|
Name |
Accession |
Description |
Interval |
E-value |
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
1-288 |
0e+00 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 573.19 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAVQ 80
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGPQFERLLGDGSQLGIKISYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 81 ESPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEK 160
Cdd:COG1209 81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGDGLSELLREAAARESGATIFGYKVEDPERYGVVEFDEDGRVVSLEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 161 PTEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGFAWLDTGTHESLLEASTFIETI 240
Cdd:COG1209 161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGFAWLDTGTHESLLEANRFVLTI 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 518552395 241 EKRQNLKVACLEEVAYRMGYIDKQQLAVLAEPLKKNQYGQYLLRLAAE 288
Cdd:COG1209 241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANSLEKSGYGPYLLRLLDS 288
|
|
| rmlA |
TIGR01207 |
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ... |
2-286 |
0e+00 |
|
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 130274 [Multi-domain] Cd Length: 286 Bit Score: 557.39 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAVQE 81
Cdd:TIGR01207 1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPEDTPRFQRLLGDGSQWGINLSYAVQP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEKP 161
Cdd:TIGR01207 81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGHDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNGRAISIEEKP 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 162 TEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGFAWLDTGTHESLLEASTFIETIE 241
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRVYLEEGRLSVELLGRGYAWLDTGTHDSLLEASNFIQTIE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 518552395 242 KRQNLKVACLEEVAYRMGYIDKQQLAVLAEPLKKNQYGQYLLRLA 286
Cdd:TIGR01207 241 KRQGLKVACPEEIAWRNGWIDDEQLEELARPLAKNGYGQYLLRLL 285
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
1-240 |
0e+00 |
|
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: 499.79 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAVQ 80
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDLPLFKELLGDGSDLGIRITYAVQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 81 ESPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEK 160
Cdd:cd02538 81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFDENGRVLSIEEK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 161 PTEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGFAWLDTGTHESLLEASTFIETI 240
Cdd:cd02538 161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKGKLSVELLGRGFAWLDTGTHESLLEASNFVQTI 240
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-285 |
3.07e-158 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 442.19 E-value: 3.07e-158
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAVQE 81
Cdd:PRK15480 5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEKP 161
Cdd:PRK15480 85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNGTAISLEEKP 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 162 TEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGFAWLDTGTHESLLEASTFIETIE 241
Cdd:PRK15480 165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYAWLDTGTHQSLIEASNFIATIE 244
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 518552395 242 KRQNLKVACLEEVAYRMGYIDKQQLAVLAEPLKKNQYGQYLLRL 285
Cdd:PRK15480 245 ERQGLKVSCPEEIAFRKGFIDAEQVKVLAEPLKKNAYGQYLLKM 288
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
2-238 |
8.33e-102 |
|
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: 297.24 E-value: 8.33e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDK-PMIYYPMSILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAVQ 80
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 81 ESPDGLAQAFIIGEEFIGDDSV-CLVLGDNIYYGGGLSKMLQRAASRES--GATVFGYHVNDPERFGVVEFDENMQALSI 157
Cdd:pfam00483 81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDLEQAVKFHIEKAAdaTVTFGIVPVEPPTGYGVVEFDDNGRVIRF 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 158 EEKPTEPK-SNYAVTGLYFYDNDVIS-IAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGFAWLDTGTHESLLEAST 235
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYAWLDVGTWDSLWEANL 240
|
...
gi 518552395 236 FIE 238
Cdd:pfam00483 241 FLL 243
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
1-237 |
1.04e-74 |
|
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: 228.22 E-value: 1.04e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDtPRFEELFGNGHDLGIHLEYAVQ 80
Cdd:cd04189 1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTG-EEIKEALGDGSRFGVRITYILQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 81 ESPDGLAQAFIIGEEFIGDDSVCLVLGDNIyYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENmQALSIEEK 160
Cdd:cd04189 80 EEPLGLAHAVLAARDFLGDEPFVVYLGDNL-IQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDG-RIVRLVEK 157
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518552395 161 PTEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGK--LSVEIMGrgfAWLDTGTHESLLEASTFI 237
Cdd:cd04189 158 PKEPPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrvGYSIVTG---WWKDTGTPEDLLEANRLL 233
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
3-225 |
3.13e-67 |
|
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: 208.59 E-value: 3.13e-67
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDtPRFEELFGNGHDLGIHLEYAVQES 82
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLG-EQIEEYFGDGSKFGVNIEYVVQEE 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 83 PDGLAQAFIIGEEFIGDDSVCLVLGDNIYYGGgLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEKPT 162
Cdd:cd04181 80 PLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD-LSELLRFHREKGADATIAVKEVEDPSRYGVVELDDDGRVTRFVEKPT 158
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518552395 163 EPKSNYAVTGLYFYDNDVISIAKEIKPseRGELEITDVNKAYLERGKLSVEIMgrGFAWLDTG 225
Cdd:cd04181 159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGYPV--DGYWLDIG 217
|
|
| rmlA_long |
TIGR01208 |
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ... |
2-243 |
5.16e-62 |
|
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, 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. Alternate name: dTDP-D-glucose synthase
Pssm-ID: 273500 [Multi-domain] Cd Length: 353 Bit Score: 199.55 E-value: 5.16e-62
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAVQE 81
Cdd:TIGR01208 1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTGEEIKEIVGEGERFGAKITYIVQG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 82 SPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYgGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEKP 161
Cdd:TIGR01208 81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQ-DGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDGKRILKLVEKP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 162 TEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGFaWLDTGTHESLLEASTFI-ETI 240
Cdd:TIGR01208 160 KEPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGW-WKDTGKPEDLLDANRLIlDEV 238
|
...
