|
Name |
Accession |
Description |
Interval |
E-value |
| PRK09954 |
PRK09954 |
sugar kinase; |
1-360 |
0e+00 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 654.31 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 1 MNDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKGAIKGKGYILTEQEYCVSLGAVNMDIRGIADIHYPQ 80
Cdd:PRK09954 1 MNNREKEILAILRRNPLIQQNEIADILQISRSRVAAHIMDLMRKGRIKGKGYILTEQEYCVVVGAINMDIRGMADIRYPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 81 PVSNPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQSCIRLHGHNTATYLSIANPQEET 160
Cdd:PRK09954 81 AASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETLLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 161 VLAINDTHILQSLTPQLLNQYRDLLTHAGVILVDCNLTEPLLEWVFTLANAIPVFVDTVSEFKAHRIRPWLGKIHTLKPT 240
Cdd:PRK09954 161 VLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWVFTLADEIPVFVDTVSEFKAGKIKHWLAHIHTLKPT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 241 LRELQILWGEPIENEADRDRALAWLHERGTRRVVICSEDDSVFCSEAGGERFQMKLPGHTTIDSFGADDALMAGLLYSYL 320
Cdd:PRK09954 241 QPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLPDESVFCSEKDGEQFLLTAPAHTTVDSFGADDGFMAGLVYSFL 320
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 1533535909 321 DGSDFKESVAFAMACTAITRASDSINNPSLSVDNALNLLP 360
Cdd:PRK09954 321 EGYSFRDSARFAMACAAISRASGSLNNPTLSADNALSLVP 360
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
54-359 |
5.94e-92 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 278.02 E-value: 5.94e-92
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 54 LTEQEYCVSLGAVNMDIRG--IADIHYPQpvSNPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQ 131
Cdd:PRK09850 1 MREKDYVVIIGSANIDVAGysHESLNYAD--SNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQSLLTQTNQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 132 AGVNVQSCIRLHGHNTATYLSIANPQEETVLAINDTHILQSLTPQLLNQYRDLLTHAGVILVDCNLTEPLLEWVFTLANA 211
Cdd:PRK09850 79 SGVYVDKCLIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAAN 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 212 IPVFVDTVSEFKAHRIRPWLGKIHTLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVICSEDDSVFCSEAGGER 291
Cdd:PRK09850 159 VPVFVDPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGES 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533535909 292 fQMKLPGHT-TIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAITRASDSINNPSLSVDNALNLL 359
Cdd:PRK09850 239 -GWSAPIKTnVINVTGAGDAMMAGLASCWVDGMPFAESVRFAQGCSSMALSCEYTNNPDLSIANVISLV 306
|
|
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
59-342 |
1.28e-91 |
|
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238916 [Multi-domain] Cd Length: 288 Bit Score: 276.12 E-value: 1.28e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 59 YCVSLGAVNMDIRGIADIHYPQPVSNPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVqS 138
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNV-R 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 139 CIRLHGHNTATYLSIANPQEETVLAINDTHILQSLTPQLLNQYRDLLTHAGVILVDCNLTEPLLEWVFTLA--NAIPVFV 216
Cdd:cd01941 80 GIVFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAakHGVPVAF 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 217 DTVSEFKAHRIRPWLGKIHTLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVIC-SEDDSVFCSEAGGERFQMK 295
Cdd:cd01941 160 EPTSAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTlGAKGVLLSSREGGVETKLF 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1533535909 296 LPG--HTTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAITRAS 342
Cdd:cd01941 240 PAPqpETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
59-342 |
6.89e-60 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 194.87 E-value: 6.89e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 59 YCVSLGAVNMDIRGIADIHYPQPVsNPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQS 138
