|
Name |
Accession |
Description |
Interval |
E-value |
| ispH |
PRK01045 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed |
1-301 |
0e+00 |
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed
Pssm-ID: 234893 Cd Length: 298 Bit Score: 552.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 1 MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAV 80
Cdd:PRK01045 1 MKILLANPRGFCAGVDRAIEIVERALEKYGAPIYVRHEIVHNRYVVERLEKKGAIFVEELDEVPDGAIVIFSAHGVSPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 81 RNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYSnpeGGMYLVESPEDVWKITVKDENN 160
Cdd:PRK01045 81 REEAKERGLTVIDATCPLVTKVHKEVARMSREGYEIILIGHKGHPEVEGTMGQAP---GGVYLVESPEDVAKLEVKDPDK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 161 LSFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGK 240
Cdd:PRK01045 158 LALVTQTTLSVDDTAEIIAALKERFPEIQGPPKDDICYATQNRQEAVKELAPQADLVIVVGSKNSSNSNRLREVAEEAGA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490520790 241 TAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKALGGSDAHELTGREENIV 301
Cdd:PRK01045 238 PAYLIDDASEIDPEWFKGVKTVGVTAGASAPEWLVQEVIARLKELGATVVEEVEGREENIV 298
|
|
| IspH |
COG0761 |
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH [Lipid transport and metabolism]; ... |
1-289 |
2.23e-176 |
|
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH [Lipid transport and metabolism]; 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440524 Cd Length: 289 Bit Score: 489.19 E-value: 2.23e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 1 MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAV 80
Cdd:COG0761 2 MKILLAKPRGFCAGVDRAIEIVERALEKYGAPVYVLGEIVHNPQVVERLEAKGVVFVEELDEVPDGATVIFRAHGVSPEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 81 RNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYsnpEGGMYLVESPEDVWKITVKDENN 160
Cdd:COG0761 82 REEAEERGLKVIDATCPLVTKVHKEVRRLAKEGYTIVIIGHKGHPEVEGTMGQA---PGKVVVVESPEDVEALPVRDPEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 161 LSFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGK 240
Cdd:COG0761 159 LAVVSQTTLSVDDTAEIVEALKERFPEIRGPVKDTICYATQNRQDAVKELAKEVDLMLVVGGKNSSNTNRLVEVAKEAGP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490520790 241 TAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKALGGSD 289
Cdd:COG0761 239 PAYLIETAEELDPEWLEGVKTVGITAGASTPEWLVEEVIDRLRELGPEE 287
|
|
| LYTB |
pfam02401 |
LytB protein; The mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for ... |
7-283 |
5.77e-147 |
|
LytB protein; The mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis is essential in many eubacteria, plants, and the malaria parasite. The LytB gene is involved in the trunk line of the MEP pathway.
Pssm-ID: 460548 Cd Length: 270 Bit Score: 414.10 E-value: 5.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 7 NPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEvPDGAILIFSAHGVSQAVRNEAKS 86
Cdd:pfam02401 1 KPAGFCFGVKRAIEIAEEALEEFGAPVYTLGPIVHNPQVVERLEEKGVVFVEDLDE-PEGAVVIIRAHGVSPEVYEEAKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 87 RDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYsnpEGGMYLVESPEDVWKITVKDENnLSFMTQ 166
Cdd:pfam02401 80 RGLLIIDATCPLVTKVHKEVKRLAKEGYQIVIIGDKGHPEVIGTLGQA---PERAVVVEETEEVEKLLVPPEK-VAVVSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 167 TTLSVDDTSEVIDALRSRFPKIVGprKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKTAYLID 246
Cdd:pfam02401 156 TTLSVDEFEEIVEALKKRFPELRV--FNTICYATQNRQDAVRELAKEVDLMIVVGGKNSSNTKRLVEICKEAGPPTYLIE 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 490520790 247 DANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLK 283
Cdd:pfam02401 234 TADELDPEWLKGVKTVGITAGASTPDWLIEEVIDKLE 270
|
|
| lytB_ispH |
cd13944 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; The 4-hydroxy-3-methylbut-2-enyl ... |
3-282 |
2.48e-143 |
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; The 4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) reductase (called lytB or ispH) is the terminal enzyme of the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway, one of the two metabolic routes for isoprenoid biosynthesis. The MEP pathway is essential in many eubacteria, plants, and the malaria parasite. LytB converts HMBPP into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).
