|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
4-299 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 506.49 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 4 KINKAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRV 83
Cdd:COG1210 2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 84 KRQLLDEIQAICPKeVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDatadlRTENLAAMLSRYNEVGGyS 163
Cdd:COG1210 82 KEELLEEVRSISPL-ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDS-----EKPCLKQMIEVYEETGG-S 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 164 QIMVEPVPMEQVSSYGVVDCGGVDlapGESKTMTAIVEKPAVEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTD 243
Cdd:COG1210 155 VIAVQEVPPEEVSKYGIVDGEEIE---GGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTD 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1543020203 244 AIAMLMEKETVEAFHMTGKSHDCGSKLGYMKANVEYGLRHPEMADEFRAYLTDLMK 299
Cdd:COG1210 232 AIAALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLK 287
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
4-298 |
1.68e-170 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 474.01 E-value: 1.68e-170
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 4 KINKAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRV 83
Cdd:PRK13389 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 84 KRQLLDEIQAICPKEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDATADLRTENLAAMLSRYNEVgGYS 163
Cdd:PRK13389 87 KRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDET-GHS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 164 QIMVEPVpmEQVSSYGVVDCGGVDLAPGESKTMTAIVEKPAVEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTD 243
Cdd:PRK13389 166 QIMVEPV--ADVTAYGVVDCKGVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1543020203 244 AIAMLMEKETVEAFHMTGKSHDCGSKLGYMKANVEYGLRHPEMADEFRAYLTDLM 298
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEM 298
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
7-282 |
3.16e-153 |
|
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: 428.87 E-value: 3.16e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRVKRQ 86
Cdd:cd02541 2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIqAICPKEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDatadlRTENLAAMLSRYNEVGGySQIM 166
Cdd:cd02541 82 LLEEV-RIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDS-----KEPCLKQLIEAYEKTGA-SVIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVPMEQVSSYGVVDCGGVDlapGESKTMTAIVEKPAVEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTDAIA 246
Cdd:cd02541 155 VEEVPPEDVSKYGIVKGEKID---GDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1543020203 247 MLMEKETVEAFHMTGKSHDCGSKLGYMKANVEYGLR 282
Cdd:cd02541 232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
7-275 |
8.47e-153 |
|
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: 427.54 E-value: 8.47e-153
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRVKRQ 86
Cdd:TIGR01099 2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIQAICPKeVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDatadlRTENLAAMLSRYNEVGGySQIM 166
Cdd:TIGR01099 82 LLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVN-----EEPALKQMIKAYEKTGC-SIIA 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVPMEQVSSYGVVDCGGVDLAPGEsktMTAIVEKPAVEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTDAIA 246
Cdd:TIGR01099 155 VQEVPKEEVSKYGVIDGEGIEKDLYK---VKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
|
250 260
....*....|....*....|....*....
gi 1543020203 247 MLMEKETVEAFHMTGKSHDCGSKLGYMKA 275
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
7-298 |
7.67e-128 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 366.14 E-value: 7.67e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRVKRQ 86
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIQAICPKEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDATADLRTENLAAMLSRYNEVgGYSQIM 166
Cdd:PRK10122 85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNET-GRSQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVPMEqVSSYGVVDCGGVDLAPGESKTMTAIVEKPaveDAP----SNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLT 242
Cdd:PRK10122 164 AKRMPGD-LSEYSVIQTKEPLDREGKVSRIVEFIEKP---DQPqtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1543020203 243 DAIAMLMEKETVEAFHMTGKSHDCGSKLGYMKANVEYGLRHPEMADEFRAYLTDLM 298
Cdd:PRK10122 240 DAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLL 295
|
|
| galF |
TIGR01105 |
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ... |
