|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
79-377 |
6.89e-79 |
|
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: 245.19 E-value: 6.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 79 NPSSAWSIGIHLDHQTLIVVLVDLSGEIHFRRHI-LVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPFGV 157
Cdd:COG1940 1 NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIpTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 158 EGISSTGPTTLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHA 237
Cdd:COG1940 81 ETGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 238 HNAGEVGHIVVQPGGRACYCGNQGCLERYVSLQA----AYEFCGLDP--YRALPEDLLAVDEALfDRWIDSALPPLRQAI 311
Cdd:COG1940 161 GNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPAllrrARELGGAEKltAEELFAAARAGDPLA-LEVLDEAARYLGIGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294039456 312 NLLECVFDAETVVVGGTMPA---PLLEKVLARlppLYQSVRGRYLTGMRVKMGMTGTDTAALGAAALPI 377
Cdd:COG1940 240 ANLINLLDPEVIVLGGGVSAagdLLLEPIREA---LAKYALPPAREDPRIVPASLGDDAGLLGAAALAL 305
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
85-377 |
2.04e-62 |
|
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: 202.41 E-value: 2.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 85 SIGIHLDHQTLIVVLVDLSGEIHFRRHI-LVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPfgVEgiSST 163
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASDDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGL--VD--SED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 164 G-----PTTlnGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAH 238
Cdd:cd24076 79 GvvllaPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 239 NAGEVGHIVVQPGGRACYCGNQGCLERYVSLQAAYEFCGLDPYRALPEDLLAVDEALF--DRW----IDSALPPLRQAIN 312
Cdd:cd24076 157 FAGEIGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAGGEPLSLAELVEAARagDPAalaaLEEVGEYLGIGLA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294039456 313 LLECVFDAETVVVGGTMpAPLLEKVlarLPPLYQSVRGRYLTGM----RVKMGMTGTDTAALGAAALPI 377
Cdd:cd24076 237 NLVNTFNPELVVLGGAL-APLGPWL---LPPLRAEVARRALPAPardvRIVVSRLGEDAAALGAAALAI 301
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
86-375 |
1.20e-32 |
|
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: 123.99 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGATfarIGEVIQELRTLPGLDWSRVLGIGVVMPGPfgvegISSTGP 165
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEET---LVDAIAFFVDSAQRKFGELIAVGIGSPGL-----ISPKYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 166 TTLN----GWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAG 241
Cdd:pfam00480 73 YITNtpniGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 242 EVGHIVVQPGGRACYCGNQGCLERYVS---LQAAYEFCGLD-PYRALPEDLLAVDEALFDRWIDSALpPLRQAINLLECV 317
Cdd:pfam00480 153 EIGHIQLDPNGPKCGCGNHGCLETIASgraLEKRYQQKGEDlEGKDIIVLAEQGDEVAEEAVERLAR-YLAKAIANLINL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 318 FDAETVVVGGTMpaPLLEKVLARLPPLYQSVRGRYLTG--MRVKMGMTGTDTAALGAAAL 375
Cdd:pfam00480 232 FDPQAIVLGGGV--SNADGLLEAIRSLVKKYLNGYLPVppVIIVAASLGDNAGALGAAAL 289
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
144-268 |
1.60e-23 |
|
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: 99.59 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 144 VLGIGVVMPGPFGVEGISSTGPTTLnGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLG 223
Cdd:TIGR00744 58 IVAIGIGAPGPVNRQRGTVYFAVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLG 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2294039456 224 AGIFTDGHIYTGHAHNAGEVGHIVVQPGGRA-CYCGNQGCLERYVS 268
Cdd:TIGR00744 137 GGIIINGEIRHGHNGVGAEIGHIRMVPDGRLlCNCGKQGCIETYAS 182
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
99-327 |
4.08e-18 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 83.88 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 99 LVDLSGEI-HFRRH--ILVQKPQPGAtfaRIGEVIQElrTLPGLDwSRVLGIGVVMPGPFGVEG--ISSTGPTTLNGWEG 173
Cdd:PRK09698 20 LVDAEGEIlHCEKKrtAEVIAPDLVS---GLGEMIDE--YLRRFN-ARCHGIVMGFPALVSKDRrtVISTPNLPLTALDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 174 VDVESELARLSGLPVTLENDATVaaigERFHGVARHL---NSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQP 250
Cdd:PRK09698 94 YDLADKLENTLNCPVFFSRDVNL----QLLWDVKENNltqQLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGHIPLGD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 251 GGRACYCGNQGCLERYVS---LQAAYEfcglDPYRALP-EDLL--AVDEALFDRWIDSALPPLRQAINLlecvFDAETVV 324
Cdd:PRK09698 170 MTQHCGCGNPGCLETNCSgmaLRRWYE----QQPRDYPlSDLFvhAGDHPFIQSLLENLARAIATSINL----FDPDAII 241
|
...
gi 2294039456 325 VGG 327
Cdd:PRK09698 242 LGG 244
|
|
| HTH_CRP |
cd00092 |
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ... |
15-65 |
6.83e-04 |
|
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.
Pssm-ID: 238044 [Multi-domain] Cd Length: 67 Bit Score: 37.65 E-value: 6.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2294039456 15 NRRVVIEAVRLHGKLTRAELARLTALTPQTVSNIVAELQQMEILTSHAPRR 65
Cdd:cd00092 12 LSLRYGAGDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGRGK 62
|
|
| MarR_2 |
pfam12802 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
19-59 |
1.19e-03 |
|
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.