Cdd:pfam00294 1 KVVVIGEANIDLIGNVEGLPGELV-RVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQELKKEGVDTDY 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 139 CIRLHGHNTATYLSIANPQEETVLAINDTHILQsLTPQLLNQYRDLLTHAGVI----LVDCNLTEPLLEWVFTLANA--- 211
Cdd:pfam00294 80 VVIDEDTRTGTALIEVDGDGERTIVFNRGAAAD-LTPEELEENEDLLENADLLyisgSLPLGLPEATLEELIEAAKNggt 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 212 -IPVFVDTVSEFKaHRIRPWLGKIHTLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVICSEDDSVFCSEAGGE 290
Cdd:pfam00294 159 fDPNLLDPLGAAR-EALLELLPLADLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1533535909 291 RFQMKLPGHTTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAITRAS 342
Cdd:pfam00294 238 VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQK 289
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
61-339 |
7.50e-44 |
|
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar or nucleoside kinase, ribokinase family is part of the Pathway/BioSystem: Glycolysis
Pssm-ID: 440290 [Multi-domain] Cd Length: 301 Bit Score: 153.50 E-value: 7.50e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 61 VSLGAVNMDIRGIADiHYPQPVS--NPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQS 138
Cdd:COG0524 3 LVIGEALVDLVARVD-RLPKGGEtvLAGSFRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAELRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 139 CIRLHGHNTATYLSIANPQEETVLAINDTHILQsLTPQLLNqyRDLLTHAGVILVDCNL--TEPLLEWVFTLANA----- 211
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFYRGANAE-LTPEDLD--EALLAGADILHLGGITlaSEPPREALLAALEAaraag 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 212 IPVFVDTVSEFKAH-----RIRPWLGKIHTLKPTLRELQILWGEPieneaDRDRALAWLHERGTRRVVI-CSEDDSVFCS 285
Cdd:COG0524 159 VPVSLDPNYRPALWepareLLRELLALVDILFPNEEEAELLTGET-----DPEEAAAALLARGVKLVVVtLGAEGALLYT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 1533535909 286 eaGGERFQMKLPGHTTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAIT 339
Cdd:COG0524 234 --GGEVVHVPAFPVEVVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALV 285
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
79-344 |
2.36e-20 |
|
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form 2-keto-3-deoxy-6-phosphogluconate (KDGP). KDG is the common intermediate product, that allows organisms to channel D-glucuronate and/or D-galacturinate into the glycolysis and therefore use polymers, like pectin and xylan as carbon sources.
Pssm-ID: 238571 [Multi-domain] Cd Length: 294 Bit Score: 89.94 E-value: 2.36e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 79 PQPVSNPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQSCIRLHGHNTATYL-SIANPQ 157
Cdd:cd01166 17 GGRLEQADSFRKFFGGAEANVAVGLARLGHRVALVTAVGDDPFGRFILAELRREGVDTSHVRVDPGRPTGLYFlEIGAGG 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 158 EETVL--------------AINDTHILQS-------LTPQLLNQYRDLLTHA--------GVILVDCNLTEPLLewvfTL 208
Cdd:cd01166 97 ERRVLyyragsaasrltpeDLDEAALAGAdhlhlsgITLALSESAREALLEAleaakargVTVSFDLNYRPKLW----SA 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 209 ANAIPVFvdtvsefkahriRPWLGKIHTLKPTLRELQILWGEPIENEADrDRALAWlhERGTRRVVICSEDDSVFCSEAG 288
Cdd:cd01166 173 EEAREAL------------EELLPYVDIVLPSEEEAEALLGDEDPTDAA-ERALAL--ALGVKAVVVKLGAEGALVYTGG 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 289 GERFQmklPGHTT--IDSFGADDALMAGLLYSYLDGSDFKESVAFAMAC--TAITRASDS 344
Cdd:cd01166 238 GRVFV---PAYPVevVDTTGAGDAFAAGFLAGLLEGWDLEEALRFANAAaaLVVTRPGDI 294
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
63-345 |
1.21e-18 |
|
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This reaction is the first step in the ribose metabolism. It traps ribose within the cell after uptake and also prepares the sugar for use in the synthesis of nucleotides and histidine, and for entry into the pentose phosphate pathway. Ribokinase is dimeric in solution.
