|
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: 630.00 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 1 MINLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQR 80
Cdd:PRK10122 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTASADPLRYNLAAMVARFNETGRS 160
Cdd:PRK10122 81 VKRQLLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 161 QVLAKRMKGDLSEYSVIQTKEPLETEGQVSRIVEFIEKPDQPQTLDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTD 240
Cdd:PRK10122 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 658549632 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVNYGLRNLKEGAKFRTRIEKLLAN 297
Cdd:PRK10122 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
|
|
| galF |
TIGR01105 |
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ... |
1-296 |
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: 577.75 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 1 MINLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQR 80
Cdd:TIGR01105 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTASADPLRYNLAAMVARFNETGRS 160
Cdd:TIGR01105 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATADPLRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 161 QVLAKRMKGDLSEYSVIQTKEPLETEGQVSRIVEFIEKPDQPQTLDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTD 240
Cdd:TIGR01105 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 658549632 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVNYGLRNLKEGAKFRTRIEKLLA 296
Cdd:TIGR01105 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEKLLS 296
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
5-297 |
2.08e-147 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 415.20 E-value: 2.08e-147
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQRVKRQ 84
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKGKEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 LLAEVQSICPPgVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDtaSADPlryNLAAMVARFNETGRSQVLA 164
Cdd:COG1210 85 LLEEVRSISPL-ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLID--SEKP---CLKQMIEVYEETGGSVIAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 165 KRM-KGDLSEYSVIQTKeplETEGQVSRIVEFIEKPDqPQTLDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTDAIA 243
Cdd:COG1210 159 QEVpPEEVSKYGIVDGE---EIEGGVYRVTGLVEKPA-PEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658549632 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVNYGLRNLKEGAKFRTRIEKLLAN 297
Cdd:COG1210 235 ALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
5-298 |
1.74e-130 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 372.70 E-value: 1.74e-130
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQRVKRQ 84
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 LLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTASADPLRYNLAAMVARFNETGRSQVLA 164
Cdd:PRK13389 90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 165 KRMKgDLSEYSVIQTKEPLETEGQVSRIVEFIEKPdQPQTLDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTDAIAE 244
Cdd:PRK13389 170 EPVA-DVTAYGVVDCKGVELAPGESVPMVGVVEKP-KADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 658549632 245 LAKKQSVDAMLMTGDSYDCGKKMGYMQAFVNYGLRNLKEGAKFRTRIEKLLAND 298
Cdd:PRK13389 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGIK 301
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-279 |
4.86e-122 |
|
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: 349.91 E-value: 4.86e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQRVKRQ 84
Cdd:cd02541 2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 LLaEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDtaSADPlryNLAAMVARFNETGRSQVLA 164
Cdd:cd02541 82 LL-EEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID--SKEP---CLKQLIEAYEKTGASVIAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 165 KRM-KGDLSEYSVIQTKeplETEGQVSRIVEFIEKPDqPQTLDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTDAIA 243
Cdd:cd02541 156 EEVpPEDVSKYGIVKGE---KIDGDVFKVKGLVEKPK-PEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 658549632 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVNYGLR 279
Cdd:cd02541 232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-272 |
4.48e-120 |
|
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: 344.72 E-value: 4.48e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQRVKRQ 84
Cdd:TIGR01099 2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 LLAEVQSICPPgVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTASAdplryNLAAMVARFNETGRSQVLA 164
Cdd:TIGR01099 82 LLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP-----ALKQMIKAYEKTGCSIIAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 165 KRM-KGDLSEYSVIqtkEPLETEGQVSRIVEFIEKPdQPQTLDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTDAIA 243
Cdd:TIGR01099 156 QEVpKEEVSKYGVI---DGEGIEKDLYKVKNMVEKP-KPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
|
250 260
....*....|....*....|....*....