Pssm-ID: 432797 [Multi-domain] Cd Length: 60 Bit Score: 36.80 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2294039456 19 VIEAVRLHGKLTRAELARLTALTPQTVSNIVAELQQMEILT 59
Cdd:pfam12802 10 VLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVE 50
|
|
| COG2345 |
COG2345 |
Predicted transcriptional regulator, ArsR family [Transcription]; |
16-69 |
2.20e-03 |
|
Predicted transcriptional regulator, ArsR family [Transcription];
Pssm-ID: 441914 [Multi-domain] Cd Length: 217 Bit Score: 39.14 E-value: 2.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2294039456 16 RRVVIEAVRLHGKLTRAELARLTALTPQTVSNIVAELQQMEILTSHAPRRAAGR 69
Cdd:COG2345 15 RRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERETERRGRGR 68
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NagC |
COG1940 |
Sugar kinase of the NBD/HSP70 family, may contain an N-terminal HTH domain [Carbohydrate ... |
79-377 |
6.89e-79 |
|
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: 245.19 E-value: 6.89e-79
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 79 NPSSAWSIGIHLDHQTLIVVLVDLSGEIHFRRHI-LVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPFGV 157
Cdd:COG1940 1 NPDAGYVIGIDIGGTKIKAALVDLDGEVLARERIpTPAGAGPEAVLEAIAELIEELLAEAGISRGRILGIGIGVPGPVDP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 158 EGISSTGPTTLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHA 237
Cdd:COG1940 81 ETGVVLNAPNLPGWRGVPLAELLEERLGLPVFVENDANAAALAEAWFGAGRGADNVVYLTLGTGIGGGIVINGKLLRGAN 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 238 HNAGEVGHIVVQPGGRACYCGNQGCLERYVSLQA----AYEFCGLDP--YRALPEDLLAVDEALfDRWIDSALPPLRQAI 311
Cdd:COG1940 161 GNAGEIGHMPVDPDGPLCGCGNRGCLETYASGPAllrrARELGGAEKltAEELFAAARAGDPLA-LEVLDEAARYLGIGL 239
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294039456 312 NLLECVFDAETVVVGGTMPA---PLLEKVLARlppLYQSVRGRYLTGMRVKMGMTGTDTAALGAAALPI 377
Cdd:COG1940 240 ANLINLLDPEVIVLGGGVSAagdLLLEPIREA---LAKYALPPAREDPRIVPASLGDDAGLLGAAALAL 305
|
|
| ASKHA_ATPase_ROK_BsXylR-like |
cd24076 |
ATPase-like domain of Bacillus subtilis xylose repressor (XylR) and similar proteins; This ... |
85-377 |
2.04e-62 |
|
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: 202.41 E-value: 2.04e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 85 SIGIHLDHQTLIVVLVDLSGEIHFRRHI-LVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPfgVEgiSST 163
Cdd:cd24076 3 VIGVELGVDYITVVVTDLAGEVLWRREVpLPASDDPDEVLAQLAALIREALAAAPDSPLGILGIGVGVPGL--VD--SED 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 164 G-----PTTlnGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAH 238
Cdd:cd24076 79 GvvllaPNL--GWRDVPLRDLLEEALGVPVFVDNEANAAALAEKRFGAGRGVSDLVYLSAGVGIGAGIILDGELYRGASG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 239 NAGEVGHIVVQPGGRACYCGNQGCLERYVSLQAAYEFCGLDPYRALPEDLLAVDEALF--DRW----IDSALPPLRQAIN 312
Cdd:cd24076 157 FAGEIGHMTVDPDGPPCSCGNRGCWETYASERALLRAAGRLGAGGEPLSLAELVEAARagDPAalaaLEEVGEYLGIGLA 236
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2294039456 313 LLECVFDAETVVVGGTMpAPLLEKVlarLPPLYQSVRGRYLTGM----RVKMGMTGTDTAALGAAALPI 377
Cdd:cd24076 237 NLVNTFNPELVVLGGAL-APLGPWL---LPPLRAEVARRALPAPardvRIVVSRLGEDAAALGAAALAI 301
|
|
| ASKHA_NBD_ROK_TM1224-like |
cd24059 |
nucleotide-binding domain (NBD) of Thermotoga maritima N-acetylglucosamine kinase (TM1224) and ... |
85-382 |
1.52e-50 |
|
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: 171.61 E-value: 1.52e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 85 SIGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGA-TFARIGEVIQELrtlpgLDW----SRVLGIGVVMPGPFGVE- 158
Cdd:cd24059 3 VIGVEIGRDLLSAVLCDLSGNILAREKYPLDEKENPEeVLEKLYELIDRL-----LEKenikSKILGIGIGAPGPLDVEk 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 159 GISSTgPTTLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAH 238
Cdd:cd24059 78 GIILN-PPNFPGWENIPLVELLEEKFGIPVYLDNDANAAALAEKWYGKGKNYDNFIYILADEGIGAGIIINGKLYRGVDG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 239 NAGEVGHIVVQPGGRACYCGNQGCLERYVSLQA-----------AYEFcGLDPYRALPEDLLAVDEALFD--RWIDSALP 305
Cdd:cd24059 157 YAGEIGHTSIDINGPRCSCGNRGCLELYASIPAiekkarsalgsGRSF-QLDIVEALQKGDPIADEVIEEaaKYLGIGLV 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 306 PLrqaINLLECvfdaETVVVGGTMPA-------PLLEKVLARLPPL-YQSVrgryltgmRVKMGMTGTDTAALGAAALPI 377
Cdd:cd24059 236 NL---INLLNP----EAIIIGGELIYlgerylePIEKEVNSRLFGRnAREV--------RILKSSLGEDAPLLGAAALVL 300
|
....*
gi 2294039456 378 FDEFN 382
Cdd:cd24059 301 NKYFE 305
|
|
| ASKHA_ATPase_ROK |
cd23763 |
ATPase-like domain of the ROK (Repressor, ORF, Kinase) domain family; The ROK family ... |
86-375 |
2.50e-48 |
|
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: 163.79 E-value: 2.50e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQ-PGATFARIGEVIQELRTLPGLdWSRVLGIGVVMPGPFGVEGISSTG 164
Cdd:cd23763 1 IGIDIGGTKIRAALVDLDGEILARERVPTPAEEgPEAVLDRIAELIEELLAEAGV-RERILGIGIGVPGPVDPETGIVLF 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 165 PTTLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVG 244