gi 518552395 241 EKR 243
Cdd:TIGR01208 239 ERE 241
|
|
| Arch_glmU |
TIGR03992 |
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ... |
1-234 |
5.82e-52 |
|
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.
Pssm-ID: 274908 [Multi-domain] Cd Length: 393 Bit Score: 174.70 E-value: 5.82e-52
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTpRFEELFGNGHDLGIHLEYAVQ 80
Cdd:TIGR03992 1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKE-KVREYFGDGSRGGVPIEYVVQ 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 81 ESPDGLAQAFIIGEEFIgDDSVCLVLGDNIYYGGGLSKMLqraasRESGATVFGYHVNDPERFGVVEFDENmQALSIEEK 160
Cdd:TIGR03992 80 EEQLGTADALGSAKEYV-DDEFLVLNGDVLLDSDLLERLI-----RAEAPAIAVVEVDDPSDYGVVETDGG-RVTGIVEK 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518552395 161 PTEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGRGfaWLDTGTHESLLEAS 234
Cdd:TIGR03992 153 PENPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEGKVKAVELDGF--WLDVGRPWDLLDAN 224
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
2-233 |
1.81e-51 |
|
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: 168.79 E-value: 1.81e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEIlIISTPQDTPRFEELFGNGHDLGIHLEYAVQE 81
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEI-VINVGYLAEQIEEYFGDGSRFGVRITYVDEG 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 82 SP----DGLAQAfiigEEFIGDDSVCLVLGDnIYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSI 157
Cdd:COG1208 80 EPlgtgGALKRA----LPLLGDEPFLVLNGD-ILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDGRVTRF 154
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 518552395 158 EEKPTEPKSNYAVTGLYFYDNDVIsiaKEIKPSERgeLEITDVNKAYLERGKLSVEIMgRGFaWLDTGTHESLLEA 233
Cdd:COG1208 155 VEKPEEPPSNLINAGIYVLEPEIF---DYIPEGEP--FDLEDLLPRLIAEGRVYGYVH-DGY-WLDIGTPEDLLEA 223
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
1-234 |
7.20e-34 |
|
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: 124.18 E-value: 7.20e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQ--------DTPRF--EELFGNG-H 69
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGkraiedhfDRSYEleETLEKKGkT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 70 DL---------GIHLEYAVQESPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYG--GGLSKMLQRAAsrESGATVFGYHVN 138
Cdd:cd02541 81 DLleevriisdLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSkePCLKQLIEAYE--KTGASVIAVEEV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 139 DPE---RFGVV---EFDENM-QALSIEEKP--TEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGK 209
Cdd:cd02541 159 PPEdvsKYGIVkgeKIDGDVfKVKGLVEKPkpEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEP 238
|
250 260
....*....|....*....|....*.
gi 518552395 210 -LSVEIMGRgfaWLDTGTHESLLEAS 234
Cdd:cd02541 239 vYAYVFEGK---RYDCGNKLGYLKAT 261
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-233 |
1.27e-26 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 105.11 E-value: 1.27e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQ--------DT-PRFE-ELFGNG-HD 70
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGkraiedhfDRsYELEaTLEAKGkEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 71 L---------GIHLEYAVQESPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYG--GGLSKMLQRAasRESGATVFGYHVND 139
Cdd:COG1210 85 LleevrsispLANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSekPCLKQMIEVY--EETGGSVIAVQEVP 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 140 PE---RFGVVEFDENMQAL----SIEEKPT--EPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGK- 209
Cdd:COG1210 163 PEevsKYGIVDGEEIEGGVyrvtGLVEKPApeEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEEPv 242
|
250 260
....*....|....*....|....