Pssm-ID: 238579 [Multi-domain] Cd Length: 292 Bit Score: 84.91 E-value: 1.21e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 63 LGAVNMDIRGIADiHYPQP---------VSNPG----NiQCSAggVARniahnlalLGRDVHLISAVGSDFYGETLLEQT 129
Cdd:cd01174 5 VGSINVDLVTRVD-RLPKPgetvlgssfETGPGgkgaN-QAVA--AAR--------LGARVAMIGAVGDDAFGDELLENL 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 130 RQAGVNVQSCIRLHGHNTATYLSIANPQEETVLAI----NDThilqsLTPQLLNQYRDLLTHAGVILVDCNLTEPLLEWV 205
Cdd:cd01174 73 REEGIDVSYVEVVVGAPTGTAVITVDESGENRIVVvpgaNGE-----LTPADVDAALELIAAADVLLLQLEIPLETVLAA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 206 FTLANA--IPVFVDTvSEFKAHRIrPWLGKIHTLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVIC-SEDDSV 282
Cdd:cd01174 148 LRAARRagVTVILNP-APARPLPA-ELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTlGAKGAL 225
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1533535909 283 FCSEAGGERFqmklPGH--TTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAI--TR--ASDSI 345
Cdd:cd01174 226 LASGGEVEHV----PAFkvKAVDTTGAGDTFIGALAAALARGLSLEEAIRFANAAAALsvTRpgAQPSI 290
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
92-335 |
9.86e-18 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 82.49 E-value: 9.86e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 92 AGG----VARNIAHnlalLGRDVHLISAVGsDFYGETLLEQTRQAGVNVQsCIRLHGhNTATYLSIANPQEETVLAINDT 167
Cdd:COG1105 34 PGGkginVARVLKA----LGVDVTALGFLG-GFTGEFIEELLDEEGIPTD-FVPIEG-ETRINIKIVDPSDGTETEINEP 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 168 --HILQSLTPQLLNQYRDLLTHAGVILV----------DCnltepLLEWVFTL-ANAIPVFVDTVSE-----FKAHrirP 229
Cdd:COG1105 107 gpEISEEELEALLERLEELLKEGDWVVLsgslppgvppDF-----YAELIRLArARGAKVVLDTSGEalkaaLEAG---P 178
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 230 WLgkihtLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVIcS--EDDSVFCSEAGgeRFQMKLPGHTTIDSFGA 307
Cdd:COG1105 179 DL-----IKPNLEELEELLGRPLETLEDIIAAARELLERGAENVVV-SlgADGALLVTEDG--VYRAKPPKVEVVSTVGA 250
|
250 260
....*....|....*....|....*...
gi 1533535909 308 DDALMAGLLYSYLDGSDFKESVAFAMAC 335
Cdd:COG1105 251 GDSMVAGFLAGLARGLDLEEALRLAVAA 278
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
93-339 |
5.70e-14 |
|
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238917 [Multi-domain] Cd Length: 279 Bit Score: 71.19 E-value: 5.70e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 93 GGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVqSCIRLhghntatylsiaNPQEETVLA--INDTHIL 170
Cdd:cd01942 36 GGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYLEELREEGVDT-SHVRV------------VDEDSTGVAfiLTDGDDN 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 171 QSLT-------PQLLNQYRDLLTHAGVILVDcnLTEPLLEWVFTLANA-IPVFVDT---VSEFKAHRIRPWLGKIHTLKP 239
Cdd:cd01942 103 QIAYfypgamdELEPNDEADPDGLADIVHLS--SGPGLIELARELAAGgITVSFDPgqeLPRLSGEELEEILERADILFV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 240 TlrelqilwgepiENEADRDRALAWLHE----RGTRRVVI-CSEDDSVFCSEaGGERFQMKLPGHTTIDSFGADDALMAG 314
Cdd:cd01942 181 N------------DYEAELLKERTGLSEaelaSGVRVVVVtLGPKGAIVFED-GEEVEVPAVPAVKVVDTTGAGDAFRAG 247
|
250 260
....*....|....*....|....*
gi 1533535909 315 LLYSYLDGSDFKESVAFAMACTAIT 339
Cdd:cd01942 248 FLYGLLRGYDLEESLRLGNLAASLK 272
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
61-339 |
1.83e-13 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 70.54 E-value: 1.83e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 61 VSLGAVNMDIRGIADiHYPQPvsnpG------NIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGV 134