gi 658549632 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-264 |
2.68e-50 |
|
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: 165.45 E-value: 2.68e-50
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELealleqrvkrql 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 86 laevqsicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTasadplryNLAAMVARFNETGR-SQVLA 164
Cdd:cd04181 69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL--------DLSELLRFHREKGAdATIAV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 165 KRMKgDLSEYSVIQTKEpletegqVSRIVEFIEKPDQPqtlDSDLMAVGRYVLNADIWAELEKTEPGAWDriQLTDAIAE 244
Cdd:cd04181 131 KEVE-DPSRYGVVELDD-------DGRVTRFVEKPTLP---ESNLANAGIYIFEPEILDYIPEILPRGED--ELTDAIPL 197
|
250 260
....*....|....*....|
gi 658549632 245 LAKKQSVDAMLMTGDSYDCG 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 |
2.22e-41 |
|
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: 143.09 E-value: 2.22e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELealleqrvkrq 84
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 llaevqsicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIdtasadplRYNLAAMVARFNETGRS-QVL 163
Cdd:cd04189 71 -----------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLI--------QEGISPLVRDFLEEDADaSIL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 164 AKRMKgDLSEYSVIQTKEpletegqvSRIVEFIEKPDQPQtldSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTDAIA 243
Cdd:cd04189 132 LAEVE-DPRRFGVAVVDD--------GRIVRLVEKPKEPP---SNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQ 199
|
250 260 270
....*....|....*....|....*....|
gi 658549632 244 EL-AKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:cd04189 200 WLiDRGRRVGYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-272 |
4.38e-40 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 141.38 E-value: 4.38e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThssknavenhfdTSYELEALleqrvkRQ 84
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDGPQF------ER 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 LLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTasadplrYNLAAMVARFNE-TGRSQVL 163
Cdd:COG1209 64 LLGDGSQL---GIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG-------DGLSELLREAAArESGATIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 164 AKRMKgDLSEYSVIQTKEpletEGqvsRIVEFIEKPDQPQtldSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTDAIA 243
Cdd:COG1209 134 GYKVE-DPERYGVVEFDE----DG---RVVSLEEKPKEPK---SNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQ 202
|
250 260 270
....*....|....*....|....*....|.
gi 658549632 244 E-LAKKQSVDAMLMTGDS-YDCGKKMGYMQA 272
Cdd:COG1209 203 AyLERGKLVVELLGRGFAwLDTGTHESLLEA 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-272 |
6.82e-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: 139.13 E-value: 6.82e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELealleqrvkrq 84
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 llaevqsicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDtasadplrYNLAAMVARFNETGRS-QVL 163
Cdd:COG1208 70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD--------LDLAALLAFHREKGADaTLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 164 AKRMKgDLSEYSVIQTKEpletEGqvsRIVEFIEKPDQPqtlDSDLMAVGRYVLNADIWAELEKTEPgawdrIQLTDAIA 243
Cdd:COG1208 131 LVPVP-DPSRYGVVELDG----DG---RVTRFVEKPEEP---PSNLINAGIYVLEPEIFDYIPEGEP-----FDLEDLLP 194
|
250 260
....*....|....*....|....*....
gi 658549632 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:COG1208 195 RLIAEGRVYGYVHDGYWLDIGTPEDLLEA 223
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-249 |
1.71e-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: 79.48 E-value: 1.71e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELealleqrvkrql 85
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 86 laevqsicppGVTIMNVRQAQPLGLGHSI--LCARPvvgDNPFIVVLPDIIIdtasadplRYNLAAMVARFNETGRSQVL 163
Cdd:cd06426 69 ----------GVNISYVREDKPLGTAGALslLPEKP---TDPFLVMNGDILT--------NLNYEHLLDFHKENNADATV 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 164 AKRMKGDLSEYSVIQTKEpletegqvSRIVEFIEKPDQPQTLDSdlmavGRYVLNADIWAELEKTEpgawdRIQLTDAIA 243
Cdd:cd06426 128 CVREYEVQVPYGVVETEG--------GRITSIEEKPTHSFLVNA-----GIYVLEPEVLDLIPKNE-----FFDMPDLIE 189
|
....*.
