|
Name |
Accession |
Description |
Interval |
E-value |
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
1-302 |
0e+00 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 610.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 1 MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEA 80
Cdd:PRK13389 1 MAAINTKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 81 MLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFD 160
Cdd:PRK13389 81 MLEKRVKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFD 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 161 ETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQ 240
Cdd:PRK13389 161 ETGHSQIMVEPVADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQ 240
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15830992 241 LTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK 302
Cdd:PRK13389 241 LTDAIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIKK 302
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
7-296 |
1.61e-178 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 493.78 E-value: 1.61e-178
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRV 86
Cdd:COG1210 2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 87 KRQLLDEVQSICpPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHSQ 166
Cdd:COG1210 82 KEELLEEVRSIS-PLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQ-----MIEVYEETGGSV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 167 IMVEPVA--DVTAYGVVDCKGVElapGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244
Cdd:COG1210 156 IAVQEVPpeEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDA 232
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 15830992 245 IDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEE 296
Cdd:COG1210 233 IAALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKE 284
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
9-275 |
6.30e-162 |
|
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 273443 [Multi-domain] Cd Length: 260 Bit Score: 451.04 E-value: 6.30e-162
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 89 QLLDEVQSICPPhVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESdlsqdNLAEMIRRFDETGHSQIM 168
Cdd:TIGR01099 81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP-----ALKQMIKAYEKTGCSIIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 169 VEPVA--DVTAYGVVDCKGVELAPGEsvpMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAID 246
Cdd:TIGR01099 155 VQEVPkeEVSKYGVIDGEGIEKDLYK---VKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
|
250 260
....*....|....*....|....*....
gi 15830992 247 MLIEKETVEAYHMKGKSHDCGNKLGYMQA 275
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
9-282 |
7.86e-155 |
|
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose Pyrophosphorylase (UGPase) catalyzes a reversible production of UDP-Glucose and pyrophosphate (PPi) from glucose-1-phosphate and UTP. UDP-glucose plays pivotal roles in galactose utilization, in glycogen synthesis, and in the synthesis of the carbohydrate moieties of glycolipids , glycoproteins , and proteoglycans. UGPase is found in both prokaryotes and eukaryotes, although prokaryotic and eukaryotic forms of UGPase catalyze the same reaction, they share low sequence similarity.
Pssm-ID: 133021 [Multi-domain] Cd Length: 267 Bit Score: 433.11 E-value: 7.86e-155
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKR 88
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 89 QLLDEVqSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESdlsqdNLAEMIRRFDETGHSQIM 168
Cdd:cd02541 81 DLLEEV-RIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEP-----CLKQLIEAYEKTGASVIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 169 VEPVA--DVTAYGVVDCKGVElapGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAID 246
Cdd:cd02541 155 VEEVPpeDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 15830992 247 MLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIR 282
Cdd:cd02541 232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
10-296 |
1.27e-134 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 383.47 E-value: 1.27e-134
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169
Cdd:PRK10122 85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 170 EPV-ADVTAYGVVDCKGVELAPGESVPMVGVVEKP-KADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
Cdd:PRK10122 165 KRMpGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIAE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15830992 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEE 296
Cdd:PRK10122 245 LAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEK 293
|
|
| galF |
TIGR01105 |
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ... |
10-296 |
3.45e-120 |
|
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a non-catalytic subunit of the UTP-glucose pyrophosphorylase modulating the enzyme activity to increase the formation of UDP-glucose [Regulatory functions, Protein interactions]
Pssm-ID: 130175 Cd Length: 297 Bit Score: 346.63 E-value: 3.45e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
Cdd:TIGR01105 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169
Cdd:TIGR01105 85 LLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATADPLRYNLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 170 EPV-ADVTAYGVVDCKGVELAPGESVPMVGVVEKP-KADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
Cdd:TIGR01105 165 KRMpGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIAE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 15830992 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEE 296
Cdd:TIGR01105 245 LAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEK 293
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
11-267 |
2.60e-55 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 178.54 E-value: 2.60e-55
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELeamlekrvkrql 90
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 91 ldevqsicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDeyesdlsqDNLAEMIRRF-DETGHSQIMV 169
Cdd:cd04181 69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTD--------LDLSELLRFHrEKGADATIAV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 170 EPVADVTAYGVVDCKGVELapgesvpMVGVVEKPKADvaPSNLAIVGRYVLSADIWPLLAKTPPGAGDEiqLTDAIDMLI 249
Cdd:cd04181 131 KEVEDPSRYGVVELDDDGR-------VTRFVEKPTLP--ESNLANAGIYIFEPEILDYIPEILPRGEDE--LTDAIPLLI 199
|
250
....*....|....*...