7-298 |
1.43e-114 |
|
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: 332.38 E-value: 1.43e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRVKRQ 86
Cdd:TIGR01105 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIQAICPKEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDATADLRTENLAAMLSRYNEVgGYSQIM 166
Cdd:TIGR01105 85 LLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATADPLRYNLAAMIARFNET-GRSQVL 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVPMEqVSSYGVVDCGGVDLAPGESKTMTAIVEKPaveDAP----SNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLT 242
Cdd:TIGR01105 164 AKRMPGD-LSEYSVIQTKEPLDREGKVSRIVEFIEKP---DQPqtldSDLMAVGRYVLSADIWAELERTEPGAWGRIQLT 239
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1543020203 243 DAIAMLMEKETVEAFHMTGKSHDCGSKLGYMKANVEYGLRHPEMADEFRAYLTDLM 298
Cdd:TIGR01105 240 DAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEKLL 295
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
8-267 |
4.42e-61 |
|
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: 193.18 E-value: 4.42e-61
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELettlekrvkrql 87
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 88 ldeiqaicpkEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDatadlrteNLAAMLSRYNEVGGYSQIMV 167
Cdd:cd04181 69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL--------DLSELLRFHREKGADATIAV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 168 EPVpmEQVSSYGVVDCGGVDLapgesktMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEiqLTDAIAM 247
Cdd:cd04181 131 KEV--EDPSRYGVVELDDDGR-------VTRFVEKP--TLPESNLANAGIYIFEPEILDYIPEILPRGEDE--LTDAIPL 197
|
250 260
....*....|....*....|
gi 1543020203 248 LMEKETVEAFHMTGKSHDCG 267
Cdd:cd04181 198 LIEEGKVYGYPVDGYWLDIG 217
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
7-276 |
6.47e-47 |
|
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: 157.62 E-value: 6.47e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELettlekrvkrq 86
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 lldeiqaicpkEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDdatadlrtENLAAMLSRYNEVGGYSQIM 166
Cdd:COG1208 70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD--------LDLAALLAFHREKGADATLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VepVPMEQVSSYGVVDCGGVDLApgesktmTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKltppgAGDEIQLTDAIA 246
Cdd:COG1208 131 L--VPVPDPSRYGVVELDGDGRV-------TRFVEKP--EEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLP 194
|
250 260 270
....*....|....*....|....*....|
gi 1543020203 247 MLMEKETVEAFHMTGKSHDCGSKLGYMKAN 276
Cdd:COG1208 195 RLIAEGRVYGYVHDGYWLDIGTPEDLLEAN 224
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
7-276 |
1.46e-46 |
|
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: 156.57 E-value: 1.46e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELEttlekrvkrq 86
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFG---------- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 lldeiqaicpkeVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDdatadlrtENLAAMLSRYNEVGGYSQIM 166
Cdd:cd04189 72 ------------VRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQ--------EGISPLVRDFLEEDADASIL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVPmeQVSSYGVVDCggvdlapgESKTMTAIVEKPAveDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTDAIA 246
Cdd:cd04189 132 LAEVE--DPRRFGVAVV--------DDGRIVRLVEKPK--EPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQ 199
|
250 260 270
....*....|....*....|....*....|.
gi 1543020203 247 MLMEK-ETVEAFHMTGKSHDCGSKLGYMKAN 276
Cdd:cd04189 200 WLIDRgRRVGYSIVTGWWKDTGTPEDLLEAN 230
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
7-276 |
4.06e-43 |
|
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: 151.98 E-value: 4.06e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELettlekrvkrq 86
Cdd:TIGR03992 2 KAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRG----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 lldeiqaicpkEVTILHVRQGEAKGLGHAVLKARPIIgNEPFVVVLPDVILDdatadlrTENLAAMLSRYNEVggysqIM 166
Cdd:TIGR03992 71 -----------GVPIEYVVQEEQLGTADALGSAKEYV-DDEFLVLNGDVLLD-------SDLLERLIRAEAPA-----IA 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVpmEQVSSYGVVDCGGvdlapgesKTMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTDAIA 246
Cdd:TIGR03992 127 VVEV--DDPSDYGVVETDG--------GRVTGIVEKP--ENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQ 194
|
250 260 270