Cdd:cd23763 80 APNLPWWKNVPLRELLEERLGLPVVVENDANAAALGEAWFGAGRGVRNFVYITLGTGIGGGIIIDGKLYRGANGAAGEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 245 HIVVqpggracycgnqgcleryvslqaayefcgldpyralpedllavdealFDRWIDSalppLRQAINLLECVFDAETVV 324
Cdd:cd23763 160 HITV-----------------------------------------------LEEAARY----LGIGLANLINLLNPELIV 188
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 2294039456 325 VGGTMPA--PLLekvlarLPPLYQSVRGRYLTGM----RVKMGMTGTDTAALGAAAL 375
Cdd:cd23763 189 LGGGVAEagDLL------LEPIREAVRRRALPPLrrrvRIVPSELGDDAGLLGAAAL 239
|
|
| ASKHA_ATPase_ROK_CYANR |
cd24073 |
ATPase-like domain of cyclobis-(1-6)-alpha-nigerosyl repressor (CYANR) and similar proteins; ... |
86-375 |
1.82e-45 |
|
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: 158.48 E-value: 1.82e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPF-GVEGISSTG 164
Cdd:cd24073 4 VGVKLTEDRITAVLTDLRGNVLASHTLPLDSGDPEAVAEAIAEAVAELLAQAGLSPDRLLGIGVGLPGLVdAETGICRWS 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 165 PttLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVG 244
Cdd:cd24073 84 P--LLGWRDVPLAELLEERLGLPVYVENDVNALALAEHWFGAGRGLDNFAVVTIGRGIGCGLVVDGRLYRGAHGGAGEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 245 HIVVQPGGRACYCGNQGCLERYVSLQA---AYEFCGLDPYRALPEDLLA-------VDEALFD---RWIDSALPPLrqaI 311
Cdd:cd24073 162 HTTVDPDGPPCRCGKRGCLEAYASDPAilrQAREAGLRGEPLTIEDLLAaaragdpAARAILRragRALGLALANL---V 238
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2294039456 312 NLlecvFDAETVVVGGtmpapllEKVLA---RLPPLYQSVRGRYLTGMRVKMGMT----GTDTAALGAAAL 375
Cdd:cd24073 239 NL----LDPELIIISG-------EGVRAgdlLFEPMREALRAHVFPGLASDLELVihpwGDEAWARGAAAL 298
|
|
| ASKHA_NBD_ROK_FnNanK-like |
cd24068 |
nucleotide-binding domain (NBD) of Fusobacterium nucleatum N-acetylmannosamine kinase and ... |
99-375 |
7.32e-41 |
|
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: 146.16 E-value: 7.32e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 99 LVDLSGEI--HFRRHILVQKPQPgATFARIGEVIQELRTLPgldwsRVLGIGVVMPG---PfgVEG-ISSTGPTtLNGWE 172
Cdd:cd24068 16 LVDADGEIleKDSVPTPASKGGD-AILERLLEIIAELKEKY-----DIEGIGISSAGqvdP--KTGeVIYATDN-LPGWT 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 173 GVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGG 252
Cdd:cd24068 87 GTNLKEELEERFGLPVAVENDVNCAALAEKWLGAAKGLDDFLCLTLGTGIGGAIILDGRLYRGANGSAGELGHMVVDPGG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 253 RACYCGNQGCLERYVS---LQAAYEFCGLDPY--------RALPEDLLAvdEALFDRWIDSalppLRQAINLLECVFDAE 321
Cdd:cd24068 167 RPCCCGGKGCLEQYASgtaLVRRVAEALGEPGidgreifdLADAGDPLA--KEVVEEFAED----LATGLANLVHIFDPE 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2294039456 322 TVVVGGTMPA------PLLEKVLARL--PPLYQSVrgryltgmRVKMGMTGTDTAALGAAAL 375
Cdd:cd24068 241 VIVIGGGISAqgelflEELREELRKLlmPPLLDAT--------KIEPAKLGNDAGLLGAAYL 294
|
|
| ASKHA_ATPase_ROK_Lmo0178-like |
cd24071 |
ATPase-like domain of Listeria monocytogenes Lmo0178 and similar proteins; This subfamily ... |
86-271 |
8.52e-35 |
|
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: 130.48 E-value: 8.52e-35
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKP-QPGATFARIGEVIQELRTLPGLDwSRVLGIGVVMPGPfgvegISSTG 164
Cdd:cd24071 4 IGVKIEEGYLVLALTDLKGKILEKTRIPFDHEtDPEKVIELIAENIKKLIKNKHVE-KKLLGIGIAVSGL-----VDSKK 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 165 PT----TLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNA 240
Cdd:cd24071 78 GIvirsTILGWENVELKKILKEKFKIPVFIDNDVNSFALAELWKGKGKGYSNFICVTVGAGIGSSLVIDGKLYTGNFGGA 157
|
170 180 190
....*....|....*....|....*....|.
gi 2294039456 241 GEVGHIVVQPGGRACYCGNQGCLERYVSLQA 271
Cdd:cd24071 158 GEIGHMTIQPDGRKCYCGQKGCLEAYASFEA 188
|
|
| ASKHA_ATPase_ROK_SaXylR-like |
cd24077 |
ATPase-like domain of Staphylococcus aureus xylose repressor (XylR) and similar proteins; This ... |
83-274 |
1.51e-33 |
|
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: 126.50 E-value: 1.51e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 83 AWSIGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVvmpgpfGVEGIss 162
Cdd:cd24077 1 GYSIGIDLGYNYISLMLTYLDGEIISSKQIKLLDISFENILEILKSIIQELISQAPKTPYGLVGIGI------GIHGI-- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 163 tgpTTLNG--------WEGVDVESELARLSGLPVTLENDATVAAIGER-FhgvARHLNSFVYLYIGTGLGAGIFTDGHIY 233
Cdd:cd24077 73 ---VDENEiiftpyydLEDIDLKEKLEEKFNVPVYLENEANLSALAERtF---SEDYDNLISISIHSGIGAGIIINNQLY 146
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 2294039456 234 TGHAHNAGEVGHIVVQPGGRACYCGNQGCLERYVSLQAAYE 274
Cdd:cd24077 147 RGYNGFAGEIGHMIIVPNGKPCPCGNKGCLEQYASEKALLK 187
|
|
| ASKHA_NBD_ROK_BsGLK-like |
cd24062 |
nucleotide-binding domain (NBD) of Bacillus subtilis glucokinase (GLK) and similar proteins; ... |
84-375 |
1.96e-33 |
|
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: 126.64 E-value: 1.96e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 84 WSIGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGAT-FARIGEVIQELRTLPGLDWSRVLGIGVVMPGPFGVEGISS 162