gi 15830992 250 EKETVEAYHMKGKSHDCG 267
Cdd:cd04181 200 EEGKVYGYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
9-251 |
1.54e-45 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 153.88 E-value: 1.54e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEamlekrvkr 88
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFG--------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 89 qlldevqsicpphVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDvildeyesDLSQDNLAEMIRRFDETGHS-QI 167
Cdd:cd04189 72 -------------VRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGD--------NLIQEGISPLVRDFLEEDADaSI 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 168 MVEPVADVTAYGVVDCKGvelapgESVpmVGVVEKPKAdvAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
Cdd:cd04189 131 LLAEVEDPRRFGVAVVDD------GRI--VRLVEKPKE--PPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQW 200
|
....
gi 15830992 248 LIEK 251
Cdd:cd04189 201 LIDR 204
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
10-278 |
1.33e-43 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 150.63 E-value: 1.33e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThssknsienhfdTSFELEamlekRVKRQ 89
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDGP-----QFERL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 LLDEVQSICppHVTImqVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEyesdlsqDNLAEMIRRFDE-TGHSQIM 168
Cdd:COG1209 65 LGDGSQLGI--KISY--AVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG-------DGLSELLREAAArESGATIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 169 VEPVADVTAYGVV--DCKGVelapgesvpMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAID 246
Cdd:COG1209 134 GYKVEDPERYGVVefDEDGR---------VVSLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQ 202
|
250 260 270
....*....|....*....|....*....|....*..
gi 15830992 247 MLIEKETVEAYHMkGKSH---DCGNKLGYMQA--FVE 278
Cdd:COG1209 203 AYLERGKLVVELL-GRGFawlDTGTHESLLEAnrFVL 238
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
10-267 |
2.58e-42 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 150.05 E-value: 2.58e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEamlekrvkrq 89
Cdd:TIGR03992 2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGG---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 lldevqsicpphVTIMQVRQGLAKGLGHAVLCAHPVVgDEPVAVILPDVILDeyesdlsQDNLAEMIRRFDETghsqIMV 169
Cdd:TIGR03992 72 ------------VPIEYVVQEEQLGTADALGSAKEYV-DDEFLVLNGDVLLD-------SDLLERLIRAEAPA----IAV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 170 EPVADVTAYGVVDCKGVELapgesvpmVGVVEKPKAdvAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDMLI 249
Cdd:TIGR03992 128 VEVDDPSDYGVVETDGGRV--------TGIVEKPEN--PPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLI 197
|
250
....*....|....*...
gi 15830992 250 EKETVEAYHMKGKSHDCG 267
Cdd:TIGR03992 198 DEGKVKAVELDGFWLDVG 215
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
10-275 |
3.53e-40 |
|
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein s [Translation, ribosomal structure and biogenesis, Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440821 [Multi-domain] Cd Length: 238 Bit Score: 140.29 E-value: 3.53e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELeamlekrvkrq 89
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 lldevqsicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEyesdlsqdNLAEMIRRFDETGHS-QIM 168
Cdd:COG1208 70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDL--------DLAALLAFHREKGADaTLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 169 VEPVADVTAYGVvdckgVELAPGESVpmVGVVEKPKAdvAPSNLAIVGRYVLSADIWPLLAKtppgaGDEIQLTDAIDML 248
Cdd:COG1208 131 LVPVPDPSRYGV-----VELDGDGRV--TRFVEKPEE--PPSNLINAGIYVLEPEIFDYIPE-----GEPFDLEDLLPRL 196
|
250 260
....*....|....*....|....*..