Pssm-ID: 260116 Cd Length: 275 Bit Score: 404.87 E-value: 2.48e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 3 ILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAVRN 82
Cdd:cd13944 1 IILAKPAGFCFGVKRAIDIAEKALEEYGGPVYTLGPIIHNPQVVERLEKKGVKFVDDLDEVPEGGTVIIRAHGVSPEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 83 EAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYsnpEGGMYLVESPEDVWKITVKDENNLS 162
Cdd:cd13944 81 EAKERGLEVIDATCPLVKKVQKIVKKLAKEGYQVVIIGDKGHPEVIGILGYA---PGKAIVVESLEEAEKLPLYDLKKVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 163 FMTQTTLSVDDTSEVIDALRSRFPKIVGPrkDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKTA 242
Cdd:cd13944 158 VVSQTTQSVDEFEEIVEALKKRFPEIEVF--NTICYATQNRQEAARELAKEVDLMIVVGGKNSSNTKRLAEIAKEAGPPT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490520790 243 YLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRL 282
Cdd:cd13944 236 YLIETADELDPEWLKGVKKIGITAGASTPDWIIEEVIDRL 275
|
|
| ispH_lytB |
TIGR00216 |
(E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate reductase (IPP and DMAPP forming); The IspH ... |
3-285 |
1.49e-117 |
|
(E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate reductase (IPP and DMAPP forming); The IspH protein (previously designated LytB) has now been recognized as the last enzyme in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Escherichia coli LytB protein had been found to regulate the activity of RelA (guanosine 3',5'-bispyrophosphate synthetase I), which in turn controls the level of a regulatory metabolite. It is involved in penicillin tolerance and the stringent response. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 272965 Cd Length: 282 Bit Score: 340.10 E-value: 1.49e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 3 ILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERG-AIFIEQISEVPDGAILIFSAHGVSQAVR 81
Cdd:TIGR00216 2 IILAKPRGFCFGVKRAIQMAEEALKEPGKPVYTLGEIVHNPQVVERLRERGvVFFLEDLDEVAAGDTVIFRAHGVPPEVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 82 NEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYSnpeGGMYLVESPEDVWKITVKDENNL 161
Cdd:TIGR00216 82 EELEKKGLEVIDATCPLVTKVHNAAKKYAKEGYHVILIGKKNHPEVIGTRGYAP---DGAILVETKEDLENFKFADEKRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 162 SFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKT 241
Cdd:TIGR00216 159 GVVSQTTLSQEDTKEIVAALKARYPQKEVPAFNTICYATQNRQDAVRELAPEVDLMIVIGGKNSSNTTRLFEIAEEHGGP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490520790 242 AYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKAL 285
Cdd:TIGR00216 239 SYLIETAEELPEEWLKGVKVVGITAGASTPDWIIEEVIRKLKEL 282
|
|
|
|
Name |
Accession |
Description |
Interval |
E-value |
| ispH |
PRK01045 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed |
1-301 |
0e+00 |
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Reviewed
Pssm-ID: 234893 Cd Length: 298 Bit Score: 552.81 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 1 MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAV 80
Cdd:PRK01045 1 MKILLANPRGFCAGVDRAIEIVERALEKYGAPIYVRHEIVHNRYVVERLEKKGAIFVEELDEVPDGAIVIFSAHGVSPAV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 81 RNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYSnpeGGMYLVESPEDVWKITVKDENN 160
Cdd:PRK01045 81 REEAKERGLTVIDATCPLVTKVHKEVARMSREGYEIILIGHKGHPEVEGTMGQAP---GGVYLVESPEDVAKLEVKDPDK 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 161 LSFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGK 240
Cdd:PRK01045 158 LALVTQTTLSVDDTAEIIAALKERFPEIQGPPKDDICYATQNRQEAVKELAPQADLVIVVGSKNSSNSNRLREVAEEAGA 237
