|
Name |
Accession |
Description |
Interval |
E-value |
| YeiC_kinase_like |
cd01941 |
YeiC-like sugar kinase. Found in eukaryotes and bacteria, YeiC-like kinase is part of the ... |
59-343 |
9.38e-123 |
|
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: 355.47 E-value: 9.38e-123
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 59 PIVCIGAANVDRKFYVHKNLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEMIKRLSTPFMNLDHV 138
Cdd:cd01941 1 EIVVIGAANIDLRGKVSGSLVPGTSNPGHVKQSPGGVGRNIAENLARLGVSVALLSAVGDDSEGESILEESEKAGLNVRG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 139 QQFENASTGSYTALISKEGDMTYGLADMEVFDYITPEFLIKRSHLLKKAKCIIVDLNLGKEALNFLCAYTTKHQIKLVIT 218
Cdd:cd01941 81 IVFEGRSTASYTAILDKDGDLVVALADMDIYELLTPDFLRKIREALKEAKPIVVDANLPEEALEYLLALAAKHGVPVAFE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 219 TVSSPKMKNMPDSLHAIDWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKELIYRSGEEEIIKSVMP 298
Cdd:cd01941 161 PTSAPKLKKLFYLLHAIDLLTPNRAELEALAGALIENNEDENKAAKILLLPGIKNVIVTLGAKGVLLSSREGGVETKLFP 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 612901457 299 ---SNSVKDVTGAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTIET 343
Cdd:cd01941 241 apqPETVVNVTGAGDAFVAGLVAGLLEGMSLDDSLRFAQAAAALTLES 288
|
|
| PRK09954 |
PRK09954 |
sugar kinase; |
1-328 |
8.14e-44 |
|
sugar kinase;
Pssm-ID: 182165 [Multi-domain] Cd Length: 362 Bit Score: 155.09 E-value: 8.14e-44
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 1 MSDSEKEILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYVMGKAYVLNEDYPIVCIGAANVDRKFYVHKNLVA 80
Cdd:PRK09954 1 MNNREKEILAILRRNPLIQQNEIADILQISRSRVAAHIMDLMRKGRIKGKGYILTEQEYCVVVGAINMDIRGMADIRYPQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 81 ETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEM-IKRLSTPFMNLDHVQQFENASTGSYTALISKEGDM 159
Cdd:PRK09954 81 AASHPGTIHCSAGGVGRNIAHNLALLGRDVHLLSAIGDDFYGETlLEETRRAGVNVSGCIRLHGQSTSTYLAIANRQDET 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 160 TYGLADMEVFDYITPEFLIKRSHLLKKAKCIIVDLNLGKEALNFLcaYTTKHQIKLVITTVSSPKMKNMPDSLHAIDWII 239
Cdd:PRK09954 161 VLAINDTHILQQLTPQLLNGSRDLIRHAGVVLADCNLTAEALEWV--FTLADEIPVFVDTVSEFKAGKIKHWLAHIHTLK 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 240 TNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGvKELIY---RSGEEEIIKSvmPSNSVKDVTGAGDSFCAAV 316
Cdd:PRK09954 239 PTQPELEILWGQAITSDADRNAAVNALHQQGVQQIFVYLP-DESVFcseKDGEQFLLTA--PAHTTVDSFGADDGFMAGL 315
|
330
....*....|..
gi 612901457 317 VYSWLNGMSTED 328
Cdd:PRK09954 316 VYSFLEGYSFRD 327
|
|
| RbsK |
COG0524 |
Sugar or nucleoside kinase, ribokinase family [Carbohydrate transport and metabolism]; Sugar ... |
60-344 |
3.27e-42 |
|
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: 149.26 E-value: 3.27e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRKFYVHKNLVAETSNPVTS-TRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEMIKR-LSTPFMNLDH 137
Cdd:COG0524 2 VLVIGEALVDLVARVDRLPKGGETVLAGSfRRSPGGAAANVAVALARLGARVALVGAVGDDPFGDFLLAeLRAEGVDTSG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 138 VQQFENASTGSYTALISKEGDMTYGLAdMEVFDYITPEFLikRSHLLKKAKCIIVDL-----NLGKEALNFLCAYTTKHQ 212
Cdd:COG0524 82 VRRDPGAPTGLAFILVDPDGERTIVFY-RGANAELTPEDL--DEALLAGADILHLGGitlasEPPREALLAALEAARAAG 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 213 IKLVITTVSSPKMKN-----MPDSLHAIDWIITNKDETETYLNlkiesTDDLKIAAKRWNDLGVKNVIVTNGVKELIYRS 287
Cdd:COG0524 159 VPVSLDPNYRPALWEparelLRELLALVDILFPNEEEAELLTG-----ETDPEEAAAALLARGVKLVVVTLGAEGALLYT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 612901457 288 GEEEIIKSVMPSNsVKDVTGAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTIETK 344
Cdd:COG0524 234 GGEVVHVPAFPVE-VVDTTGAGDAFAAGFLAGLLEGLDLEEALRFANAAAALVVTRP 289
|
|
| PfkB |
pfam00294 |
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine ... |
60-346 |
5.62e-41 |
|
pfkB family carbohydrate kinase; This family includes a variety of carbohydrate and pyrimidine kinases.