gi 15830992 249 IEKETVEAYHMKGKSHDCGNKLGYMQA 275
Cdd:COG1208 197 IAEGRVYGYVHDGYWLDIGTPEDLLEA 223
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
10-279 |
4.70e-23 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 95.01 E-value: 4.70e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDK-PLIQYVVNECIAAGITEIVLVThssknsieNHFDtSFELEamlekrvkR 88
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH-RFMLN--------E 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 89 QLLDEvqSICPPHVTIMQvrQGLAKGLGHAVLCAHPVVGDEPV-AVILPDVIldeyesdLSQDNLAEMIRRFDETGHSQ- 166
Cdd:pfam00483 64 LLGDG--SKFGVQITYAL--QPEGKGTAPAVALAADFLGDEKSdVLVLGGDH-------IYRMDLEQAVKFHIEKAADAt 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 167 --IMVEPVADVTAYGVVDckgvelaPGESVPMVGVVEKPKADVApSNLAIVGRYVLSADIWPLLAKT---PPGAGDEIql 241
Cdd:pfam00483 133 vtFGIVPVEPPTGYGVVE-------FDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDFLAKYleeLKRGEDEI-- 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 15830992 242 TDAIDMLIEKETVEAYHMKGKSH--DCGNKLGYMQAFVEY 279
Cdd:pfam00483 203 TDILPKALEDGKLAYAFIFKGYAwlDVGTWDSLWEANLFL 242
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
9-259 |
5.03e-19 |
|
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is the short form of glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.
Pssm-ID: 133019 [Multi-domain] Cd Length: 240 Bit Score: 84.16 E-value: 5.03e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 9 KKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVthssknSIENHFDtsfeleamlekRVKR 88
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII------STPEDLP-----------LFKE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 89 QLLDEVQSICPPHVTImqvrQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSqdnlaEMIRRFDE-TGHSQI 167
Cdd:cd02538 64 LLGDGSDLGIRITYAV----QPKPGGLAQAFIIGEEFIGDDPVCLILGDNIF--YGQGLS-----PILQRAAAqKEGATV 132
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 168 MVEPVADVTAYGVvdckgVELAPGESVpmVGVVEKPKAdvAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
Cdd:cd02538 133 FGYEVNDPERYGV-----VEFDENGRV--LSIEEKPKK--PKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNE 203
|
250
....*....|..
gi 15830992 248 LIEKETVEAYHM 259
Cdd:cd02538 204 YLEKGKLSVELL 215
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
10-275 |
2.34e-17 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 79.15 E-value: 2.34e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFEleamlekrvkrq 89
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 lldevqsicPPHVTI-MQVRQGL--AKGLGHAVlcahPVVGDEPVAVILPDVILDeyesdlsqDNLAEMIRRFDETGHSQ 166
Cdd:cd06422 69 ---------GLRITIsDEPDELLetGGGIKKAL----PLLGDEPFLVVNGDILWD--------GDLAPLLLLHAWRMDAL 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 167 IMVEPVADVTAY-GVVDckgVELAPGesvpmvGVVeKPKADVAPSNLAIVGRYVLSADiwpLLAKTPPGAGDeiqLTDAI 245
Cdd:cd06422 128 LLLLPLVRNPGHnGVGD---FSLDAD------GRL-RRGGGGAVAPFTFTGIQILSPE---LFAGIPPGKFS---LNPLW 191
|
250 260 270
....*....|....*....|....*....|
gi 15830992 246 DMLIEKETVEAYHMKGKSHDCGNKLGYMQA 275
Cdd:cd06422 192 DRAIAAGRLFGLVYDGLWFDVGTPERLLAA 221
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
11-275 |
2.94e-15 |
|
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133048 [Multi-domain] Cd Length: 220 Bit Score: 73.31 E-value: 2.94e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHF-DTSfeleamlEKRVKRQ 89
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgDGS-------KFGVNIS 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 LLDEvqsicpphvtimQVRQGLAKGLGhaVLCAHPvvgDEPVAVILPDVildeyesdLSQDNLAEMIRRFDETGHSQIMV 169
Cdd:cd06426 74 YVRE------------DKPLGTAGALS--LLPEKP---TDPFLVMNGDI--------LTNLNYEHLLDFHKENNADATVC 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 170 EPVADVT-AYGVVDCKGVElapgesvpMVGVVEKPKAdvapSNLAIVGRYVLSADIWPLLAKtppgaGDEIQLTDAIDML 248
Cdd:cd06426 129 VREYEVQvPYGVVETEGGR--------ITSIEEKPTH----SFLVNAGIYVLEPEVLDLIPK-----NEFFDMPDLIEKL 191
|
250 260
....*....|....*....|....*...
