|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
3-287 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 545.40 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 3 KVTKAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEARG 82
Cdd:COG1210 2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 83 KEKLLELVRSIKPsHVDCFYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPPVMKQMVDVFDHYHSSVIGVEE 162
Cdd:COG1210 82 KEELLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQE 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 163 IPPSETKSYGIVDGKEWEESIIKMSAIVEKPEPEVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDAIEALLADE 242
Cdd:COG1210 161 VPPEEVSKYGIVDGEEIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKEE 240
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1524947418 243 QVLAYKYQGTRYDCGSKLGYLKATVEFALRHPEVGTEFDAYLRTR 287
Cdd:COG1210 241 PVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-272 |
3.84e-164 |
|
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: 456.22 E-value: 3.84e-164
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 5 TKAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEARGKE 84
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 85 KLLELVRsIKPSHVDCFYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPPVMKQMVDVFDHYHSSVIGVEEIP 164
Cdd:cd02541 81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 165 PSETKSYGIVDGKEWEESIIKMSAIVEKPEPEVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDAIEALLADEQV 244
Cdd:cd02541 160 PEDVSKYGIVKGEKIDGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
|
250 260
....*....|....*....|....*...
gi 1524947418 245 LAYKYQGTRYDCGSKLGYLKATVEFALR 272
Cdd:cd02541 240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
6-265 |
3.37e-151 |
|
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: 423.30 E-value: 3.37e-151
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEARGKEK 85
Cdd:TIGR01099 2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 LLELVRSIKPShVDCFYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPPVMKQMVDVFDHYHSSVIGVEEIPP 165
Cdd:TIGR01099 82 LLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVPK 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 166 SETKSYGIVDGKEWEESIIKMSAIVEKPEPEVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDAIEALLADEQVL 245
Cdd:TIGR01099 161 EEVSKYGVIDGEGIEKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETVL 240
|
250 260
....*....|....*....|
gi 1524947418 246 AYKYQGTRYDCGSKLGYLKA 265
Cdd:TIGR01099 241 AYKFNGKRYDCGSKLGYLEA 260
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
3-286 |
3.96e-102 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 300.67 E-value: 3.96e-102
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 3 KVTKAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEARG 82
Cdd:PRK13389 7 KVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRV 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 83 KEKLLELVRSIKPSHVDCFYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPPVMKQ-----MVDVFDHYHSSV 157
Cdd:PRK13389 87 KRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHSQ 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 158 IGVEeiPPSETKSYGIVDGKEWE----ESiIKMSAIVEKPEPEVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTD 233
Cdd:PRK13389 167 IMVE--PVADVTAYGVVDCKGVElapgES-VPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 1524947418 234 AIEALLADEQVLAYKYQGTRYDCGSKLGYLKATVEFALRHPEVGTEFDAYLRT 286
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEE 296
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
6-280 |
1.14e-85 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 258.67 E-value: 1.14e-85
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEARGKEK 85
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 LLELVRSIKPSHVDCFYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNP--PV---MKQMVDVFDHYHSSVIGV 160
Cdd:PRK10122 85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASadPLrynLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 161 EEIpPSETKSYGIVDGKEWEESIIKMSAIV---EKPE-PEVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDAIE 236
Cdd:PRK10122 165 KRM-PGDLSEYSVIQTKEPLDREGKVSRIVefiEKPDqPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 1524947418 237 ALLADEQVLAYKYQGTRYDCGSKLGYLKATVEFALRHPEVGTEF 280
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKF 287
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
7-257 |
5.42e-54 |
|
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: 174.69 E-value: 5.42e-54
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 7 AVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEieaeleargkekl 86
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 87 lelvrsikpSHVDCFYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNppvMKQMVDvFDHYHSSVIGVEEIPPS 166
Cdd:cd04181 68 ---------FGVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLR-FHREKGADATIAVKEVE 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 167 ETKSYGIVDGKEWEesiiKMSAIVEKPEPEvaPSNLGVVGRYILKPRIFEHLRALKPgaGGELQLTDAIEALLADEQVLA 246
Cdd:cd04181 135 DPSRYGVVELDDDG----RVTRFVEKPTLP--ESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYG 206
|
250
....*....|.
