|
Name |
Accession |
Description |
Interval |
E-value |
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
2-286 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 528.45 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 2 KPIRKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELEMR 81
Cdd:COG1210 1 MKIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAK 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 82 HKDKLLEHVRNILPPnITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSILGVE 161
Cdd:COG1210 81 GKEELLEEVRSISPL-ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKPCLKQMIEVYEETGGSVIAVQ 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 162 TVEASQTGSYGIVETEQL-KQFQRITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGIAKLLDH 240
Cdd:COG1210 160 EVPPEEVSKYGIVDGEEIeGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAKE 239
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 488154311 241 EFVLAHPFEGTRYDCGSKLGYLEATVAYGLKHPETGEPFRRLLEKY 286
Cdd:COG1210 240 EPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-264 |
8.08e-167 |
|
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: 462.59 E-value: 8.08e-167
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 5 RKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELEMRHKD 84
Cdd:TIGR01099 1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 85 KLLEHVRNILPPnITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSILGVETVE 164
Cdd:TIGR01099 81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEPALKQMIKAYEKTGCSIIAVQEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 165 ASQTGSYGIVETEQLKQFQ-RITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGIAKLLDHEFV 243
Cdd:TIGR01099 160 KEEVSKYGVIDGEGIEKDLyKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLENETV 239
|
250 260
....*....|....*....|.
gi 488154311 244 LAHPFEGTRYDCGSKLGYLEA 264
Cdd:TIGR01099 240 LAYKFNGKRYDCGSKLGYLEA 260
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-271 |
9.53e-163 |
|
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: 452.76 E-value: 9.53e-163
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 5 RKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELEMRHKD 84
Cdd:cd02541 1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 85 KLLEHVRnILPPNITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSILGVETVE 164
Cdd:cd02541 81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSKEPCLKQLIEAYEKTGASVIAVEEVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 165 ASQTGSYGIVETEQL-KQFQRITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGIAKLLDHEFV 243
Cdd:cd02541 160 PEDVSKYGIVKGEKIdGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLEEEPV 239
|
250 260
....*....|....*....|....*...
gi 488154311 244 LAHPFEGTRYDCGSKLGYLEATVAYGLK 271
Cdd:cd02541 240 YAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
2-284 |
5.89e-104 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 305.29 E-value: 5.89e-104
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 2 KPIRKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELEMR 81
Cdd:PRK13389 6 TKVKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKR 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 82 HKDKLLEHVRNILPPNITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQ-----MVEVYGRSGNS 156
Cdd:PRK13389 86 VKRQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQdnlaeMIRRFDETGHS 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 157 ILGVETVEasQTGSYGIVETE--QLKQFQR--ITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTD 232
Cdd:PRK13389 166 QIMVEPVA--DVTAYGVVDCKgvELAPGESvpMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTD 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 488154311 233 GIAKLLDHEFVLAHPFEGTRYDCGSKLGYLEATVAYGLKHPETGEPFRRLLE 284
Cdd:PRK13389 244 AIDMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLE 295
|
|
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
6-285 |
8.19e-88 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 264.06 E-value: 8.19e-88
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELEMRHKDK 85
Cdd:PRK10122 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 86 LLEHVRNILPPNITCLYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKG-----ALKQMVEVYGRSGNSILGV 160
Cdd:PRK10122 85 LLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASAdplryNLAAMIARFNETGRSQVLA 164
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 161 ETVEASQTgSYGIVETEQL----KQFQRITGIVEKP-KPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGIA 235
Cdd:PRK10122 165 KRMPGDLS-EYSVIQTKEPldreGKVSRIVEFIEKPdQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDAIA 243
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|
gi 488154311 236 KLLDHEFVLAHPFEGTRYDCGSKLGYLEATVAYGLKHPETGEPFRRLLEK 285
Cdd:PRK10122 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEK 293
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
7-256 |
2.60e-57 |
|
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: 183.17 E-value: 2.60e-57
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 7 AVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYEletelemrhkdkl 86
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSK------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 87 lehvrniLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPkgaLKQMVEVYGRSGN--SILGVETVE 164
Cdd:cd04181 68 -------FGVNIE--YVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDLD---LSELLRFHREKGAdaTIAVKEVED 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 165 ASQtgsYGIVETEqlkQFQRITGIVEKPKPEdaPSNLAVVGRYILTPRIFDLLtnLPRGAGNEIQLTDGIAKLLDHEFVL 244
Cdd:cd04181 136 PSR---YGVVELD---DDGRVTRFVEKPTLP--ESNLANAGIYIFEPEILDYI--PEILPRGEDELTDAIPLLIEEGKVY 205
|
250
....*....|..