gi 15830992 249 IEK-ETVEAYHMKGKSHDCGNKLGYMQA 275
Cdd:cd06426 192 IKEgKKVGVFPIHEYWLDIGRPEDYEKA 219
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
10-73 |
4.21e-13 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 67.57 E-value: 4.21e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFD 73
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA 64
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
7-301 |
4.47e-13 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 68.16 E-value: 4.47e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSknsienhfDTSfeleamlekRV 86
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DTP---------RF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 87 KRQLLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQDNLAEMIRrfdETGhSQ 166
Cdd:PRK15480 65 QQLLGDGSQW----GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIF--YGHDLPKLMEAAVNK---ESG-AT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 167 IMVEPVADVTAYGVV--DCKGVELAPGESvPMvgvveKPKadvapSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDA 244
Cdd:PRK15480 135 VFAYHVNDPERYGVVefDQNGTAISLEEK-PL-----QPK-----SNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDI 203
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 15830992 245 IDMLIEKETVeAYHMKGKshdcgnklGYmqAFVEYGIRHNTL-GTEFKAWLEEEMGIK 301
Cdd:PRK15480 204 NRIYMEQGRL-SVAMMGR--------GY--AWLDTGTHQSLIeASNFIATIEERQGLK 250
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
10-76 |
1.12e-12 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 65.74 E-value: 1.12e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSF 76
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSK 68
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
10-77 |
1.89e-12 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 65.37 E-value: 1.89e-12
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEI-VLVTHSSKNSIENHFDTSFE 77
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLRSFPL 70
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
11-183 |
1.63e-11 |
|
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.
Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 62.57 E-value: 1.63e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQL 90
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 91 LdevqsicpphvtimqvrqglakGLGHAVLCAHPVVGDEPVAVILPDVILDEyesdlsqdNLAEMIRRFDETGHSQIM-V 169
Cdd:cd06915 81 L----------------------GTGGAIKNALPKLPEDQFLVLNGDTYFDV--------DLLALLAALRASGADATMaL 130
|
170
....*....|....
gi 15830992 170 EPVADVTAYGVVDC 183
Cdd:cd06915 131 RRVPDASRYGNVTV 144
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
11-79 |
2.45e-11 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 62.25 E-value: 2.45e-11
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15830992 11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELE 79
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK 69
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
11-259 |
8.73e-11 |
|
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440820 [Multi-domain] Cd Length: 457 Bit Score: 61.97 E-value: 8.73e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMlpatK-AIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDtsfeleamlEKRVKrq 89
Cdd:COG1207 5 VVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA---------DLDVE-- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 lldevqsicpphvTIMQVRQglaKGLGHAVLCAHPVVG--DEPVAVILPDVILdeyesdLSQDNLAEMIRRFDETGHS-Q 166
Cdd:COG1207 70 -------------FVLQEEQ---LGTGHAVQQALPALPgdDGTVLVLYGDVPL------IRAETLKALLAAHRAAGAAaT 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 167 IMVEPVADVTAYGVVdckgVELAPGEsvpMVGVVE-KpkaDVAPSNLAI----VGRYVL-SADIWPLLAK-TPPGAGDEI 239
Cdd:COG1207 128 VLTAELDDPTGYGRI----VRDEDGR---VLRIVEeK---DATEEQRAIreinTGIYAFdAAALREALPKlSNDNAQGEY 197
|
250 260
....*....|....*....|.
gi 15830992 240 QLTDAIDMLI-EKETVEAYHM 259
Cdd:COG1207 198 YLTDVIAIARaDGLKVAAVQP 218
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
11-260 |
3.13e-10 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 59.07 E-value: 3.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMlpatK-AIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKnsienhfdtsfeleamlekrvkrq 89
Cdd:cd02540 1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGA------------------------ 52
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 llDEVQSICP-PHVTImqVRQGLAKGLGHAVLCAHPVVGD--EPVAVILPDVILdeyesdLSQDNLAEMIRRFDETGHSQ 166
Cdd:cd02540 53 --EQVKKALAnPNVEF--VLQEEQLGTGHAVKQALPALKDfeGDVLVLYGDVPL------ITPETLQRLLEAHREAGADV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 167 IMV--EPvADVTAYGVVDCKGvelapGESVpmVGVVEkpKADVAPSNLAIV----GRYVLSA-DIWPLLAK-TPPGAGDE 238
Cdd:cd02540 123 TVLtaEL-EDPTGYGRIIRDG-----NGKV--LRIVE--EKDATEEEKAIRevnaGIYAFDAeFLFEALPKlTNNNAQGE 192
|
250 260
....*....|....*....|...