gi 518552395 210 LSVEIMGRgfaWLDTGTHESLLEA 233
Cdd:COG1210 243 YAYEFEGK---RYDCGDKLGYLKA 263
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
4-233 |
2.73e-25 |
|
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: 100.32 E-value: 2.73e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEIlIISTPQDTPRFEELFGNGHDLGIHLEYAVQESP 83
Cdd:cd06915 2 VILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRI-VLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 84 DGLAQAFIIGEEFIGDDSVCLVLGDNiYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEEKPTE 163
Cdd:cd06915 81 LGTGGAIKNALPKLPEDQFLVLNGDT-YFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDGDGRVIAFVEKGPG 159
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518552395 164 PKSNYAVTGLYFYDNDVISIAKEIKPSergeLEiTDVNKAYLERGKLsveimgRGFA----WLDTGTHESLLEA 233
Cdd:cd06915 160 AAPGLINGGVYLLRKEILAEIPADAFS----LE-ADVLPALVKRGRL------YGFEvdgyFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
4-233 |
3.51e-23 |
|
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: 94.50 E-value: 3.51e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEIlIISTPQDTPRFEELFGNGHDLGIHLEYAVQESP 83
Cdd:cd06426 2 VIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNF-YISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 84 DGLAQAFIIGEEFIgDDSVCLVLGD---NIYYggglSKMLQRAASRESGATVFG--YHVNDPerFGVVEFDENMqALSIE 158
Cdd:cd06426 81 LGTAGALSLLPEKP-TDPFLVMNGDiltNLNY----EHLLDFHKENNADATVCVreYEVQVP--YGVVETEGGR-ITSIE 152
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518552395 159 EKPTEpksNYAV-TGLYFYDNDVIsiaKEIKPSERgeLEITDVNKAYLERG-KLSV-EIMGRgfaWLDTGTHESLLEA 233
Cdd:cd06426 153 EKPTH---SFLVnAGIYVLEPEVL---DLIPKNEF--FDMPDLIEKLIKEGkKVGVfPIHEY---WLDIGRPEDYEKA 219
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
1-233 |
5.10e-23 |
|
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: 94.58 E-value: 5.10e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKE-ILIIS-TPQDTPRFEELFGNghDLGIHLEYA 78
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEiILAVNyRPEDMVPFLKEYEK--KLGIKITFS 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 79 VQESPDGLAQAFIIGEEFIGDDSVC-LVLGDNIYYGGGLSKMLQ--RAASREsgATVFGYHVNDPERFGVVEFDENM-QA 154
Cdd:cd06425 79 IETEPLGTAGPLALARDLLGDDDEPfFVLNSDVICDFPLAELLDfhKKHGAE--GTILVTKVEDPSKYGVVVHDENTgRI 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 155 LSIEEKPTEPKSNYAVTGLYFYDNDVI--------SIAKEIKP--SERGELEITDVNkaylergklsveimgrGFaWLDT 224
Cdd:cd06425 157 ERFVEKPKVFVGNKINAGIYILNPSVLdriplrptSIEKEIFPkmASEGQLYAYELP----------------GF-WMDI 219
|
....*....
gi 518552395 225 GTHESLLEA 233
Cdd:cd06425 220 GQPKDFLKG 228
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
2-233 |
9.07e-19 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 82.62 E-value: 9.07e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEIlIIST---PQdtpRFEELFGN-GHDLGIHLEY 77
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRI-VVNThhlAD---QIEAHLGDsRFGLRITISD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 78 ---AVQESPDGLAQAfiigEEFIGDDSVCLVLGDnIYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENmQA 154
Cdd:cd06422 77 epdELLETGGGIKKA----LPLLGDEPFLVVNGD-ILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLD-AD 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 518552395 155 LSIEEKPTEPKSNYAVTGLYFYDNDVISiakEIKPserGELEITDVNKAYLERGKLSVEIMgRGFaWLDTGTHESLLEA 233
Cdd:cd06422 151 GRLRRGGGGAVAPFTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAGRLFGLVY-DGL-WFDVGTPERLLAA 221
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-199 |
1.37e-15 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 75.33 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIsTPQDTPRFEELFGNGHDLGIHLEYAVQE 81