Cdd:cd24062 1 WIVGIDVGGTTIKMAFLTQEGEIVQKWEIPTNKLEGGENiITDIAESIQQLLEELGYSKEDLIGIGVGVPGPVDVETGTV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 163 TGPTTLnGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGE 242
Cdd:cd24062 81 EVAVNL-GWKNFPLKDKLEALTGIPVVIDNDANAAALGEMWKGAGQGAKDLVFITLGTGVGGGVIANGKIVHGANGAAGE 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 243 VGHIVVQP-GGRACYCGNQGCLERYVS--------LQAAYEFCG--LDPYRALPEDLLAVD--------EALFDRWIDSA 303
Cdd:cd24062 160 IGHITVNPeGGAPCNCGKTGCLETVASatgivriaREELEEGKGssALRILALGGELTAKDvfeaakagDELALAVVDTV 239
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2294039456 304 LPPLRQAINLLECVFDAETVVVGGTMPAPlLEKVLARLPPLYQS-VRGRYLTGMRVKMGMTGTDTAALGAAAL 375
Cdd:cd24062 240 ARYLGLALANLANTLNPEKIVIGGGVSAA-GEFLLSPVKEYFDRfTFPRVRQDTEIVLATLGNDAGVIGAAWL 311
|
|
| ROK |
pfam00480 |
ROK family; This family, known as ROK (Repressor, ORF, Kinase) includes the xylose operon ... |
86-375 |
1.20e-32 |
|
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: 123.99 E-value: 1.20e-32
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGATfarIGEVIQELRTLPGLDWSRVLGIGVVMPGPfgvegISSTGP 165
Cdd:pfam00480 1 IGIDIGGTKIAAALFDEEGEILARERVPTPTTTTEET---LVDAIAFFVDSAQRKFGELIAVGIGSPGL-----ISPKYG 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 166 TTLN----GWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAG 241
Cdd:pfam00480 73 YITNtpniGWDNFDLVEKLEERFNVPVFFENDANAAALAEAVFGASKDVQNVIYVTVGTGVGGGVISNGKLFTGRNGVAG 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 242 EVGHIVVQPGGRACYCGNQGCLERYVS---LQAAYEFCGLD-PYRALPEDLLAVDEALFDRWIDSALpPLRQAINLLECV 317
Cdd:pfam00480 153 EIGHIQLDPNGPKCGCGNHGCLETIASgraLEKRYQQKGEDlEGKDIIVLAEQGDEVAEEAVERLAR-YLAKAIANLINL 231
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 318 FDAETVVVGGTMpaPLLEKVLARLPPLYQSVRGRYLTG--MRVKMGMTGTDTAALGAAAL 375
Cdd:pfam00480 232 FDPQAIVLGGGV--SNADGLLEAIRSLVKKYLNGYLPVppVIIVAASLGDNAGALGAAAL 289
|
|
| ASKHA_NBD_ROK_TtHK-like |
cd24065 |
nucleotide-binding domain (NBD) of Thermus thermophilus hexokinase (HK) and similar proteins; ... |
85-373 |
1.13e-31 |
|
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: 121.28 E-value: 1.13e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 85 SIGIHLDHQTLIVVLVDlSGEIHFRrhilVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPFGVEGISSTG 164
Cdd:cd24065 2 TIGLDLGGTKIAAGVVD-GGRILSR----LVVPTPREGGEAVLDALARAVEALQAEAPGVEAVGLGVPGPLDFRRGRVRF 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 165 PTTLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVG 244
Cdd:cd24065 77 APNIPGLTDFPIRRGLAERLGLPVVLENDANAAALAEHHYGAARGTESSVYVTISTGIGGGLVLGGRVLRGRHGQAGEIG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 245 HIVVQPGGRACYCGNQGCLE-----RYVSLQAAYEFCGLDPYRALpEDLLAVDEALFDRWIDSALPPLRQAINLLECVFD 319
Cdd:cd24065 157 HTTVLPGGPMCGCGLVGCLEalasgRALARDASFAYGRPMSTAEL-FELAQQGEPKALRIVEQAAAHLGIGLANLQKALD 235
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 320 AETVVVGGTMP---APLLEKVLARLPplyqsvrgRYLTGMRV---KMGMTGTDTAALGAA 373
Cdd:cd24065 236 PEVFVLGGGVAqvgDYYLLPVQEAAR--------RYTEGWHApplRLAHLGTDAGVIGAA 287
|
|
| ASKHA_NBD_ROK_SgGLK-like |
cd24061 |
nucleotide-binding domain (NBD) of Streptomyces griseus glucokinase (GLK) and similar proteins; ... |
99-327 |
1.96e-30 |
|
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: 118.61 E-value: 1.96e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 99 LVDLSGEIhFRRHILVQKPQPGATFARIGEVIQELRtlpglDWSRVLGIGVVMPGpfGVEGISSTGPTTLN-GWEGVDVE 177
Cdd:cd24061 15 VVDEEGEI-LATERVPTPPTADGIVDAIVEAVEELR-----EGHDVSAVGVAAAG--FVDADRATVLFAPNiAWRNEPLK 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 178 SELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGRACYC 257
Cdd:cd24061 87 DLLEARIGLPVVIENDANAAAWAEYRFGAGRGTDDMVMITVGTGLGGGIVIGGKLLRGAFGIAGEFGHIRVVPDGLLCGC 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 258 GNQGCLERYVS----LQAAYEFCGLDPYRALPEDLLAVDEALFDRWIDSAL---PP------------LRQAINLLECVF 318
Cdd:cd24061 167 GSRGCWEQYASgralVRYAKEAANATPEGAAVLLADGSVDGITGKHISEAAragDPvaldalrelarwLGAGLASLAALL 246
|
....*....
gi 2294039456 319 DAETVVVGG 327
Cdd:cd24061 247 DPELFVIGG 255
|
|
| ASKHA_NBD_ROK_TmGLK-like |
cd24064 |
nucleotide-binding domain (NBD) of Thermotoga maritima glucokinase (GLK) and similar proteins; ... |
86-327 |
8.58e-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: 8.58e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHI--LVQKPQPGATfARIGEVIQELrtlpgLDWSRVLGIGVVMPGPFGVE-GISS 162
Cdd:cd24064 2 IGIDLGGTDTKIGIVDENGDILKKKTIdtKVENGKEDVI-NRIAETVNEL-----IEEMELLGIGIGSPGSIDREnGIVR 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 163 TGPTtLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGE 242
Cdd:cd24064 76 FSPN-FPDWRNFPLVPLIEERTGIKVFLENDANAFALGEWWFGNAKGSNHIIGLTLGTGVGSGVICHGQLLTGYDGIAAE 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 243 VGHIVVQPGGRACYCGNQGCLERYVSLQAAYEFC--GLDPY----RALPEDLLA--VDEA----------LFDRWIDSal 304
Cdd:cd24064 155 LGHVIVEPNGPICGCGNRGCVEAFASATAIIRYAreSRKRYpdslAGESEKINAkhVFDAarkndplatmVFRRVVDA-- 232
|
250 260
....*....|....*....|...