gi 1524947418 247 YKYQGTRYDCG 257
Cdd:cd04181 207 YPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-265 |
1.18e-48 |
|
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: 161.58 E-value: 1.18e-48
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEargkek 85
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRIT------ 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 llelvrsikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNppvMKQMVDVFDHYHSSV-IGVEEIP 164
Cdd:cd04189 76 ----------------YILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDADAsILLAEVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 165 -PSetkSYGIVDGKEweESIIKmsaIVEKPEPEvaPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDAIEALLAD-E 242
Cdd:cd04189 137 dPR---RFGVAVVDD--GRIVR---LVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRgR 206
|
250 260
....*....|....*....|...
gi 1524947418 243 QVLAYKYQGTRYDCGSKLGYLKA 265
Cdd:cd04189 207 RVGYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
6-259 |
5.27e-47 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 159.10 E-value: 5.27e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAiedhfdksyEIEAELEaRGKEK 85
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEDGP---------QFERLLG-DGSQL 71
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 LLELVrsikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNppVMKQMVDVFDHYHS-SVIGVEEIP 164
Cdd:COG1209 72 GIKIS-----------YAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGD--GLSELLREAAARESgATIFGYKVE 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 165 -PSetkSYGIV----DGKeweesIIKmsaIVEKPEpeVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDAIEALL 239
Cdd:COG1209 139 dPE---RYGVVefdeDGR-----VVS---LEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYL 205
|
250 260
....*....|....*....|..
gi 1524947418 240 ADEQ-VLAYKYQGTR-YDCGSK 259
Cdd:COG1209 206 ERGKlVVELLGRGFAwLDTGTH 227
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-265 |
4.25e-38 |
|
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: 134.51 E-value: 4.25e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEargkek 85
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRIT------ 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 llelvrsikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNppvMKQMVDVFDHYHS--SVIGVEEI 163
Cdd:COG1208 75 ----------------YVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLD---LAALLAFHREKGAdaTLALVPVP 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 164 PPSEtksYGIVDGKEWEesiiKMSAIVEKpePEVAPSNLGVVGRYILKPRIFEHLRalkpgAGGELQLTDAIEALLADEQ 243
Cdd:COG1208 136 DPSR---YGVVELDGDG----RVTRFVEK--PEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGR 201
|
250 260
....*....|....*....|..
gi 1524947418 244 VLAYKYQGTRYDCGSKLGYLKA 265
Cdd:COG1208 202 VYGYVHDGYWLDIGTPEDLLEA 223
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-266 |
7.22e-24 |
|
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: 96.94 E-value: 7.22e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDK-PLIQYAVEEAIAAGITEMIFVTGRSKRA-IEDHFDKSYEIEAELEargk 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQEHRFmLNELLGDGSKFGVQIT---- 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 84 ekllelvrsikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPF-AVILADDLLDGNPPvmKQMVDVFDHYHS----SVI 158
Cdd:pfam00483 77 ------------------YALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRMDL--EQAVKFHIEKAAdatvTFG 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 159 GVEEIPPSEtksYGIVdgKEWEESIIKmsAIVEKPEPEVApSNLGVVGRYILKPRIFEHL-RALKPGAGGELQLTDAIEA 237
Cdd:pfam00483 137 IVPVEPPTG---YGVV--EFDDNGRVI--RFVEKPKLPKA-SNYASMGIYIFNSGVLDFLaKYLEELKRGEDEITDILPK 208
|
250 260 270
....*....|....*....|....*....|..