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLV-THSSKNSIENHFDTSFELEAMLEKRVKR 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 82 S----------------------PDGLAQAFIIGEEFIGDDSVCLVLGDNIY--YGGGLSK-----MLQRAAsrESGAT- 131
Cdd:PRK13389 89 QlldevqsicpphvtimqvrqglAKGLGHAVLCAHPVVGDEPVAVILPDVILdeYESDLSQdnlaeMIRRFD--ETGHSq 166
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 518552395 132 VFGYHVNDPERFGVVEFD-------ENMQALSIEEKPT--EPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITD 199
Cdd:PRK13389 167 IMVEPVADVTAYGVVDCKgvelapgESVPMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
3-234 |
2.70e-15 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 75.11 E-value: 2.70e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLYPLTKATSKqlmpvydkPMIYY---------PMSILMLAGIKEILIIStpQDTPRfeELF---GNGH- 69
Cdd:COG0448 4 AIILAGGRGSRLGPLTKDRAK--------PAVPFggkyriidfPLSNCVNSGIRRVGVLT--QYKSH--SLNdhiGSGKp 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 70 -DL-----GIHLEYAVQESPD-----GLAQAFIIGEEFIGD---DSVCLVLGDNIY---YggglSKMLQRAasRESGA-- 130
Cdd:COG0448 72 wDLdrkrgGVFILPPYQQREGedwyqGTADAVYQNLDFIERsdpDYVLILSGDHIYkmdY----RQMLDFH--IESGAdi 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 131 TVFGYHVNDPE--RFGVVEFDENMQALSIEEKPTEPKSNYAVTGLYFYDNDV-ISIAKEIKPSERGELeITDVNKAYLER 207
Cdd:COG0448 146 TVACIEVPREEasRFGVMEVDEDGRITEFEEKPKDPKSALASMGIYVFNKDVlIELLEEDAPNSSHDF-GKDIIPRLLDR 224
|
250 260 270
....*....|....*....|....*....|
gi 518552395 208 GKlsveIMG---RGFaWLDTGTHESLLEAS 234
Cdd:COG0448 225 GK----VYAyefDGY-WRDVGTIDSYYEAN 249
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
1-57 |
8.34e-15 |
|
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: 71.54 E-value: 8.34e-15
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQD 57
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEE 57
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-199 |
8.44e-14 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 69.92 E-value: 8.44e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIsTPQDTPRFEELFGNGHDLGIHLEYAV- 79
Cdd:PRK10122 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLV-THASKNAVENHFDTSYELESLLEQRVk 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 80 ---------------------QESPDGLAQAFIIGEEFIGDDSVCLVLGDNIYYGG-------GLSKMLQRAasRESG-A 130
Cdd:PRK10122 83 rqllaevqsicppgvtimnvrQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplryNLAAMIARF--NETGrS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 131 TVFGYHV-NDPERFGVVEFDENM-------QALSIEEKPTEPK---SNYAVTGLYFYDNDVISIAKEIKPSERGELEITD 199
Cdd:PRK10122 161 QVLAKRMpGDLSEYSVIQTKEPLdregkvsRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
|
|
| glgC |
PRK05293 |
glucose-1-phosphate adenylyltransferase; Provisional |
1-234 |
3.57e-12 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179997 [Multi-domain] Cd Length: 380 Bit Score: 66.04 E-value: 3.57e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDK-PMIYYPMSILMLAGIKEILIIStpQDTPRfeEL---FGNGH--DL--- 71
Cdd:PRK05293 4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLT--QYQPL--ELnnhIGIGSpwDLdri 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 72 --GIHL--EYAVQESPD---GLAQAFIIGEEFIGDDSVCLVL---GDNIY---YggglSKMLQRAASRESGATVFGYHV- 137
Cdd:PRK05293 80 ngGVTIlpPYSESEGGKwykGTAHAIYQNIDYIDQYDPEYVLilsGDHIYkmdY----DKMLDYHKEKEADVTIAVIEVp 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 138 -NDPERFGVVEFDENMQALSIEEKPTEPKSNYAVTGLYFYDNDVIsiaKE-IKPSERGELEITDVNK----AYLERGKLS 211
Cdd:PRK05293 156 wEEASRFGIMNTDENMRIVEFEEKPKNPKSNLASMGIYIFNWKRL---KEyLIEDEKNPNSSHDFGKnvipLYLEEGEKL 232
|
250 260
....*....|....*....|...
