|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-297 |
0e+00 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 629.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
Cdd:PRK10122 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATADPLRYNLAAMVARFNETGRS 160
Cdd:PRK10122 81 VKRQLLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 161 QVLAKRMKGDLSEYSVIQTKEPLDNEGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
Cdd:PRK10122 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344236 241 AIAELAKKQSVDAILMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEQLLHE 297
Cdd:PRK10122 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
|
|
| galF |
TIGR01105 |
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ... |
1-297 |
0e+00 |
|
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: 597.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
Cdd:TIGR01105 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATADPLRYNLAAMVARFNETGRS 160
Cdd:TIGR01105 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATADPLRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 161 QVLAKRMKGDLSEYSVIQTKEPLDNEGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
Cdd:TIGR01105 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344236 241 AIAELAKKQSVDAILMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEQLLHE 297
Cdd:TIGR01105 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEKLLSE 297
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-297 |
3.70e-148 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 416.74 E-value: 3.70e-148
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 VKRQLLAEVQSICPPgVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATadplrYNLAAMVARFNETGRS 160
Cdd:COG1210 81 GKEELLEEVRSISPL-ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEK-----PCLKQMIEVYEETGGS 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 161 QVLAKRM-KGDLSEYSVIQTKEpldNEGKVSRIVEFIEKPDqPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLT 239
Cdd:COG1210 155 VIAVQEVpPEEVSKYGIVDGEE---IEGGVYRVTGLVEKPA-PEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLT 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*...
gi 1137344236 240 DAIAELAKKQSVDAILMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEQLLHE 297
Cdd:COG1210 231 DAIAALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
5-295 |
2.77e-128 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 367.31 E-value: 2.77e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 LLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATADPLRYNLAAMVARFNETGRSQVLA 164
Cdd:PRK13389 90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 165 KRMKgDLSEYSVIQTKEPLDNEGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIAE 244
Cdd:PRK13389 170 EPVA-DVTAYGVVDCKGVELAPGESVPMVGVVEKP-KADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1137344236 245 LAKKQSVDAILMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEQLL 295
Cdd:PRK13389 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEM 298
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-279 |
2.69e-121 |
|
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: 347.98 E-value: 2.69e-121
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:cd02541 2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 LLaEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATAdplryNLAAMVARFNETGRSQVLA 164
Cdd:cd02541 82 LL-EEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEP-----CLKQLIEAYEKTGASVIAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 165 KRM-KGDLSEYSVIQTKEpldNEGKVSRIVEFIEKPDqPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIA 243
Cdd:cd02541 156 EEVpPEDVSKYGIVKGEK---IDGDVFKVKGLVEKPK-PEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 1137344236 244 ELAKKQSVDAILMTGDSYDCGKKMGYMQAFVKYGLR 279
Cdd:cd02541 232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-272 |
4.83e-119 |
|
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: 342.03 E-value: 4.83e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:TIGR01099 2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 LLAEVQSICPPgVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATAdplryNLAAMVARFNETGRSQVLA 164
Cdd:TIGR01099 82 LLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP-----ALKQMIKAYEKTGCSIIAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 165 KRM-KGDLSEYSVIQTKEpldNEGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIA 243
Cdd:TIGR01099 156 QEVpKEEVSKYGVIDGEG---IEKDLYKVKNMVEKP-KPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
|
250 260
....*....|....*....|....*....
