|
Name |
Accession |
Description |
Interval |
E-value |
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
84-406 |
0e+00 |
|
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: 534.97 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 84 AWHYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDSPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGI 163
Cdd:cd24074 1 GWQFLSIRIGRGYITLALRDLNGRLLAEERYPLPAKDNDPFLDRLLESISEFFSRHQKKLERLTAIAITLPGIIDPESGI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 164 VHRMPFYeDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLV 243
Cdd:cd24074 81 VHRLPFY-DIKNLPLGEALEQHTGLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 244 EIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHGQPLTVDSLCQAALRGDLLAKDIITGVGAHVG 323
Cdd:cd24074 160 ELGHTQIDPYGKRCYCGNHGCLETVASIPAILEQANQLLEQSPDSMLHGQPISIESLCQAALAGDPLAQDIIIQVGRHLG 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 324 RILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAALVKDAMYNGSLLIRL 403
Cdd:cd24074 240 RILAILVNLFNPEKILIGSPLNNAAEILFPALSQSIRQQSLPAYSQHLQIESTKFYNDGTMPGAALIKDALYDGSLLLKL 319
|
...
gi 446147402 404 LQG 406
Cdd:cd24074 320 LQG 322
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
86-400 |
2.45e-100 |
|
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: 300.82 E-value: 2.45e-100
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 86 HYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDSPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIVH 165
Cdd:cd24075 2 HILAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINPKTGVVH 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 166 RMPFYEdVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEI 245
Cdd:cd24075 82 YMPHIQ-VKSWPIVEELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 246 GHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHGQPLTVDSLCQAALRGDLLAKDIITGVGAHVGRI 325
Cdd:cd24075 161 GHIQIEPLGERCHCGNFGCLETVASNAAIEQRVKKLLKQGYASQLTLQDCTIKDICQAALNGDQLAQDVIKRAGRYLGKV 240
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147402 326 LAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAALVKDAMYNGSLL 400
Cdd:cd24075 241 IAILINLLNPQKIIIAGEITQADKVLLPVIKKCIQSQALPDFRQELKIVASQLDHNSAIGAFALVKRALLEGGLL 315
|
|
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
82-390 |
3.11e-83 |
|
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: 256.75 E-value: 3.11e-83
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 82 TEAWHYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDSP-LLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTE 160
Cdd:COG1940 2 PDAGYVIGIDIGGTKIKAALVDLDGEVLARERIPTPAGAGPEaVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDPE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 161 NGIVHRMPFYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSS 240
Cdd:COG1940 82 TGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGANG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 241 SLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNqsmssmlhGQPLTVDSLCQAALRGDLLAKDIITGVGA 320
Cdd:COG1940 162 NAGEIGHMPVDPDGPLCGCGNRGCLETYASGPALLRRARELGG--------AEKLTAEELFAAARAGDPLALEVLDEAAR 233
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 321 HVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAALV 390
Cdd:COG1940 234 YLGIGLANLINLLDPEVIVLGGGVSAAGDLLLEPIREALAKYALPPAREDPRIVPASLGDDAGLLGAAAL 303
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
86-388 |
1.01e-68 |
|
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: 219.38 E-value: 1.01e-68
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 86 HYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDS-PLLDRIISHIDqFFIRHQKKLERLTSIAITLPGIIDTENGIV 164
Cdd:cd24059 2 YVIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPeEVLEKLYELID-RLLEKENIKSKILGIGIGAPGPLDVEKGII 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 165 HRMPFYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVE 244
Cdd:cd24059 81 LNPPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDGYAGE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 245 IGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHgqpltvdsLCQAALRGDLLAKDIITGVGAHVGR 324
Cdd:cd24059 161 IGHTSIDINGPRCSCGNRGCLELYASIPAIEKKARSALGSGRSFQLD--------IVEALQKGDPIADEVIEEAAKYLGI 232