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 490520790 241 TAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKALGGSDAHELTGREENIV 301
Cdd:PRK01045 238 PAYLIDDASEIDPEWFKGVKTVGVTAGASAPEWLVQEVIARLKELGATVVEEVEGREENIV 298
|
|
| IspH |
COG0761 |
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH [Lipid transport and metabolism]; ... |
1-289 |
2.23e-176 |
|
4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH [Lipid transport and metabolism]; 4-Hydroxy-3-methylbut-2-enyl diphosphate reductase IspH is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440524 Cd Length: 289 Bit Score: 489.19 E-value: 2.23e-176
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 1 MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAV 80
Cdd:COG0761 2 MKILLAKPRGFCAGVDRAIEIVERALEKYGAPVYVLGEIVHNPQVVERLEAKGVVFVEELDEVPDGATVIFRAHGVSPEV 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 81 RNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYsnpEGGMYLVESPEDVWKITVKDENN 160
Cdd:COG0761 82 REEAEERGLKVIDATCPLVTKVHKEVRRLAKEGYTIVIIGHKGHPEVEGTMGQA---PGKVVVVESPEDVEALPVRDPEK 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 161 LSFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGK 240
Cdd:COG0761 159 LAVVSQTTLSVDDTAEIVEALKERFPEIRGPVKDTICYATQNRQDAVKELAKEVDLMLVVGGKNSSNTNRLVEVAKEAGP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 490520790 241 TAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKALGGSD 289
Cdd:COG0761 239 PAYLIETAEELDPEWLEGVKTVGITAGASTPEWLVEEVIDRLRELGPEE 287
|
|
| LYTB |
pfam02401 |
LytB protein; The mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for ... |
7-283 |
5.77e-147 |
|
LytB protein; The mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway for isoprenoid biosynthesis is essential in many eubacteria, plants, and the malaria parasite. The LytB gene is involved in the trunk line of the MEP pathway.
Pssm-ID: 460548 Cd Length: 270 Bit Score: 414.10 E-value: 5.77e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 7 NPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEvPDGAILIFSAHGVSQAVRNEAKS 86
Cdd:pfam02401 1 KPAGFCFGVKRAIEIAEEALEEFGAPVYTLGPIVHNPQVVERLEEKGVVFVEDLDE-PEGAVVIIRAHGVSPEVYEEAKE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 87 RDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYsnpEGGMYLVESPEDVWKITVKDENnLSFMTQ 166
Cdd:pfam02401 80 RGLLIIDATCPLVTKVHKEVKRLAKEGYQIVIIGDKGHPEVIGTLGQA---PERAVVVEETEEVEKLLVPPEK-VAVVSQ 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 167 TTLSVDDTSEVIDALRSRFPKIVGprKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKTAYLID 246
Cdd:pfam02401 156 TTLSVDEFEEIVEALKKRFPELRV--FNTICYATQNRQDAVRELAKEVDLMIVVGGKNSSNTKRLVEICKEAGPPTYLIE 233
|
250 260 270
....*....|....*....|....*....|....*..
gi 490520790 247 DANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLK 283
Cdd:pfam02401 234 TADELDPEWLKGVKTVGITAGASTPDWLIEEVIDKLE 270
|
|
| lytB_ispH |
cd13944 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; The 4-hydroxy-3-methylbut-2-enyl ... |
3-282 |
2.48e-143 |
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; The 4-hydroxy-3-methylbut-2-enyl diphosphate (HMBPP) reductase (called lytB or ispH) is the terminal enzyme of the mevalonate-independent 2-C-methyl-D-erythritol 4-phosphate (MEP) pathway, one of the two metabolic routes for isoprenoid biosynthesis. The MEP pathway is essential in many eubacteria, plants, and the malaria parasite. LytB converts HMBPP into isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP).