gi 1137344236 244 ELAKKQSVDAILMTGDSYDCGKKMGYMQA 272
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-264 |
6.82e-51 |
|
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: 166.99 E-value: 6.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkrql 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 86 laevqsicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDatadplryNLAAMVARFNETGR-SQVLA 164
Cdd:cd04181 69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL--------DLSELLRFHREKGAdATIAV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 165 KRMKgDLSEYSVIQTkeplDNEGkvsRIVEFIEKPDQPqtlDSDLMAVGRYVLSADIWAELERTEPGawGRIQLTDAIAE 244
Cdd:cd04181 131 KEVE-DPSRYGVVEL----DDDG---RVTRFVEKPTLP---ESNLANAGIYIFEPEILDYIPEILPR--GEDELTDAIPL 197
|
250 260
....*....|....*....|
gi 1137344236 245 LAKKQSVDAILMTGDSYDCG 264
Cdd:cd04181 198 LIEEGKVYGYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-272 |
1.18e-43 |
|
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: 148.87 E-value: 1.18e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkrq 84
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 llaevqsicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDAtadplrynLAAMVARFNETGRS-QVL 163
Cdd:cd04189 71 -----------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG--------ISPLVRDFLEEDADaSIL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 164 AKRMKgDLSEYSVIQTKEpldnegkvSRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIA 243
Cdd:cd04189 132 LAEVE-DPRRFGVAVVDD--------GRIVRLVEKPKEPP---SNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQ 199
|
250 260 270
....*....|....*....|....*....|
gi 1137344236 244 EL-AKKQSVDAILMTGDSYDCGKKMGYMQA 272
Cdd:cd04189 200 WLiDRGRRVGYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-272 |
5.30e-43 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 149.08 E-value: 5.30e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELEslleqRVKRq 84
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDGP-----QFER- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 LLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDatadplrYNLAAMVARFNE-TGRSQVL 163
Cdd:COG1209 64 LLGDGSQL---GIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG-------DGLSELLREAAArESGATIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 164 AKRMKgDLSEYSVIQtkepLDNEGKVSRIVefiEKPDQPQtldSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTDAIA 243
Cdd:COG1209 134 GYKVE-DPERYGVVE----FDEDGRVVSLE---EKPKEPK---SNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQ 202
|
250 260 270
....*....|....*....|....*....|.
gi 1137344236 244 E-LAKKQSVDAILMTGDS-YDCGKKMGYMQA 272
Cdd:COG1209 203 AyLERGKLVVELLGRGFAwLDTGTHESLLEA 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-272 |
1.52e-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: 141.06 E-value: 1.52e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkrq 84
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 llaevqsicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDdatadplrYNLAAMVARFNETGRS-QVL 163
Cdd:COG1208 70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD--------LDLAALLAFHREKGADaTLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 164 AKRMKgDLSEYSVIQtkepLDNEGkvsRIVEFIEKPDQPqtlDSDLMAVGRYVLSADIWAELERTEPgawgrIQLTDAIA 243
Cdd:COG1208 131 LVPVP-DPSRYGVVE----LDGDG---RVTRFVEKPEEP---PSNLINAGIYVLEPEIFDYIPEGEP-----FDLEDLLP 194
|
250 260
....*....|....*....|....*....
gi 1137344236 244 ELAKKQSVDAILMTGDSYDCGKKMGYMQA 272
Cdd:COG1208 195 RLIAEGRVYGYVHDGYWLDIGTPEDLLEA 223
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-240 |
7.28e-18 |
|
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: 80.70 E-value: 7.28e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLleqrvkRQ 84
Cdd:cd02538 2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDLPLF------KE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 LLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDatadplrYNLAAMVARFNE-TGRSQVL 163
Cdd:cd02538 64 LLGDGSDL---GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYG-------QGLSPILQRAAAqKEGATVF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344236 164 AKRMKgDLSEYSVIQtkepLDNEGKVSRIvefIEKPDQPQtldSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
Cdd:cd02538 134 GYEVN-DPERYGVVE----FDENGRVLSI---EEKPKKPK---SNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-249 |
4.04e-17 |
|
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: 78.32 E-value: 4.04e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkrql 85
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 86 laevqsicppGVTIMNVRQAQPLGLGHSI--LCARPvvgDNPFIVVLPDIIIddatadplRYNLAAMVARFNETGRSQVL 163
Cdd:cd06426 69 ----------GVNISYVREDKPLGTAGALslLPEKP---TDPFLVMNGDILT--------NLNYEHLLDFHKENNADATV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 164 AKRMKGDLSEYSVIQTKEpldnegkvSRIVEFIEKPDQPQTLDSdlmavGRYVLSADIwaeLERTEPGAwgRIQLTDAIA 243
Cdd:cd06426 128 CVREYEVQVPYGVVETEG--------GRITSIEEKPTHSFLVNA-----GIYVLEPEV---LDLIPKNE--FFDMPDLIE 189
|
....*.