Cdd:PTZ00292 19 VVVGSSNTDLIGYVD-RMPQV----GetlhgtSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDGFGSDTIKNFKRNGV 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 135 NVQSCIRLhgHNTATYLS-----IANPQEETVLAINDTHilqSLTPQLLNQYRDLLTHAGVILVdCNLTEPL-------- 201
Cdd:PTZ00292 94 NTSFVSRT--ENSSTGLAmifvdTKTGNNEIVIIPGANN---ALTPQMVDAQTDNIQNICKYLI-CQNEIPLettldalk 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 202 ---LEWVFTLANAIPVfvdtVSEFKAHRIRPWLGKIHTLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVICSE 278
Cdd:PTZ00292 168 eakERGCYTVFNPAPA----PKLAEVEIIKPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLG 243
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533535909 279 DDSvfCSEAGGERFQMKLPGHT--TIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAIT 339
Cdd:PTZ00292 244 ANG--CLIVEKENEPVHVPGKRvkAVDTTGAGDCFVGSMAYFMSRGKDLKESCKRANRIAAIS 304
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
63-338 |
2.41e-13 |
|
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like group is part of the ribokinase/pfkB sugar kinase superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238922 [Multi-domain] Cd Length: 265 Bit Score: 69.37 E-value: 2.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 63 LGAVNMDIRGIADiHYPQP--VSNPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVqsci 140
Cdd:cd01947 5 VGHVEWDIFLSLD-APPQPggISHSSDSRESPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSLEELESGGDKH---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 141 rlhghntatylsianpqeetVLAINDTHilqslTPQLLNqyrdLLTHAG--VILVDCNLTEPLLEWVfTLANAIPVFVD- 217
Cdd:cd01947 80 --------------------TVAWRDKP-----TRKTLS----FIDPNGerTITVPGERLEDDLKWP-ILDEGDGVFITa 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 218 TVSEFKAHRIRPWLG----------KIHTLKPTLRELQILwgepIENEADRDRALAWLHERG-TRRVVICSEDDSVFCSE 286
Cdd:cd01947 130 AAVDKEAIRKCRETKlvilqvtprvRVDELNQALIPLDIL----IGSRLDPGELVVAEKIAGpFPRYLIVTEGELGAILY 205
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1533535909 287 AGGERFQMKLPGHTTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAI 338
Cdd:cd01947 206 PGGRYNHVPAKKAKVPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAI 257
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
61-339 |
1.08e-12 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 67.97 E-value: 1.08e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 61 VSLGAVNMD-IRGIAdiHYPQP----VSNpgNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVN 135
Cdd:PRK11142 6 VVLGSINADhVLNLE--SFPRPgetlTGR--HYQVAFGGKGANQAVAAARLGADIAFIACVGDDSIGESMRQQLAKDGID 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 136 VQSCIRLHGHNTATYLSIANPQEETVLAI----NDthilqSLTPQLLNQYRDLLTHAGVILVdcNLTEPLlewvftlana 211
Cdd:PRK11142 82 TAPVSVIKGESTGVALIFVNDEGENSIGIhagaNA-----ALTPALVEAHRELIANADALLM--QLETPL---------- 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 212 ipvfvDTVSE----FKAHRIR------P-------WLGKIHTLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVV 274
Cdd:PRK11142 145 -----ETVLAaakiAKQHGTKvilnpaParelpdeLLALVDIITPNETEAEKLTGIRVEDDDDAAKAAQVLHQKGIETVL 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533535909 275 ICSEDDSVFCSEAGgerFQMKLPGHTT--IDSFGADD----ALMAGLlysyLDGSDFKESVAFAMACTAIT 339
Cdd:PRK11142 220 ITLGSRGVWLSENG---EGQRVPGFRVqaVDTIAAGDtfngALVTAL----LEGKPLPEAIRFAHAAAAIA 283
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
92-335 |
1.59e-12 |
|
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. FruK plays an important role in the predominant pathway for fructose utilisation.This group also contains tagatose-6-phophate kinase, an enzyme of the tagatose 6-phosphate pathway, which responsible for breakdown of the galactose moiety during lactose metabolism by bacteria such as L. lactis.