gi 1524947418 238 LLADEQVlAYKYQGTRY---DCGSKLGYLKAT 266
Cdd:pfam00483 209 ALEDGKL-AYAFIFKGYawlDVGTWDSLWEAN 239
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
6-233 |
5.86e-22 |
|
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: 91.87 E-value: 5.86e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRskraiED--HFDKsyeieaeLEARGK 83
Cdd:cd02538 2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP-----EDlpLFKE-------LLGDGS 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 84 EKLLELVrsikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPpvMKQMVDVFDHYHS--SVIGVE 161
Cdd:cd02538 70 DLGIRIT-----------YAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQG--LSPILQRAAAQKEgaTVFGYE 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1524947418 162 EIPPSEtksYGIVdgkEWEESIiKMSAIVEKPEpeVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTD 233
Cdd:cd02538 137 VNDPER---YGVV---EFDENG-RVLSIEEKPK--KPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
2-266 |
5.17e-15 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 73.55 E-value: 5.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 2 LKVTKAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFV-----TGRSKRAIEDhfdksyeiea 76
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIstpqdTPRFQQLLGD---------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 77 elearGKEKLLELVRSIKPShvdcfyvrqPEalGLGHAVLCAEKLVADNPFAVILADDLLDGN--PPVMKQMVDvfdhyH 154
Cdd:PRK15480 71 -----GSQWGLNLQYKVQPS---------PD--GLAQAFIIGEEFIGGDDCALVLGDNIFYGHdlPKLMEAAVN-----K 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 155 SSVIGVEEIPPSETKSYGIVDGKEweesiiKMSAIVEKPEPEVAPSNLGVVGRYILKPRIFEHLRALKPGAGGELQLTDa 234
Cdd:PRK15480 130 ESGATVFAYHVNDPERYGVVEFDQ------NGTAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD- 202
|
250 260 270
....*....|....*....|....*....|....*
gi 1524947418 235 IEALLADEQVLAYKYQGTRY---DCGSKLGYLKAT 266
Cdd:PRK15480 203 INRIYMEQGRLSVAMMGRGYawlDTGTHQSLIEAS 237
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
13-265 |
6.51e-15 |
|
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is involved in the biosynthesis, export or translocation of capsule. It is a subfamily of nucleotidyl transferases that transfer nucleotides onto phosphosugars.
Pssm-ID: 133065 [Multi-domain] Cd Length: 223 Bit Score: 72.20 E-value: 6.51e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 13 GLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELEargkekllelvrs 92
Cdd:cd06915 7 GLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIY------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 93 ikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNppvMKQMVDVFDHyHSSVIGVEEIPPSETKSYG 172
Cdd:cd06915 74 ---------YVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDVD---LLALLAALRA-SGADATMALRRVPDASRYG 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 173 --IVDGkewEESIIkmsAIVEK-PEPEVAPSNLGVvgrYILKPRIFEHLRALKPgaggeLQLTDAIEALLADEQVLAYKY 249
Cdd:cd06915 141 nvTVDG---DGRVI---AFVEKgPGAAPGLINGGV---YLLRKEILAEIPADAF-----SLEADVLPALVKRGRLYGFEV 206
|
250
....*....|....*.