gi 1137344236 244 ELAKKQ 249
Cdd:cd06426 190 KLIKEG 195
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-272 |
1.14e-16 |
|
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: 77.21 E-value: 1.14e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYEleslleqrvkrql 85
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 86 laevqsicpPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDdatadplrYNLAAMVARFNETGRSQVLA- 164
Cdd:cd06915 68 ---------GGIRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFD--------VDLLALLAALRASGADATMAl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 165 KRMKgDLSEYSVIQtkepLDNEGkvsRIVEFIEKP--DQPQTLDSdlmavGRYVLSADIWAELERTEPGAwgriqLTDAI 242
Cdd:cd06915 131 RRVP-DASRYGNVT----VDGDG---RVIAFVEKGpgAAPGLING-----GVYLLRKEILAEIPADAFSL-----EADVL 192
|
250 260 270
....*....|....*....|....*....|
gi 1137344236 243 AELAKKQSVDAILMTGDSYDCGKKMGYMQA 272
Cdd:cd06915 193 PALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-276 |
7.68e-16 |
|
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: 75.37 E-value: 7.68e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDK-PMIQYIVDEIVAAGIKEIVLVThasknavenhfdTSYELESLLEQrvkr 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL------------TQEHRFMLNEL---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 84 qlLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPF-IVVLP-DIIIDDAtadplrynLAAMVARFNETGRSQ 161
Cdd:pfam00483 65 --LGDGSKF---GVQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGgDHIYRMD--------LEQAVKFHIEKAADA 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 162 -VLAKRMKGDL-SEYSVIQTkeplDNEGKVSRiveFIEKPDQPqtLDSDLMAVGRYVLSADIWAEL-ERTEPGAWGRIQL 238
Cdd:pfam00483 132 tVTFGIVPVEPpTGYGVVEF----DDNGRVIR---FVEKPKLP--KASNYASMGIYIFNSGVLDFLaKYLEELKRGEDEI 202
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1137344236 239 TDAIAELAKKQSVDAILMTGDS--YDCGKKMGYMQAFVKY 276
Cdd:pfam00483 203 TDILPKALEDGKLAYAFIFKGYawLDVGTWDSLWEANLFL 242
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-150 |
1.76e-15 |
|
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: 73.76 E-value: 1.76e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYEleslleqrvkrq 84
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF------------ 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1137344236 85 llaevqsicPPGVTIMNVRqAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATADPLRYNLAAM 150
Cdd:cd06422 69 ---------GLRITISDEP-DELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRM 124
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
4-230 |
2.61e-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: 73.40 E-value: 2.61e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVL-VTHASKNavenhfdtsyeLESLLEQRVK 82
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPED-----------MVPFLKEYEK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 83 RqllaevqsicpPGVTIMNVRQAQPLGLGHSILCARPVVG--DNPFIVVLPDIIIDdatadplrYNLAAMVARFNETGR- 159
Cdd:cd06425 70 K-----------LGIKITFSIETEPLGTAGPLALARDLLGddDEPFFVLNSDVICD--------FPLAELLDFHKKHGAe 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137344236 160 SQVLAKRMKgDLSEYSVIQTKEpldNEGKVSRiveFIEKPDQPQtldSDLMAVGRYVLSADIwaeLERTEP 230
Cdd:cd06425 131 GTILVTKVE-DPSKYGVVVHDE---NTGRIER---FVEKPKVFV---GNKINAGIYILNPSV---LDRIPL 188
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-258 |
2.17e-13 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 68.34 E-value: 2.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthasknavenhfdTSYELEsLLEQRVKRq 84
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV-------------TGYKAE-LIEEALAR- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 llaevqsiCPPGVT-IMNVRQAQpLGLGHSILCARPVVGDnPFIVVLPDIIIDDatadplrynlaAMVARFNETGRSQVL 163
Cdd:COG1213 66 --------PGPDVTfVYNPDYDE-TNNIYSLWLAREALDE-DFLLLNGDVVFDP-----------AILKRLLASDGDIVL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 164 A---KRMKGDLSEYSVIqtkepLDNEGkvsRIVEFIEKPDQPqtlDSDLMAVGRYVLSADIWAELER--TEPGAWGRIQL 238
Cdd:COG1213 125 LvdrKWEKPLDEEVKVR-----VDEDG---RIVEIGKKLPPE---EADGEYIGIFKFSAEGAAALREalEALIDEGGPNL 193
|
250 260
....*....|....*....|...