Pssm-ID: 260116 Cd Length: 275 Bit Score: 404.87 E-value: 2.48e-143
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 3 ILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAVRN 82
Cdd:cd13944 1 IILAKPAGFCFGVKRAIDIAEKALEEYGGPVYTLGPIIHNPQVVERLEKKGVKFVDDLDEVPEGGTVIIRAHGVSPEVYE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 83 EAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYsnpEGGMYLVESPEDVWKITVKDENNLS 162
Cdd:cd13944 81 EAKERGLEVIDATCPLVKKVQKIVKKLAKEGYQVVIIGDKGHPEVIGILGYA---PGKAIVVESLEEAEKLPLYDLKKVG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 163 FMTQTTLSVDDTSEVIDALRSRFPKIVGPrkDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKTA 242
Cdd:cd13944 158 VVSQTTQSVDEFEEIVEALKKRFPEIEVF--NTICYATQNRQEAARELAKEVDLMIVVGGKNSSNTKRLAEIAKEAGPPT 235
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 490520790 243 YLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRL 282
Cdd:cd13944 236 YLIETADELDPEWLKGVKKIGITAGASTPDWIIEEVIDRL 275
|
|
| ispH_lytB |
TIGR00216 |
(E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate reductase (IPP and DMAPP forming); The IspH ... |
3-285 |
1.49e-117 |
|
(E)-4-hydroxy-3-methyl-but-2-enyl pyrophosphate reductase (IPP and DMAPP forming); The IspH protein (previously designated LytB) has now been recognized as the last enzyme in the biosynthesis of isopentenyl diphosphate (IPP) and dimethylallyl diphosphate (DMAPP). Escherichia coli LytB protein had been found to regulate the activity of RelA (guanosine 3',5'-bispyrophosphate synthetase I), which in turn controls the level of a regulatory metabolite. It is involved in penicillin tolerance and the stringent response. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 272965 Cd Length: 282 Bit Score: 340.10 E-value: 1.49e-117
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 3 ILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERG-AIFIEQISEVPDGAILIFSAHGVSQAVR 81
Cdd:TIGR00216 2 IILAKPRGFCFGVKRAIQMAEEALKEPGKPVYTLGEIVHNPQVVERLRERGvVFFLEDLDEVAAGDTVIFRAHGVPPEVR 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 82 NEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYSnpeGGMYLVESPEDVWKITVKDENNL 161
Cdd:TIGR00216 82 EELEKKGLEVIDATCPLVTKVHNAAKKYAKEGYHVILIGKKNHPEVIGTRGYAP---DGAILVETKEDLENFKFADEKRL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 162 SFMTQTTLSVDDTSEVIDALRSRFPKIVGPRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGKT 241
Cdd:TIGR00216 159 GVVSQTTLSQEDTKEIVAALKARYPQKEVPAFNTICYATQNRQDAVRELAPEVDLMIVIGGKNSSNTTRLFEIAEEHGGP 238
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 490520790 242 AYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKAL 285
Cdd:TIGR00216 239 SYLIETAEELPEEWLKGVKVVGITAGASTPDWIIEEVIRKLKEL 282
|
|
| PRK00087 |
PRK00087 |
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1; |
1-292 |
9.53e-76 |
|
bifunctional 4-hydroxy-3-methylbut-2-enyl diphosphate reductase/30S ribosomal protein S1;
Pssm-ID: 234623 [Multi-domain] Cd Length: 647 Bit Score: 244.09 E-value: 9.53e-76
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 1 MQILLANPRGFCAGVDRAISIVENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIEQISEVPDGAILIFSAHGVSQAV 80