Pssm-ID: 238570 [Multi-domain] Cd Length: 289 Bit Score: 67.17 E-value: 1.59e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 92 AGGVARNIAHNLALLGRDVHLISAVGSDFyGETLLEQTRQAGVNVQsCIRLHGhNTATYLSIANPQ-EETVL-----AIN 165
Cdd:cd01164 35 AGGKGINVARVLKDLGVEVTALGFLGGFT-GDFFEALLKEEGIPDD-FVEVAG-ETRINVKIKEEDgTETEInepgpEIS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 166 DTHIlqsltPQLLNQYRDLLTHAGVILVDCNL-----TEPLLEWVfTLANA--IPVFVDTVSE--FKAHRIRPWLgkiht 236
Cdd:cd01164 112 EEEL-----EALLEKLKALLKKGDIVVLSGSLppgvpADFYAELV-RLAREkgARVILDTSGEalLAALAAKPFL----- 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 237 LKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVICSEDD-SVFCSeaGGERFQMKLPGHTTIDSFGADDALMAGL 315
Cdd:cd01164 181 IKPNREELEELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADgALLVT--KDGVYRASPPKVKVVSTVGAGDSMVAGF 258
|
250 260
....*....|....*....|
gi 1533535909 316 LYSYLDGSDFKESVAFAMAC 335
Cdd:cd01164 259 VAGLAQGLSLEEALRLAVAA 278
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
79-338 |
3.02e-09 |
|
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the lipopolysaccharide (LPS) core precursor ADP-L-glycero-D-manno-heptose. LPS plays an important role in maintaining the structural integrity of the bacterial outer membrane of gram-negative bacteria. RfaE consists of two domains, a sugar kinase domain, represented here, and a domain belonging to the cytidylyltransferase superfamily.
Pssm-ID: 238577 [Multi-domain] Cd Length: 304 Bit Score: 57.57 E-value: 3.02e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 79 PQPVSNPGNIQCSAGGVArNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQsCIRLHGHNTATYLS-IANPQ 157
Cdd:cd01172 26 PVPVVKVEREEIRLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDLLRKLLEKEGIDTD-GIVDEGRPTTTKTRvIARNQ 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 158 EetVLAI---NDTHILQSLTPQLLNQYRDLLTHA-GVILVDCN---LTEPLLEWVFTLAN--AIPVFVD--TVSEFKAHR 226
Cdd:cd01172 104 Q--LLRVdreDDSPLSAEEEQRLIERIAERLPEAdVVILSDYGkgvLTPRVIEALIAAARelGIPVLVDpkGRDYSKYRG 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 227 IrpwlgkihTL-KPTLRELQILWGEPIENEAD-RDRALAWLHERGTRRVVIC-SEDD-SVFcsEAGGERfqMKLPGHTT- 301
Cdd:cd01172 182 A--------TLlTPNEKEAREALGDEINDDDElEAAGEKLLELLNLEALLVTlGEEGmTLF--ERDGEV--QHIPALAKe 249
|
250 260 270
....*....|....*....|....*....|....*...
gi 1533535909 302 -IDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAI 338
Cdd:cd01172 250 vYDVTGAGDTVIATLALALAAGADLEEAAFLANAAAGV 287
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
63-337 |
3.55e-09 |
|
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time. .
Pssm-ID: 238920 [Multi-domain] Cd Length: 284 Bit Score: 56.92 E-value: 3.55e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 63 LGAVNMDIRGIADiHYPQPVS--NPGNIQCSAGGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQSCI 140
Cdd:cd01945 5 VGLAVLDLIYLVA-SFPGGDGkiVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEGVDTSFIV 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 141 RLHGHNTA-TYLSIANPQEETVL--AINDTHILQSLTPQLLNQYRdllthagVILVDCNLTEPLLEwVFTLANA----IP 213
Cdd:cd01945 84 VAPGARSPiSSITDITGDRATISitAIDTQAAPDSLPDAILGGAD-------AVLVDGRQPEAALH-LAQEARArgipIP 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 214 VFVDTVSEFKAHRIrpwLGKIHTLKPTLRELQILWGEPieneadRDRALAWLHERGTRRVVICSEDDSVFCSEAGGERFQ 293
Cdd:cd01945 156 LDLDGGGLRVLEEL---LPLADHAICSENFLRPNTGSA------DDEALELLASLGIPFVAVTLGEAGCLWLERDGELFH 226
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1533535909 294 MKLPGHTTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTA 337
Cdd:cd01945 227 VPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREALRFASAAAA 270
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
61-320 |
5.40e-09 |
|
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including carbohydrates and aromatic small molecules, all are phosphorylated at a hydroxyl group. The superfamily includes ribokinase, fructokinase, ketohexokinase, 2-dehydro-3-deoxygluconokinase, 1-phosphofructokinase, the minor 6-phosphofructokinase (PfkB), inosine-guanosine kinase, and adenosine kinase. Even though there is a high degree of structural conservation within this superfamily, their multimerization level varies widely, monomeric (e.g. adenosine kinase), dimeric (e.g. ribokinase), and trimeric (e.g THZ kinase).