gi 15830992 239 IQLTDAIDMLI-EKETVEAYHMK 260
Cdd:cd02540 193 YYLTDIIALAVaDGLKVAAVLAD 215
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
10-224 |
1.33e-09 |
|
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain and a C-terminal Lefthanded-beta-Helix fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes, such as cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133047 [Multi-domain] Cd Length: 233 Bit Score: 57.22 E-value: 1.33e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVL-VTHSSKNsienhfdtsfeLEAMLEKRVKR 88
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPED-----------MVPFLKEYEKK 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 89 QlldEVQSICpphvTIMQVRQGLAKGLGHA--VLCahpvVGDEPVAVILPDVILDeYEsdlsqdnLAEMIRRFDETGH-S 165
Cdd:cd06425 71 L---GIKITF----SIETEPLGTAGPLALArdLLG----DDDEPFFVLNSDVICD-FP-------LAELLDFHKKHGAeG 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 166 QIMVEPVADVTAYGVVDCKgvelapgESVPMV-GVVEKPKADVapSNLAIVGRYVLSADI 224
Cdd:cd06425 132 TILVTKVEDPSKYGVVVHD-------ENTGRIeRFVEKPKVFV--GNKINAGIYILNPSV 182
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
9-134 |
1.57e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 52.14 E-value: 1.57e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 9 KKAVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT-HSSknsienhfdtsfeleamleKRVK 87
Cdd:PRK14354 3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGA-------------------EEVK 60
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 15830992 88 RQLLDEVQsicpphvTIMQVRQglaKGLGHAVLCAHPVVGDEP--VAVI 134
Cdd:PRK14354 61 EVLGDRSE-------FALQEEQ---LGTGHAVMQAEEFLADKEgtTLVI 99
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
11-75 |
1.67e-07 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 51.07 E-value: 1.67e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 15830992 11 AVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTS 75
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS 67
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
11-179 |
1.32e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 49.48 E-value: 1.32e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIEnhfdtsfeleamlekrvkrql 90
Cdd:PRK14353 8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 91 lDEVQSICPPHVTIMQVRQglaKGLGHAVLCAHPVV--GDEPVAVILPDVILdeyesdLSQDNLAEMI-RRFDETGHSQI 167
Cdd:PRK14353 64 -AAAAKIAPDAEIFVQKER---LGTAHAVLAAREALagGYGDVLVLYGDTPL------ITAETLARLReRLADGADVVVL 133
|
170
....*....|..
gi 15830992 168 MVEPvADVTAYG 179
Cdd:PRK14353 134 GFRA-ADPTGYG 144
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
11-124 |
4.17e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 47.82 E-value: 4.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHF----DTSFELEAmlekrv 86
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFagdgDVSFALQE------ 76
|
90 100 110
....*....|....*....|....*....|....*...
gi 15830992 87 kRQLldevqsicpphvtimqvrqglakGLGHAVLCAHP 124
Cdd:PRK14355 77 -EQL-----------------------GTGHAVACAAP 90
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
12-218 |
7.27e-06 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 46.09 E-value: 7.27e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 12 VIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVThsskNSIENhfdTSFELEAMLEKRVkrqll 91
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC----RDEHN---TKFHLDESLKLLA----- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 92 devqsicpPHVTIMQVrQGLAKGLGHAVL-CAHPVVGDEPVAVILPDVILDeyesdlsqDNLAEMIRRFDETGHSQ--IM 168
Cdd:cd04183 70 --------PNATVVEL-DGETLGAACTVLlAADLIDNDDPLLIFNCDQIVE--------SDLLAFLAAFRERDLDGgvLT 132
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 15830992 169 VEPVADVTAYGVVDCKGVELAPGESVPMvgvvekpkadvapSNLAIVGRY 218
Cdd:cd04183 133 FFSSHPRWSYVKLDENGRVIETAEKEPI-------------SDLATAGLY 169
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
11-62 |
1.11e-05 |
|
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.
Pssm-ID: 133009 [Multi-domain] Cd Length: 218 Bit Score: 45.59 E-value: 1.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 15830992 11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAG-ITEIVLVTH 62
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
12-271 |
1.15e-05 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 46.51 E-value: 1.15e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 12 VIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT-HSSKnsienhfdtsfELEAMLEKrvkrql 90
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTgHGAE-----------QVEAALQG------ 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 91 ldevqsicpPHVTImqVRQGLAKGLGHAVLCAHPVV--GDEPVAVILPDVILdeyesdLSQDNLAEMIRRFDETGHS-QI 167
Cdd:PRK14358 71 ---------SGVAF--ARQEQQLGTGDAFLSGASALteGDADILVLYGDTPL------LRPDTLRALVADHRAQGSAmTI 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 168 MVEPVADVTAYGvvdckgvELAPGESVPMVGVVEkpKADVAPSNLAI----VGRYVLSADIwPLLAK--TPPGAGDEIQL 241
Cdd:PRK14358 134 LTGELPDATGYG-------RIVRGADGAVERIVE--QKDATDAEKAIgefnSGVYVFDARA-PELARriGNDNKAGEYYL 203
|
250 260 270
....*....|....*....|....*....|.