gi 658549632 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 |
2.58e-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: 76.05 E-value: 2.58e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYElealleqrvkrql 85
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 86 laevqsicpPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTasadplryNLAAMVARFNETGRSQVLA- 164
Cdd:cd06915 68 ---------GGIRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDV--------DLLALLAALRASGADATMAl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 165 KRMKgDLSEYSVIQTKEpletegqVSRIVEFIEKP--DQPQTLDSdlmavGRYVLNADIWAELEKTEPGAwdriqLTDAI 242
Cdd:cd06915 131 RRVP-DASRYGNVTVDG-------DGRVIAFVEKGpgAAPGLING-----GVYLLRKEILAEIPADAFSL-----EADVL 192
|
250 260 270
....*....|....*....|....*....|
gi 658549632 243 AELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:cd06915 193 PALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
4-238 |
1.31e-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: 74.55 E-value: 1.31e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVL-VTHSSKNAVEnhfdtsyELEAlLEQRvk 82
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPEDMVP-------FLKE-YEKK-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 83 rqllaevqsicpPGVTIMNVRQAQPLGLGHSILCARPVVG--DNPFIVVLPDIIIDtasadplrYNLAAMVARFNETGR- 159
Cdd:cd06425 71 ------------LGIKITFSIETEPLGTAGPLALARDLLGddDEPFFVLNSDVICD--------FPLAELLDFHKKHGAe 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 658549632 160 SQVLAKRMKgDLSEYSVIQTKeplETEGQVSRiveFIEKPDQPQtldSDLMAVGRYVLNADIwaelektepgaWDRIQL 238
Cdd:cd06425 131 GTILVTKVE-DPSKYGVVVHD---ENTGRIER---FVEKPKVFV---GNKINAGIYILNPSV-----------LDRIPL 188
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-221 |
1.60e-15 |
|
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: 74.21 E-value: 1.60e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDK-PMIQYIVDEIVAAGIKEIVLVThssknaveNHFDtsyeleallEQRVKR 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEH---------RFMLNE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 84 QLLAEVQSicppGVTIMNVRQAQPLGLGHSILCARPVVGDNPF-IVVLP-DIIIdtasadplRYNLAAMVARFNETGRSQ 161
Cdd:pfam00483 64 LLGDGSKF----GVQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGgDHIY--------RMDLEQAVKFHIEKAADA 131
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658549632 162 -VLAKRMKGDL-SEYSVIqtkeplETEGQvSRIVEFIEKPDQPqtLDSDLMAVGRYVLNADI 221
Cdd:pfam00483 132 tVTFGIVPVEPpTGYGVV------EFDDN-GRVIRFVEKPKLP--KASNYASMGIYIFNSGV 184
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-150 |
1.26e-14 |
|
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: 71.45 E-value: 1.26e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYElealleqrvkrq 84
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF------------ 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 658549632 85 llaevqsicPPGVTIMNVRqAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTASADPLRYNLAAM 150
Cdd:cd06422 69 ---------GLRITISDEP-DELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRM 124
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-240 |
1.62e-14 |
|
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: 71.45 E-value: 1.62e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThssknavenhfdTSYELEALleqrvkRQ 84
Cdd:cd02538 2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDLPLF------KE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 LLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIdtasADPlryNLAAMVARFNE-TGRSQVL 163
Cdd:cd02538 64 LLGDGSDL---GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIF----YGQ---GLSPILQRAAAqKEGATVF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658549632 164 AKRMKgDLSEYSVIQtkepLETEGqvsRIVEFIEKPDQPQtldSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTD 240
Cdd:cd02538 134 GYEVN-DPERYGVVE----FDENG---RVLSIEEKPKKPK---SNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-248 |
6.23e-12 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 64.11 E-value: 6.23e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthssknavenhfdTSYELEaLLEQRVKRq 84
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV-------------TGYKAE-LIEEALAR- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 llaevqsiCPPGVT-IMNVRQAQpLGLGHSILCARPVVGDnPFIVVLPDIIIDtasadplrynlAAMVARFNETGRSQVL 163
Cdd:COG1213 66 --------PGPDVTfVYNPDYDE-TNNIYSLWLAREALDE-DFLLLNGDVVFD-----------PAILKRLLASDGDIVL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 164 A---KRMKGDLSEYSVIqtkepLETEGqvsRIVEFIEKPDQPqtlDSDLMAVGRYVLNADIWAELEKTEPGAWDRIQ--- 237
Cdd:COG1213 125 LvdrKWEKPLDEEVKVR-----VDEDG---RIVEIGKKLPPE---EADGEYIGIFKFSAEGAAALREALEALIDEGGpnl 193
|
250
....*....|..
gi 658549632 238 -LTDAIAELAKK 248
Cdd:COG1213 194 yYEDALQELIDE 205
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-249 |
2.59e-10 |
|
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate uridyltransferase (GlmU). GlmU is an essential bacterial enzyme with both an acetyltransferase and an uridyltransferase activity which have been mapped to the C-terminal and N-terminal domains, respectively. This family represents the N-terminal uridyltransferase. GlmU performs the last two steps in the synthesis of UDP-N-acetylglucosamine (UDP-GlcNAc), which is an essential precursor in both the peptidoglycan and the lipopolysaccharide metabolic pathways in Gram-positive and Gram-negative bacteria, respectively.