gi 2294039456 305 ppLRQAINLLECVFDAETVVVGG 327
Cdd:cd24064 233 --LAIAIGGFVHIFNPEIIIIGG 253
|
|
| ASKHA_NBD_ROK_ApGLK-like |
cd24063 |
nucleotide-binding domain (NBD) of Aeropyrum pernix glucokinase (GLK) and similar proteins; ... |
97-375 |
4.39e-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: 112.05 E-value: 4.39e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 97 VVLVDLSGEIHFRRHILVQKPQPGATFA-RIGEVIQELRTLPGLDwsRVLGIGVVMPGPFGVEGISSTGPTTLNGWEgVD 175
Cdd:cd24063 14 AGLVDEDGRILLKIRQPTPKTGDPGTVSeQVLGLIETLLSKAGKD--SIEGIGVSSAGPLDLRKGTIVNSPNIKGKE-IP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 176 VESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGR-A 254
Cdd:cd24063 91 LVEPLKEEFNIPVALLNDAVAAALGEHLFGAGRGTSNLVYITISTGIGGGVIVDGRLLLGKNGNAAEVGHLVVDTESGlK 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 255 CYCGNQGCLERYVSLQA----AYEFCGLDPYRALPE---------------DLLAVDEALFDRWIDSALPPLRQAINLLE 315
Cdd:cd24063 171 CGCGGYGHWEAFASGRGiprfAREWAEGFSSRTSLKlrnpggegitakevfSAARKGDPLALKIIEKLARYNGRGIANVI 250
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2294039456 316 CVFDAETVVVGGTM---PAPLLEKVLARLPPLYqsvrgRYLTGMRVKMGMTGTDTAALGAAAL 375
Cdd:cd24063 251 NAYDPELIVIGGSVfnnNKDILDPLIEYLEKNP-----AISKGPEIVLSELGDDVGLIGALAL 308
|
|
| ASKHA_ATPase_ROK_YphH-like |
cd24072 |
ATPase-like domain of Escherichia coli protein YphH and similar proteins; This subfamily ... |
83-310 |
2.39e-26 |
|
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: 107.12 E-value: 2.39e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 83 AWSIGIHLDHQTLIVVLVDLSGEIHF---RRHILVQKPQpgatfARIGEVIQELRTLPGLDWSRVLGIGVVMPGPFG-VE 158
Cdd:cd24072 1 AWVLGIVVSPNSLRAQVGNACGELLGefeYRVITLETPE-----ALIDEIIDCIDRLLKLWKDRVKGIALAIQGLVDsHK 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 159 GISSTGPTTlnGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAH 238
Cdd:cd24072 76 GVSLWSPGA--PWRNIEIKYLLEERYGIPVFVENDCNMLALAEKWQGELRQSRDFCVINLDYGIGSAIVIDNKLYIGASS 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2294039456 239 NAGEVGHIVVQPGGRACYCGNQGCLERYVSLQA----AYEFCGLDPYRALPEDLLAvdEALFDRWIDSAlPPLRQA 310
Cdd:cd24072 154 GSGEIGHTKVNPDGARCDCGRRGCLETVASNSAlkrnARVTLKLGPVSADPEKLTM--EQLIEALEEGE-PIATQI 226
|
|
| ASKHA_NBD_ROK_AlsK |
cd24070 |
nucleotide-binding domain (NBD) of D-allose kinase (AlsK) and similar proteins; AlsK (EC 2.7.1. ... |
168-345 |
2.47e-25 |
|
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: 104.17 E-value: 2.47e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 168 LNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIV 247
Cdd:cd24070 84 IPGLDGVNLADILENKLGIPVILERDVNLLLLYDMRAGNLDDEGVVLGFYIGTGIGNAILINGKPLRGKNGVAGELGHIP 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 248 VQPGGRACYCGNQGCLERYVS---LQAAYEFCGLD-PYRALPEDllAVDEALFDRWIDSALPPLRQAINLlecvFDAETV 323
Cdd:cd24070 164 VYGNGKPCGCGNTGCLETYASgraLEEIAEEHYPDtPILDIFVD--HGDEPELDEFVEDLALAIATEINI----LDPDAV 237
|
170 180
....*....|....*....|....*....
gi 2294039456 324 VVGG---TMPA-P---LLEKVLARLPPLY 345
Cdd:cd24070 238 ILGGgviDMKGfPretLEEYIRKHLRKPY 266
|
|
| ASKHA_NBD_ROK_GNE |
cd24060 |
nucleotide-binding domain (NBD) of bifunctional UDP-N-acetylglucosamine 2-epimerase ... |
84-268 |
1.62e-24 |
|
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: 102.11 E-value: 1.62e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 84 WSIGIHLDHQTLIVVLVDLSGEIHFRRhilvQKPQPGATFARIGEVIQ---ELRTLPGLDWSRVLGIGV-----VMPGpf 155
Cdd:cd24060 1 SALAVDLGGTNLRVAIVSMKGEIVKKY----TQPNPKTYEERIDLILQmcvEAASEAVKLNCRILGVGIstggrVNPR-- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 156 gvEGISSTGPTTLNGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTG 235
Cdd:cd24060 75 --EGIVLHSTKLIQEWSSVDLRTPISDALHLPVWVDNDGNCAALAERKFGHGKGVENFVTVITGTGIGGGIILNHELIHG 152
|
170 180 190
....*....|....*....|....*....|...