gi 518552395 212 VEIMGRGFaWLDTGTHESLLEAS 234
Cdd:PRK05293 233 YAYPFKGY-WKDVGTIESLWEAN 254
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
1-52 |
6.44e-12 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 63.43 E-value: 6.44e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 518552395 1 MKGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILII 52
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVV 52
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
4-233 |
1.60e-11 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 62.64 E-value: 1.60e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQDTpRFEELFgnghDLGIHLEYAVQESP 83
Cdd:cd02523 2 IILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKE-QIEELL----KKYPNIKFVYNPDY 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 84 D--GLAQAFIIGEEFIGDDsvCLVL-GDNIYYGGGLSKMLqrAASRESGATVFGYHVNDPERFGVVeFDENMQALSIEEK 160
Cdd:cd02523 77 AetNNIYSLYLARDFLDED--FLLLeGDVVFDPSILERLL--SSPADNAILVDKKTKEWEDEYVKD-LDDAGVLLGIISK 151
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 518552395 161 PTEPKSNYAVT-GLYFYDND----VISIAKEIKPSERGELEITDVNKAYLERGKLSVEIMGrGFAWLDTGTHESLLEA 233
Cdd:cd02523 152 AKNLEEIQGEYvGISKFSPEdadrLAEALEELIEAGRVNLYYEDALQRLISEEGVKVKDIS-DGFWYEIDDLEDLERA 228
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
4-200 |
1.98e-09 |
|
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: 56.75 E-value: 1.98e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYpltKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIsTPQDTPRFEELFGNghdlgIHLEYAVQESP 83
Cdd:cd02540 2 VILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV-VGHGAEQVKKALAN-----PNVEFVLQEEQ 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 84 DGLAQAFIIGEEFI-GDDSVCLVLgdniyYG-------GGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQAL 155
Cdd:cd02540 73 LGTGHAVKQALPALkDFEGDVLVL-----YGdvplitpETLQRLLEAHREAGADVTVLTAELEDPTGYGRIIRDGNGKVL 147
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 518552395 156 SI-EEK---PTEPKSNYAVTGLYFYDNDVISIA-KEIKPS-ERGELEITDV 200
Cdd:cd02540 148 RIvEEKdatEEEKAIREVNAGIYAFDAEFLFEAlPKLTNNnAQGEYYLTDI 198
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-216 |
2.77e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 57.53 E-value: 2.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRlypLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIstpqdtprfeelFGNGHD-----LGIHLEYA 78
Cdd:PRK14354 6 IILAAGKGTR---MKSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTV------------VGHGAEevkevLGDRSEFA 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 79 VQESPDGLAQAFIIGEEFIGD-DSVCLVL-GDN-IYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQAL 155
Cdd:PRK14354 71 LQEEQLGTGHAVMQAEEFLADkEGTTLVIcGDTpLITAETLKNLIDFHEEHKAAATILTAIAENPTGYGRIIRNENGEVE 150
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 518552395 156 SI-EEK---PTEPKSNYAVTGLYFYDNDVISIA-KEIKP-SERGELEITDVNKAYLERGKL--------SVEIMG 216
Cdd:PRK14354 151 KIvEQKdatEEEKQIKEINTGTYCFDNKALFEAlKKISNdNAQGEYYLTDVIEILKNEGEKvgayqtedFEESLG 225
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
2-52 |
4.94e-09 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 55.63 E-value: 4.94e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 518552395 2 KGIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILII 52
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV 51
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
4-200 |
1.28e-07 |
|
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: 52.34 E-value: 1.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYpltKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIstpqdtprfeelFGNGHDL------GIHLEY 77
Cdd:COG1207 6 VILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVV------------VGHGAEQvraalaDLDVEF 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 78 AVQESPDGLAQAFIIGEEFI-GDDSVCLVLgdniyYG-------GGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFD 149
Cdd:COG1207 71 VLQEEQLGTGHAVQQALPALpGDDGTVLVL-----YGdvpliraETLKALLAAHRAAGAAATVLTAELDDPTGYGRIVRD 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*..
gi 518552395 150 ENMQALSI-EEK---PTEPKSNYAVTGLYFYDNDVISIA-KEIKPSE-RGELEITDV 200
Cdd:COG1207 146 EDGRVLRIvEEKdatEEQRAIREINTGIYAFDAAALREAlPKLSNDNaQGEYYLTDV 202
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
3-213 |
1.31e-07 |
|
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.
Pssm-ID: 133050 [Multi-domain] Cd Length: 257 Bit Score: 51.49 E-value: 1.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGG--SGTRLYPLTKATSKQLMPVYDKPMIYYPMS-ILMLAGIKEILIISTPQDTPRFEELFGNGHDLGIHLEYAV 79
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEaCAKVPDLKEVLLIGFYPESVFSDFISDAQQEFNVPIRYLQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 80 QESPDGLAQAF-----IIGEefiGDDSVCLVLGDNIYYGGGLSKMLQRAASRESGATVFGYHVNDPE--RFGVVEFDENM 152
Cdd:cd06428 81 EYKPLGTAGGLyhfrdQILA---GNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTILGTEASREQasNYGCIVEDPST 157
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518552395 153 -QALSIEEKPTEPKSNYAVTGLYFYDNDVISIAKEIKPSERGELEITDVNKAYLERGKLSVE 213
Cdd:cd06428 158 gEVLHYVEKPETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVIRLE 219
|
|
| glgC |
PRK02862 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-163 |
1.60e-07 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 179486 [Multi-domain] Cd Length: 429 Bit Score: 51.81 E-value: 1.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLYPLTKATSKQLMPVYDK-PMIYYPMSILMLAGIKEILIIStpQ-----------DTPRFEElFGNGhd 70
Cdd:PRK02862 6 AIILGGGAGTRLYPLTKLRAKPAVPLAGKyRLIDIPISNCINSGINKIYVLT--QfnsaslnrhisQTYNFDG-FSGG-- 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 71 lgiHLE-YAVQESPD------GLAQA-----FIIGEEFIgdDSVCLVLGDNIY---YggglSKMLQRaaSRESGA--TVF 133
Cdd:PRK02862 81 ---FVEvLAAQQTPEnpswfqGTADAvrkylWHFQEWDV--DEYLILSGDQLYrmdY----RLFVQH--HRETGAdiTLA 149
|
170 180 190
....*....|....*....|....*....|..