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 446147402 325 ILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAA 388
Cdd:cd24059 233 GLVNLINLLNPEAIIIGGELIYLGERYLEPIEKEVNSRLFGRNAREVRILKSSLGEDAPLLGAA 296
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
85-367 |
1.63e-64 |
|
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: 208.56 E-value: 1.63e-64
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 85 WHYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDSPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIV 164
Cdd:cd24073 1 AYVVGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVDAETGIC 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 165 HRMPFY--EDVkemPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSL 242
Cdd:cd24073 81 RWSPLLgwRDV---PLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 243 VEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQsmssmlhGQPLTVDSLCQAALRGDLLAKDIITGVGAHV 322
Cdd:cd24073 158 GEIGHTTVDPDGPPCRCGKRGCLEAYASDPAILRQAREAGLR-------GEPLTIEDLLAAARAGDPAARAILRRAGRAL 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 446147402 323 GRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAY 367
Cdd:cd24073 231 GLALANLVNLLDPELIIISGEGVRAGDLLFEPMREALRAHVFPGL 275
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
85-388 |
1.96e-60 |
|
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: 197.79 E-value: 1.96e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 85 WHYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDD-SPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGI 163
Cdd:cd24076 1 GAVIGVELGVDYITVVVTDLAGEVLWRREVPLPASDDpDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGLVDSEDGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 164 VHRMPF--YEDVkemPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHaGSSS 241
Cdd:cd24076 81 VLLAPNlgWRDV---PLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYR-GASG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 242 LV-EIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQsmssmlhGQPLTVDSLCQAALRGDLLAKDIITGVGA 320
Cdd:cd24076 157 FAgEIGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAG-------GEPLSLAELVEAARAGDPAALAALEEVGE 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147402 321 HVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAA 388
Cdd:cd24076 230 YLGIGLANLVNTFNPELVVLGGALAPLGPWLLPPLRAEVARRALPAPARDVRIVVSRLGEDAAALGAA 297
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
118-388 |
2.50e-50 |
|
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: 171.70 E-value: 2.50e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 118 LKDDSPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIVhrmpfYEDV----KEMPLGEALEQHTGVPVYIQ 193
Cdd:cd24062 34 LEGGENIITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTV-----EVAVnlgwKNFPLKDKLEALTGIPVVID 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 194 HDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPY-GKRCYCGNHGCLETIASVD 272
Cdd:cd24062 109 NDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGEIGHITVNPEgGAPCNCGKTGCLETVASAT 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 273 SILELAQLRLNQS-----MSSMLHGQPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKA 347
Cdd:cd24062 189 GIVRIAREELEEGkgssaLRILALGGELTAKDVFEAAKAGDELALAVVDTVARYLGLALANLANTLNPEKIVIGGGVSAA 268
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 446147402 348 ADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAA 388
Cdd:cd24062 269 GEFLLSPVKEYFDRFTFPRVRQDTEIVLATLGNDAGVIGAA 309
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
86-390 |
2.84e-49 |
|
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: 169.00 E-value: 2.84e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 86 HYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDSP-LLDRIISHIDQFfIRHQKKLERLTSIAITLPGIIDTENGIV 164
Cdd:cd24071 2 YIIGVKIEEGYLVLALTDLKGKILEKTRIPFDHETDPEkVIELIAENIKKL-IKNKHVEKKLLGIGIAVSGLVDSKKGIV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 165 HRMPF--YEDVkemPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSL 242
Cdd:cd24071 81 IRSTIlgWENV---ELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGA 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 243 VEIGHTQVDPYGKRCYCGNHGCLETIASVDSI-LELAQLRLNQSMSSMLHGQPLTVDSLCQAALRGDLLAKDIITGVGAH 321