gi 15830992 242 TDAIDML-IEKETVEAYhmkgKSHDCGNKLG 271
Cdd:PRK14358 204 TDLLGLYrAGGAQVRAF----KLSDPDEVLG 230
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
10-181 |
3.84e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 44.75 E-value: 3.84e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 10 KAVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSknsienhfdtsfeleamlekrvkrq 89
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEA------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 90 llDEVQSICPPHVTIMQVRQGLakGLGHAVLCAHPVVG-DEPVAVILPDVILdeyesdLSQDNLAEMIRRFDETGHS-QI 167
Cdd:PRK14357 54 --ELVKKLLPEWVKIFLQEEQL--GTAHAVMCARDFIEpGDDLLILYGDVPL------ISENTLKRLIEEHNRKGADvTI 123
|
170
....*....|....
gi 15830992 168 MVEPVADVTAYGVV 181
Cdd:PRK14357 124 LVADLEDPTGYGRI 137
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
11-90 |
4.31e-05 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]
Pssm-ID: 213532 Cd Length: 217 Bit Score: 43.82 E-value: 4.31e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 11 AVIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVnECIAA--GITEIVLVTHSsknsienhfDTSFELEAMLEKRVKR 88
Cdd:TIGR00453 2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHAL-DAFLAhpAIDEVVVVVSP---------DDTEFFQKYLVARAVP 68
|
..
gi 15830992 89 QL 90
Cdd:TIGR00453 69 KI 70
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
12-62 |
5.39e-05 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 43.58 E-value: 5.39e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 15830992 12 VIPVAGLGTRMlpaTKAIPKEMLPLVDKPLIQYVVNECIAAG-ITEIVLVTH 62
Cdd:COG1211 1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
11-73 |
7.40e-05 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 42.84 E-value: 7.40e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 15830992 11 AVIPVAGLGTRMlpatkAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFD 73
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
11-61 |
1.09e-04 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 42.16 E-value: 1.09e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 15830992 11 AVIPVAGLGTRMLPatkaiPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
Cdd:cd04182 3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVL 48
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
11-62 |
5.28e-04 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 40.50 E-value: 5.28e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15830992 11 AVIPVAGLGTRMlpatKA-IPKEMLPLVDKPLIQYVVNECIAAG-ITEIVLVTH 62
Cdd:PRK00155 6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
11-63 |
3.60e-03 |
|
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional
Pssm-ID: 236492 [Multi-domain] Cd Length: 378 Bit Score: 38.68 E-value: 3.60e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 15830992 11 AVIPVAGLGTRmlpATKAIPKEMLPLVDKPLIQYVVNECIAAG-ITEIVLVTHS 63
Cdd:PRK09382 8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHP 58
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-258 |
4.79e-03 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 38.47 E-value: 4.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 6 TKVKKAVIPVAGLGTRMLpatKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKnsienhfdtsfeleaMLEK 84
Cdd:PRK09451 3 NSAMSVVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVyGHGGD---------------LLKQ 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 85 RVKRQLLDEVqsicpphvtiMQVRQglaKGLGHAVLCAHPVVGD-EPVAVILPDVILdeyesdLSQDNLAEMIRRFDETG 163
Cdd:PRK09451 65 TLADEPLNWV----------LQAEQ---LGTGHAMQQAAPFFADdEDILMLYGDVPL------ISVETLQRLRDAKPQGG 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15830992 164 HSQIMVEpVADVTAYG-VVDCKGvelapgesvPMVGVVEkpKADVAPSNLAI----VGRYVLS-ADIWPLLAK-TPPGAG 236
Cdd:PRK09451 126 IGLLTVK-LDNPTGYGrITRENG---------KVVGIVE--QKDATDEQRQIqeinTGILVANgADLKRWLAKlTNNNAQ 193
|
250 260
....*....|....*....|...
gi 15830992 237 DEIQLTDAIDMLI-EKETVEAYH 258
Cdd:PRK09451 194 GEYYITDIIALAHqEGREIVAVH 216
|
|
| |