Pssm-ID: 425587 [Multi-domain] Cd Length: 294 Bit Score: 145.95 E-value: 5.62e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRKFYVHKnLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEMIKR-LSTPFMNLDHV 138
Cdd:pfam00294 2 VVVIGEANIDLIGNVEG-LPGELVRVSTVEKGPGGKGANVAVALARLGGDVAFIGAVGDDNFGEFLLQeLKKEGVDTDYV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 139 QQFENASTGSYTALISKEGDMTYGLADMEVFDYITPEFLIKRShLLKKAKCI----IVDLNLGKEALNFLCayTTKHQIK 214
Cdd:pfam00294 81 VIDEDTRTGTALIEVDGDGERTIVFNRGAAADLTPEELEENED-LLENADLLyisgSLPLGLPEATLEELI--EAAKNGG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 215 LVITTVSSPKMKNMPDSLHAI---DWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKELIYRSGEEE 291
Cdd:pfam00294 158 TFDPNLLDPLGAAREALLELLplaDLLKPNEEELEALTGAKLDDIEEALAALHKLLAKGIKTVIVTLGADGALVVEGDGE 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 612901457 292 IIKSVMPSNSVKDVTGAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTIETKYT 346
Cdd:pfam00294 238 VHVPAVPKVKVVDTTGAGDSFVGGFLAGLLAGKSLEEALRFANAAAALVVQKSGA 292
|
|
| PRK09850 |
PRK09850 |
pseudouridine kinase; Provisional |
56-324 |
1.08e-31 |
|
pseudouridine kinase; Provisional
Pssm-ID: 182111 [Multi-domain] Cd Length: 313 Bit Score: 121.63 E-value: 1.08e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 56 EDYpIVCIGAANVDRKFYVHKNLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQDSEWE-MIKRLSTPFMN 134
Cdd:PRK09850 4 KDY-VVIIGSANIDVAGYSHESLNYADSNPGKIKFTPGGVGRNIAQNLALLGNKAWLLSAVGSDFYGQsLLTQTNQSGVY 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 135 LDHVQQFENASTGSYTALISKEGDMTYGLADMEVFDYITPEFLIKRSHLLKKAKCIIVDLNLGKEALNFLCAYTTKhqIK 214
Cdd:PRK09850 83 VDKCLIVPGENTSSYLSLLDNTGEMLVAINDMNISNAITAEYLAQHREFIQRAKVIVADCNISEEALAWILDNAAN--VP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 215 LVITTVSSPKMKNMPDSLHAIDWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKELIYRSGEEEIIK 294
Cdd:PRK09850 161 VFVDPVSAWKCVKVRDRLNQIHTLKPNRLEAETLSGIALSGREDVAKVAAWFHQHGLNRLVLSMGGDGVYYSDISGESGW 240
|
250 260 270
....*....|....*....|....*....|
gi 612901457 295 SVMPSNSVKDVTGAGDSFCAAVVYSWLNGM 324
Cdd:PRK09850 241 SAPIKTNVINVTGAGDAMMAGLASCWVDGM 270
|
|
| ribokinase |
cd01174 |
Ribokinase catalyses the phosphorylation of ribose to ribose-5-phosphate using ATP. This ... |
59-328 |
6.10e-25 |
|
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: 102.63 E-value: 6.10e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 59 PIVCIGAANVDRKFYVHKnLVA--ETsnpVTSTR---SIGG------VArniaenLGRLGETVAFLSASGQDSEWE-MIK 126
Cdd:cd01174 1 KVVVVGSINVDLVTRVDR-LPKpgET---VLGSSfetGPGGkganqaVA------AARLGARVAMIGAVGDDAFGDeLLE 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 127 RLSTPFMNLDHVQQFENASTGsyTALI--SKEGD---MTYGLADMEVfdyiTPEFLIKRSHLLKKAKCIIVDLNLGKEAL 201
Cdd:cd01174 71 NLREEGIDVSYVEVVVGAPTG--TAVItvDESGEnriVVVPGANGEL----TPADVDAALELIAAADVLLLQLEIPLETV 144
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 202 NFLCAYTTKHQIKLVITtvSSPKMKNMPDSLHAIDWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVK 281
Cdd:cd01174 145 LAALRAARRAGVTVILN--PAPARPLPAELLALVDILVPNETEAALLTGIEVTDEEDAEKAARLLLAKGVKNVIVTLGAK 222
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 612901457 282 ELIYRSGEEEIIksvMPSNSVK--DVTGAGDSFCAAVVYSWLNGMSTED 328
Cdd:cd01174 223 GALLASGGEVEH---VPAFKVKavDTTGAGDTFIGALAAALARGLSLEE 268
|
|
| ribokinase_group_A |
cd01942 |
Ribokinase-like subgroup A. Found in bacteria and archaea, this subgroup is part of the ... |
59-343 |
8.64e-20 |
|
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: 88.14 E-value: 8.64e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 59 PIVCIGAANVDRKFYVHKNLVAETSNPVTS-TRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEMI-KRLSTPFMNLD 136
Cdd:cd01942 1 DVAVVGHLNYDIILKVESFPGPFESVLVKDlRREFGGSAGNTAVALAKLGLSPGLVAAVGEDFHGRLYlEELREEGVDTS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 137 HVQQFENASTGSYTALISKEGDMTYG-----LADMEVFDYITPEFLIKRSHLLKKAKCIIVDLNLGKEALNFlcAYTTKH 211
Cdd:cd01942 81 HVRVVDEDSTGVAFILTDGDDNQIAYfypgaMDELEPNDEADPDGLADIVHLSSGPGLIELARELAAGGITV--SFDPGQ 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 212 QIKLVittvSSPKMKNMpdsLHAIDWIITNKDETETYLNLKIESTDDLkiaakrwnDLGVKNVIVTNGVK-ELIYRSGEE 290
Cdd:cd01942 159 ELPRL----SGEELEEI---LERADILFVNDYEAELLKERTGLSEAEL--------ASGVRVVVVTLGPKgAIVFEDGEE 223
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 612901457 291 EIIKSVMPSNSVkDVTGAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTIET 343
Cdd:cd01942 224 VEVPAVPAVKVV-DTTGAGDAFRAGFLYGLLRGYDLEESLRLGNLAASLKVER 275
|
|
| KdgK |
cd01166 |
2-keto-3-deoxygluconate kinase (KdgK) phosphorylates 2-keto-3-deoxygluconate (KDG) to form ... |
60-337 |
1.77e-18 |
|
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: 84.55 E-value: 1.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDrkfyvhknLVAETSNPVTSTRSI----GGVARNIAENLGRLGETVAFLSASGQDS-EWEMIKRLSTPFMN 134
Cdd:cd01166 2 VVTIGEVMVD--------LSPPGGGRLEQADSFrkffGGAEANVAVGLARLGHRVALVTAVGDDPfGRFILAELRREGVD 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 135 LDHVQQFENASTGSYTALISKEGD--MTY-------GLADMEVFDY-------------ITP-------EFLIKrshLLK 185
Cdd:cd01166 74 TSHVRVDPGRPTGLYFLEIGAGGErrVLYyragsaaSRLTPEDLDEaalagadhlhlsgITLalsesarEALLE---ALE 150
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 186 KAK----CIIVDLNL---------GKEALNFLCAYTtkhqiklvittvsspkmknmpdslhaiDWIITNKDETETYLnlK 252
Cdd:cd01166 151 AAKargvTVSFDLNYrpklwsaeeAREALEELLPYV---------------------------DIVLPSEEEAEALL--G 201
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 253 IESTDDLKIAAKRWNdLGVKNVIVTNGVKELIYRSGEEEIIKSVMPSNsVKDVTGAGDSFCAAVVYSWLNGMSTEDILIA 332
Cdd:cd01166 202 DEDPTDAAERALALA-LGVKAVVVKLGAEGALVYTGGGRVFVPAYPVE-VVDTTGAGDAFAAGFLAGLLEGWDLEEALRF 279
|
....*
gi 612901457 333 GMVNA 337
Cdd:cd01166 280 ANAAA 284
|
|
| PTZ00292 |
PTZ00292 |
ribokinase; Provisional |
59-337 |
1.54e-16 |
|
ribokinase; Provisional
Pssm-ID: 185541 [Multi-domain] Cd Length: 326 Bit Score: 79.40 E-value: 1.54e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 59 PIVCIGAANVDRKFYV-HKNLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQD-SEWEMIKRLSTPFMNLD 136
Cdd:PTZ00292 17 DVVVVGSSNTDLIGYVdRMPQVGETLHGTSFHKGFGGKGANQAVMASKLGAKVAMVGMVGTDgFGSDTIKNFKRNGVNTS 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 137 HVQQFENASTGSYTALISKEGdmtyglADMEVF------DYITPEFLIK-RSHLLKKAKCII----VDLNLGKEALNflc 205
Cdd:PTZ00292 97 FVSRTENSSTGLAMIFVDTKT------GNNEIViipganNALTPQMVDAqTDNIQNICKYLIcqneIPLETTLDALK--- 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 206 aYTTKHQIKLVITTVSSPKMKNMP---DSLHAIDWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKE 282
Cdd:PTZ00292 168 -EAKERGCYTVFNPAPAPKLAEVEiikPFLKYVSLFCVNEVEAALITGMEVTDTESAFKASKELQQLGVENVIITLGANG 246
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 612901457 283 LIYRSGEEEIIKsvMPSNSVK--DVTGAGDSFCAAVVYSWLNGMSTED-ILIAGMVNA 337
Cdd:PTZ00292 247 CLIVEKENEPVH--VPGKRVKavDTTGAGDCFVGSMAYFMSRGKDLKEsCKRANRIAA 302
|
|
| FruK |
COG1105 |
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism]; |
241-334 |
1.51e-15 |
|
1-phosphofructokinase or 6-phosphofructokinase II [Carbohydrate transport and metabolism];
Pssm-ID: 440722 [Multi-domain] Cd Length: 304 Bit Score: 76.33 E-value: 1.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 241 NKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKELIYRSgEEEIIKSVMPSNSVKDVTGAGDSFCAAVVYSW 320
Cdd:COG1105 184 NLEELEELLGRPLETLEDIIAAARELLERGAENVVVSLGADGALLVT-EDGVYRAKPPKVEVVSTVGAGDSMVAGFLAGL 262
|
90
....*....|....