gi 518552395 134 GYHVN--DPERFGVVEFDENMQALSIEEKPTE 163
Cdd:PRK02862 150 VLPVDekDASGFGLMKTDDDGRITEFSEKPKG 181
|
|
| CDP-ME_synthetase |
cd02516 |
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ... |
4-75 |
6.41e-07 |
|
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: 49.06 E-value: 6.41e-07
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518552395 4 IILAGGSGTRlypLTKATSKQLMPVYDKPMIYYPMSILM-LAGIKEILIISTPQDTPRFEELFGNGHDLGIHL 75
Cdd:cd02516 4 IILAAGSGSR---MGADIPKQFLELGGKPVLEHTLEAFLaHPAIDEIVVVVPPDDIDLAKELAKYGLSKVVKI 73
|
|
| glgC |
PRK00725 |
glucose-1-phosphate adenylyltransferase; Provisional |
4-166 |
8.24e-07 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234824 [Multi-domain] Cd Length: 425 Bit Score: 49.84 E-value: 8.24e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYPLTKATSKQLMPVYDK-PMIYYPMSILMLAGIKEILIISTPQdtprfeelfgnGHDLGIHLE------ 76
Cdd:PRK00725 19 LILAGGRGSRLKELTDKRAKPAVYFGGKfRIIDFALSNCINSGIRRIGVLTQYK-----------AHSLIRHIQrgwsff 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 77 -YAVQESPDGL-AQAFIIGEE-FIGD-DSVC--------------LVL-GDNIY---YggglSKMLQRaaSRESGA--TV 132
Cdd:PRK00725 88 rEELGEFVDLLpAQQRVDEENwYRGTaDAVYqnldiirrydpkyvVILaGDHIYkmdY----SRMLAD--HVESGAdcTV 161
|
170 180 190
....*....|....*....|....*....|....*.
gi 518552395 133 FGYHVNDPE--RFGVVEFDENMQALSIEEKPTEPKS 166
Cdd:PRK00725 162 ACLEVPREEasAFGVMAVDENDRITAFVEKPANPPA 197
|
|
| IspD |
COG1211 |
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ... |
4-64 |
9.51e-07 |
|
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis
Pssm-ID: 440824 Cd Length: 224 Bit Score: 48.59 E-value: 9.51e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518552395 4 IILAGGSGTRlypLTKATSKQLMPVYDKPMIYYPMSILMLAG-IKEILIISTPQDTPRFEEL 64
Cdd:COG1211 1 IIPAAGSGSR---MGAGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIEYFEEL 59
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
3-233 |
1.17e-06 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 49.44 E-value: 1.17e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLYPLTKATSKQLMP---VYDkpMIYYPMSILMLAGIKEILII----StpqdtprfeelfgngHDLGIHL 75
Cdd:PRK00844 8 AIVLAGGEGKRLMPLTADRAKPAVPfggSYR--LIDFVLSNLVNSGYLRIYVLtqykS---------------HSLDRHI 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 76 EYAVQESpdGLAQAFI--------IGEE--------------FIGD---DSVCLVLGDNIYyggglsKMLQR---AASRE 127
Cdd:PRK00844 71 SQTWRLS--GLLGNYItpvpaqqrLGKRwylgsadaiyqslnLIEDedpDYVVVFGADHVY------RMDPRqmvDFHIE 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 128 SGA--TVFGYHV--NDPERFGVVEFDENMQALSIEEKPTEPKS-------NYAVTGLYFYDNDVISiaKEIKPSERGELE 196
Cdd:PRK00844 143 SGAgvTVAAIRVprEEASAFGVIEVDPDGRIRGFLEKPADPPGlpddpdeALASMGNYVFTTDALV--DALRRDAADEDS 220
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 518552395 197 ITDVNK----AYLERGKLSV------EIMG-----RGFaWLDTGTHESLLEA 233
Cdd:PRK00844 221 SHDMGGdiipRLVERGRAYVydfstnEVPGaterdRGY-WRDVGTIDAYYDA 271
|
|
| GDP-M1P_Guanylyltransferase |
cd02509 |
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ... |
1-52 |
1.24e-06 |
|
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.