gi 1524947418 250 QGTRYDCGSKLGYLKA 265
Cdd:cd06915 207 DGYFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
13-241 |
1.77e-14 |
|
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: 71.00 E-value: 1.77e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 13 GLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHF----DKSYEIEaeleargkeklle 88
Cdd:cd06426 7 GKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFgdgsKFGVNIS------------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 89 lvrsikpshvdcfYVRQPEALGLGHAV-LCAEKLvaDNPFAVILADDLLDGNPpvmKQMVDvFDHYHSSVIGVE------ 161
Cdd:cd06426 74 -------------YVREDKPLGTAGALsLLPEKP--TDPFLVMNGDILTNLNY---EHLLD-FHKENNADATVCvreyev 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 162 EIPpsetksYGIVDGKEweesiIKMSAIVEKPEpEVAPSNLGVvgrYILKPRIFEHlraLKPGAggELQLTDAIEALLAD 241
Cdd:cd06426 135 QVP------YGVVETEG-----GRITSIEEKPT-HSFLVNAGI---YVLEPEVLDL---IPKNE--FFDMPDLIEKLIKE 194
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-75 |
7.65e-13 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 66.49 E-value: 7.65e-13
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524947418 7 AVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIE 75
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK 69
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-266 |
9.86e-12 |
|
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: 63.38 E-value: 9.86e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIF-VTGRSKRAIEdhFDKSYEIEAELEargke 84
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPEDMVP--FLKEYEKKLGIK----- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 85 kllelvrsIKPSHVDcfyvrqpEALGLGHAVLCAEKLVA--DNPFAViLADDLLDGNPpvMKQMVDvFDHYHSS-----V 157
Cdd:cd06425 75 --------ITFSIET-------EPLGTAGPLALARDLLGddDEPFFV-LNSDVICDFP--LAELLD-FHKKHGAegtilV 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 158 IGVEEipPSEtksYGIVDGKEwEESIIKmsAIVEKPEPEVapSNLGVVGRYILKPRIFEHLralkpgaggELQLTdAIE- 236
Cdd:cd06425 136 TKVED--PSK---YGVVVHDE-NTGRIE--RFVEKPKVFV--GNKINAGIYILNPSVLDRI---------PLRPT-SIEk 195
|
250 260 270
....*....|....*....|....*....|....
gi 1524947418 237 ----ALLADEQVLAYKYQGTRYDCGSKLGYLKAT 266
Cdd:cd06425 196 eifpKMASEGQLYAYELPGFWMDIGQPKDFLKGM 229
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-249 |
7.48e-11 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 61.03 E-value: 7.48e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGrskraiedhfdksYEieaeleargKEK 85
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTG-------------YK---------AEL 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 LLELVRSIKPsHVDCFYVRQPEALGLGHAVLCAEKLVADnPFAVILADDLLDgnPPVMKQMVdvfDHYHSSVIGV----E 161
Cdd:COG1213 59 IEEALARPGP-DVTFVYNPDYDETNNIYSLWLAREALDE-DFLLLNGDVVFD--PAILKRLL---ASDGDIVLLVdrkwE 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 162 EIPPSETKSYGIVDGKeweesIIKMSaivEKPEPEVApsnlgvVGRYI--------LKPRIFEHLRALKPGAGGELQLTD 233
Cdd:COG1213 132 KPLDEEVKVRVDEDGR-----IVEIG---KKLPPEEA------DGEYIgifkfsaeGAAALREALEALIDEGGPNLYYED 197
|
250
....*....|....*.
gi 1524947418 234 AIEALLADEQVLAYKY 249
Cdd:COG1213 198 ALQELIDEGGPVKAVD 213
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-143 |
2.68e-10 |
|
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: 59.12 E-value: 2.68e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFdksyeieaeleaRGKEK 85
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL------------GDSRF 68
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524947418 86 LLELVRSIKPshvdcfyvrqPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPPVM 143
Cdd:cd06422 69 GLRITISDEP----------DELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPL 116
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
12-248 |
1.10e-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: 58.50 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 12 AGLGTRFLPATkasPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDksyeieaeleargkekllelvr 91
Cdd:COG1207 10 AGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALA---------------------- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 92 sikpsHVDCFYVRQPEALGLGHAVLCAEKLVADNPFAV-ILADD--LLDgnPPVMKQMVDVF--DHYHSSVIGVEEIPPS 166
Cdd:COG1207 65 -----DLDVEFVLQEEQLGTGHAVQQALPALPGDDGTVlVLYGDvpLIR--AETLKALLAAHraAGAAATVLTAELDDPT 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 167 etkSYG-IV---DGkeweesiiKMSAIVE----KPE----PEVapsNLGVvgrYILK-PRIFEHLRALKPG-AGGELQLT 232
Cdd:COG1207 138 ---GYGrIVrdeDG--------RVLRIVEekdaTEEqraiREI---NTGI---YAFDaAALREALPKLSNDnAQGEYYLT 200
|
250
....*....|....*..