gi 612901457 321 LNGMSTEDILIAGM 334
Cdd:COG1105 263 ARGLDLEEALRLAV 276
|
|
| PRK11142 |
PRK11142 |
ribokinase; Provisional |
93-328 |
1.70e-15 |
|
ribokinase; Provisional
Pssm-ID: 236858 [Multi-domain] Cd Length: 306 Bit Score: 76.06 E-value: 1.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 93 GGVARNIAENLGRLGETVAFLSASGQDSEWE-MIKRLSTPFMNLDHVQQFENASTGsyTALI--SKEGDMTYGLAdMEVF 169
Cdd:PRK11142 39 GGKGANQAVAAARLGADIAFIACVGDDSIGEsMRQQLAKDGIDTAPVSVIKGESTG--VALIfvNDEGENSIGIH-AGAN 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 170 DYITPEFLIKRSHLLKKAKCIIVDLNLGKEALNFLCAYTTKHQIKLVITtvSSPKMKnMPDSLHA-IDwIIT-NKDETET 247
Cdd:PRK11142 116 AALTPALVEAHRELIANADALLMQLETPLETVLAAAKIAKQHGTKVILN--PAPARE-LPDELLAlVD-IITpNETEAEK 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 248 YLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKEL-IYRSGEEEIIksvmPSNSVK--DVTGAGDSFCAAVVYSWLNGM 324
Cdd:PRK11142 192 LTGIRVEDDDDAAKAAQVLHQKGIETVLITLGSRGVwLSENGEGQRV----PGFRVQavDTIAAGDTFNGALVTALLEGK 267
|
....
gi 612901457 325 STED 328
Cdd:PRK11142 268 PLPE 271
|
|
| adenosine_kinase |
cd01168 |
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside ... |
58-333 |
3.51e-15 |
|
Adenosine kinase (AK) catalyzes the phosphorylation of ribofuranosyl-containing nucleoside analogues at the 5'-hydroxyl using ATP or GTP as the phosphate donor.The physiological function of AK is associated with the regulation of extracellular adenosine levels and the preservation of intracellular adenylate pools. Adenosine kinase is involved in the purine salvage pathway.
Pssm-ID: 238573 [Multi-domain] Cd Length: 312 Bit Score: 75.34 E-value: 3.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 58 YPIVCIGAANVDRKFYVHKNLVAETSNPVTSTRSI------------------GGVARNIAENLGRLGETVAFLSASGQD 119
Cdd:cd01168 2 YDVLGLGNALVDILAQVDDAFLEKLGLKKGDMILAdmeeqeellaklpvkyiaGGSAANTIRGAAALGGSAAFIGRVGDD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 120 SEWEMI-KRLSTPFMNLdHVQQFENASTGSYTALISKEGDMTYgLADMEVFDYITPEFLIKrsHLLKKAKCIIVD---LN 195
Cdd:cd01168 82 KLGDFLlKDLRAAGVDT-RYQVQPDGPTGTCAVLVTPDAERTM-CTYLGAANELSPDDLDW--SLLAKAKYLYLEgylLT 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 196 LGKEALNFLCAYTTKHQiKLVITTVSSPKMKN-----MPDSLHAIDWIITNKDETETYLnlKIESTDDLKIAAKRWNdLG 270
Cdd:cd01168 158 VPPEAILLAAEHAKENG-VKIALNLSAPFIVQrfkeaLLELLPYVDILFGNEEEAEALA--EAETTDDLEAALKLLA-LR 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612901457 271 VKNVIVTNGVKELIYRSGEEEI-IKSVMPSNSVkDVTGAGDSFCAAVVYSWLNGMSTEDILIAG 333
Cdd:cd01168 234 CRIVVITQGAKGAVVVEGGEVYpVPAIPVEKIV-DTNGAGDAFAGGFLYGLVQGEPLEECIRLG 296
|
|
| bac_FRK |
cd01167 |
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for ... |
60-323 |
5.68e-14 |
|
Fructokinases (FRKs) mainly from bacteria and plants are enzymes with high specificity for fructose, as are all FRKs, but they catalyzes the conversion of fructose to fructose-6-phosphate, which is an entry point into glycolysis via conversion into glucose-6-phosphate. This is in contrast to FRKs [or ketohexokinases (KHKs)] from mammalia and halophilic archaebacteria, which phosphorylate fructose to fructose-1-phosphate.