Pssm-ID: 238177 [Multi-domain] Cd Length: 196 Bit Score: 55.56 E-value: 5.40e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 61 VSLGAVNMDIRGIADIHYPQPVSNPGNI-QCSAGGVARNIAHNLALLGRDVHLISAvgsdfygetlleqtrqagvnvqSC 139
Cdd:cd00287 3 LVVGSLLVDVILRVDALPLPGGLVRPGDtEERAGGGAANVAVALARLGVSVTLVGA----------------------DA 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 140 IrlhghntatYLSIANPQEETVLAIndthilqsltPQLLNQYrdllthagVILVDCNLTEPLLEWVFTLANAIPVFVDTv 219
Cdd:cd00287 61 V---------VISGLSPAPEAVLDA----------LEEARRR--------GVPVVLDPGPRAVRLDGEELEKLLPGVDI- 112
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 220 sefkahrirpwlgkihtLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVI-CSEDDSVFCSEaGGERFQMKLPG 298
Cdd:cd00287 113 -----------------LTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVtLGEKGAIVATR-GGTEVHVPAFP 174
|
250 260
....*....|....*....|..
gi 1533535909 299 HTTIDSFGADDALMAGLLYSYL 320
Cdd:cd00287 175 VKVVDTTGAGDAFLAALAAGLA 196
|
|
| fruK |
PRK09513 |
1-phosphofructokinase; Provisional |
219-339 |
8.05e-09 |
|
1-phosphofructokinase; Provisional
Pssm-ID: 181923 [Multi-domain] Cd Length: 312 Bit Score: 56.24 E-value: 8.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 219 VSEFKAHrirPWLgkihtLKPTLRELQILWGEPIENEADRDRALAWLHERGTRRVVIC-SEDDSVFCSEAGGerFQMKLP 297
Cdd:PRK09513 174 VAGLKAA---PWL-----VKPNRRELEIWAGRKLPELKDVIEAAHALREQGIAHVVISlGAEGALWVNASGE--WIAKPP 243
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 1533535909 298 GHTTIDSFGADDALMAGLLYSYLDGSDFKESVAFAMACTAIT 339
Cdd:PRK09513 244 ACDVVSTVGAGDSMVGGLIYGLLMRESSEHTLRLATAVSALA 285
|
|
| HTH_24 |
pfam13412 |
Winged helix-turn-helix DNA-binding; |
3-47 |
6.73e-07 |
|
Winged helix-turn-helix DNA-binding;
Pssm-ID: 404317 [Multi-domain] Cd Length: 45 Bit Score: 45.50 E-value: 6.73e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1533535909 3 DREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKGAI 47
Cdd:pfam13412 1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
|
|
| PRK11316 |
PRK11316 |
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose ... |
79-217 |
4.48e-06 |
|
bifunctional D-glycero-beta-D-manno-heptose-7-phosphate kinase/D-glycero-beta-D-manno-heptose 1-phosphate adenylyltransferase HldE;
Pssm-ID: 183085 [Multi-domain] Cd Length: 473 Bit Score: 48.29 E-value: 4.48e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 79 PQPVSNPGNIQCSAGGVArNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVQsCIRLHGHNTATYLSIA--NP 156
Cdd:PRK11316 37 PVPVVKVNQIEERPGGAA-NVAMNIASLGAQARLVGLTGIDEAARALSKLLAAVGVKCD-FVSVPTHPTITKLRVLsrNQ 114
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1533535909 157 Q------EETVLAINDThilqsltpQLLNQYRDLLTHAGV-ILVDCN---LTEPllEWVFTLANA--IPVFVD 217
Cdd:PRK11316 115 QlirldfEEGFEGVDPQ--------PLLERIEQALPSIGAlVLSDYAkgaLASV--QAMIQLARKagVPVLID 177
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
243-341 |
5.79e-05 |
|
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5'-phosphate (PLP), by catalyzing the phosphorylation of the precursor vitamin B6 in the presence of Zn2+ and ATP. Mammals are unable to synthesize PLP de novo and require its precursors in the form of vitamin B6 (pyridoxal, pyridoxine, and pyridoxamine) from their diet. Pyridoxal kinase encoding genes are also found in many other species including yeast and bacteria.