gi 1524947418 233 DAIEALLAD-EQVLAYK 248
Cdd:COG1207 201 DVIAIARADgLKVAAVQ 217
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-72 |
7.82e-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: 54.57 E-value: 7.82e-09
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSY 72
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSK 68
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
12-247 |
3.71e-08 |
|
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: 52.90 E-value: 3.71e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 12 AGLGTRFlpatKAS-PKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRskraiedhfdksyeieaelearGKEKLLELV 90
Cdd:cd02540 6 AGKGTRM----KSDlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGH----------------------GAEQVKKAL 59
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 91 rsikpSHVDCFYVRQPEALGLGHAVLCA-EKLVADNPFAVILADD--LLDGNppVMKQMVDVFDHYHS--SVIGVEeipP 165
Cdd:cd02540 60 -----ANPNVEFVLQEEQLGTGHAVKQAlPALKDFEGDVLVLYGDvpLITPE--TLQRLLEAHREAGAdvTVLTAE---L 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 166 SETKSYG--IVDGKEweesiiKMSAIVE--------KPEPEVapsNLGVvgrYILK-PRIFEHLRALKP-GAGGELQLTD 233
Cdd:cd02540 130 EDPTGYGriIRDGNG------KVLRIVEekdateeeKAIREV---NAGI---YAFDaEFLFEALPKLTNnNAQGEYYLTD 197
|
250
....*....|....
gi 1524947418 234 AIEALLADEQVLAY 247
Cdd:cd02540 198 IIALAVADGLKVAA 211
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-73 |
4.13e-08 |
|
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: 52.66 E-value: 4.13e-08
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1524947418 6 KAVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITE-MIFVTGRSKRAIEDHFDKSYE 73
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDvIVVVPEEEQAEISTYLRSFPL 70
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
8-248 |
5.26e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 53.83 E-value: 5.26e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 8 VFPVAGLGTRFlpaTKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRaiedhfdksyEIEAELEARGkekll 87
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAE----------QVEAALQGSG----- 72
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 88 elVRsikpshvdcfYVRQPEALGLGHAVLC-AEKLVADNPFAVILADDLLDGNPPVMKQMVDvfDHY-HSSVIGVEEIPP 165
Cdd:PRK14358 73 --VA----------FARQEQQLGTGDAFLSgASALTEGDADILVLYGDTPLLRPDTLRALVA--DHRaQGSAMTILTGEL 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 166 SETKSYG-IVDGKEWE-ESIIKMSAIVEKpEPEVAPSNLGVvgrYILKPRIFEHLRAL-KPGAGGELQLTDAIEALLAD- 241
Cdd:PRK14358 139 PDATGYGrIVRGADGAvERIVEQKDATDA-EKAIGEFNSGV---YVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGg 214
|
....*..
gi 1524947418 242 EQVLAYK 248
Cdd:PRK14358 215 AQVRAFK 221
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-248 |
1.25e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 52.53 E-value: 1.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 7 AVFPVAGLGTRFlpatKAS-PKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRskraiedhfdKSYEIEAELEARGKek 85
Cdd:PRK14354 5 AIILAAGKGTRM----KSKlPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGH----------GAEEVKEVLGDRSE-- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 llelvrsikpshvdcfYVRQPEALGLGHAVLCAEKLVADNPFAVIladdLLDGNPPV-----MKQMVD--VFDHYHSSVI 158
Cdd:PRK14354 69 ----------------FALQEEQLGTGHAVMQAEEFLADKEGTTL----VICGDTPLitaetLKNLIDfhEEHKAAATIL 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 159 GVEEIPPSetkSYG-IVdgKEWEESIIKmsaIVE-----KPEPEVAPSNLGVvgrYIL-KPRIFEHLRALKP-GAGGELQ 230
Cdd:PRK14354 129 TAIAENPT---GYGrII--RNENGEVEK---IVEqkdatEEEKQIKEINTGT---YCFdNKALFEALKKISNdNAQGEYY 197
|
250
....*....|....*....