Pssm-ID: 238572 [Multi-domain] Cd Length: 295 Bit Score: 71.51 E-value: 5.68e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRkfyvhknLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEMIKRLSTPF-MNLDHV 138
Cdd:cd01167 2 VVCFGEALIDF-------IPEGSGAPETFTKAPGGAPANVAVALARLGGKAAFIGKVGDDEFGDFLLETLKEAgVDTRGI 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 139 QQFENASTGsyTAL--ISKEGDMTY-----GLADMEVFDYITPEFLIK----------------RSHLLK-----KAKCI 190
Cdd:cd01167 75 QFDPAAPTT--LAFvtLDADGERSFefyrgPAADLLLDTELNPDLLSEadilhfgsialasepsRSALLElleaaKKAGV 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 191 IV--DLNLgKEALnflcaYTTKHQIKLVITTvsspkmknmpdSLHAIDWIITNKDETETYLNLKIEStddlKIAAKRWND 268
Cdd:cd01167 153 LIsfDPNL-RPPL-----WRDEEEARERIAE-----------LLELADIVKLSDEELELLFGEEDPE----EIAALLLLF 211
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 612901457 269 lGVKNVIVTNGVKELIYRSGEEEIIksvMPSNSVK--DVTGAGDSFCAAVVYSWLNG 323
Cdd:cd01167 212 -GLKLVLVTRGADGALLYTKGGVGE---VPGIPVEvvDTTGAGDAFVAGLLAQLLSR 264
|
|
| Guanosine_kinase_like |
cd01947 |
Guanosine kinase-like sugar kinases. Found in bacteria and archaea, the guanosine kinase-like ... |
60-343 |
1.41e-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: 70.14 E-value: 1.41e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRKFYVHKNLVAETSNPVTSTR-SIGGVARNIAENLGRLGETVAFLSASGQDSEWEMI-KRLSTpfMNLDH 137
Cdd:cd01947 2 IAVVGHVEWDIFLSLDAPPQPGGISHSSDSReSPGGGGANVAVQLAKLGNDVRFFSNLGRDEIGIQSlEELES--GGDKH 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 138 VQQFENASTGSYTALISKEGDMTY---GLADMEVFD----------YITPEflikrshllkkakciIVDlnlgKEALNFl 204
Cdd:cd01947 80 TVAWRDKPTRKTLSFIDPNGERTItvpGERLEDDLKwpildegdgvFITAA---------------AVD----KEAIRK- 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 205 CAYTtkhqiKLVITTVSSP-KMKNMPDSLHAIDWIITNKDETEtylnlkiESTDDLKIAAKRwndlgVKNVIVTNGVKEL 283
Cdd:cd01947 140 CRET-----KLVILQVTPRvRVDELNQALIPLDILIGSRLDPG-------ELVVAEKIAGPF-----PRYLIVTEGELGA 202
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 284 IYRSGEEEIIKSVMPSNsVKDVTGAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTIET 343
Cdd:cd01947 203 ILYPGGRYNHVPAKKAK-VPDSTGAGDSFAAGFIYGLLKGWSIEEALELGAQCGAICVSH 261
|
|
| ribokinase_pfkB_like |
cd00287 |
ribokinase/pfkB superfamily: Kinases that accept a wide variety of substrates, including ... |
60-321 |
7.60e-13 |
|
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: 66.73 E-value: 7.60e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRKFYV-HKNLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGqdsewemikrlstpfmnldhv 138
Cdd:cd00287 2 VLVVGSLLVDVILRVdALPLPGGLVRPGDTEERAGGGAANVAVALARLGVSVTLVGADA--------------------- 60
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 139 qqfenASTGSYTALiskegdmtygladmevfdyitPEFLIKRSHLLKKAKCIIVdLNLGKEALnflcayttkhqiklvit 218
Cdd:cd00287 61 -----VVISGLSPA---------------------PEAVLDALEEARRRGVPVV-LDPGPRAV----------------- 96
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 219 tvsSPKMKNMPDSLHAIDWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKELIY--RSGEEEIIKSV 296
Cdd:cd00287 97 ---RLDGEELEKLLPGVDILTPNEEEAEALTGRRDLEVKEAAEAAALLLSKGPKVVIVTLGEKGAIVatRGGTEVHVPAF 173
|
250 260
....*....|....*....|....*
gi 612901457 297 MPSnsVKDVTGAGDSFCAAVVYSWL 321
Cdd:cd00287 174 PVK--VVDTTGAGDAFLAALAAGLA 196
|
|
| FruK_PfkB_like |
cd01164 |
1-phosphofructokinase (FruK), minor 6-phosphofructokinase (pfkB) and related sugar kinases. ... |
175-330 |
8.69e-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: 64.86 E-value: 8.69e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 175 EFLIKRSHLLKKAKCIIV----DLNLGKEALNFLCAYTTKHQIKLVITTvSSPKMknmpdsLHAID---WIIT-NKDETE 246
Cdd:cd01164 117 ALLEKLKALLKKGDIVVLsgslPPGVPADFYAELVRLAREKGARVILDT-SGEAL------LAALAakpFLIKpNREELE 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 247 TYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVKELIYRSGEEeIIKSVMPSNSVKDVTGAGDSFCAAVVYSWLNGMST 326
Cdd:cd01164 190 ELFGRPLGDEEDVIAAARKLIERGAENVLVSLGADGALLVTKDG-VYRASPPKVKVVSTVGAGDSMVAGFVAGLAQGLSL 268
|
....
gi 612901457 327 EDIL 330
Cdd:cd01164 269 EEAL 272
|
|
| RfaE_like |
cd01172 |
RfaE encodes a bifunctional ADP-heptose synthase involved in the biosynthesis of the ... |
60-328 |
4.98e-10 |
|
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: 59.88 E-value: 4.98e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRkfYVH---KNLVAETSNPVTSTRS----IGGVArNIAENLGRLGETVAFLSASGQDSEWE-MIKRLSTP 131
Cdd:cd01172 2 VLVVGDVILDE--YLYgdvERISPEAPVPVVKVEReeirLGGAA-NVANNLASLGAKVTLLGVVGDDEAGDlLRKLLEKE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 132 FMNLDHVQQfENASTGSYTALISKegdmTYGLA--DMEVFDYITPE---FLIKR-SHLLKKAKCIIV-DLNLGkeALNF- 203
Cdd:cd01172 79 GIDTDGIVD-EGRPTTTKTRVIAR----NQQLLrvDREDDSPLSAEeeqRLIERiAERLPEADVVILsDYGKG--VLTPr 151
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 204 LCAYTTKHQIKLVITTVSSPKMKNMPDSLHAiDWIITNKDETETYLNLKIESTDDLKIAAKR-WNDLGVKNVIVTNGVK- 281
Cdd:cd01172 152 VIEALIAAARELGIPVLVDPKGRDYSKYRGA-TLLTPNEKEAREALGDEINDDDELEAAGEKlLELLNLEALLVTLGEEg 230
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 612901457 282 -ELIYRSGEEEIIKSVmpSNSVKDVTGAGDSFCAAVVYSWLNGMSTED 328
Cdd:cd01172 231 mTLFERDGEVQHIPAL--AKEVYDVTGAGDTVIATLALALAAGADLEE 276
|
|
| PRK09813 |
PRK09813 |
fructoselysine 6-kinase; Provisional |
93-343 |
1.99e-08 |
|
fructoselysine 6-kinase; Provisional
Pssm-ID: 182090 [Multi-domain] Cd Length: 260 Bit Score: 54.74 E-value: 1.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 93 GGVARNIAENLGRLGETVAFLSASGQDSEWEMIKR-LSTPFMNLDHVQQFENASTGSYTALISKE---GDMTYG-LADME 167
Cdd:PRK09813 23 GGNAVNVAVYCTRYGIQPGCITWVGDDDYGTKLKQdLARMGVDISHVHTKHGVTAQTQVELHDNDrvfGDYTEGvMADFA 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 168 VFDyitpeflikrshllkkakciivdlnlgkEALNFLCAYTTKH------------QIKLVITTVS--------SPKMKN 227
Cdd:PRK09813 103 LSE----------------------------EDYAWLAQYDIVHaaiwghaedafpQLHAAGKLTAfdfsdkwdSPLWQT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 228 MPDSLhaiDWII-TNKDETETylnlkiestddLKIAAKRWNDLGVKNVIVTNGVKELIYRSGEEEIIKSVMPSNsVKDVT 306
Cdd:PRK09813 155 LVPHL---DYAFaSAPQEDEF-----------LRLKMKAIVARGAGVVIVTLGENGSIAWDGAQFWRQAPEPVT-VVDTM 219
|
250 260 270
....*....|....*....|....*....|....*..