Cdd:cd24071 158 GEIGHMTIQPDGRKCYCGQKGCLEAYASFEALvNEIKELTESYPLSLLKELEDFEIEKVREAAEEGDSVATELFKKAGEY 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446147402 322 VGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAALV 390
Cdd:cd24071 238 LGIGIKNLINIFNPEAIIIGGEGLEFKDYFLPKIIEIAKENFFGKAGRNVIILVDSLGEDAWVLGAALL 306
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
88-392 |
4.21e-49 |
|
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: 168.29 E-value: 4.21e-49
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 88 LSLRISRGEIFLALRDLSSKlVVEEAQELALKDDSPllDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDTENGIVHRM 167
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGE-ILARERVPTPTTTTE--ETLVDAIAFFVDSAQRKFGELIAVGIGSPGLISPKYGYITNT 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 168 PfYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGH 247
Cdd:pfam00480 78 P-NIGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAGEIGH 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 248 TQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNqsmssmlhgqPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILA 327
Cdd:pfam00480 157 IQLDPNGPKCGCGNHGCLETIASGRALEKRYQQKGE----------DLEGKDIIVLAEQGDEVAEEAVERLARYLAKAIA 226
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446147402 328 IMVNLFNPQKILIGSPLSkAADILFPVISDSIRQQAL-PAYSQHISVESTQFSNQGTMAGAA-LVKD 392
Cdd:pfam00480 227 NLINLFDPQAIVLGGGVS-NADGLLEAIRSLVKKYLNgYLPVPPVIIVAASLGDNAGALGAAaLAKQ 292
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
117-389 |
1.75e-44 |
|
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: 156.18 E-value: 1.75e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 117 ALKDDSPLLDRIISHIDQFfirhqKKLERLTSIAITLPGIIDTENGIVHR----MPFYedvKEMPLGEALEQHTGVPVYI 192
Cdd:cd24068 33 ASKGGDAILERLLEIIAEL-----KEKYDIEGIGISSAGQVDPKTGEVIYatdnLPGW---TGTNLKEELEERFGLPVAV 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 193 QHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLETIASVD 272
Cdd:cd24068 105 ENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMVVDPGGRPCCCGGKGCLEQYASGT 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 273 SILELAQLRLNQSmssmlhgqPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILF 352
Cdd:cd24068 185 ALVRRVAEALGEP--------GIDGREIFDLADAGDPLAKEVVEEFAEDLATGLANLVHIFDPEVIVIGGGISAQGELFL 256
|
250 260 270
....*....|....*....|....*....|....*..
gi 446147402 353 PVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAAL 389
Cdd:cd24068 257 EELREELRKLLMPPLLDATKIEPAKLGNDAGLLGAAY 293
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
144-388 |
7.10e-44 |
|
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: 154.58 E-value: 7.10e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 144 ERLTSIAITLPGIIDTENGIVHRMPFYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHN 223
Cdd:cd24064 54 MELLGIGIGSPGSIDRENGIVRFSPNFPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTG 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 224 VGAGVITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSmLHGQPLTVDS--LC 301
Cdd:cd24064 134 VGSGVICHGQLLTGYDGIAAELGHVIVEPNGPICGCGNRGCVEAFASATAIIRYARESRKRYPDS-LAGESEKINAkhVF 212
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 302 QAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQ 381
Cdd:cd24064 213 DAARKNDPLATMVFRRVVDALAIAIGGFVHIFNPEIIIIGGGISRAGSFLLDPIREKTKKYVMLSFQDTYSIELSNLVED 292
|
....*..
gi 446147402 382 GTMAGAA 388
Cdd:cd24064 293 AGILGAA 299
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
92-390 |
4.25e-43 |
|
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: 150.69 E-value: 4.25e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 92 ISRGEIFLALRDLSSKLVVEEAQELALKDDSP-LLDRIISHIDQFfIRHQKKLERLTSIAITLPGIIDTENGIVHRMPFY 170
Cdd:cd23763 5 IGGTKIRAALVDLDGEILARERVPTPAEEGPEaVLDRIAELIEEL-LAEAGVRERILGIGIGVPGPVDPETGIVLFAPNL 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 171 EDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQV 250
Cdd:cd23763 84 PWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIGHITV 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 251 dpygkrcycgnhgcletiasvdsilelaqlrlnqsmssmlhgqpltvdslcqaalrgdllakdiITGVGAHVGRILAIMV 330
Cdd:cd23763 164 ----------------------------------------------------------------LEEAARYLGIGLANLI 179