gi 1524947418 231 LTDAIEALLAD-EQVLAYK 248
Cdd:PRK14354 198 LTDVIEILKNEgEKVGAYQ 216
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
7-71 |
5.17e-07 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 49.53 E-value: 5.17e-07
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1524947418 7 AVFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKS 71
Cdd:cd04197 3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS 67
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-236 |
7.63e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 50.15 E-value: 7.63e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 6 KAVFPVAGLGTRFlpaTKASPKEMLPVVDKPLIQYAVEEAIAAGiTEMIFVTGRSKraiedhfdksyeieaeleargkek 85
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEA------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 86 llELVRSIKPSHVDCFYvrQPEALGLGHAVLCAEKLVADNPFAVILADDLLDGNPPVMKQMVD--VFDHYHSSVIGVEEI 163
Cdd:PRK14357 54 --ELVKKLLPEWVKIFL--QEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEehNRKGADVTILVADLE 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 164 PPS-------ETKSYGIVDGKEWEESIIKMSAIvekpepevapsNLGVvgrYILKPR-IFEHLRALKP-GAGGELQLTDA 234
Cdd:PRK14357 130 DPTgygriirDGGKYRIVEDKDAPEEEKKIKEI-----------NTGI---YVFSGDfLLEVLPKIKNeNAKGEYYLTDA 195
|
..
gi 1524947418 235 IE 236
Cdd:PRK14357 196 VN 197
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-118 |
9.47e-07 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 49.74 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 7 AVFPVAGLGTRFlpaTKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFDKSYEIEAELeargkekl 86
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL-------- 74
|
90 100 110
....*....|....*....|....*....|..
gi 1524947418 87 lelvrsikpshvdcfyvrQPEALGLGHAVLCA 118
Cdd:PRK14355 75 ------------------QEEQLGTGHAVACA 88
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
12-158 |
6.65e-06 |
|
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: 45.63 E-value: 6.65e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 12 AGLGTRFlpatkASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGrskraiedhfDKSYEIEAELEARGkekllelvr 91
Cdd:cd04182 8 AGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG----------AEADAVRAALAGLP--------- 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1524947418 92 sikpshVDCFYVRQPEaLGLGHAVLCA-EKLVADNPFAVILADDLLDGNPPVMKQMVDVFDHYHSSVI 158
Cdd:cd04182 64 ------VVVVINPDWE-EGMSSSLAAGlEALPADADAVLILLADQPLVTAETLRALIDAFREDGAGIV 124
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
12-136 |
3.72e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 44.85 E-value: 3.72e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1524947418 12 AGLGTRFlpatKAS-PKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHfdksyeieaeleargkekllelV 90
Cdd:PRK14353 13 AGEGTRM----KSSlPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAA----------------------A 66
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 1524947418 91 RSIKPSHVdcfYVRQPEALGLGHAVLCAEKLVADNpfavilADDLL 136
Cdd:PRK14353 67 AKIAPDAE---IFVQKERLGTAHAVLAAREALAGG------YGDVL 103
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
12-69 |
3.82e-05 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 43.61 E-value: 3.82e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1524947418 12 AGLGTRFlpatkASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTGRSKRAIEDHFD 69
Cdd:COG2068 11 AGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA 63
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
8-71 |
3.61e-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: 3.61e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1524947418 8 VFPVAGLGTRFLPATKASPKEMLPVVDKPLIQYAVEEAIAAGITEMIFVTgrSKRAIEDHFDKS 71
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLDE 63
|
|
| |