....*....|....*....|....*....|
gi 1543020203 247 MLMEKETVEAFHMTGKSHDCGSKLGYMKAN 276
Cdd:TIGR03992 195 LLIDEGKVKAVELDGFWLDVGRPWDLLDAN 224
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
7-276 |
8.05e-43 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 148.70 E-value: 8.05e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHssknaieNHFDKSFElettlekrvkrQ 86
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST-------PEDGPQFE-----------R 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIQAICPKeVTIlhVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDatadlrtENLAAMLSRYNEVGGYSQIM 166
Cdd:COG1209 64 LLGDGSQLGIK-ISY--AVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG-------DGLSELLREAAARESGATIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPV--PmeqvSSYGVVDcggVDlapgESKTMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTDA 244
Cdd:COG1209 134 GYKVedP----ERYGVVE---FD----EDGRVVSLEEKP--KEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDA 200
|
250 260 270
....*....|....*....|....*....|....*
gi 1543020203 245 IAMLMEKETVEAFHMtGKSH---DCGSKLGYMKAN 276
Cdd:COG1209 201 NQAYLERGKLVVELL-GRGFawlDTGTHESLLEAN 234
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
7-279 |
2.85e-27 |
|
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: 106.18 E-value: 2.85e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDK-PLIQYIVNECISAGITEIVLVThssknaieNHFDkSFELEttlekrvkR 85
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH-RFMLN--------E 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 86 QLLDEIQaicpKEVTILHVRQGEAKGLGHAVLKARPIIGNEPF-VVVLP-DVILDDAtadlrtenLAAMLSRYNEVGGYS 163
Cdd:pfam00483 64 LLGDGSK----FGVQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGgDHIYRMD--------LEQAVKFHIEKAADA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 164 QIMVEPVPMEQVSSYGVVDcggvdlaPGESKTMTAIVEKPAVEDApSNLAVVGRYVLSEKIWD-LLKLTPPGAGDEIQLT 242
Cdd:pfam00483 132 TVTFGIVPVEPPTGYGVVE-------FDDNGRVIRFVEKPKLPKA-SNYASMGIYIFNSGVLDfLAKYLEELKRGEDEIT 203
|
250 260 270
....*....|....*....|....*....|....*....
gi 1543020203 243 DAI-AMLMEKETVEAFHMTGKS-HDCGSKLGYMKANVEY 279
Cdd:pfam00483 204 DILpKALEDGKLAYAFIFKGYAwLDVGTWDSLWEANLFL 242
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
7-259 |
2.92e-20 |
|
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: 87.25 E-value: 2.92e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVthSSKNAIEnhfdksfelettlekRVKRQ 86
Cdd:cd02538 2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII--STPEDLP---------------LFKEL 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIQAicpkEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILDDatadlrtENLAAMLSRYNEVGGYSQIM 166
Cdd:cd02538 65 LGDGSDL----GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYG-------QGLSPILQRAAAQKEGATVF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 167 VEPVPMEQvsSYGVVDcggVDlapgESKTMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTDAIA 246
Cdd:cd02538 134 GYEVNDPE--RYGVVE---FD----ENGRVLSIEEKP--KKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNN 202
|
250
....*....|...
gi 1543020203 247 MLMEKETVEAFHM 259
Cdd:cd02538 203 EYLEKGKLSVELL 215
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
7-152 |
4.09e-19 |
|
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: 83.77 E-value: 4.09e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFElettlekrvkrq 86
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF------------ 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1543020203 87 lldeiqaicPKEVTILHvrqgEAKGL---GHAVLKARPIIGNEPFVVVLPDVILDDATADLRTENLAAM 152
Cdd:cd06422 69 ---------GLRITISD----EPDELletGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRM 124
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
8-276 |
3.51e-18 |
|
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: 81.02 E-value: 3.51e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHF-DKSfelettlekrvkrq 86
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgDGS-------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 lldeiqaicPKEVTILHVRqgEAKGLGHA----VLKARPiigNEPFVVVLPDVilddatadLRTENLAAMLSRYNEVGGY 162
Cdd:cd06426 67 ---------KFGVNISYVR--EDKPLGTAgalsLLPEKP---TDPFLVMNGDI--------LTNLNYEHLLDFHKENNAD 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 163 SQIMVEP----VPmeqvssYGVVDCGGVDlapgesktMTAIVEKPaVEDAPSNlavVGRYVLSEKiwdLLKLTPPGAgdE 238
Cdd:cd06426 125 ATVCVREyevqVP------YGVVETEGGR--------ITSIEEKP-THSFLVN---AGIYVLEPE---VLDLIPKNE--F 181
|
250 260 270
....*....|....*....|....*....|....*....