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 331 NLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAALV 390
Cdd:cd23763 180 NLLNPELIVLGGGVAEAGDLLLEPIREAVRRRALPPLRRRVRIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
86-388 |
2.86e-41 |
|
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: 147.95 E-value: 2.86e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 86 HYLSLRISRGEIFLALRDLSSKLVVEEaqELALKDDSP---LLDRIISHIDQffiRHQKKLERLTSIAITLPGIIDTENG 162
Cdd:cd24072 2 WVLGIVVSPNSLRAQVGNACGELLGEF--EYRVITLETpeaLIDEIIDCIDR---LLKLWKDRVKGIALAIQGLVDSHKG 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 163 IVHRMPFYEDVkEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSL 242
Cdd:cd24072 77 VSLWSPGAPWR-NIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASSGS 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 243 VEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQLRLnQSMSSMLHGQPLTVDSLCQAALRGDLLAKDIITGVGAHV 322
Cdd:cd24072 156 GEIGHTKVNPDGARCDCGRRGCLETVASNSALKRNARVTL-KLGPVSADPEKLTMEQLIEALEEGEPIATQIFDRAANAI 234
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446147402 323 GRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRQQALPAYSQHI--SVESTQFSNQGTMAGAA 388
Cdd:cd24072 235 GRSLANILNLLNPEQVLLYGRGCRAGDLLLPAIRRAIAENPFSQHATQIgfGQLSTEQGCAQQALGLV 302
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
86-390 |
3.06e-35 |
|
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: 131.51 E-value: 3.06e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 86 HYLSLRISRGEIFLALRDLSSKLVVEEAQELALKDDSPLLDRIISHIDQFFIRHQKKLERLTSIAITLPGIIDtENGIVH 165
Cdd:cd24077 2 YSIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGIGIHGIVD-ENEIIF 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 166 rMPFYeDVKEMPLGEALEQHTGVPVYIQHD--ISAwtMAEALFgaSRGARDVIQVVIDHNVGAGVITDGHLLH-----AG 238
Cdd:cd24077 81 -TPYY-DLEDIDLKEKLEEKFNVPVYLENEanLSA--LAERTF--SEDYDNLISISIHSGIGAGIIINNQLYRgyngfAG 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 239 ssslvEIGHTQVDPYGKRCYCGNHGCLETIASVDSILElaqlRLNQSMSSmlhgQPLTVDSLCQAALRGDLLAKDIITGV 318
Cdd:cd24077 155 -----EIGHMIIVPNGKPCPCGNKGCLEQYASEKALLK----ELSEKKGL----ETLTFDDLIQLYNEGDPEALELIDQF 221
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446147402 319 GAHVGRILAIMVNLFNPQKILIGSPLSKAadilFPVISDSIRQQALPAYSQHISVESTQFSNQGTMAGAALV 390
Cdd:cd24077 222 IKYLAIGINNIINTFNPEIIIINSSLINE----IPELLEKIKEQLSSSFNKYVEILISTLGKNATLLGGAAV 289
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
119-388 |
1.07e-33 |
|
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: 127.47 E-value: 1.07e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 119 KDDSPLLDRIISHIDQFFIRHQkklerLTSIAITLPGIIDTENGIVHRMPFYeDVKEMPLGEALEQHTGVPVYIQHDISA 198
Cdd:cd24061 32 PTADGIVDAIVEAVEELREGHD-----VSAVGVAAAGFVDADRATVLFAPNI-AWRNEPLKDLLEARIGLPVVIENDANA 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 199 WTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELA 278
Cdd:cd24061 106 AAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRVVPDGLLCGCGSRGCWEQYASGRALVRYA 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 279 QLRLN------QSMSSMLHGQPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILF 352
Cdd:cd24061 186 KEAANatpegaAVLLADGSVDGITGKHISEAARAGDPVALDALRELARWLGAGLASLAALLDPELFVIGGGVSDAGDLLL 265
|
250 260 270
....*....|....*....|....*....|....*...
gi 446147402 353 PVISDSIRqQALPAYSQH--ISVESTQFSNQGTMAGAA 388
Cdd:cd24061 266 DPIREAFE-RWLPGRGWRpiPRLRTAQLGNDAGLIGAA 302
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
149-390 |
2.43e-32 |
|
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: 123.59 E-value: 2.43e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 149 IAITLPGIIDTENGIVHRMPFYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGV 228
Cdd:cd24065 59 VGLGVPGPLDFRRGRVRFAPNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGL 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 229 ITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAqlrlnqsmsSMLHGQPLTVDSLCQAALRGD 308
Cdd:cd24065 139 VLGGRVLRGRHGQAGEIGHTTVLPGGPMCGCGLVGCLEALASGRALARDA---------SFAYGRPMSTAELFELAQQGE 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 309 LLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILF-PVISDSIRQ-QALPAysqhISVESTQFSNQGTMAG 386
Cdd:cd24065 210 PKALRIVEQAAAHLGIGLANLQKALDPEVFVLGGGVAQVGDYYLlPVQEAARRYtEGWHA----PPLRLAHLGTDAGVIG 285
|
....