gi 612901457 307 GAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTIET 343
Cdd:PRK09813 220 GAGDSFIAGFLCGWLAGMTLPQAMAQGTACAAKTIQY 256
|
|
| HTH_24 |
pfam13412 |
Winged helix-turn-helix DNA-binding; |
3-47 |
1.02e-07 |
|
Winged helix-turn-helix DNA-binding;
Pssm-ID: 404317 [Multi-domain] Cd Length: 45 Bit Score: 47.81 E-value: 1.02e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 612901457 3 DSEKEILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYV 47
Cdd:pfam13412 1 ETDRKILNLLQENPRISQRELAERLGLSPSTVNRRLKRLEEEGVI 45
|
|
| Phos_pyr_kin |
pfam08543 |
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate ... |
238-316 |
6.06e-07 |
|
Phosphomethylpyrimidine kinase; This enzyme EC:2.7.4.7 is part of the Thiamine pyrophosphate (TPP) synthesis pathway, TPP is an essential cofactor for many enzymes.
Pssm-ID: 430062 [Multi-domain] Cd Length: 246 Bit Score: 50.17 E-value: 6.06e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 238 IIT-NKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNG--------VKELIYRSGEEEIIKSVMPSNsvKDVTGA 308
Cdd:pfam08543 122 LITpNLPEAEALTGRKIKTLEDMKEAAKKLLALGAKAVLIKGGhlegeeavVTDVLYDGGGFYTLEAPRIPT--KNTHGT 199
|
....*...
gi 612901457 309 GDSFCAAV 316
Cdd:pfam08543 200 GCTLSAAI 207
|
|
| RfaE |
COG2870 |
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane ... |
93-328 |
8.32e-07 |
|
ADP-heptose synthase, bifunctional sugar kinase/adenylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442117 [Multi-domain] Cd Length: 321 Bit Score: 50.19 E-value: 8.32e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 93 GG---VARNIAenlgRLGETVAFLSASGQDSEWEMIKRL------STPFMNLDhvqqfENASTGSYTALISKEGDMtygL 163
Cdd:COG2870 56 GGaanVAANLA----ALGAQVTLVGVVGDDEAGRELRRLleeagiDTDGLVVD-----PRRPTTTKTRVIAGGQQL---L 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 164 -ADMEVFDYITPEF---LIKR-SHLLKKAKCIIV-DLnlGKEALNF-LCAYTTKHQIKLVITTVSSPKMKNMPDSLHAid 236
Cdd:COG2870 124 rLDFEDRFPLSAELearLLAAlEAALPEVDAVILsDY--GKGVLTPeLIQALIALARAAGKPVLVDPKGRDFSRYRGA-- 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 237 WIIT-NKDETETYLNLKIESTDDLKIAAKR-WNDLGVKNVIVTNGVKELIYRSGEEEIIKSVMPSNSVKDVTGAGDSFCA 314
Cdd:COG2870 200 TLLTpNLKEAEAAVGIPIADEEELVAAAAElLERLGLEALLVTRGEEGMTLFDADGPPHHLPAQAREVFDVTGAGDTVIA 279
|
250
....*....|....
gi 612901457 315 AVVYSWLNGMSTED 328
Cdd:COG2870 280 TLALALAAGASLEE 293
|
|
| MarR_2 |
pfam12802 |
MarR family; The Mar proteins are involved in the multiple antibiotic resistance, a ... |
1-47 |
4.01e-06 |
|
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: 43.73 E-value: 4.01e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 612901457 1 MSDSEKEILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYV 47
Cdd:pfam12802 3 LTPAQFRVLLALARNPGLTVAELARRLGISKQTVSRLVKRLEAKGLV 49
|
|
| COG3398 |
COG3398 |
Predicted transcriptional regulator, contains two HTH domains [Transcription]; |
2-58 |
1.49e-05 |
|
Predicted transcriptional regulator, contains two HTH domains [Transcription];
Pssm-ID: 442625 [Multi-domain] Cd Length: 159 Bit Score: 44.87 E-value: 1.49e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612901457 2 SDSEKEILKRIKDNPFISQRELAEAIGLSRPSVANIIS-----GLIQKEYV-MGKAYVLNEDY 58
Cdd:COG3398 96 RETPRRILLYLLENPGATNKELAEELGISRSTVSWHLKrleedGLVERERDgRNVRYYLNPPE 158
|
|
| ribokinase_group_D |
cd01937 |
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ... |
60-333 |
2.02e-05 |
|
Ribokinase-like subgroup D. Found in bacteria and archaea, this subgroup is part of the ribokinase/pfkB superfamily. Its oligomerization state is unknown at this time.