gi 488154311 245 AHPFEGTRYDCG 256
Cdd:cd04181 206 GYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
6-264 |
1.05e-51 |
|
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: 169.29 E-value: 1.05e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYEletelemrhkdk 85
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSR------------ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 86 llehvrniLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPkgaLKQMVEVYGRSG-NSILGVETVE 164
Cdd:cd04189 70 --------FGVRIT--YILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEG---ISPLVRDFLEEDaDASILLAEVE 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 165 asQTGSYGIVETEQlkqfQRITGIVEKPKPEdaPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGIAKLLDHEF-V 243
Cdd:cd04189 137 --DPRRFGVAVVDD----GRIVRLVEKPKEP--PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRrV 208
|
250 260
....*....|....*....|.
gi 488154311 244 LAHPFEGTRYDCGSKLGYLEA 264
Cdd:cd04189 209 GYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-264 |
2.29e-45 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 154.86 E-value: 2.29e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 5 RKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNkrsiedhfdkayeletelemrhkd 84
Cdd:COG1209 1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPE------------------------ 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 85 kLLEHVRNIL------PPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDApkGALKQMVEVY--GRSGNS 156
Cdd:COG1209 57 -DGPQFERLLgdgsqlGIKIS--YAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG--DGLSELLREAaaRESGAT 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 157 ILG--VETVEAsqtgsYGIVEteqLKQFQRITGIVEKPKpeDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGI 234
Cdd:COG1209 132 IFGykVEDPER-----YGVVE---FDEDGRVVSLEEKPK--EPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDAN 201
|
250 260 270
....*....|....*....|....*....|..
gi 488154311 235 AKLLDHEF-VLAHPFEGTR-YDCGSKLGYLEA 264
Cdd:COG1209 202 QAYLERGKlVVELLGRGFAwLDTGTHESLLEA 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
6-264 |
2.22e-43 |
|
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: 147.99 E-value: 2.22e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYEletelemrhkdk 85
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSR------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 86 llehvrniLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPkgaLKQMVEVYGRSGN--SILGVETv 163
Cdd:COG1208 69 --------FGVRIT--YVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTDLD---LAALLAFHREKGAdaTLALVPV- 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 164 eaSQTGSYGIVETEqlkQFQRITGIVEkpKPEDAPSNLAVVGRYILTPRIFDLLTnlprgAGNEIQLTDGIAKLLDHEFV 243
Cdd:COG1208 135 --PDPSRYGVVELD---GDGRVTRFVE--KPEEPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIAEGRV 202
|
250 260
....*....|....*....|.