gi 1543020203 239 IQLTDAIAMLMEK-ETVEAFHMTGKSHDCGSKLGYMKAN 276
Cdd:cd06426 182 FDMPDLIEKLIKEgKKVGVFPIHEYWLDIGRPEDYEKAN 220
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
8-275 |
2.92e-15 |
|
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: 73.36 E-value: 2.92e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLEKRVKRQL 87
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 88 LdeiqaicpkevtilhvrqgeakGLGHAVLKARPIIGNEPFVVVLPDVILDdatadlrtENLAAMLSRYNEVGGYSQIMV 167
Cdd:cd06915 81 L----------------------GTGGAIKNALPKLPEDQFLVLNGDTYFD--------VDLLALLAALRASGADATMAL 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 168 epVPMEQVSSYGVVDCGGvdlapgeSKTMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLTPPgaGDEiqlTDAIAM 247
Cdd:cd06915 131 --RRVPDASRYGNVTVDG-------DGRVIAFVEKG--PGAAPGLINGGVYLLRKEILAEIPADAF--SLE---ADVLPA 194
|
250 260
....*....|....*....|....*...
gi 1543020203 248 LMEKETVEAFHMTGKSHDCGSKLGYMKA 275
Cdd:cd06915 195 LVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
7-239 |
6.22e-15 |
|
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: 72.63 E-value: 6.22e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVL-VTHSSKNAIEnhFDKSFelettlEKRVkr 85
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPEDMVP--FLKEY------EKKL-- 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 86 qlldEIQAICPKEVTILhvrqgeakGLGHAVLKARPIIG--NEPFVVVLPDVILDDAtadlrtenLAAMLSRYNEVGGYS 163
Cdd:cd06425 72 ----GIKITFSIETEPL--------GTAGPLALARDLLGddDEPFFVLNSDVICDFP--------LAELLDFHKKHGAEG 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1543020203 164 QIMVEPVpmEQVSSYGVVdcggvdLAPGESKTMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEI 239
Cdd:cd06425 132 TILVTKV--EDPSKYGVV------VHDENTGRIERFVEKP--KVFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI 197
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
7-140 |
1.65e-14 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 71.43 E-value: 1.65e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKsfelettlekrvkrq 86
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALAR--------------- 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1543020203 87 lldeiqaiCPKEVTILHVRQGEAKGLGHAVLKARPIIgNEPFVVVLPDVILDDA 140
Cdd:COG1213 66 --------PGPDVTFVYNPDYDETNNIYSLWLAREAL-DEDFLLLNGDVVFDPA 110
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
7-144 |
2.06e-14 |
|
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: 70.77 E-value: 2.06e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEI-VLVTHSSKNAIENHFDksfelETTLEKRVKR 85
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLR-----SFPLNLKQKL 76
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1543020203 86 QLLDEIQAicpkevtilhvrqgEAKGLGHAVLKARPIIgNEPFVVVLPDVILDDATADL 144
Cdd:cd04198 77 DEVTIVLD--------------EDMGTADSLRHIRKKI-KKDFLVLSCDLITDLPLIEL 120
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
7-182 |
2.07e-14 |
|
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: 70.75 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELEttLEKRVKRQ 86
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSS--LSSKMIVD 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 LLDEIQAicpkevtilhvrqgEAKGLGHAVLKARPIIgNEPFVVVLPDVILD-------DATADLRTENLAAMLSRYnev 159
Cdd:cd02507 80 VITSDLC--------------ESAGDALRLRDIRGLI-RSDFLLLSCDLVSNiplsellEERRKKDKNAIATLTVLL--- 141
|
170 180
....*....|....*....|...