Pssm-ID: 133003 [Multi-domain] Cd Length: 274 Bit Score: 48.73 E-value: 1.24e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 518552395 1 MKGIILAGGSGTRLYPL-TKATSKQLMPVY-DKPMIyyPMSILMLAGI---KEILII 52
Cdd:cd02509 1 IYPVILAGGSGTRLWPLsRESYPKQFLKLFgDKSLL--QQTLDRLKGLvppDRILVV 55
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-208 |
1.68e-06 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 48.82 E-value: 1.68e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLyplTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIsTPQDTPRFE-ELFGNGhdlgihLEYAVQES 82
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVV-TGHGAEQVEaALQGSG------VAFARQEQ 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 83 PDGLAQAFIIGEEFI--GDDSVCLVLGDN-IYYGGGLSKMLQRAASRESGATVFGYHVNDPERFGVVEFDENMQALSIEE 159
Cdd:PRK14358 81 QLGTGDAFLSGASALteGDADILVLYGDTpLLRPDTLRALVADHRAQGSAMTILTGELPDATGYGRIVRGADGAVERIVE 160
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 518552395 160 KPTEPKSNYAV----TGLYFYDNDVISIAKEI-KPSERGELEITDVNKAYLERG 208
Cdd:PRK14358 161 QKDATDAEKAIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGG 214
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-232 |
1.87e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 48.61 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 1 MKGIILAGGSGTRL---YPltkatsKQLMPVYDKPMIYYpmsILMLAG--IKEILIIstpqdtprfeelFGNGHD----- 70
Cdd:PRK14357 1 MRALVLAAGKGTRMkskIP------KVLHKISGKPMINW---VIDTAKkvAQKVGVV------------LGHEAElvkkl 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 71 LGIHLEYAVQESPDGLAQAFIIGEEFIGDDSVCLVL-GDN--IYYgGGLSKMLQRAASRESGATVFGYHVNDPERFGVVE 147
Cdd:PRK14357 60 LPEWVKIFLQEEQLGTAHAVMCARDFIEPGDDLLILyGDVplISE-NTLKRLIEEHNRKGADVTILVADLEDPTGYGRII 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 148 FDENMQALsIEEK--PTEPKSNYAV-TGLYFYDND-VISIAKEIKP-SERGELEITDVNKaYLERGKL-----SVEIMG- 216
Cdd:PRK14357 139 RDGGKYRI-VEDKdaPEEEKKIKEInTGIYVFSGDfLLEVLPKIKNeNAKGEYYLTDAVN-FAEKVRVvktedLLEITGv 216
|
250
....*....|....*....
gi 518552395 217 ---RGFAWLDTGTHESLLE 232
Cdd:PRK14357 217 ntrIQLAWLEKQLRMRILE 235
|
|
| ADP_Glucose_PP |
cd02508 |
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ... |
3-132 |
2.65e-06 |
|
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.
Pssm-ID: 133002 [Multi-domain] Cd Length: 200 Bit Score: 47.15 E-value: 2.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLYPLTKATSKQLMPV---YDkpMIYYPMSILMLAGIKEILIIStpQDTPR--FEEL------FGNGHDL 71
Cdd:cd02508 1 AIILAGGEGTRLSPLTKKRAKPAVPFggrYR--LIDFPLSNMVNSGIRNVGVLT--QYKSRslNDHLgsgkewDLDRKNG 76
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 518552395 72 GIHLEYAVQESPD----GLAQAFIIGEEFIGD---DSVCLVLGDNIY---YggglSKMLQRAasRESGATV 132
Cdd:cd02508 77 GLFILPPQQRKGGdwyrGTADAIYQNLDYIERsdpEYVLILSGDHIYnmdY----REMLDFH--IESGADI 141
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
4-64 |
4.02e-06 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 46.67 E-value: 4.02e-06
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 518552395 4 IILAGGSGTRLypltKA-TSKQLMPVYDKPMIYYPMSILMLAG-IKEILIISTPQDTPRFEEL 64
Cdd:PRK00155 7 IIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPDDRPDFAEL 65
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-216 |
4.46e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 47.43 E-value: 4.46e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRlypLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPQdTPRFEELFGNGHDlgihLEYAVQESP 83
Cdd:PRK14355 7 IILAAGKGTR---MKSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ-AEKVREHFAGDGD----VSFALQEEQ 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 84 DGLAQAFIIGEEFI--GDDSVCLVLGDN-IYYGGGLSKMLqrAASRESGA--TVFGYHVNDPERFGVVEFDENMQALSI- 157
Cdd:PRK14355 79 LGTGHAVACAAPALdgFSGTVLILCGDVpLLRAETLQGML--AAHRATGAavTVLTARLENPFGYGRIVRDADGRVLRIv 156
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 518552395 158 EEK---PTEPKSNYAVTGLYFYDNDVI--SIAKEIKPSERGELEITDVNKAYLERGKL--------SVEIMG 216
Cdd:PRK14355 157 EEKdatPEERSIREVNSGIYCVEAAFLfdAIGRLGNDNAQGEYYLTDIVAMAAAEGLRclafpvadPDEIMG 228
|
|
| CpsB |
COG0836 |
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis]; |
1-52 |
8.73e-06 |
|
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440598 [Multi-domain] Cd Length: 347 Bit Score: 46.60 E-value: 8.73e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 518552395 1 MKGIILAGGSGTRLYPL-TKATSKQLMPVY-DKPMIYypMSILMLAGI---KEILII 52
Cdd:COG0836 3 IYPVILAGGSGTRLWPLsRESYPKQFLPLLgEKSLLQ--QTVERLAGLvppENILVV 57
|
|
| PLN02241 |
PLN02241 |
glucose-1-phosphate adenylyltransferase |
3-52 |
2.44e-05 |
|
glucose-1-phosphate adenylyltransferase
Pssm-ID: 215133 [Multi-domain] Cd Length: 436 Bit Score: 45.23 E-value: 2.44e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 518552395 3 GIILAGGSGTRLYPLTKATSKQLMPV---YDkpMIYYPMSILMLAGIKEILII 52
Cdd:PLN02241 6 AIILGGGAGTRLFPLTKRRAKPAVPIggnYR--LIDIPMSNCINSGINKIYVL 56
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
6-64 |
2.61e-04 |
|
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: 41.03 E-value: 2.61e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 518552395 6 LAGGSGTRLypltKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIISTPqDTPRFEEL 64
Cdd:COG2266 1 MAGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSP-NTPKTREY 54
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
4-209 |
3.69e-04 |
|
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.