gi 2294039456 236 HAHNAGEVGHIVVQPGGRACYCGNQGCLERYVS 268
Cdd:cd24060 153 SSFCAAELGHIVVSLDGPDCMCGSHGCVEAYAS 185
|
|
| ASKHA_ATPase_ROK_NagC |
cd24075 |
ATPase-like domain of N-acetylglucosamine repressor (NagC) and similar proteins; NagC acts as ... |
86-268 |
2.74e-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: 101.67 E-value: 2.74e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGIGVVMPGPFG-VEGISSTG 164
Cdd:cd24075 4 LAVRLGRHDLTLGLYDLSGELLAEHTVPLTALNQEALLSQLIEEIAQFLKSHRRKTQRLIAISITLPGLINpKTGVVHYM 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 165 P-TTLNGWEGVDvesELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEV 243
Cdd:cd24075 84 PhIQVKSWPIVE---ELEQRFNVPCFIGNDIRSLALAEHYFGASKDCKDSILVRIHHGIGAGIIIDGKLFLGQNGNAGEI 160
|
170 180
....*....|....*....|....*
gi 2294039456 244 GHIVVQPGGRACYCGNQGCLERYVS 268
Cdd:cd24075 161 GHIQIEPLGERCHCGNFGCLETVAS 185
|
|
| ROK_glcA_fam |
TIGR00744 |
ROK family protein (putative glucokinase); This model models one branch of the ROK superfamily ... |
144-268 |
1.60e-23 |
|
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: 99.59 E-value: 1.60e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 144 VLGIGVVMPGPFGVEGISSTGPTTLnGWEGVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLG 223
Cdd:TIGR00744 58 IVAIGIGAPGPVNRQRGTVYFAVNL-DWKQEPLKEKVEARVGLPVVVENDANAAALGEYKKGAGKGARDVICITLGTGLG 136
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 2294039456 224 AGIFTDGHIYTGHAHNAGEVGHIVVQPGGRA-CYCGNQGCLERYVS 268
Cdd:TIGR00744 137 GGIIINGEIRHGHNGVGAEIGHIRMVPDGRLlCNCGKQGCIETYAS 182
|
|
| ASKHA_NBD_ROK_EcNanK-like |
cd24069 |
nucleotide-binding domain (NBD) of Escherichia coli N-acetylmannosamine kinase and similar ... |
103-375 |
4.00e-23 |
|
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: 97.74 E-value: 4.00e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 103 SGEIHFRRHILVQKPQPGATFARigeVIQELRTLPGLDWSRVlgiGVVMPGPFGVEGISSTGPTTLNGWEGVDVESELAR 182
Cdd:cd24069 17 NGQIIDRRQIPTPRSGTPEALAD---ALASLLADYQGQFDRV---AVASTGIIRDGVLTALNPKNLGGLSGFPLADALQQ 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 183 LSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGRACYCGNQGC 262
Cdd:cd24069 91 LLGVPVVLLNDAQAAAWGEYQAGDGEGVGNLVFITVSTGVGGGLVLNGQLLTGPNGLAGHIGHTLADPPGPVCGCGRRGC 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 263 LE-----RYVSLQAAyefcgldpyRALPEDLLAVDeaLFDRW----------IDSALPPLRQAINLLECVFDAETVVVGG 327
Cdd:cd24069 171 VEaiasgTAIAAAAS---------EILGEPVDAKD--VFERArsgdeeaarlIDRAARALADLIADLKATLDLDCVVIGG 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 2294039456 328 TM---PA--PLLEKVLARLPPLYQSVrgryltgmrVKMGMTGTDTAALGAAAL 375
Cdd:cd24069 240 SVglaEGflERVEQYLADEPAIFRVS---------LEPARLGQDAGLLGAALL 283
|
|
| ASKHA_NBD_ROK-like |
cd24152 |
nucleotide-binding domain (NBD) of an uncharacterized subgroup of the ROK family; This ... |
99-327 |
4.57e-23 |
|
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: 97.64 E-value: 4.57e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 99 LVDLSGEIHFRRHILVQKPQPGATFARIGEVIQELRTLpgldwsrVLGIGVVMPGPFGVEG--ISSTGPTTLNgwEGVDV 176
Cdd:cd24152 16 LVDENGNIIKKGKIPTPKDSLEEFLDYIKKIIKRYDEE-------IDGIAISAPGVIDPETgiIYGGGALPYL--KGFNL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 177 ESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGR--- 253
Cdd:cd24152 87 KEELEERCNLPVSIENDAKCAALAELWLGSLKGIKNGAVIVLGTGIGGAIIIDGKLYRGSHFFAGEFSYLLTDDDDKdll 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2294039456 254 --ACYCGNQGCLERYVSLQAAYEFCGLDPYRALPEDLLAVDEAlFDRWIDSalppLRQAINLLECVFDAETVVVGG 327
Cdd:cd24152 167 ffSGLASMFGLVKRYNKAKGLEPLDGEEIFEKYAKGDEAAKKI-LDEYIRN----LAKLIYNIQYILDPEVIVIGG 237
|
|
| ASKHA_ATPase_ROK_Mlc |
cd24074 |
ATPase-like domain of protein Mlc and similar proteins; Mlc, also called making large colonies ... |
185-375 |
6.38e-22 |
|
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: 95.07 E-value: 6.38e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 185 GLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGRACYCGNQGCLE 264
Cdd:cd24074 103 GLPVYVQHDISAWTLAERFFGAAKGAKNIIQIVIDDDIGAGVITDGQLLHAGSSRLGELGHTQIDPYGKRCYCGNHGCLE 182
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 265 RYVSLQA-----------------------AYEFCGLdpyrALPEDLLAVDealfdrWIDSALPPLRQAINLLECVFDAE 321
Cdd:cd24074 183 TVASIPAileqanqlleqspdsmlhgqpisIESLCQA----ALAGDPLAQD------IIIQVGRHLGRILAILVNLFNPE 252
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2294039456 322 TVVVGGTMPA------PLLEK-VLARLPPLYQSvrgrYLTGMRVKMGMTGTD-TAALGAAAL 375
Cdd:cd24074 253 KILIGSPLNNaaeilfPALSQsIRQQSLPAYSQ----HLQIESTKFYNDGTMpGAALIKDAL 310
|
|
| ASKHA_NBD_ROK_EcFRK-like |
cd24066 |
nucleotide-binding domain (NBD) of Escherichia coli fructokinase (FRK) and similar proteins; ... |
86-349 |
1.17e-21 |
|
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: 93.81 E-value: 1.17e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHIlvqkPQPGATFARIGEVIQEL--RTLPGLDWSRVLGIGvvMPGpfgveGISS- 162
Cdd:cd24066 2 IGIDLGGTKIEGIALDRAGRELLRRRV----PTPRGDYEATLDAIADLveEAEEELGAPATVGIG--TPG-----SISPr 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 163 TGP------TTLNGwegVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGH 236
Cdd:cd24066 71 TGLvknansTWLNG---KPLKADLEARLGRPVRIENDANCFALSEATDGAGAGAGVVFGVILGTGVGGGIVVNGRVLTGA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 237 AHNAGEVGHIVVQPG------GRACYCGNQGCLERYVS---LQAAYEFCGlDPYRALPEDLLAVD------EALFDRWID 301
Cdd:cd24066 148 NGIAGEWGHNPLPWPdedelpGPPCYCGKRGCVETFLSgpaLERDYARLT-GKTLSAEEIVALARagdaaaVATLDRFLD 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 2294039456 302 SALPPLRQAINLLecvfDAETVVVGGTMpapllekvlARLPPLYQSVR 349
Cdd:cd24066 227 RLGRALANVINIL----DPDVIVLGGGL---------SNIDELYTEGP 261
|
|
| PRK09698 |
PRK09698 |
D-allose kinase; Provisional |
99-327 |
4.08e-18 |
|
D-allose kinase; Provisional
Pssm-ID: 182034 [Multi-domain] Cd Length: 302 Bit Score: 83.88 E-value: 4.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 99 LVDLSGEI-HFRRH--ILVQKPQPGAtfaRIGEVIQElrTLPGLDwSRVLGIGVVMPGPFGVEG--ISSTGPTTLNGWEG 173
Cdd:PRK09698 20 LVDAEGEIlHCEKKrtAEVIAPDLVS---GLGEMIDE--YLRRFN-ARCHGIVMGFPALVSKDRrtVISTPNLPLTALDL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 174 VDVESELARLSGLPVTLENDATVaaigERFHGVARHL---NSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQP 250
Cdd:PRK09698 94 YDLADKLENTLNCPVFFSRDVNL----QLLWDVKENNltqQLVLGAYLGTGMGFAVWMNGAPWTGAHGVAGELGHIPLGD 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 251 GGRACYCGNQGCLERYVS---LQAAYEfcglDPYRALP-EDLL--AVDEALFDRWIDSALPPLRQAINLlecvFDAETVV 324
Cdd:PRK09698 170 MTQHCGCGNPGCLETNCSgmaLRRWYE----QQPRDYPlSDLFvhAGDHPFIQSLLENLARAIATSINL----FDPDAII 241
|
...