Pssm-ID: 238912 [Multi-domain] Cd Length: 254 Bit Score: 45.47 E-value: 2.02e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDrkfyvhknlvaETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQD--SEWEMIKRLSTPFMNLDH 137
Cdd:cd01937 2 IVIIGHVTID-----------EIVTNGSGVVKPGGPATYASLTLSRLGLTVKLVTKVGRDypDKWSDLFDNGIEVISLLS 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 138 VQ--QFENASTGSYTALI-----SKEGDMTYGLADMEVFDYI---TPEFLIKRshLLKKAKCIIVDLNlgkealNFLCAY 207
Cdd:cd01937 71 TEttTFELNYTNEGRTRTllakcAAIPDTESPLSTITAEIVIlgpVPEEISPS--LFRKFAFISLDAQ------GFLRRA 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 208 TTKHQIKLVITtvsspkmkNMPDSLHAIDWIItnkdetetylnlkiESTDDLKIAAKRWNDLGVKNVIVTNGVKE-LIYR 286
Cdd:cd01937 143 NQEKLIKCVIL--------KLHDVLKLSRVEA--------------EVISTPTELARLIKETGVKEIIVTDGEEGgYIFD 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 612901457 287 SGEEEIIKSvmPSNSVKDVTGAGDSFCAAVVYSWLngmSTEDILIAG 333
Cdd:cd01937 201 GNGKYTIPA--SKKDVVDPTGAGDVFLAAFLYSRL---SGKDIKEAA 242
|
|
| ribokinase_group_B |
cd01945 |
Ribokinase-like subgroup B. Found in bacteria and plants, this subgroup is part of the ... |
60-330 |
2.43e-05 |
|
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: 45.36 E-value: 2.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRKFYV-HKNLVAETSNPVTSTRSIGGVARNIAENLGRLGETVAFLSASGQDSEWEMIKRLSTPF-MNLDH 137
Cdd:cd01945 2 VLGVGLAVLDLIYLVaSFPGGDGKIVATDYAVIGGGNAANAAVAVARLGGQARLIGVVGDDAIGRLILAELAAEgVDTSF 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 138 VQQFENASTgSYTALISKEGD---------MTYGLADMevfdyiTPEFLIKRSH-LLKKAKCIIVDLNLGKEAlnflcay 207
Cdd:cd01945 82 IVVAPGARS-PISSITDITGDratisitaiDTQAAPDS------LPDAILGGADaVLVDGRQPEAALHLAQEA------- 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 208 ttkHQIKL-VITTVSSPKMKNMPDSLHAIDWIITNKdetETYLNLKIESTDDLKIAAKRwndLGVKNVIVTNGVKELIYR 286
Cdd:cd01945 148 ---RARGIpIPLDLDGGGLRVLEELLPLADHAICSE---NFLRPNTGSADDEALELLAS---LGIPFVAVTLGEAGCLWL 218
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 612901457 287 SGEEEIIKSVMPSNSVKDVTGAGDSFCAAVVYSWLNGMSTEDIL 330
Cdd:cd01945 219 ERDGELFHVPAFPVEVVDTTGAGDVFHGAFAHALAEGMPLREAL 262
|
|
| PTZ00247 |
PTZ00247 |
adenosine kinase; Provisional |
230-341 |
3.81e-05 |
|
adenosine kinase; Provisional
Pssm-ID: 240328 [Multi-domain] Cd Length: 345 Bit Score: 45.02 E-value: 3.81e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 230 DSLHAI----DWIITNKDETETYLNLKIESTDDLKIAAKRWNDLGVKN------VIVTNGVKELIYRSGEEEIIKSVMP- 298
Cdd:PTZ00247 206 ERLLQVlpyvDILFGNEEEAKTFAKAMKWDTEDLKEIAARIAMLPKYSgtrprlVVFTQGPEPTLIATKDGVTSVPVPPl 285
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 612901457 299 -SNSVKDVTGAGDSFCAAVVYSWLNGMSTEDILIAGMVNAKKTI 341
Cdd:PTZ00247 286 dQEKIVDTNGAGDAFVGGFLAQYANGKDIDRCVEAGHYSAQVII 329
|
|
| pyridoxal_pyridoxamine_kinase |
cd01173 |
Pyridoxal kinase plays a key role in the synthesis of the active coenzyme pyridoxal-5 ... |
237-330 |
5.04e-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: 44.50 E-value: 5.04e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 237 WIIT-NKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVT------NGVKELIYRSGEEEIIKSVMPSNSVKDVTGAG 309
Cdd:cd01173 138 DIITpNQFELELLTGKKINDLEDAKAAARALHAKGPKTVVVTsveladDDRIEMLGSTATEAWLVQRPKIPFPAYFNGTG 217
|
90 100
....*....|....*....|.
gi 612901457 310 DSFCAAVVYSWLNGMSTEDIL 330
Cdd:cd01173 218 DLFAALLLARLLKGKSLAEAL 238
|
|
| PRK12413 |
PRK12413 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
238-328 |
5.63e-05 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183513 [Multi-domain] Cd Length: 253 Bit Score: 44.28 E-value: 5.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 238 IIT-NKDETETYLNLKIESTDDLKIAAKRWNDLGVKNVIVTNGVK-------ELIYRSGEEEIIKS-VMPSNSvkdvTGA 308
Cdd:PRK12413 132 VITpNLVEAELLSGKEIKTLEDMKEAAKKLYDLGAKAVVIKGGNRlsqkkaiDLFYDGKEFVILESpVLEKNN----IGA 207
|
90 100
....*....|....*....|
gi 612901457 309 GDSFCAAVVYSWLNGMSTED 328
Cdd:PRK12413 208 GCTFASSIASQLVKGKSPLE 227
|
|
| HTH_ASNC |
smart00344 |
helix_turn_helix ASNC type; AsnC: an autogenously regulated activator of asparagine synthetase ... |
8-76 |
7.10e-05 |
|
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: 41.73 E-value: 7.10e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612901457 8 ILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYVMGKAYVLNE---DYPIVCIGAANVDRKFYVHK 76
Cdd:smart00344 8 ILEELQKDARISLAELAKKVGLSPSTVHNRVKRLEEEGVIKGYTAVLNPkklGLSVTAFVGVTLENPDKLEE 79
|
|
| Fructoselysine_kinase_like |
cd01940 |
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a ... |
60-332 |
1.02e-04 |
|
Fructoselysine kinase-like. Fructoselysine is a fructoseamine formed by glycation, a non-enzymatic reaction of glucose with a primary amine followed by an Amadori rearrangement, resulting in a protein that is modified at the amino terminus and at the lysine side chains. Fructoseamines are typically metabolized by fructoseamine-3-kinase, especially in higher eukaryotes. In E. coli, fructoselysine kinase has been shown in vitro to catalyze the phosphorylation of fructoselysine. It is proposed that fructoselysine is released from glycated proteins during human digestion and is partly metabolized by bacteria in the hind gut using a protein such as fructoselysine kinase. This family is found only in bacterial sequences, and its oligomeric state is currently unknown.