Pssm-ID: 238578 [Multi-domain] Cd Length: 254 Bit Score: 44.11 E-value: 5.79e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 243 ELQILWGEPIENEADRDRALAWLHERGTRRVVI----CSEDDSVFC-SEAGGERFQMKLPGHTTIDSF-GADDALMAGLL 316
Cdd:cd01173 146 ELELLTGKKINDLEDAKAAARALHAKGPKTVVVtsveLADDDRIEMlGSTATEAWLVQRPKIPFPAYFnGTGDLFAALLL 225
|
90 100
....*....|....*....|....*
gi 1533535909 317 YSYLDGSDFKEsvAFAMACTAITRA 341
Cdd:cd01173 226 ARLLKGKSLAE--ALEKALNFVHEV 248
|
|
| HTH_11 |
pfam08279 |
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins. |
6-52 |
9.83e-05 |
|
HTH domain; This family includes helix-turn-helix domains in a wide variety of proteins.
Pssm-ID: 429896 [Multi-domain] Cd Length: 52 Bit Score: 39.72 E-value: 9.83e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1533535909 6 KQILKILRRN-PLIQQHEIADILQISRSRVAAHIMDLTRKG----AIKGKGY 52
Cdd:pfam08279 1 LQILQLLLEArGPISGQELAEKLGVSRRTIRRDIKILEELGvpieAEPGRGY 52
|
|
| Lrp |
COG1522 |
DNA-binding transcriptional regulator, Lrp family [Transcription]; |
1-54 |
2.14e-04 |
|
DNA-binding transcriptional regulator, Lrp family [Transcription];
Pssm-ID: 441131 [Multi-domain] Cd Length: 138 Bit Score: 40.92 E-value: 2.14e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1533535909 1 MNDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKGAIKGKGYIL 54
Cdd:COG1522 3 LDEIDRRILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVIRGYGAVV 56
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
93-339 |
2.31e-04 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 42.42 E-value: 2.31e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 93 GGVARNIAHNLALLGRDVHLISAVGSDFYGETLLEQTRQAGVNVqSCIRLHGHNTA-TYLSIANpqeetvlaiNDthilq 171
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQDLARMGVDI-SHVHTKHGVTAqTQVELHD---------ND----- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 172 sltpQLLNQYRDllthaGViLVDCNLTEPLLEWVFT---LANAIpvfvdtvsefkahrirpWlGKIHTLKPTLRELQIL- 247
Cdd:PRK09813 88 ----RVFGDYTE-----GV-MADFALSEEDYAWLAQydiVHAAI-----------------W-GHAEDAFPQLHAAGKLt 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 248 -------WGEPI-----------------ENEADRDRaLAWLHERGTrRVVICSEDDSVFCSEAGGERFQMKLPGHTTID 303
Cdd:PRK09813 140 afdfsdkWDSPLwqtlvphldyafasapqEDEFLRLK-MKAIVARGA-GVVIVTLGENGSIAWDGAQFWRQAPEPVTVVD 217
|
250 260 270
....*....|....*....|....*....|....*.