gi 2294039456 325 VGG 327
Cdd:PRK09698 242 LGG 244
|
|
| PRK05082 |
PRK05082 |
N-acetylmannosamine kinase; Provisional |
99-346 |
5.97e-18 |
|
N-acetylmannosamine kinase; Provisional
Pssm-ID: 235338 [Multi-domain] Cd Length: 291 Bit Score: 83.42 E-value: 5.97e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 99 LVDLSGEIHFRRHILV-QKPQPGATFARIGEVIQELRTLpgLDWSRVLGIGVVMPGpfgveGISSTGPTTLNGWEGVDVE 177
Cdd:PRK05082 17 LVGEDGQIRQRRQIPTpASQTPEALRQALSALVSPLQAQ--ADRVAVASTGIINDG-----ILTALNPHNLGGLLHFPLV 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 178 SELARLSGLPVTLENDATVAAIGErFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGRACYC 257
Cdd:PRK05082 90 QTLEQLTDLPTIALNDAQAAAWAE-YQALPDDIRNMVFITVSTGVGGGIVLNGKLLTGPGGLAGHIGHTLADPHGPVCGC 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 258 GNQGCLE-----RYVSLQAAYEFCGLDPyRALPEDLLAVDE---ALFDRwidSAlpplrQAI-NL---LECVFDAETVVV 325
Cdd:PRK05082 169 GRRGCVEaiasgRAIAAAAQGWLAGCDA-KTIFERAGQGDEqaqALINR---SA-----QAIaRLiadLKATLDCQCVVL 239
|
250 260
....*....|....*....|....*.
gi 2294039456 326 GGTMP-----APLLEKVLARLPPLYQ 346
Cdd:PRK05082 240 GGSVGlaegyLELVQAYLAQEPAIYH 265
|
|
| ASKHA_NBD_ROK_NAGK |
cd24057 |
nucleotide-binding domain (NBD) of N-acetyl-D-glucosamine kinase (NAGK) and similar proteins; ... |
173-375 |
2.72e-17 |
|
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: 81.51 E-value: 2.72e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 173 GVDVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVqPGG 252
Cdd:cd24057 85 GRPLRADLSARLGRPVRIDNDANCFALSEAWDGAGRGYPSVFGLILGTGVGGGLVVNGRLVGGRSGIAGEWGHGPL-PAD 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 253 R----------ACYCGNQGCLERYVS------LQAAYEFCGLDP------YRALPEDLLAVdealFDRWIDSALPPLRqa 310
Cdd:cd24057 164 AlllgydlpvlRCGCGQTGCLETYLSgrglerLYAHLYGEELDApeiiaaWAAGDPQAVAH----VDRWLDLLAGCLA-- 237
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2294039456 311 iNLLeCVFDAETVVVGGTmpapllekvLARLPPLYQ----SVRGRYLTGM---RVKMGMTGTDTAALGAAAL 375
Cdd:cd24057 238 -NIL-TALDPDVVVLGGG---------LSNFPALIAelpaALPAHLLSGArtpRIVPARHGDAGGVRGAAFL 298
|
|
| PRK09557 |
PRK09557 |
fructokinase; Reviewed |
86-344 |
6.22e-16 |
|
fructokinase; Reviewed
Pssm-ID: 236565 [Multi-domain] Cd Length: 301 Bit Score: 77.76 E-value: 6.22e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 86 IGIHLDHQTLIVVLVDLSGEIHFRRHILVQKPQPGATFARIGEVIQELRTLPGLDWSRVLGI-GVVMPGPFGVEGISSTg 164
Cdd:PRK09557 3 IGIDLGGTKIEVIALDDAGEELFRKRLPTPRDDYQQTIEAIATLVDMAEQATGQRGTVGVGIpGSISPYTGLVKNANST- 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 165 ptTLNGWEgvdVESELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVG 244
Cdd:PRK09557 82 --WLNGQP---LDKDLSARLNREVRLANDANCLAVSEAVDGAAAGKQTVFAVIIGTGCGAGVAINGRVHIGGNGIAGEWG 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 245 H---------IVVQPGGRACYCGNQGCLERYVS---LQAAYEFCGLDPYR-----ALPEDLLAVDEALFDRWIDSALPPL 307
Cdd:PRK09557 157 HnplpwmdedELRYRNEVPCYCGKQGCIETFISgtgFATDYRRLSGKALKgseiiRLVEEGDPVAELAFRRYEDRLAKSL 236
|
250 260 270
....*....|....*....|....*....|....*..