gi 488154311 244 LAHPFEGTRYDCGSKLGYLEA 264
Cdd:COG1208 203 YGYVHDGYWLDIGTPEDLLEA 223
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
6-268 |
1.16e-27 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 106.95 E-value: 1.16e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDK-PLIQYAVEEAVEAGCTEMVFVTG-RNKRSIEDHFDKAYELETELemrhk 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELLGDGSKFGVQI----- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 84 dkllehvrnilppnitcLYIRQAEALGLGHAVLCARAAIGDEPF-AVILADDLI--DAPKGALKQMVEVYGRSGNSILGV 160
Cdd:pfam00483 76 -----------------TYALQPEGKGTAPAVALAADFLGDEKSdVLVLGGDHIyrMDLEQAVKFHIEKAADATVTFGIV 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 161 ETVEASqtgSYGIVETEQLkqfQRITGIVEKPKpEDAPSNLAVVGRYILTPRIFD-LLTNLPRGAGNEIQLTDGIAKLL- 238
Cdd:pfam00483 139 PVEPPT---GYGVVEFDDN---GRVIRFVEKPK-LPKASNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALe 211
|
250 260 270
....*....|....*....|....*....|.
gi 488154311 239 DHEFVLAHPFEGTR-YDCGSKLGYLEATVAY 268
Cdd:pfam00483 212 DGKLAYAFIFKGYAwLDVGTWDSLWEANLFL 242
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-232 |
3.57e-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: 92.25 E-value: 3.57e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 5 RKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRnkrsiEDhfdkayeleteleMRHKD 84
Cdd:cd02538 1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP-----ED-------------LPLFK 62
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 85 KLLEHVRNiLPPNITclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAP--KGALKQMVEVygRSGNSILGVET 162
Cdd:cd02538 63 ELLGDGSD-LGIRIT--YAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGQglSPILQRAAAQ--KEGATVFGYEV 137
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 163 VEASQtgsYGIVEteqLKQFQRITGIVEKPKpeDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTD 232
Cdd:cd02538 138 NDPER---YGVVE---FDENGRVLSIEEKPK--KPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
13-240 |
2.45e-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: 70.23 E-value: 2.45e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 13 GMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFdkayeletelemrhkdkllehvRN 92
Cdd:cd06426 7 GKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF----------------------GD 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 93 ILPPNITCLYIRQAEALGLGHAVLCARAAIgDEPFAVILADDLIDAPKGALKQmvevYGRSGNSILGVETVEASQTGSYG 172
Cdd:cd06426 65 GSKFGVNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNLNYEHLLD----FHKENNADATVCVREYEVQVPYG 139
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 488154311 173 IVETEQlkqfQRITGIVEKPKpedaPSNLAVVGRYILTPRIFDLLTNlprgaGNEIQLTDGIAKLLDH 240
Cdd:cd06426 140 VVETEG----GRITSIEEKPT----HSFLVNAGIYVLEPEVLDLIPK-----NEFFDMPDLIEKLIKE 194
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
12-235 |
3.61e-14 |
|
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: 71.98 E-value: 3.61e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFLPATkasPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFdkayeletelemrhkdkllehvr 91
Cdd:COG1207 10 AGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL----------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 92 nilpPNITCLYIRQAEALGLGHAVLCARAAI-GDEPFAVILADD--LIDApkGALKQMVEVYGRSGNSiLGVETVEASQT 168
Cdd:COG1207 64 ----ADLDVEFVLQEEQLGTGHAVQQALPALpGDDGTVLVLYGDvpLIRA--ETLKALLAAHRAAGAA-ATVLTAELDDP 136
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 488154311 169 GSYG-IVETEQlkqfQRITGIVE-KpkpeDA-PSNLAV----VGRYIL-TPRIFDLLTNL-PRGAGNEIQLTDGIA 235
Cdd:COG1207 137 TGYGrIVRDED----GRVLRIVEeK----DAtEEQRAIreinTGIYAFdAAALREALPKLsNDNAQGEYYLTDVIA 204
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
7-249 |
3.97e-14 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 72.08 E-value: 3.97e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 7 AVFPVAGMGTRFlpaTKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELemrhkdkl 86
Cdd:PRK14355 6 AIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL-------- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 87 lehvrnilppnitclyirQAEALGLGHAVLCARAAIgdEPFA---VILADD--LIDApkGALKQMVEVYGRSGnSILGVE 161
Cdd:PRK14355 75 ------------------QEEQLGTGHAVACAAPAL--DGFSgtvLILCGDvpLLRA--ETLQGMLAAHRATG-AAVTVL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 162 TVEASQTGSYGIVeteqLKQFQ-RITGIVEK--PKPEDAPSNLAVVGRY-ILTPRIFDLLTNLPR-GAGNEIQLTDGIAK 236
Cdd:PRK14355 132 TARLENPFGYGRI----VRDADgRVLRIVEEkdATPEERSIREVNSGIYcVEAAFLFDAIGRLGNdNAQGEYYLTDIVAM 207
|
250
....*....|....