Cdd:PRK00087 1 MEIILAKKAGFCFGVKRAVDTAIKTAEELKGKIYTLGPLIHNNQVVEKLKKKGIKPIEDIDELNEGDTIIIRSHGVPPEV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 81 RNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGqYSNPEGgmYLVESPEDVWKITVKDenN 160
Cdd:PRK00087 81 LEELKDKGLKVIDATCPFVKNIQKLAKKYYEEGYQIVIVGDKNHPEVIGING-WCNNSA--IIVEDGEEAEKLPFDK--K 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 161 LSFMTQTTLSVDDTSEVIDALRSRFPKIVgpRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQRMGK 240
Cdd:PRK00087 156 ICVVSQTTEKQENFEKVLKELKKKGKEVK--VFNTICNATEVRQEAAEKLAKKVDVMIVVGGKNSSNTTKLYEICKSNCT 233
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 490520790 241 TAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKALGGSDAHE 292
Cdd:PRK00087 234 NTIHIENAGELPEEWFKGVKIIGVTAGASTPDWIIEEVIKKMSELDNMEEVE 285
|
|
| PRK12360 |
PRK12360 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional |
1-285 |
1.22e-60 |
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional
Pssm-ID: 237075 Cd Length: 281 Bit Score: 194.95 E-value: 1.22e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 1 MQILLANPRGFCAGVDRAISIVENALAI-YGAPIYVRHEVVHNRYVVDSLRERG--AIFIEQISEVPDGAILIFSAHGVS 77
Cdd:PRK12360 1 MKILIAKNAGFCFGVKRAIDTAYDEIEKnDGKKIYTLGPLIHNNQVVSDLEEKGvkTIEESEIDSLKEGDVVIIRSHGVS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 78 QAVRNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQYSNPEggmYLVESPEDVWKITVKD 157
Cdd:PRK12360 81 KKVYKDLKDKGLEIIDATCPFVKKIQNIVEEYYNKGYSIIIVGDKNHPEVIGINGWCDNSA---YIVNSIEEVENIPFLD 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 158 enNLSFMTQTTLSVDDTSEVIDALRSRFPKIVgpRKDDICYATTNRQEAVRALAEQADVVLVVGSKNSSNSNRLAELAQR 237
Cdd:PRK12360 158 --KACVVAQTTIIPELWEDILNVIKLKSKELV--FFNTICSATKKRQESAKELSKEVDVMIVIGGKHSSNTQKLVKICEK 233
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 490520790 238 MGKTAYLIDDANDIQEAWVQNAACVGVTAGASAPDVLVQNVITRLKAL 285
Cdd:PRK12360 234 NCPNTFHIETADELDLEMLKDYKIIGITAGASTPDWIIEEVIKKIKNL 281
|
|
| PRK13371 |
PRK13371 |
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional |
2-290 |
1.07e-34 |
|
4-hydroxy-3-methylbut-2-enyl diphosphate reductase; Provisional
Pssm-ID: 237367 Cd Length: 387 Bit Score: 130.05 E-value: 1.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 2 QILLANPRGFCAGVDRAISIVENALAIY-GAPIYVRHEVVHNRYVVDSLRERGAIFIEQI------SEVPDGAILIFSAH 74
Cdd:PRK13371 39 TIKLARAFGFCWGVERAVAMAYETRRHFpDERIWITNEIIHNPSVNQHLREMGVRFIPVEkgvkdfSVVTPGDVVILPAF 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 75 GVSqaVRNEAKSRDL--TVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTMGQysnpeGGMYLV----ESPE 148
Cdd:PRK13371 119 GAT--VQEMQLLNEKgcHIVDTTCPWVSKVWNTVEKHKKKDFTSIIHGKYKHEETRATSSF-----AGTYLVvldlEEAQ 191
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 149 DVWKITVKDENNLSFMT-----------------------QTTLSVDDTSEVIDALRSRFPKIVGPRK--------DDIC 197
Cdd:PRK13371 192 YVADYILGGGDREEFLErfakayspgfdpdrdlervgvanQTTMLKSETEEIGKLFERTMLRKYGPANlnehflsfNTIC 271
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 198 YATTNRQEAVRALAEQ-ADVVLVVGSKNSSNSNRLAELAQRMGKTAYLIDDANDI-----------------QEAWVQNA 259
Cdd:PRK13371 272 DATQERQDAMFSLVEEpLDLMVVIGGYNSSNTTHLQEIAIERGIPSYHIDSPERIlsgnsiehkplgkelvvTENWLPEG 351
|
330 340 350
....*....|....*....|....*....|..