gi 446147402 387 AALV 390
Cdd:cd24065 286 AALA 289
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
124-389 |
3.10e-28 |
|
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: 112.82 E-value: 3.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 124 LLDRIISHIDQFF-IRHQKKLErltSIAITLPGIIDTENGIVHRMPFYEDvKEMPLGEALEQHTGVPVYIQHDISAWTMA 202
Cdd:cd24063 40 VSEQVLGLIETLLsKAGKDSIE---GIGVSSAGPLDLRKGTIVNSPNIKG-KEIPLVEPLKEEFNIPVALLNDAVAAALG 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 203 EALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDP-YGKRCYCGNHGCLETIASVDSILELAQLR 281
Cdd:cd24063 116 EHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHLVVDTeSGLKCGCGGYGHWEAFASGRGIPRFAREW 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 282 L-NQSMSSMLH-----GQPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSKAADILF-PV 354
Cdd:cd24063 196 AeGFSSRTSLKlrnpgGEGITAKEVFSAARKGDPLALKIIEKLARYNGRGIANVINAYDPELIVIGGSVFNNNKDILdPL 275
|
250 260 270
....*....|....*....|....*....|....*.
gi 446147402 355 ISdsiRQQALPAYSQHISVESTQF-SNQGTMAGAAL 389
Cdd:cd24063 276 IE---YLEKNPAISKGPEIVLSELgDDVGLIGALAL 308
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
145-389 |
1.09e-26 |
|
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase/N-acetylmannosamine kinase (GNE) and similar proteins; GNE (EC 3.2.1.183/EC 2.7.1.60), also called UDP-GlcNAc-2-epimerase/ManAc kinase, is a bi-functional enzyme that plays a key role in sialic acid biosynthesis. It regulates and initiates biosynthesis of N-acetylneuraminic acid (NeuAc), a precursor of sialic acids. It plays an essential role in early development and required for normal sialylation in hematopoietic cells. Sialylation is implicated in cell adhesion, signal transduction, tumorigenicity and metastatic behavior of malignant cells. GNE is the only human protein that contains a kinase domain belonging to the ROK (repressor, ORF, kinase) family. Mutations of the GNE protein cause sialurea or autosomal recessive inclusion body myopathy/Nonaka myopathy.
Pssm-ID: 466910 [Multi-domain] Cd Length: 305 Bit Score: 108.27 E-value: 1.09e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 145 RLTSIAITLPGIIDTENGIV-HRMPFYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHN 223
Cdd:cd24060 59 RILGVGISTGGRVNPREGIVlHSTKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTG 138
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 224 VGAGVITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILELAQlRLNQSMSSMLHG------QPLTV 297
Cdd:cd24060 139 IGGGIILNHELIHGSSFCAAELGHIVVSLDGPDCMCGSHGCVEAYASGMALQREAK-KLHDEDLLLVEGmsvtndEEVTA 217
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 298 DSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLskaADILFPVISDSIRQQALPAySQHISVESTQ 377
Cdd:cd24060 218 KHLIQAAKLGNAKAQKILRTAGTALGLGIVNILHTLNPSLVILSGVL---ASHYENIVKDVIAQRALPS-VQNVDVVVSD 293
|
250
....*....|..
gi 446147402 378 FSNQGTMAGAAL 389
Cdd:cd24060 294 LVDPALLGAASM 305
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
148-346 |
1.81e-20 |
|
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: 90.73 E-value: 1.81e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 148 SIAITLPGIIDTENGIV--------HRMPFYEDvkemplgeaLEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVV 219
Cdd:cd24066 58 TVGIGTPGSISPRTGLVknanstwlNGKPLKAD---------LEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVI 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 220 IDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPY------GKRCYCGNHGCLETIASvDSILELAQLRlnqsmssmLHGQ 293
Cdd:cd24066 129 LGTGVGGGIVVNGRVLTGANGIAGEWGHNPLPWPdedelpGPPCYCGKRGCVETFLS-GPALERDYAR--------LTGK 199
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 446147402 294 PLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLSK 346
Cdd:cd24066 200 TLSAEEIVALARAGDAAAVATLDRFLDRLGRALANVINILDPDVIVLGGGLSN 252
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
117-341 |
1.94e-20 |
|
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: 90.69 E-value: 1.94e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 117 ALKDDSPLLDRIISHIDQFFIRHQKKLErltSIAITLPGIIDTENGIVHRMPFYEDVKEMPLGEALEQHTGVPVYIQHDI 196
Cdd:cd24070 34 DLLRAGDPVEVLADLIREYIEEAGLKPA---AIVIGVPGTVDKDRRTVISTPNIPGLDGVNLADILENKLGIPVILERDV 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 197 SAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLETIASVDSILE 276
Cdd:cd24070 111 NLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHIPVYGNGKPCGCGNTGCLETYASGRALEE 190
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 446147402 277 LAQlrlnqsmssmLHGQPltVDSLCQAALRGDllAKDIITGVgAHVGRILAIMVNLFNPQKILIG 341
Cdd:cd24070 191 IAE----------EHYPD--TPILDIFVDHGD--EPELDEFV-EDLALAIATEINILDPDAVILG 240
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
174-389 |
3.16e-20 |
|
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar proteins; N-acetylmannosamine kinase (NanK; EC 2.7.1.60), also called ManNAc kinase, or N-acetyl-D-mannosamine kinase, catalyzes the phosphorylation of N-acetylmannosamine (ManNAc) to ManNAc-6-P. It has also low level glucokinase activity in vitro. This subfamily also contains Brucella melitensis bifunctional enzyme NanE/NanK (EC 5.1.3.9/EC 2.7.1.60), which also converts N-acetylmannosamine-6-phosphate (ManNAc-6-P) to N-acetylglucosamine-6-phosphate (GlcNAc-6-P). Members of this subfamily belong to the kinase (ROK) family, a group of proteins that have sugar kinase and/or transcriptional repressor activities.