gi 1543020203 160 gGYSQIMVEPVPMEQVSSYGVVD 182
Cdd:cd02507 142 -ASPPVSTEQSKKTEEEDVIAVD 163
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
8-77 |
1.16e-12 |
|
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: 66.10 E-value: 1.16e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELET 77
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF 70
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
8-259 |
2.52e-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: 63.89 E-value: 2.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMlpatK-AIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFdksfelettlekrvkrq 86
Cdd:COG1207 5 VVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL----------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 lldeiqaicpKEVTILHVRQGEAKGLGHAVLKARPIIGNEP-FVVVLP-DVILddatadLRTENLAAMLSRYNEVGgySQ 164
Cdd:COG1207 64 ----------ADLDVEFVLQEEQLGTGHAVQQALPALPGDDgTVLVLYgDVPL------IRAETLKALLAAHRAAG--AA 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 165 IMVEPVPMEQVSSYGVVDCggvdlapGESKTMTAIVE-KpaveDA-PSNLAV----VGRYVL-SEKIWDLL-KLTPPGAG 236
Cdd:COG1207 126 ATVLTAELDDPTGYGRIVR-------DEDGRVLRIVEeK----DAtEEQRAIreinTGIYAFdAAALREALpKLSNDNAQ 194
|
250 260
....*....|....*....|....
gi 1543020203 237 DEIQLTDAIAML-MEKETVEAFHM 259
Cdd:COG1207 195 GEYYLTDVIAIArADGLKVAAVQP 218
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
8-259 |
3.52e-11 |
|
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: 61.76 E-value: 3.52e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMlpatK-AIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIEnhfdksfelettlekrvkrq 86
Cdd:cd02540 1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVK-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 lldeiQAICPKEVTIlhVRQGEAKGLGHAVLKARPIIG--NEPFVVVLPDVILddatadLRTENLAAMLSRYNEVGgySQ 164
Cdd:cd02540 57 -----KALANPNVEF--VLQEEQLGTGHAVKQALPALKdfEGDVLVLYGDVPL------ITPETLQRLLEAHREAG--AD 121
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 165 IMVEPVPMEQVSSYGVV---DCGGVdlapgesktmTAIVEKpavEDA-PSNLAVV----GRYVL-SEKIWDLL-KLTPPG 234
Cdd:cd02540 122 VTVLTAELEDPTGYGRIirdGNGKV----------LRIVEE---KDAtEEEKAIRevnaGIYAFdAEFLFEALpKLTNNN 188
|
250 260
....*....|....*....|....*.
gi 1543020203 235 AGDEIQLTDAIAMLM-EKETVEAFHM 259
Cdd:cd02540 189 AQGEYYLTDIIALAVaDGLKVAAVLA 214
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
4-251 |
1.46e-10 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 60.84 E-value: 1.46e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 4 KINKAVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAienhfdksfelettlekRV 83
Cdd:PRK15480 2 KTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTP-----------------RF 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 84 KRQLLDEIQAicpkEVTILHVRQGEAKGLGHAVLKARPIIGNEPFVVVLPDVILddATADLRTENLAAmlsryneVGGYS 163
Cdd:PRK15480 65 QQLLGDGSQW----GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIF--YGHDLPKLMEAA-------VNKES 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 164 QIMVEPVPMEQVSSYGVVDCggvdlapGESKTMTAIVEKPAveDAPSNLAVVGRYVLSEKIWDLLKLTPPGAGDEIQLTD 243
Cdd:PRK15480 132 GATVFAYHVNDPERYGVVEF-------DQNGTAISLEEKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
|
....*...
gi 1543020203 244 AIAMLMEK 251
Cdd:PRK15480 203 INRIYMEQ 210
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
8-136 |
3.72e-08 |
|
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: 53.00 E-value: 3.72e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSfelettleKRVKRql 87
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS--------KWSKP-- 72
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1543020203 88 ldeiqAICPKEVTILHVRqgEAKGLGHAV--LKARPIIGNePFVVVLPDVI 136
Cdd:cd04197 73 -----KSSLMIVIIIMSE--DCRSLGDALrdLDAKGLIRG-DFILVSGDVV 115
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
8-231 |
2.56e-07 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. 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 that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH 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 including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 50.72 E-value: 2.56e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAG--LGTRMLPATKAIPKEMLPIVDKPLIQYIVNECIS-AGITEIVLVTHSSknaiENHFdKSFELETTLEKRVK 84
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYP----ESVF-SDFISDAQQEFNVP 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 85 RQLLDEIQAIcpkevtilhvrqGEAKGLGH---AVLKARPiignEPFVVVLPDVILDDAtadlrtenLAAMLSRYNEVGG 161
Cdd:cd06428 76 IRYLQEYKPL------------GTAGGLYHfrdQILAGNP----SAFFVLNADVCCDFP--------LQELLEFHKKHGA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 162 YSQIMVEPVPMEQVSSYGVVdcggvdLAPGESKTMTAIVEKPavEDAPSNLAVVGRYVLSEKIWDLLKLT 231
Cdd:cd06428 132 SGTILGTEASREQASNYGCI------VEDPSTGEVLHYVEKP--ETFVSDLINCGVYLFSPEIFDTIKKA 193
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
8-179 |
3.95e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 50.90 E-value: 3.95e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELETTLekrvkrql 87
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 88 ldeiqaicpkevtilhvrQGEAKGLGHAVLKARPIIgnEPFVVVLpdVILDDATADLRTENLAAMLSRYNEVGgySQIMV 167
Cdd:PRK14355 75 ------------------QEEQLGTGHAVACAAPAL--DGFSGTV--LILCGDVPLLRAETLQGMLAAHRATG--AAVTV 130
|
170
....*....|..