gi 1137344236 239 --TDAIAELAKK-QSVDAILMTG 258
Cdd:COG1213 194 yyEDALQELIDEgGPVKAVDIGG 216
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-272 |
2.41e-12 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 65.85 E-value: 2.41e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASknavenhfDTSYeleslleqr 80
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DTPR--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 vKRQLLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDDATADPLrynlaaMVARFNETGRS 160
Cdd:PRK15480 64 -FQQLLGDGSQW---GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKL------MEAAVNKESGA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 161 QVLAKRMKgDLSEYSVIQtkepLDNEGKVsriVEFIEKPDQPQtldSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
Cdd:PRK15480 134 TVFAYHVN-DPERYGVVE----FDQNGTA---ISLEEKPLQPK---SNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
|
250 260 270
....*....|....*....|....*....|....*
gi 1137344236 241 aIAELAKKQSVDAILMTGDSY---DCGKKMGYMQA 272
Cdd:PRK15480 203 -INRIYMEQGRLSVAMMGRGYawlDTGTHQSLIEA 236
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-249 |
7.28e-12 |
|
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: 63.69 E-value: 7.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAGLGMHMlpatK-AIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVEnhfdtsyeleslleqrvkrq 84
Cdd:cd02540 1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVK-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 85 llaevQSICPPGVTImnVRQAQPLGLGHSILCARPVV-----------GDNPFivvlpdiiIDDATadplrynLAAMVAR 153
Cdd:cd02540 57 -----KALANPNVEF--VLQEEQLGTGHAVKQALPALkdfegdvlvlyGDVPL--------ITPET-------LQRLLEA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 154 FNETGRSQVLAKRMKGDLSEYS-VIqtkepLDNEGKVSRIVEfiEKPDQPQTLDSDLMAVGRYVLSA-DIWAELERTEP- 230
Cdd:cd02540 115 HREAGADVTVLTAELEDPTGYGrII-----RDGNGKVLRIVE--EKDATEEEKAIREVNAGIYAFDAeFLFEALPKLTNn 187
|
250
....*....|....*....
gi 1137344236 231 GAWGRIQLTDAIaELAKKQ 249
Cdd:cd02540 188 NAQGEYYLTDII-ALAVAD 205
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-253 |
5.36e-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: 61.09 E-value: 5.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELEslleqrvkrql 85
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 86 laevqsicppgvTIMNVRQAQPlGLGHSILCARPVVGDNpFIVVLPDIIIDDATADPL----RYNLAAMVARFNEtgrsq 161
Cdd:cd02523 70 ------------FVYNPDYAET-NNIYSLYLARDFLDED-FLLLEGDVVFDPSILERLlsspADNAILVDKKTKE----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 162 vlakrmkgdlseySVIQTKEPLDNEGKVSRIVEFIEKPDQPQtldsdLMAVGRYVLSADIWAEL--------ERTEPGAW 233
Cdd:cd02523 131 -------------WEDEYVKDLDDAGVLLGIISKAKNLEEIQ-----GEYVGISKFSPEDADRLaealeeliEAGRVNLY 192
|
250 260
....*....|....*....|
gi 1137344236 234 griqLTDAIAELAKKQSVDA 253
Cdd:cd02523 193 ----YEDALQRLISEEGVKV 208
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-72 |
1.75e-10 |
|
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: 59.59 E-value: 1.75e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEI-VLVTHASKNAVENHFDTSYE 72
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLRSFPL 70
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-254 |
2.30e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 60.65 E-value: 2.30e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVEnhfdtsyeleslleqr 80
Cdd:PRK14353 3 DRTCLAIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA---------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 vkrqllAEVQSICPPGVTimnVRQAQPLGLGHSILCARP-----------VVGDNPFIvvlpdiiiddaTADPLRynlaA 149
Cdd:PRK14353 64 ------AAAAKIAPDAEI---FVQKERLGTAHAVLAAREalaggygdvlvLYGDTPLI-----------TAETLA----R 119
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 150 MVARFNETGRSQVLAKRMKgDLSEYSVIQTKepldnEGKVSRIVEFIEKPDQPQTLD---SDLMAVGRyvlsADIWAELE 226
Cdd:PRK14353 120 LRERLADGADVVVLGFRAA-DPTGYGRLIVK-----GGRLVAIVEEKDASDEERAITlcnSGVMAADG----ADALALLD 189
|
250 260
....*....|....*....|....*....