Pssm-ID: 238915 [Multi-domain] Cd Length: 264 Bit Score: 43.50 E-value: 1.02e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 60 IVCIGAANVDRkfYVHKNLVAetsnpvtstrsIGGVARNIAENLGRLGETVAFLSASGQDSEWEMIKR-LSTPFMNLDHV 138
Cdd:cd01940 2 LAAIGDNVVDK--YLHLGKMY-----------PGGNALNVAVYAKRLGHESAYIGAVGNDDAGAHVRStLKRLGVDISHC 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 139 QQFEnASTGsYTALISKEGDMTYGLADmevfdyitpeflikrshllkkaKCIIVDLNLGKEALNFLCAYTTKHqikLVIT 218
Cdd:cd01940 69 RVKE-GENA-VADVELVDGDRIFGLSN----------------------KGGVAREHPFEADLEYLSQFDLVH---TGIY 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 219 TVSSPKMKNMPdSLHAIDWIIT---NKDETETYLNLKI------------ESTDDLKIAAKRWNDLGVKNVIVTNGVKEL 283
Cdd:cd01940 122 SHEGHLEKALQ-ALVGAGALISfdfSDRWDDDYLQLVCpyvdfaffsasdLSDEEVKAKLKEAVSRGAKLVIVTRGEDGA 200
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 612901457 284 IYRSGEEEIIKSVMPSNSVkDVTGAGDSFCAAVVYSWLNGMstEDILIA 332
Cdd:cd01940 201 IAYDGAVFYSVAPRPVEVV-DTLGAGDSFIAGFLLSLLAGG--TAIAEA 246
|
|
| MarR |
COG1846 |
DNA-binding transcriptional regulator, MarR family [Transcription]; |
8-47 |
1.04e-04 |
|
DNA-binding transcriptional regulator, MarR family [Transcription];
Pssm-ID: 441451 [Multi-domain] Cd Length: 142 Bit Score: 41.88 E-value: 1.04e-04
10 20 30 40
....*....|....*....|....*....|....*....|
gi 612901457 8 ILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYV 47
Cdd:COG1846 43 VLAALAEAGGLTQSELAERLGLTKSTVSRLLDRLEEKGLV 82
|
|
| PLN02379 |
PLN02379 |
pfkB-type carbohydrate kinase family protein |
235-328 |
1.20e-04 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178005 [Multi-domain] Cd Length: 367 Bit Score: 43.63 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 612901457 235 IDWIITNKDETETYLNLKIESTDD--LKIAAKRwndlgVKNVIVTNGVKELIYRSGEEEI-IKSVMPSNSVkDVTGAGDS 311
Cdd:PLN02379 233 IDLCFANEDEARELLRGEQESDPEaaLEFLAKY-----CNWAVVTLGSKGCIARHGKEVVrVPAIGETNAV-DATGAGDL 306
|
90
....*....|....*..
gi 612901457 312 FCAAVVYSWLNGMSTED 328
Cdd:PLN02379 307 FASGFLYGLIKGLSLEE 323
|
|
| HTH_MARR |
smart00347 |
helix_turn_helix multiple antibiotic resistance protein; |
7-47 |
2.48e-04 |
|
helix_turn_helix multiple antibiotic resistance protein;
Pssm-ID: 197670 [Multi-domain] Cd Length: 101 Bit Score: 39.88 E-value: 2.48e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 612901457 7 EILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYV 47
Cdd:smart00347 14 LVLRILYEEGPLSVSELAKRLGVSPSTVTRVLDRLEKKGLV 54
|
|
| COG2512 |
COG2512 |
Predicted transcriptional regulator, contains CW (cell wall-binding) repeats and an HTH domain ... |
1-59 |
3.06e-04 |
|
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: 39.13 E-value: 3.06e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612901457 1 MSDSEKEILKRIKDNP-FISQRELAEAIGLSRPSVANIISGLIQKEYV------MGKAYVLNEDYP 59
Cdd:COG2512 13 LLEDERRVLELLRENGgRMTQSEIVKETGWSKSKVSRLLSRLEERGLIekervgRENVVELPEDEP 78
|
|
| MarR_EPS |
TIGR04176 |
EPS-associated transcriptional regulator, MarR family; Members of this family of MarR-family ... |
8-44 |
3.73e-04 |
|
EPS-associated transcriptional regulator, MarR family; Members of this family of MarR-family transcriptional regulators are associated with long genomic loci consisting of genes encoding enzymes for the biosynthesis of exopolysaccharides. These genes include glycosyl transferases, sugar modifying enzymes (epimerases, isomerases, methyltransferases, aminotransferases, etc.), and exopolysaccharide polymerases (wzx, wzy). In Leptospira interrogans, borgpeterenii and biflexa, this gene is observed first in unidirectional EPS biosynthesis loci as long as 90 genes. MarR genes (pfam01407) are known to bind to DNA regions with palindromic or pseudopalindromic sequences as homodimers, and to bind small molecules as triggers for conformational changes controlling on/off states.
Pssm-ID: 275030 Cd Length: 105 Bit Score: 39.55 E-value: 3.73e-04
10 20 30
....*....|....*....|....*....|....*..
gi 612901457 8 ILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQK 44
Cdd:TIGR04176 9 VLRLLEENPELSQRELAKELGISLGKVNYCLKALIDK 45
|
|
| HTH_XRE |
cd00093 |
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the ... |
7-40 |
3.78e-04 |
|
Helix-turn-helix XRE-family like proteins. Prokaryotic DNA binding proteins belonging to the xenobiotic response element family of transcriptional regulators.
Pssm-ID: 238045 [Multi-domain] Cd Length: 58 Bit Score: 38.30 E-value: 3.78e-04
10 20 30
....*....|....*....|....*....|....
gi 612901457 7 EILKRIKDNPFISQRELAEAIGLSRPSVANIISG 40
Cdd:cd00093 2 ERLKELRKEKGLTQEELAEKLGVSRSTISRIENG 35
|
|
| HTH_XRE |
smart00530 |
Helix-turn-helix XRE-family like proteins; |
6-40 |
1.29e-03 |
|
Helix-turn-helix XRE-family like proteins;
Pssm-ID: 197775 [Multi-domain] Cd Length: 56 Bit Score: 36.73 E-value: 1.29e-03
10 20 30
....*....|....*....|....*....|....*
gi 612901457 6 KEILKRIKdnpfISQRELAEAIGLSRPSVANIISG 40
Cdd:smart00530 3 KELREEKG----LTQEELAEKLGVSRSTLSRIENG 33
|
|
| PLN02341 |
PLN02341 |
pfkB-type carbohydrate kinase family protein |
267-337 |
1.43e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 215195 [Multi-domain] Cd Length: 470 Bit Score: 40.58 E-value: 1.43e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 612901457 267 NDLGVKNVIVTNGVKE--LIYRSGEeeiikSVMPSNSVK--DVTGAGDSFCAAVVYSWLNGMSTEDIL-IAGMVNA 337
Cdd:PLN02341 315 PGIRTKWVVVKMGSKGsiLVTRSSV-----SCAPAFKVNvvDTVGCGDSFAAAIALGYIHNLPLVNTLtLANAVGA 385
|
|
| LexA |
COG1974 |
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, ... |
1-48 |