gi 490520790 260 AC-VGVTAGASAPDVLVQNVITRLKALGGSDA 290
Cdd:PRK13371 352 PVtVGITSGASTPDKVVEDVIEKIFALKEDAR 383
|
|
| PLN02821 |
PLN02821 |
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase |
5-282 |
1.83e-28 |
|
1-hydroxy-2-methyl-2-(E)-butenyl 4-diphosphate reductase
Pssm-ID: 215440 Cd Length: 460 Bit Score: 114.13 E-value: 1.83e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 5 LANPRGFCAGVDRAISIV-ENALAIYGAPIYVRHEVVHNRYVVDSLRERGAIFIE------QISEVPDGAILIFSAHGVS 77
Cdd:PLN02821 110 LAKAYGFCWGVERAVQIAyEARKQFPDEKLWITNEIIHNPTVNKRLEEMNVQFIEveeggkDFSVVGEGDVVILPAFGAS 189
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 78 QAVRNEAKSRDLTVFDATCPLVTKVHMEVARSSRRGEEAILIGHAGHPEVEGTM---GQY---SNPEGGMY--------- 142
Cdd:PLN02821 190 VEEMQTLNDKNVQIVDTTCPWVSKVWNTVEKHKKKDYTSVIHGKYAHEETVATAsfaGKYiivKNMKEATYvcdyilggq 269
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 143 LVESPEDVWKITVKDENNLS-------------FMTQTTLSVDDTSEVIDALRSRFPKIVGPRK--------DDICYATT 201
Cdd:PLN02821 270 LDGSSGTKEEFLEKFKNAVSkgfdpdtdlvkvgIANQTTMLKGETEEIGKLLEKTMMQKYGVENvndhfmsfNTICDATQ 349
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 490520790 202 NRQEAVRALAEQA-DVVLVVGSKNSSNSNRLAELAQRMGKTAYLIDDANDI-----------------QEAWV-QNAACV 262
Cdd:PLN02821 350 ERQDAMYKLVEEKlDLMLVVGGWNSSNTSHLQEIAEHKGIPSYWIDSEERIgpgntiahklnhgelveKENWLpEGPVTI 429
|
330 340
....*....|....*....|
gi 490520790 263 GVTAGASAPDVLVQNVITRL 282
Cdd:PLN02821 430 GVTSGASTPDKVVEDVLDKV 449
|
|
| PBP1_ABC_ligand_binding-like |
cd19982 |
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type ... |
206-250 |
5.42e-03 |
|
type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems predicted to be involved in transport of amino acids, peptides, or inorganic ions; This subgroup includes the type 1 periplasmic ligand-binding domain of uncharacterized ABC (ATPase Binding Cassette)-type active transport systems that are predicted to be involved in transport of amino acids, peptides, or inorganic ions. This subgroup has high sequence similarity to members of the family of hydrophobic amino acid transporters (HAAT), such as leucine-isoleucine-valine binding protein (LIVBP); however, their ligand specificity has not been determined experimentally.
Pssm-ID: 380637 [Multi-domain] Cd Length: 302 Bit Score: 38.03 E-value: 5.42e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 490520790 206 AVRALAEQADVVLVVGSKNSSNSNRLAELAQRMgKTAYLIDDAND 250
Cdd:cd19982 58 AAEKLVSQDKVPLIVGGYSSGITLPVAAVAERQ-KIPLLVPTAAD 101
|
|
|