gi 1137344236 227 R-TEPGAWGRIQLTDaIAELAKKQSVDAI 254
Cdd:PRK14353 190 RvGNDNAKGEYYLTD-IVAIARAEGLRVA 217
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
2-194 |
2.58e-10 |
|
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: 60.81 E-value: 2.58e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 2 MNLKAVIPVAGLGMHMlpatK-AIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTsyeleslleqr 80
Cdd:COG1207 1 SPLAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 vkrqllaevqsicpPGVTImnVRQAQPLGLGHSILCARPVV-GDNPFIVVLP-DI-IIDDATadplrynLAAMVARFNET 157
Cdd:COG1207 66 --------------LDVEF--VLQEEQLGTGHAVQQALPALpGDDGTVLVLYgDVpLIRAET-------LKALLAAHRAA 122
|
170 180 190
....*....|....*....|....*....|....*...
gi 1137344236 158 GRS-QVLAKRMKgDLSEYSVIQTkeplDNEGKVSRIVE 194
Cdd:COG1207 123 GAAaTVLTAELD-DPTGYGRIVR----DEDGRVLRIVE 155
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
4-81 |
7.22e-10 |
|
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: 57.65 E-value: 7.22e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1137344236 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRV 81
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIV 78
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-220 |
2.11e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 57.83 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLeqr 80
Cdd:PRK14355 1 MNNLAAIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 81 vkrqllaevqsicppgvtimnvrQAQPLGLGHSILCARP-----------VVGDNPfivvlpdiIIDDATadplrynLAA 149
Cdd:PRK14355 75 -----------------------QEEQLGTGHAVACAAPaldgfsgtvliLCGDVP--------LLRAET-------LQG 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1137344236 150 MVARFNETGRS-QVLAKRMKGDLSEYSVIQtkeplDNEGKVSRIVEfiEKPDQPQTLDSDLMAVGRYVLSAD 220
Cdd:PRK14355 117 MLAAHRATGAAvTVLTARLENPFGYGRIVR-----DADGRVLRIVE--EKDATPEERSIREVNSGIYCVEAA 181
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-127 |
6.91e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 56.38 E-value: 6.91e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 2 MNLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthASKNAvenhfdtsyeleslleQRV 81
Cdd:PRK14354 1 MNRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV--VGHGA----------------EEV 59
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344236 82 KRQLLAEVQSicppgvtimnVRQAQPLGLGHSILCARP-----------VVGDNPFI 127
Cdd:PRK14354 60 KEVLGDRSEF----------ALQEEQLGTGHAVMQAEEfladkegttlvICGDTPLI 106
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-240 |
1.20e-07 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 52.67 E-value: 1.20e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 4 LKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT-HASKnavenhfdtsyELESLLEQrvk 82
Cdd:PRK14358 8 LDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTgHGAE-----------QVEAALQG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 83 rqllaevqsicpPGVTImnVRQAQPLGLGHSILCARPVVGDNPfivvlPDIIIDDATADPLR-YNLAAMVARFNETGRSQ 161
Cdd:PRK14358 71 ------------SGVAF--ARQEQQLGTGDAFLSGASALTEGD-----ADILVLYGDTPLLRpDTLRALVADHRAQGSAM 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 162 VLAKRMKGDLSEYSVIQTkeplDNEGKVSRIVEfiEKPDQPQTLDSDLMAVGRYVLSADIwAELER--TEPGAWGRIQLT 239
Cdd:PRK14358 132 TILTGELPDATGYGRIVR----GADGAVERIVE--QKDATDAEKAIGEFNSGVYVFDARA-PELARriGNDNKAGEYYLT 204
|
.