gi 2294039456 308 RQAINLLecvfDAETVVVGGTMPAplLEKVLARLPPL 344
Cdd:PRK09557 237 AHVINIL----DPDVIVLGGGMSN--VDRLYPTLPAL 267
|
|
| ASKHA_NBD_ROK_BsFRK-like |
cd24067 |
nucleotide-binding domain (NBD) of Bacillus subtilis fructokinase (FRK) and similar proteins; ... |
119-250 |
1.15e-14 |
|
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: 73.73 E-value: 1.15e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 119 PGATfarIGEVIQELRTLPgldwSRVLGIGVVMPGPFGVEGISST----GPTTLNGWEGVDVESELARLSGLPVTLENDA 194
Cdd:cd24067 33 PEET---LQAVIDFFREQE----EPIDAIGIASFGPIDLNPTSPTygyiTTTPKPGWRNFDILGALKRAFPVPVGFDTDV 105
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 2294039456 195 TVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNagEVGHIVVQP 250
Cdd:cd24067 106 NAAALAEYRWGAAKGLDSLAYITVGTGIGVGLVVNGKPVHGLLHP--EMGHIRVPR 159
|
|
| PRK13310 |
PRK13310 |
N-acetyl-D-glucosamine kinase; Provisional |
179-268 |
1.15e-11 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 183967 [Multi-domain] Cd Length: 303 Bit Score: 65.01 E-value: 1.15e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 179 ELARLSGLPVTLENDATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVqP-------G 251
Cdd:PRK13310 91 DLSARLGRDVRLDNDANCFALSEAWDDEFTQYPLVMGLILGTGVGGGLVFNGKPISGRSYITGEFGHMRL-PvdaltllG 169
|
90 100
....*....|....*....|.
gi 2294039456 252 GRA----CYCGNQGCLERYVS 268
Cdd:PRK13310 170 WDAplrrCGCGQKGCIENYLS 190
|
|
| ASKHA_NBD_ROK_PPGK |
cd24058 |
nucleotide-binding domain (NBD) of polyphosphate glucokinase (PPGK) and similar proteins; PPGK ... |
114-246 |
1.38e-10 |
|
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: 61.05 E-value: 1.38e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 114 VQKPQPgATFARIGEVIQELrtLPGLDWSRVLGIGVvmPGPFgVEGISSTGPTTLNGWEGVDVESELARLSGLPVTLEND 193
Cdd:cd24058 30 IPTPQP-ATPEAVADVVAEL--VAHFPWFGPVGVGF--PGVV-RRGVVRTAANLDKSWIGFDAAKLLSKRLGRPVRVLND 103
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 2294039456 194 ATVAAIGERFHGVARHLNSFV-YLYIGTGLGAGIFTDGHIYtghaHNAgEVGHI 246
Cdd:cd24058 104 ADAAGLAEMKGGAGKGEKGVVlVLTLGTGIGSALFVDGHLV----PNT-ELGHL 152
|
|
| PRK13311 |
PRK13311 |
N-acetyl-D-glucosamine kinase; Provisional |
117-268 |
1.43e-10 |
|
N-acetyl-D-glucosamine kinase; Provisional
Pssm-ID: 106271 [Multi-domain] Cd Length: 256 Bit Score: 61.20 E-value: 1.43e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 117 PQPGATFARIGEVIQELrTLPGLDWSRVLG-IGVVMPG-PFGVEGISSTG--PTTLngweGVDVESELARLSGLPVTLEN 192
Cdd:PRK13311 30 PTPREDYPQLLQILRDL-TEEADTYCGVQGsVGIGIPGlPNADDGTVFTAnvPSAM----GQPLQADLSRLIQREVRIDN 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2294039456 193 DATVAAIGERFHGVARHLNSFVYLYIGTGLGAGIFTDGHIYTGHAHNAGEVGHIVVQPGGR----------ACYCGNQGC 262
Cdd:PRK13311 105 DANCFALSEAWDPEFRTYPTVLGLILGTGVGGGLIVNGSIVSGRNHITGEFGHFRLPVDALdilgadiprvPCGCGHRGC 184
|
....*.
gi 2294039456 263 LERYVS 268
Cdd:PRK13311 185 IENYIS 190
|
|
| HTH_CRP |
cd00092 |
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic ... |
15-65 |
6.83e-04 |
|
helix_turn_helix, cAMP Regulatory protein C-terminus; DNA binding domain of prokaryotic regulatory proteins belonging to the catabolite activator protein family.
Pssm-ID: 238044 [Multi-domain] Cd Length: 67 Bit Score: 37.65 E-value: 6.83e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 2294039456 15 NRRVVIEAVRLHGKLTRAELARLTALTPQTVSNIVAELQQMEILTSHAPRR 65
Cdd:cd00092 12 LSLRYGAGDLVQLPLTRQEIADYLGLTRETVSRTLKELEEEGLISRRGRGK 62
|
|
| MarR_2 |
pfam12802 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
19-59 |
1.19e-03 |
|
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a non-specific resistance system. The expression of the mar operon is controlled by a repressor, MarR. A large number of compounds induce transcription of the mar operon. This is thought to be due to the compound binding to MarR, and the resulting complex stops MarR binding to the DNA. With the MarR repression lost, transcription of the operon proceeds. The structure of MarR is known and shows MarR as a dimer with each subunit containing a winged-helix DNA binding motif.
Pssm-ID: 432797 [Multi-domain] Cd Length: 60 Bit Score: 36.80 E-value: 1.19e-03
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 2294039456 19 VIEAVRLHGKLTRAELARLTALTPQTVSNIVAELQQMEILT 59
Cdd:pfam12802 10 VLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLVE 50
|
|
| COG2345 |
COG2345 |
Predicted transcriptional regulator, ArsR family [Transcription]; |
16-69 |
2.20e-03 |
|
Predicted transcriptional regulator, ArsR family [Transcription];
Pssm-ID: 441914 [Multi-domain] Cd Length: 217 Bit Score: 39.14 E-value: 2.20e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 2294039456 16 RRVVIEAVRLHGKLTRAELARLTALTPQTVSNIVAELQQMEILTSHAPRRAAGR 69
Cdd:COG2345 15 RRRILELLKRAGPVTAAELAEALGLTPNAVRRHLDALEEEGLVERETERRGRGR 68
|
|
| COG2512 |
COG2512 |
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ... |
14-70 |
6.67e-03 |
|
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain [General function prediction only];
Pssm-ID: 442002 [Multi-domain] Cd Length: 80 Bit Score: 35.27 E-value: 6.67e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 2294039456 14 HNRRVVIEAVRLH-GKLTRAELARLTALTPQTVSNIVAELQQMEILTshapRRAAGRG 70
Cdd:COG2512 15 EDERRVLELLRENgGRMTQSEIVKETGWSKSKVSRLLSRLEERGLIE----KERVGRE 68
|
|
| |
