYLAEDAGVTqprhacFAVAGPVD--GDRVR 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 77 NANSTWlngqPFD-KDLSARLQ-REVRLANDANCLAVSEAVDGAA------AGAQTVFA--VIIGTGCGAGVAF---NGR 143
Cdd:pfam02685 73 LTNLPW----VISiEELRATLGlDAVLLINDFEAVAYAIPRLGADdlvqlgGGKPDPGAprAVLGPGTGLGVAGlipRGG 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 144 AHIggnGTAGEWGHNPLPWMDEDE---LRY----REEVPcycgkqgcIETFISGTGFATDYRRLSGH------ALKGSEI 210
Cdd:pfam02685 149 RWI---VLPGEGGHVDFAPRSEREielLRYlrrrFGHVS--------AERVLSGPGLVNLYRALCALdgitpeLLTPADI 217
|
250
....*....|....*.
gi 1447699304 211 -IRLVEESDPVAELAL 225
Cdd:pfam02685 218 tAAALAGDDPLAREAL 233
|
|
| Hydant_A_N |
pfam05378 |
Hydantoinase/oxoprolinase N-terminal region; This family is found at the N-terminus of the ... |
2-63 |
1.87e-03 |
|
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: 38.42 E-value: 1.87e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1447699304 2 RIGIDLGGTKTEVIALGDAGEQLYRHRLPTPRDDYRQTI-ETIATLVDMAEQATGQRGTVGMG 63
Cdd:pfam05378 1 RIGIDVGGTFTDAVALDEGDGEVAVIKVLTTPDDPVEGIrEALEELLGELGPRTGKVDTVRHG 63
|
|
| BcrAD_BadFG |
pfam01869 |
BadF/BadG/BcrA/BcrD ATPase family; This family includes the BadF and BadG proteins that are ... |
3-296 |
2.16e-03 |
|
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: 38.87 E-value: 2.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAGEQLYRHR-LPTPRDDYRQTiETIATLVDMAEQATGQRGTVGMGIPGSISPYTGVVKNanst 81
Cdd:pfam01869 1 LGIDGGSTKTKAVLMDDDGEVLGRAIaGSANFESVGVE-AAERNLKDAITEALEEAGLKLDDIEYMFLGLTGYGRA---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 82 wLNGQPFDKDLSarlQREVRLAND-ANCLAvseavdGAAAGAQTVFaVIIGTGCgAGVAFNGR--AHIGGNG-TAGEWGH 157
Cdd:pfam01869 76 -GVDGHFGKDIV---REEITVHADgAVALA------PGTRGEDGVI-DIGGTGS-KVIGLDGGkvVRFGGNGqCAGGEGS 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 158 npLPWMDEDELRYREEvpcycgKQGCI--ETFISGTGFATDYRRLSG----HALKGSEI-IRLVEESdpVAELALRryel 230
Cdd:pfam01869 144 --FLEIAARALGAVVR------ELDGLapKTTLNKGAINSTCAVFAEqvviNALSGGETaEDILAGA--ARSIALR---- 209
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1447699304 231 rlAKSLAHVVNIlDPDVIVLGGGMSNVDRLYQTVPQLIKQFVFGGECETPVrkakHGDSSGVRGAA 296
Cdd:pfam01869 210 --VAALAKRLGF-VPDEVVLTGGVAKNAGLVKALRDYLKENILGVKVNVHP----DPQYAGAIGAA 268
|
|
| ASKHA_NBD_DdNAGK-like |
cd24081 |
nucleotide-binding domain (NBD) of Dictyostelium discoideum N-acetyl-D-glucosamine kinase ... |
3-156 |
7.82e-03 |
|
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: 37.30 E-value: 7.82e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 3 IGIDLGGTKTEVIALGDAG---EQLYRHRLPTPRDDY--------RQTIE-TIATLVDmaeQATGQRGTVG---MGIPGS 67
Cdd:cd24081 2 LGIDGGGTKTTCVAVDAATlgdNLLVLGRAVAGSSNYnsvgeeaaRRAIEeAIAGALK---QAGVPRSAVRavcLGISGV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1447699304 68 ISPY-TGVVKNanstWLNgQPFDKDlsarlqREVRLANDAnclavSEAVDGAAAGAQTVFAVIIGTGCGA-GVAFNGR-A 144
Cdd:cd24081 79 DRPAdAERVRS----WLR-ELFPEN------VKVFVFNDA-----VAALASGTAGKLHGCVLIAGTGTIAyGFNEDGKrA 142
|
170
....*....|...
gi 1447699304 145 HIGGNGTA-GEWG 156
Cdd:cd24081 143 RAGGWGPLlGDRG 155
|
|
| |