gi 1543020203 168 EPVPMEQVSSYG 179
Cdd:PRK14355 131 LTARLENPFGYG 142
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-254 |
2.58e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 48.61 E-value: 2.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 7 KAVIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSknaienhfdksfelettlekrvkrq 86
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGHEA------------------------- 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 87 llDEIQAICPKEVTILHvrQGEAKGLGHAVLKARPIIG-NEPFVVVLPDVILddatadLRTENLAAMLSRYNEVGGYSQI 165
Cdd:PRK14357 54 --ELVKKLLPEWVKIFL--QEEQLGTAHAVMCARDFIEpGDDLLILYGDVPL------ISENTLKRLIEEHNRKGADVTI 123
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 166 MVepVPMEQVSSYG--VVDCGGVDlapgesktmtaIVEKpavEDAPSNLAVV-----GRYVLSEK--IWDLLKLTPPGAG 236
Cdd:PRK14357 124 LV--ADLEDPTGYGriIRDGGKYR-----------IVED---KDAPEEEKKIkeintGIYVFSGDflLEVLPKIKNENAK 187
|
250
....*....|....*...
gi 1543020203 237 DEIQLTDAIAMLMEKETV 254
Cdd:PRK14357 188 GEYYLTDAVNFAEKVRVV 205
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-153 |
3.90e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 47.93 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 1 MPNKINKAVIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHfdksfelettle 80
Cdd:PRK14353 1 MTDRTCLAIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAA------------ 65
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1543020203 81 krVKRQLldeiqaicpKEVTIlhVRQGEAKGLGHAVLKARPII--GNEPFVVVLPDVILddatadLRTENLAAML 153
Cdd:PRK14353 66 --AAKIA---------PDAEI--FVQKERLGTAHAVLAAREALagGYGDVLVLYGDTPL------ITAETLARLR 121
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-158 |
4.58e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 47.52 E-value: 4.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 6 NKAVIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVT-HSSknaienhfdksfelettleKRVK 84
Cdd:PRK14354 3 RYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGA-------------------EEVK 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1543020203 85 RQLLDEIQaicpkevtilHVRQGEAKGLGHAVLKARPIIGNEPFVVVlpdVILDDaTADLRTENLAAMLSRYNE 158
Cdd:PRK14354 61 EVLGDRSE----------FALQEEQLGTGHAVMQAEEFLADKEGTTL---VICGD-TPLITAETLKNLIDFHEE 120
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
8-59 |
4.08e-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: 43.67 E-value: 4.08e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1543020203 8 AVIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVNECISAG-ITEIVLVTH 59
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
8-70 |
1.13e-04 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 42.07 E-value: 1.13e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1543020203 8 AVIPVAGLGTRMlpatkAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFD 70
Cdd:COG2068 6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
|
|
| ispD |
TIGR00453 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ... |
8-59 |
1.73e-04 |
|
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: 41.89 E-value: 1.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1543020203 8 AVIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVnECISA--GITEIVLVTH 59
Cdd:TIGR00453 2 AVIPAAGRGTRF---GSGVPKQYLELGGRPLLEHAL-DAFLAhpAIDEVVVVVS 51
|
|
| G1P_cytidylyltransferase |
cd02524 |
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ... |
8-229 |
3.34e-04 |
|
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.