gi 1137344236 240 D 240
Cdd:PRK14358 205 D 205
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-127 |
2.99e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 48.22 E-value: 2.99e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 4 LKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHasknavenhfdtSYELeslleqrvkr 83
Cdd:PRK14357 1 MRALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGH------------EAEL---------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1137344236 84 qllaeVQSICPPGVTImnVRQAQPLGLGHSILCARPVV----------GDNPFI 127
Cdd:PRK14357 56 -----VKKLLPEWVKI--FLQEEQLGTAHAVMCARDFIepgddllilyGDVPLI 102
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-70 |
2.38e-05 |
|
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: 44.52 E-value: 2.38e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1137344236 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTS 70
Cdd:cd04197 1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS 67
|
|
| glmU |
PRK09451 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-130 |
4.85e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 181867 [Multi-domain] Cd Length: 456 Bit Score: 44.63 E-value: 4.85e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMLpatKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLV-THASknavenhfdtsyeleSLLEQ 79
Cdd:PRK09451 3 NSAMSVVILAAGKGTRMY---SDLPKVLHTLAGKPMVQHVIDAANELGAQHVHLVyGHGG---------------DLLKQ 64
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1137344236 80 RVKRQLLaevqsicppgvtimN-VRQAQPLGLGHSILCARPVVGDNPFIVVL 130
Cdd:PRK09451 65 TLADEPL--------------NwVLQAEQLGTGHAMQQAAPFFADDEDILML 102
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
6-228 |
3.92e-04 |
|
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: 41.09 E-value: 3.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAG--LGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVA-AGIKEIVLVThasknavenhFDTSYELESLLEqRVK 82
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIG----------FYPESVFSDFIS-DAQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 83 RQllaevqsicpPGVTIMNVRQAQPLGLGHSILCARPVV-GDNP--FIVVLPDIIIDdatadplrYNLAAMVARFNETGR 159
Cdd:cd06428 70 QE----------FNVPIRYLQEYKPLGTAGGLYHFRDQIlAGNPsaFFVLNADVCCD--------FPLQELLEFHKKHGA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1137344236 160 SQVL--AKRMKGDLSEYSVIQTKEpldnegKVSRIVEFIEKpdqPQTLDSDLMAVGRYVLSADIWAELERT 228
Cdd:cd06428 132 SGTIlgTEASREQASNYGCIVEDP------STGEVLHYVEK---PETFVSDLINCGVYLFSPEIFDTIKKA 193
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
1-129 |
9.08e-04 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 39.73 E-value: 9.08e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 1 MMNLKAVIPVAGLGMHMlpatKA-IPKEMLPIVDKPMIQYIVDEIVAAG-IKEIVLVTHASknavenhfDTSYELESLLE 78
Cdd:PRK00155 1 MMMVYAIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPD--------DRPDFAELLLA 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 1137344236 79 QRVKRQllaevqsICPPGVTimnvRQaqplglgHSILCARPVVGDNPFIVV 129
Cdd:PRK00155 69 KDPKVT-------VVAGGAE----RQ-------DSVLNGLQALPDDDWVLV 101
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
26-62 |
1.12e-03 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 39.10 E-value: 1.12e-03
10 20 30
....*....|....*....|....*....|....*..
gi 1137344236 26 KEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThaSKNA 62
Cdd:COG2266 14 KPLLEICGKPMIDRVIDALEESCIDKIYVAV--SPNT 48
|
|
| MPP_Mre11_N |
cd00840 |
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ... |
240-283 |
1.75e-03 |
|
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277319 [Multi-domain] Cd Length: 186 Bit Score: 38.79 E-value: 1.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 1137344236 240 DAIAELAKKQSVDAILMTGDSYDCGKKMGYMQAFVKYGLRNLKE 283
Cdd:cd00840 29 EEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-164 |
5.24e-03 |
|
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: 37.15 E-value: 5.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 6 AVIPVAGLG--MHMlpatkaiPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVenhfdtsyeleslleqrvkR 83
Cdd:cd04182 3 AIILAAGRSsrMGG-------NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAV-------------------R 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1137344236 84 QLLAevqsicPPGVTIMNVRQAQpLGLGHSILCA-RPVVGDNPFIVVLPdiiiddatAD-PL--RYNLAAMVARFNETGR 159
Cdd:cd04182 57 AALA------GLPVVVVINPDWE-EGMSSSLAAGlEALPADADAVLILL--------ADqPLvtAETLRALIDAFREDGA 121
|
....*
gi 1137344236 160 SQVLA 164
Cdd:cd04182 122 GIVAP 126
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
6-59 |
8.59e-03 |
|
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: 36.73 E-value: 8.59e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1137344236 6 AVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAG-IKEIVLVTHAS 59
Cdd:cd02516 3 AIILAAGSGSRM---GADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPD 54
|
|
| |