Pssm-ID: 466919 [Multi-domain] Cd Length: 283 Bit Score: 90.04 E-value: 3.16e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 174 KEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAGSSSLVEIGHTQVDPY 253
Cdd:cd24069 80 SGFPLADALQQLLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADPP 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 254 GKRCYCGNHGCLETIASVDSILELAQLRLnqsmssmlhGQPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLF 333
Cdd:cd24069 160 GPVCGCGRRGCVEAIASGTAIAAAASEIL---------GEPVDAKDVFERARSGDEEAARLIDRAARALADLIADLKATL 230
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 446147402 334 NPQKILIGSPLSKAADILFPVISdsiRQQALPAYSqHISVESTQFSNQGTMAGAAL 389
Cdd:cd24069 231 DLDCVVIGGSVGLAEGFLERVEQ---YLADEPAIF-RVSLEPARLGQDAGLLGAAL 282
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
132-387 |
3.17e-20 |
|
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: 89.93 E-value: 3.17e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 132 IDQFFIRHQKKLERltsIAITLPGIIDTENGIVHRMPFYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRG 211
Cdd:cd24152 43 IKKIIKRYDEEIDG---IAISAPGVIDPETGIIYGGGALPYLKGFNLKEELEERCNLPVSIENDAKCAALAELWLGSLKG 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 212 ARDVIQVVIDHNVGAGVITDGHLLH-----AGssslvEIGHTQVDPYGKRCYCGNHGCletiaSVDSILELaqlrlnqsM 286
Cdd:cd24152 120 IKNGAVIVLGTGIGGAIIIDGKLYRgshffAG-----EFSYLLTDDDDKDLLFFSGLA-----SMFGLVKR--------Y 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 287 SSMLHGQPLTVDSLCQAALRGDLLAKDIitgVGAHVGRILAIMVNL---FNPQKILIGSPLSkAADILFPVISDSIRQ-- 361
Cdd:cd24152 182 NKAKGLEPLDGEEIFEKYAKGDEAAKKI---LDEYIRNLAKLIYNIqyiLDPEVIVIGGGIS-EQPLFIEDLKKEVNEil 257
|
250 260
....*....|....*....|....*.
gi 446147402 362 QALPAYSQHISVESTQFSNQGTMAGA 387
Cdd:cd24152 258 ANRPGSIPKPEIKACKFGNDANLLGA 283
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
148-390 |
9.84e-19 |
|
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: 85.75 E-value: 9.84e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 148 SIAITLPGIIDTENGIV--HRMPFyedVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVG 225
Cdd:cd24057 59 PVGIGIPGVIDPEDGTLitANIPA---AKGRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 226 AGVITDGHLLHAGSSSLVEIGHT------QVDPYG---KRCYCGNHGCLETIASVDSILELAQlrlnqsmssMLHGQPLT 296
Cdd:cd24057 136 GGLVVNGRLVGGRSGIAGEWGHGplpadaLLLGYDlpvLRCGCGQTGCLETYLSGRGLERLYA---------HLYGEELD 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 297 VDSLCQAALRGDLLAkdiitgvGAHVGR-------ILAIMVNLFNPQKILIGSPLSKAADILfPVISDSIRQQALPAYSQ 369
Cdd:cd24057 207 APEIIAAWAAGDPQA-------VAHVDRwldllagCLANILTALDPDVVVLGGGLSNFPALI-AELPAALPAHLLSGART 278
|
250 260
....*....|....*....|.