Pssm-ID: 133020 [Multi-domain] Cd Length: 229 Bit Score: 59.07 E-value: 2.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMlpatK-AIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVEnhfdtsyelealleqrvkrq 84
Cdd:cd02540 1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVK-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 85 llaevQSICPPGVTImnVRQAQPLGLGHSILCARPVV-----------GDNPFIvvlpdiiidTASAdplrynLAAMVAR 153
Cdd:cd02540 57 -----KALANPNVEF--VLQEEQLGTGHAVKQALPALkdfegdvlvlyGDVPLI---------TPET------LQRLLEA 114
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 154 FNETGRSQVLAKRMKGDLSEYSVIQTKEpletEGQVSRIVEfiEKPDQPQTLDSDLMAVGRYVLNA-DIWAELEKTEPga 232
Cdd:cd02540 115 HREAGADVTVLTAELEDPTGYGRIIRDG----NGKVLRIVE--EKDATEEEKAIREVNAGIYAFDAeFLFEALPKLTN-- 186
|
250 260
....*....|....*....|.
gi 658549632 233 wDRIQ----LTDAIaELAKKQ 249
Cdd:cd02540 187 -NNAQgeyyLTDII-ALAVAD 205
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-72 |
3.21e-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: 58.82 E-value: 3.21e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEI-VLVTHSSKNAVENHFDTSYE 72
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDViVVVPEEEQAEISTYLRSFPL 70
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-272 |
4.13e-10 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 59.30 E-value: 4.13e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 1 MINLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSknavenhfDTSYelealleqr 80
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DTPR--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 81 vKRQLLAEVQSIcppGVTIMNVRQAQPLGLGHSILCARPVVGDNPFIVVLPDIIIDTASADPLrynlaaMVARFNETGRS 160
Cdd:PRK15480 64 -FQQLLGDGSQW---GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKL------MEAAVNKESGA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 161 QVLAKRMKgDLSEYSVIQtkepLETEGQVsriVEFIEKPDQPQtldSDLMAVGRYVLNADIWAELEKTEPGAWDRIQLTD 240
Cdd:PRK15480 134 TVFAYHVN-DPERYGVVE----FDQNGTA---ISLEEKPLQPK---SNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
|
250 260 270
....*....|....*....|....*....|....*
gi 658549632 241 aIAELAKKQSVDAMLMTGDSY---DCGKKMGYMQA 272
Cdd:PRK15480 203 -INRIYMEQGRLSVAMMGRGYawlDTGTHQSLIEA 236
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-156 |
4.67e-10 |
|
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: 58.40 E-value: 4.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEalleqrvkrql 85
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK----------- 69
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 658549632 86 laevqsicppgvTIMNVRQAQPlGLGHSILCARPVVGDNpFIVVLPDIIIDTASADPL----RYNLAAMVARFNE 156
Cdd:cd02523 70 ------------FVYNPDYAET-NNIYSLYLARDFLDED-FLLLEGDVVFDPSILERLlsspADNAILVDKKTKE 130
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
4-81 |
1.42e-09 |
|
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: 56.88 E-value: 1.42e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 658549632 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLEQRV 81
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIV 78
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
3-130 |
2.80e-09 |
|
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: 57.34 E-value: 2.80e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 3 NLKAVIPVAGLGMHMlpatK-AIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTsyelealleqrv 81
Cdd:COG1207 2 PLAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD------------ 65
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 658549632 82 krqllaevqsicpPGVTImnVRQAQPLGLGHSILCARPVV-GDNPFIVVL 130
Cdd:COG1207 66 -------------LDVEF--VLQEEQLGTGHAVQQALPALpGDDGTVLVL 100
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-253 |
1.59e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 55.25 E-value: 1.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVEnhfdtsyelealleqrvkrql 85
Cdd:PRK14353 8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 86 lAEVQSICPPGVTimnVRQAQPLGLGHSILCARP-----------VVGDNPFIvvlpdiiidtaSADPLRynlaAMVARF 154
Cdd:PRK14353 64 -AAAAKIAPDAEI---FVQKERLGTAHAVLAAREalaggygdvlvLYGDTPLI-----------TAETLA----RLRERL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 155 NETGRSQVLAKRmkgdlseysviqTKEP------LETEGQVSRIVEFIEKPDQPQTLD---SDLMAVGRyvlnADIWAEL 225
Cdd:PRK14353 125 ADGADVVVLGFR------------AADPtgygrlIVKGGRLVAIVEEKDASDEERAITlcnSGVMAADG----ADALALL 188
|
250 260
....*....|....*....|....*....