Pssm-ID: 133026 [Multi-domain] Cd Length: 231 Bit Score: 41.09 E-value: 3.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYpmSILMLAGIKE---ILIISTPQDTPRF--EELFGNGHDLGIHLeya 78
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEW--VIESLAKIFDsrfIFICRDEHNTKFHldESLKLLAPNATVVE--- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 79 VQESPDGLAQAFIIGEEFI-GDDSVCLVLGDNIYYGGGLSKMLQRAASRESGA--TVFGYHvndpERFGVVEFDENMQAL 155
Cdd:cd04183 77 LDGETLGAACTVLLAADLIdNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGvlTFFSSH----PRWSYVKLDENGRVI 152
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 518552395 156 SIEEKptEPKSNYAVTGLYFYDN--DVISIAKE-IKP--SERGELEITDVNKAYLERGK 209
Cdd:cd04183 153 ETAEK--EPISDLATAGLYYFKSgsLFVEAAKKmIRKddSVNGEFYISPLYNELILDGK 209
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-160 |
6.84e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 40.62 E-value: 6.84e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 4 IILAGGSGTRlypLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILIIStpqdtprfeelfGNGHD--------LGIHL 75
Cdd:PRK14353 9 IILAAGEGTR---MKSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVV------------GPGAEavaaaaakIAPDA 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 76 EYAVQESPDGLAQAFIIGEEFI--GDDSVCLVLGDN-IYYGGGLSKMLQRAASReSGATVFGYHVNDPERFG-VVEFDEN 151
Cdd:PRK14353 74 EIFVQKERLGTAHAVLAAREALagGYGDVLVLYGDTpLITAETLARLRERLADG-ADVVVLGFRAADPTGYGrLIVKGGR 152
|
....*....
gi 518552395 152 MQALsIEEK 160
Cdd:PRK14353 153 LVAI-VEEK 160
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
3-135 |
7.24e-04 |
|
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.
Pssm-ID: 463715 [Multi-domain] Cd Length: 159 Bit Score: 39.49 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLypltkATSKQLMPVYDKPMIYYpmSILMLAGIKEILIISTPqdtprFEELFGNGHDLGIHleYAVQES 82
Cdd:pfam12804 1 AVILAGGRSSRM-----GGDKALLPLGGKPLLER--VLERLRPAGDEVVVVAN-----DEEVLAALAGLGVP--VVPDPD 66
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 518552395 83 PD-----GLAQAFiigEEFIGDDSVCLVLGDNIYYGGG-LSKMLQRAASRESGATVFGY 135
Cdd:pfam12804 67 PGqgplaGLLAAL---RAAPGADAVLVLACDMPFLTPElLRRLLAAAEESGADIVVPVY 122
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
3-52 |
2.99e-03 |
|
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: 37.97 E-value: 2.99e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 518552395 3 GIILAGGSGTRLYPLTKATSKQLMPVYDKPMIYYPMSILMLAGIKEILII 52
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVF 52
|
|
| MobA |
COG0746 |
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ... |
1-64 |
5.77e-03 |
|
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis
Pssm-ID: 440509 [Multi-domain] Cd Length: 188 Bit Score: 37.09 E-value: 5.77e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 518552395 1 MKGIILAGGSGTRLypltkATSKQLMPVYDKPMIYYpmSILMLAGIKEILIISTPQDtPRFEEL 64
Cdd:COG0746 5 ITGVILAGGRSRRM-----GQDKALLPLGGRPLLER--VLERLRPQVDEVVIVANRP-ERYAAL 60
|
|
| |