gi 446147402 370 HIsVESTQFSNQGTMAGAALV 390
Cdd:cd24057 279 PR-IVPARHGDAGGVRGAAFL 298
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
174-389 |
6.37e-14 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 71.87 E-value: 6.37e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 174 KEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGaRDVIQVVIDHNVGAGVITDGHLlHAGSSSLV-EIGHTQVDP 252
Cdd:PRK05082 84 LHFPLVQTLEQLTDLPTIALNDAQAAAWAEYQALPDDI-RNMVFITVSTGVGGGIVLNGKL-LTGPGGLAgHIGHTLADP 161
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 253 YGKRCYCGNHGCLETIASVDSILELAQLRLNQSMSSMLHgqpltvdslcQAALRGDLLAKDIITGVGAHVGRILAIMVNL 332
Cdd:PRK05082 162 HGPVCGCGRRGCVEAIASGRAIAAAAQGWLAGCDAKTIF----------ERAGQGDEQAQALINRSAQAIARLIADLKAT 231
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 446147402 333 FNPQKILIGSPLSKAADILfPVISDSIRQQALPaYsqHISVESTQFSNQGTMAGAAL 389
Cdd:PRK05082 232 LDCQCVVLGGSVGLAEGYL-ELVQAYLAQEPAI-Y--HVPLLAAHYRHDAGLLGAAL 284
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
123-341 |
1.34e-11 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 65.00 E-value: 1.34e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 123 PLLDRIISHIDQFFIRHqkkLERLTSIAITLPGIIDTENGIVHRMPFYEDVKE--MPLGEALEQHTGVPVYIQHDIS--- 197
Cdd:PRK09698 42 DLVSGLGEMIDEYLRRF---NARCHGIVMGFPALVSKDRRTVISTPNLPLTALdlYDLADKLENTLNCPVFFSRDVNlql 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 198 AWtmaealfgasrgarDVIQVVIDHNV----------GAGVITDGHLLHAGSSSLVEIGHTQVDPYGKRCYCGNHGCLET 267
Cdd:PRK09698 119 LW--------------DVKENNLTQQLvlgaylgtgmGFAVWMNGAPWTGAHGVAGELGHIPLGDMTQHCGCGNPGCLET 184
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446147402 268 IAS---VDSILElAQLRlNQSMSSML--HGQPLTVDSLCqaalrgDLLAKDIITGvgahvgrilaimVNLFNPQKILIG 341
Cdd:PRK09698 185 NCSgmaLRRWYE-QQPR-DYPLSDLFvhAGDHPFIQSLL------ENLARAIATS------------INLFDPDAIILG 243
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
148-345 |
1.27e-10 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 61.97 E-value: 1.27e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 148 SIAITLPGIIDTENGIVHR--------MPFYEDvkempLGEALEQhtgvPVYIQHDISAWTMAEALFGASRGARDVIQVV 219
Cdd:PRK09557 59 TVGVGIPGSISPYTGLVKNanstwlngQPLDKD-----LSARLNR----EVRLANDANCLAVSEAVDGAAAGKQTVFAVI 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 220 IDHNVGAGVITDGHLlHAGSSSLV-EIGHTQV-----DPYGKR----CYCGNHGCLETIAS----VDSILELAqlrlnqs 285
Cdd:PRK09557 130 IGTGCGAGVAINGRV-HIGGNGIAgEWGHNPLpwmdeDELRYRnevpCYCGKQGCIETFISgtgfATDYRRLS------- 201
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 286 mssmlhGQPLTVDSLCQAALRGDLLAKDIITGVGAHVGRILAIMVNLFNPQKILIGSPLS 345
Cdd:PRK09557 202 ------GKALKGSEIIRLVEEGDPVAELAFRRYEDRLAKSLAHVINILDPDVIVLGGGMS 255
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
148-388 |
4.17e-09 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 57.31 E-value: 4.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 148 SIAITLPGIIDTENGIVH--RMPFyedVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVG 225
Cdd:PRK13310 59 SVGIGIPGMPETEDGTLYaaNVPA---ASGKPLRADLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVG 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 226 AGVITDGHLlHAGSSSLV-EIGHTQVdPYGK-----------RCYCGNHGCLETIASVdsilelaqlRLNQSMSSMLHGQ 293
Cdd:PRK13310 136 GGLVFNGKP-ISGRSYITgEFGHMRL-PVDAltllgwdaplrRCGCGQKGCIENYLSG---------RGFEWLYQHYYGE 204
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 294 PLTVDSLCQAALRGDLLAKdiitgvgAHVGR---ILAIMV-NLF---NPQKILIGSPLSKaadilFPVISDSIrQQALPA 366
Cdd:PRK13310 205 PLQAPEIIALYYQGDEQAV-------AHVERyldLLAICLgNILtivDPHLVVLGGGLSN-----FDAIYEQL-PKRLPR 271
|
250 260
....*....|....*....|....*.