gi 658549632 226 EK-TEPGAWDRIQLTDaIAELAKKQSVDA 253
Cdd:PRK14353 189 DRvGNDNAKGEYYLTD-IVAIARAEGLRV 216
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-219 |
1.73e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 55.37 E-value: 1.73e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 4 LKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT-HSSKnavenhfdtsyELEALLEQrvk 82
Cdd:PRK14358 8 LDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTgHGAE-----------QVEAALQG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 83 rqllaevqsicpPGVTImnVRQAQPLGLGHSILCARPVVGDNPfivvlPDIIIDTASADPLR-YNLAAMVARFNETGRSQ 161
Cdd:PRK14358 71 ------------SGVAF--ARQEQQLGTGDAFLSGASALTEGD-----ADILVLYGDTPLLRpDTLRALVADHRAQGSAM 131
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 658549632 162 VLAKRMKGDLSEYSVIQTKEpletEGQVSRIVEfiEKPDQPQTLDSDLMAVGRYVLNA 219
Cdd:PRK14358 132 TILTGELPDATGYGRIVRGA----DGAVERIVE--QKDATDAEKAIGEFNSGVYVFDA 183
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-220 |
2.12e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 54.75 E-value: 2.12e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 1 MINLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTSYELEALLeqr 80
Cdd:PRK14355 1 MNNLAAIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 81 vkrqllaevqsicppgvtimnvrQAQPLGLGHSILCARP-----------VVGDNPfivvlpdiIIDTASadplrynLAA 149
Cdd:PRK14355 75 -----------------------QEEQLGTGHAVACAAPaldgfsgtvliLCGDVP--------LLRAET-------LQG 116
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 658549632 150 MVARFNETGRS-QVLAKRMKGDLSEYSVIQtkeplETEGQVSRIVEfiEKPDQPQTLDSDLMAVGRYVLNAD 220
Cdd:PRK14355 117 MLAAHRATGAAvTVLTARLENPFGYGRIVR-----DADGRVLRIVE--EKDATPEERSIREVNSGIYCVEAA 181
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
3-127 |
5.31e-08 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 53.68 E-value: 5.31e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 3 NLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT-HSSKnavenhfdtsyELEALLEQRV 81
Cdd:PRK14354 2 NRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGAE-----------EVKEVLGDRS 67
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 658549632 82 KRqllaevqsicppgvtimnVRQAQPLGLGHSILCARP-----------VVGDNPFI 127
Cdd:PRK14354 68 EF------------------ALQEEQLGTGHAVMQAEEfladkegttlvICGDTPLI 106
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-127 |
3.18e-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: 3.18e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 4 LKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHssknavenhfdtSYELealleqrvkr 83
Cdd:PRK14357 1 MRALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGH------------EAEL---------- 55
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 658549632 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 |
1.41e-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: 45.29 E-value: 1.41e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 658549632 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHSSKNAVENHFDTS 70
Cdd:cd04197 1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS 67
|
|
| MPP_Mre11_N |
cd00840 |
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ... |
232-283 |
7.31e-04 |
|
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: 39.56 E-value: 7.31e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 658549632 232 AWDRIQLTDAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVNYGLRNLKE 283
Cdd:cd00840 21 EEDFFKAFEEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
26-62 |
1.17e-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: 1.17e-03
10 20 30
....*....|....*....|....*....|....*..
gi 658549632 26 KEMLPIVDKPMIQYIVDEIVAAGIKEIVLVThsSKNA 62
Cdd:COG2266 14 KPLLEICGKPMIDRVIDALEESCIDKIYVAV--SPNT 48
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
6-129 |
7.98e-03 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 37.04 E-value: 7.98e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLGMHMlpatKA-IPKEMLPIVDKPMIQYIVDEIVAAG-IKEIVLVTHSSknavenhfDTSYELEALLEQRVKR 83
Cdd:PRK00155 6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPD--------DRPDFAELLLAKDPKV 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 658549632 84 QllaevqsICPPGVTimnvRQaqplglgHSILCARPVVGDNPFIVV 129
Cdd:PRK00155 74 T-------VVAGGAE----RQ-------DSVLNGLQALPDDDWVLV 101
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-164 |
8.86e-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: 36.38 E-value: 8.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 6 AVIPVAGLG--MHMlpatkaiPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVthssknavenhfdTSYELEALleqrvkR 83
Cdd:cd04182 3 AIILAAGRSsrMGG-------NKLLLPLDGKPLLRHALDAALAAGLSRVIVV-------------LGAEADAV------R 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 658549632 84 QLLAevqsicPPGVTIMNVRQAQpLGLGHSILCA-RPVVGDNPFIVVL----PDIIIDTasadplrynLAAMVARFNETG 158
Cdd:cd04182 57 AALA------GLPVVVVINPDWE-EGMSSSLAAGlEALPADADAVLILladqPLVTAET---------LRALIDAFREDG 120
|
....*.
gi 658549632 159 RSQVLA 164
Cdd:cd04182 121 AGIVAP 126
|
|
| |