gi 1533535909 304 SFGADDALMAGLLYSYLDGSDFKESVAFAMACTAIT 339
Cdd:PRK09813 218 TMGAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKT 253
|
|
| cas_HTH |
TIGR01884 |
CRISPR locus-related DNA-binding protein; Most but not all examples of this family are ... |
2-56 |
3.42e-04 |
|
CRISPR locus-related DNA-binding protein; Most but not all examples of this family are associated with CRISPR loci, a combination of DNA repeats and characteristic proteins encoded near the repeat cluster. The C-terminal region of this protein is homologous to DNA-binding helix-turn-helix domains with predicted transcriptional regulatory activity. [Regulatory functions, DNA interactions, , ]
Pssm-ID: 273852 [Multi-domain] Cd Length: 203 Bit Score: 41.19 E-value: 3.42e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 2 NDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKGAI-----KGKGYILTE 56
Cdd:TIGR01884 142 SREELKILEVLKATGEKSVKNIAKKLGKSLSTISRHLAELEKKGLVeqkgrKGKRYSLTK 201
|
|
| HTH_ASNC |
smart00344 |
helix_turn_helix ASNC type; AsnC: an autogenously regulated activator of asparagine synthetase ... |
1-54 |
7.43e-04 |
|
helix_turn_helix ASNC type; AsnC: an autogenously regulated activator of asparagine synthetase A transcription in Escherichia coli)
Pssm-ID: 214628 [Multi-domain] Cd Length: 108 Bit Score: 38.65 E-value: 7.43e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1533535909 1 MNDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKGAIKGKGYIL 54
Cdd:smart00344 1 LDEIDRKILEELQKDARISLAELAKKVGLSPSTVHNRVKRLEEEGVIKGYTAVL 54
|
|
| BirA |
COG1654 |
Biotin operon repressor [Transcription]; |
1-57 |
7.73e-04 |
|
Biotin operon repressor [Transcription];
Pssm-ID: 441260 [Multi-domain] Cd Length: 324 Bit Score: 41.12 E-value: 7.73e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1533535909 1 MNDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKG----AIKGKGYILTEQ 57
Cdd:COG1654 2 MSSTRLKLLRLLADGEFHSGEELAEELGVSRAAVWKHIKALRELGyeieSVPGKGYRLAEP 62
|
|
| COG3398 |
COG3398 |
Predicted transcriptional regulator, contains two HTH domains [Transcription]; |
1-48 |
8.71e-04 |
|
Predicted transcriptional regulator, contains two HTH domains [Transcription];
Pssm-ID: 442625 [Multi-domain] Cd Length: 159 Bit Score: 39.48 E-value: 8.71e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1533535909 1 MNDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKGAIK 48
Cdd:COG3398 19 DNDTRRRIYEYIRENPGIHFREIVRDLGLNRGTLRYHLRRLEREGKIT 66
|
|
| PTZ00344 |
PTZ00344 |
pyridoxal kinase; Provisional |
239-334 |
1.17e-03 |
|
pyridoxal kinase; Provisional
Pssm-ID: 240372 [Multi-domain] Cd Length: 296 Bit Score: 40.45 E-value: 1.17e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1533535909 239 PTLRELQILWGEPIENEADRDRALAWLHERGTRRVVICS--EDDS----------VFCSEAGGERFQMKLPGHTtiDSFG 306
Cdd:PTZ00344 145 PNQFEASLLSGVEVKDLSDALEAIDWFHEQGIPVVVITSfrEDEDpthlrfllscRDKDTKNNKRFTGKVPYIE--GRYT 222
|
90 100
....*....|....*....|....*...
gi 1533535909 307 ADDALMAGLLYSYLDGSDFKESVAFAMA 334
Cdd:PTZ00344 223 GTGDLFAALLLAFSHQHPMDLAVGKAMG 250
|
|
| COG3398 |
COG3398 |
Predicted transcriptional regulator, contains two HTH domains [Transcription]; |
2-45 |
1.79e-03 |
|
Predicted transcriptional regulator, contains two HTH domains [Transcription];
Pssm-ID: 442625 [Multi-domain] Cd Length: 159 Bit Score: 38.71 E-value: 1.79e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1533535909 2 NDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKG 45
Cdd:COG3398 96 RETPRRILLYLLENPGATNKELAEELGISRSTVSWHLKRLEEDG 139
|
|
| MarR_2 |
pfam12802 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
1-45 |
4.03e-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: 35.26 E-value: 4.03e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1533535909 1 MNDREKQILKILRRNPLIQQHEIADILQISRSRVAAHIMDLTRKG 45
Cdd:pfam12802 3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKG 47
|
|
| Sigma70_r4 |
pfam04545 |
Sigma-70, region 4; Region 4 of sigma-70 like sigma-factors are involved in binding to the -35 ... |
1-34 |
5.95e-03 |
|
Sigma-70, region 4; Region 4 of sigma-70 like sigma-factors are involved in binding to the -35 promoter element via a helix-turn-helix motif. Due to the way Pfam works, the threshold has been set artificially high to prevent overlaps with other helix-turn-helix families. Therefore there are many false negatives.
Pssm-ID: 461347 [Multi-domain] Cd Length: 50 Bit Score: 34.33 E-value: 5.95e-03
10 20 30
....*....|....*....|....*....|....
gi 1533535909 1 MNDREKQILKiLRRNPLIQQHEIADILQISRSRV 34
Cdd:pfam04545 5 LPPRERQVLV-LRYGEGLTLEEIGERLGISRERV 37
|
|
| |