gi 446147402 367 YSQHIS----VESTQFSNQGTMAGAA 388
Cdd:PRK13310 272 HLLPVArvprIEKARHGDAGGVRGAA 297
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
177-270 |
1.91e-07 |
|
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: 52.16 E-value: 1.91e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 177 PLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNVGAGVITDGHLLHAgsssLV--EIGHTQV---- 250
Cdd:cd24067 86 DILGALKRAFPVPVGFDTDVNAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHG----LLhpEMGHIRVprhp 161
|
90 100
....*....|....*....|....
gi 446147402 251 --DPYGKRC-YcgnHG-CLETIAS 270
Cdd:cd24067 162 ddDGFPGVCpF---HGdCLEGLAS 182
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
149-389 |
2.00e-07 |
|
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: 51.42 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 149 IAITLPGIIdtENGIVHRMP-FYEDVKEMPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVV-IDHNVGA 226
Cdd:cd24058 58 VGVGFPGVV--RRGVVRTAAnLDKSWIGFDAAKLLSKRLGRPVRVLNDADAAGLAEMKGGAGKGEKGVVLVLtLGTGIGS 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 227 GVITDGHLLHAgssslVEIGHTQVDpygkrcycgnHGCLETIASVdsilelaqlrlnqsmssmlhgqpltvdslcQAALR 306
Cdd:cd24058 136 ALFVDGHLVPN-----TELGHLEIR----------GKDAEERASL------------------------------GVRAR 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 307 GDLLAKDIitgvGAHVGRILAIMVNLFNPQKILIGSPLSKAADILFPVISDSIRqqALPAysqhisvestQFSNQGTMAG 386
Cdd:cd24058 171 EDLGWKRW----AKRVNKYLQYLERLFNPDLFIIGGGNSKKADKFLPLLDVKTP--VVPA----------VLRNDAGIVG 234
|
...
gi 446147402 387 AAL 389
Cdd:cd24058 235 AAL 237
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
148-270 |
1.29e-03 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 40.40 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446147402 148 SIAITLPGIIDTENGIVhrmpFYEDVKE---MPLGEALEQHTGVPVYIQHDISAWTMAEALFGASRGARDVIQVVIDHNV 224
Cdd:PRK13311 59 SVGIGIPGLPNADDGTV----FTANVPSamgQPLQADLSRLIQREVRIDNDANCFALSEAWDPEFRTYPTVLGLILGTGV 134
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 446147402 225 GAGVITDGHLLHAGSSSLVEIGHTQV-----DPYGKR-----CYCGNHGCLETIAS 270
Cdd:PRK13311 135 GGGLIVNGSIVSGRNHITGEFGHFRLpvdalDILGADiprvpCGCGHRGCIENYIS 190
|
|
| Fe_dep_repress |
pfam01325 |
Iron dependent repressor, N-terminal DNA binding domain; This family includes the Diphtheria ... |
20-60 |
2.67e-03 |
|
Iron dependent repressor, N-terminal DNA binding domain; This family includes the Diphtheria toxin repressor. DNA binding is through a helix-turn-helix motif.
Pssm-ID: 396062 [Multi-domain] Cd Length: 57 Bit Score: 35.81 E-value: 2.67e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 446147402 20 AVYRLIDQLGPVSRIDLSRLAQLAPASITKIVREMLEAHLV 60
Cdd:pfam01325 9 TIYTLSEEKGVVKTKDLAERLNVSPSTVSEMLKKLEKMGYV 49
|
|
| |