Pssm-ID: 133015 [Multi-domain] Cd Length: 253 Bit Score: 41.40 E-value: 3.34e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 8 AVIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVTHSSKNAIENHFDKSFELE---TTLEKRVK 84
Cdd:cd02524 1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNsdvTIDLGTNR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 85 RQLLDeiQAICPKEVTIlhVRQGEAKGLGHAVLKARPIIGN-EPFVVVLPDVIlddatADLrteNLAAMLSRYNEVGGYS 163
Cdd:cd02524 81 IELHN--SDIEDWKVTL--VDTGLNTMTGGRLKRVRRYLGDdETFMLTYGDGV-----SDV---NINALIEFHRSHGKLA 148
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1543020203 164 QIMVEPVPmeqvSSYGVVDCGGVDLApgesktmTAIVEKPAVEDAPSNlavVGRYVLSEKIWDLLK 229
Cdd:cd02524 149 TVTAVHPP----GRFGELDLDDDGQV-------TSFTEKPQGDGGWIN---GGFFVLEPEVFDYID 200
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
8-58 |
4.15e-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: 40.62 E-value: 4.15e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1543020203 8 AVIPVAGLGTRMLPatkaiPKEMLPIVDKPLIQYIVNECISAGITEIVLVT 58
Cdd:cd04182 3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVL 48
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
9-59 |
5.71e-04 |
|
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: 40.50 E-value: 5.71e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1543020203 9 VIPVAGLGTRMlpaTKAIPKEMLPIVDKPLIQYIVNECISAG-ITEIVLVTH 59
Cdd:COG1211 1 IIPAAGSGSRM---GAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-258 |
6.75e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 40.78 E-value: 6.75e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 1 MPNKINKAVIPVAGLGTRMLpatKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVthssknaienhFDKSFELettLE 80
Cdd:PRK09451 1 MLNSAMSVVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLV-----------YGHGGDL---LK 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 81 KRVKRQLLDeiqaicpkevtilHVRQGEAKGLGHAVLKARPIIGNEPFVVVL-PDVILddatadLRTENLAAMLSRYNEV 159
Cdd:PRK09451 64 QTLADEPLN-------------WVLQAEQLGTGHAMQQAAPFFADDEDILMLyGDVPL------ISVETLQRLRDAKPQG 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 160 GgysqIMVEPVPMEQVSSYGVVdcggvdlaPGESKTMTAIVEKPAVEDAPSNLAVVGRYVL-----SEKIWdLLKLTPPG 234
Cdd:PRK09451 125 G----IGLLTVKLDNPTGYGRI--------TRENGKVVGIVEQKDATDEQRQIQEINTGILvangaDLKRW-LAKLTNNN 191
|
250 260
....*....|....*....|....*
gi 1543020203 235 AGDEIQLTDAIAML-MEKETVEAFH 258
Cdd:PRK09451 192 AQGEYYITDIIALAhQEGREIVAVH 216
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
9-126 |
1.20e-03 |
|
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: 39.54 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1543020203 9 VIPVAGLGTRMLPATKAIPKEMLPIVDKPLIQYIVNECISAGITEIVLVThsSKNAIENHFDKSfelettlekrvkrqll 88
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLDE---------------- 63
|
90 100 110
....*....|....*....|....*....|....*...
gi 1543020203 89 dEIQAICPKeVTILhVRQGEAKGLGHAVLKARPIIGNE 126
Cdd:cd04183 64 -SLKLLAPN-ATVV-ELDGETLGAACTVLLAADLIDND 98
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
8-59 |
1.51e-03 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 39.35 E-value: 1.51e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1543020203 8 AVIPVAGLGTRMlpatKA-IPKEMLPIVDKPLIQYIVNECISAG-ITEIVLVTH 59
Cdd:PRK00155 6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP 55
|
|
| ispDF |
PRK09382 |
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ... |
8-60 |
3.41e-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: 3.41e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1543020203 8 AVIPVAGLGTRmlpATKAIPKEMLPIVDKPLIQYIVNECISAG-ITEIVLVTHS 60
Cdd:PRK09382 8 LVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLENLSSAPaFKEIVVVIHP 58
|
|
| |