1.78e-03 |
|
SOS-response transcriptional repressor LexA (RecA-mediated autopeptidase) [Transcription, Signal transduction mechanisms];
Pssm-ID: 441577 [Multi-domain] Cd Length: 199 Bit Score: 39.13 E-value: 1.78e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 612901457 1 MSDSEKEILKRIKD-----NPFISQRELAEAIGLSRPSVANIISGLIQKEYVM 48
Cdd:COG1974 4 LTKRQREILDFIKEyirerGYPPSQREIAEALGLSSSAVHRHLKALEKKGYLR 56
|
|
| HipB |
COG1396 |
Transcriptional regulator, contains XRE-family HTH domain [Transcription]; |
1-40 |
3.25e-03 |
|
Transcriptional regulator, contains XRE-family HTH domain [Transcription];
Pssm-ID: 441006 [Multi-domain] Cd Length: 83 Bit Score: 36.13 E-value: 3.25e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 612901457 1 MSDSEKEILKRIKD-----NpfISQRELAEAIGLSRPSVANIISG 40
Cdd:COG1396 1 MSTLKKALGERLRElrkarG--LTQEELAERLGVSRSTISRIERG 43
|
|
| VapI |
COG3093 |
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense ... |
7-40 |
3.35e-03 |
|
Plasmid maintenance system antidote protein VapI, contains XRE-type HTH domain [Defense mechanisms];
Pssm-ID: 442327 [Multi-domain] Cd Length: 87 Bit Score: 36.33 E-value: 3.35e-03
10 20 30
....*....|....*....|....*....|....*
gi 612901457 7 EILKRIKDNPF-ISQRELAEAIGLSRPSVANIISG 40
Cdd:COG3093 11 EILREEFLEPLgLSQTELAKALGVSRQRISEILNG 45
|
|
| PRK12412 |
PRK12412 |
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase; |
251-316 |
4.91e-03 |
|
bifunctional hydroxymethylpyrimidine kinase/phosphomethylpyrimidine kinase;
Pssm-ID: 183512 [Multi-domain] Cd Length: 268 Bit Score: 38.41 E-value: 4.91e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 612901457 251 LKIESTDDLKIAAKRWNDLGVKNVIVTNGVK-------ELIYRSGEEEIIKSVMPSNSvkDVTGAGDSFCAAV 316
Cdd:PRK12412 149 VKINSLEDMKEAAKKIHALGAKYVLIKGGSKlgtetaiDVLYDGETFDLLESEKIDTT--NTHGAGCTYSAAI 219
|
|
| PLN02630 |
PLN02630 |
pfkB-type carbohydrate kinase family protein |
274-333 |
5.18e-03 |
|
pfkB-type carbohydrate kinase family protein
Pssm-ID: 178237 Cd Length: 335 Bit Score: 38.63 E-value: 5.18e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 612901457 274 VIVTNGVK--ELIYRSGEEEIikSVMPSNSVkDVTGAGDSFCAAVVYSWLNGMSTEDILIAG 333
Cdd:PLN02630 206 VIVTNGKKgcRIYWKDGEMRV--PPFPAIQV-DPTGAGDSFLGGFVAGLVQGLAVPDAALLG 264
|
|
| HTH_AsnC-type |
pfam13404 |
AsnC-type helix-turn-helix domain; |
6-35 |
5.95e-03 |
|
AsnC-type helix-turn-helix domain;
Pssm-ID: 433180 [Multi-domain] Cd Length: 41 Bit Score: 34.27 E-value: 5.95e-03
10 20 30
....*....|....*....|....*....|
gi 612901457 6 KEILKRIKDNPFISQRELAEAIGLSRPSVA 35
Cdd:pfam13404 5 RKILRLLQEDARISFAELAERVGLSESTVL 34
|
|
| HTH_36 |
pfam13730 |
Helix-turn-helix domain; |
1-47 |
5.97e-03 |
|
Helix-turn-helix domain;
Pssm-ID: 463970 [Multi-domain] Cd Length: 55 Bit Score: 34.77 E-value: 5.97e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 612901457 1 MSDSEKEILKRIKD------NPFISQRELAEAIGLSRPSVANIISGLIQKEYV 47
Cdd:pfam13730 3 LSPTAKLLLLILASyankdgGCFPSVETLAKRLGLSRRTIQRAIKELEELGYL 55
|
|
| HTH_Crp_2 |
pfam13545 |
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain ... |
18-47 |
6.89e-03 |
|
Crp-like helix-turn-helix domain; This family represents a crp-like helix-turn-helix domain that is likely to bind DNA.
Pssm-ID: 463917 [Multi-domain] Cd Length: 68 Bit Score: 34.74 E-value: 6.89e-03
10 20 30
....*....|....*....|....*....|....*
gi 612901457 18 ISQRELAEAIGLSRPSVANIIS-----GLIQKEYV 47
Cdd:pfam13545 23 LTQEDLADLLGTTRETVSRVLSelrreGLIERGRI 57
|
|
| MAK32 |
cd01943 |
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the ... |
297-334 |
6.93e-03 |
|
MAK32 kinase. MAK32 is a protein found primarily in fungi that is necessary for the structural stability of L-A particles. The L-A virus particule is a specialized compartment for the transcription and replication of double-stranded RNA, known to infect yeast and other fungi. MAK32 is part of the host machinery used by the virus to multiply.
Pssm-ID: 238918 [Multi-domain] Cd Length: 328 Bit Score: 38.09 E-value: 6.93e-03
10 20 30
....*....|....*....|....*....|....*...
gi 612901457 297 MPSNSVKDVTGAGDSFCAAVVYSWLngmSTEDILIAGM 334
Cdd:cd01943 255 TKSTKVVDPTGGGNSFLGGFAAGLA---LTKSIDEACI 289
|
|
| Lrp |
COG1522 |
DNA-binding transcriptional regulator, Lrp family [Transcription]; |
1-71 |
7.45e-03 |
|
DNA-binding transcriptional regulator, Lrp family [Transcription];
Pssm-ID: 441131 [Multi-domain] Cd Length: 138 Bit Score: 36.29 E-value: 7.45e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 612901457 1 MSDSEKEILKRIKDNPFISQRELAEAIGLSRPSVANIISGLIQKEYVMGKAYVLNED---YPIVCIGAANVDRK 71
Cdd:COG1522 3 LDEIDRRILRLLQEDGRLSFAELAERVGLSESTVLRRVRRLEEAGVIRGYGAVVDPEklgLGVTAFVEVKVPPH 76
|
|
| HTH_CRP |
smart00419 |
helix_turn_helix, cAMP Regulatory protein; |
18-55 |
8.84e-03 |
|
helix_turn_helix, cAMP Regulatory protein;
Pssm-ID: 128696 [Multi-domain] Cd Length: 48 Bit Score: 33.95 E-value: 8.84e-03
10 20 30 40
....*....|....*....|....*....|....*....|
gi 612901457 18 ISQRELAEAIGLSRPSVANIISGLIQKEYVM--GKAYVLN 55
Cdd:smart00419 9 LTRQEIAELLGLTRETVSRTLKRLEKEGLISreGGRIVIL 48
|
|
| AF2118 |
COG3620 |
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain ... |
7-40 |
9.85e-03 |
|
Predicted transcriptional regulator, contains an XRE-type HTH domain (archaeal members contain CBS pair) [Transcription];
Pssm-ID: 442838 [Multi-domain] Cd Length: 95 Bit Score: 35.00 E-value: 9.85e-03
10 20 30
....*....|....*....|....*....|....
gi 612901457 7 EILKRIKDNPFISQRELAEAIGLSRPSVANIISG 40
Cdd:COG3620 20 EALRLMRKELGLSQLPVAELVGVSQSDILRIESG 53
|
|
| |