gi 488154311 237 LLDHEF-VLAHPFE 249
Cdd:PRK14355 208 AAAEGLrCLAFPVA 221
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
6-268 |
4.03e-14 |
|
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: 69.93 E-value: 4.03e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTgrNKRSiedhfdkayeletELEMRHKDK 85
Cdd:cd06425 2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAV--NYRP-------------EDMVPFLKE 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 86 LLEHvrnilpPNITCLYIRQAEALGLGHAVLCARAAIG--DEPFAVILADDLIDAPkgaLKQMVEVYGRSGN--SILgVE 161
Cdd:cd06425 67 YEKK------LGIKITFSIETEPLGTAGPLALARDLLGddDEPFFVLNSDVICDFP---LAELLDFHKKHGAegTIL-VT 136
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 162 TVEasQTGSYGIVETEQLKqfQRITGIVEKPKpeDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIqltdgIAKLLDHE 241
Cdd:cd06425 137 KVE--DPSKYGVVVHDENT--GRIERFVEKPK--VFVGNKINAGIYILNPSVLDRIPLRPTSIEKEI-----FPKMASEG 205
|
250 260
....*....|....*....|....*..
gi 488154311 242 FVLAHPFEGTRYDCGSKLGYLEATVAY 268
Cdd:cd06425 206 QLYAYELPGFWMDIGQPKDFLKGMSLY 232
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
12-235 |
1.54e-13 |
|
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: 68.31 E-value: 1.54e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFlpatKAS-PKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedhfdkayeletelemrHKdklLEHV 90
Cdd:cd02540 6 AGKGTRM----KSDlPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVG-----------------------HG---AEQV 55
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 91 RNILP-PNITclYIRQAEALGLGHAVLCARAAIGDEPFAV-ILADD--LIDApkGALKQMVEVYGRSGNSIlGVETVEAS 166
Cdd:cd02540 56 KKALAnPNVE--FVLQEEQLGTGHAVKQALPALKDFEGDVlVLYGDvpLITP--ETLQRLLEAHREAGADV-TVLTAELE 130
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488154311 167 QTGSYG-IVeteqLKQFQRITGIVEKpkpEDA-PSNLAVV----GRYIL-TPRIFDLLTNL-PRGAGNEIQLTDGIA 235
Cdd:cd02540 131 DPTGYGrII----RDGNGKVLRIVEE---KDAtEEEKAIRevnaGIYAFdAEFLFEALPKLtNNNAQGEYYLTDIIA 200
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
7-76 |
9.38e-12 |
|
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.
Pssm-ID: 133014 [Multi-domain] Cd Length: 229 Bit Score: 63.41 E-value: 9.38e-12
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 7 AVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELET 76
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF 70
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
6-148 |
1.28e-11 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 62.95 E-value: 1.28e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedhfdkaYeletelemrHKDK 85
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTG-------------Y---------KAEL 58
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488154311 86 LLEHVRNIlPPNITCLYIRQAEALGLGHAVLCARAAIgDEPFAVILADDLIDapKGALKQMVE 148
Cdd:COG1213 59 IEEALARP-GPDVTFVYNPDYDETNNIYSLWLAREAL-DEDFLLLNGDVVFD--PAILKRLLA 117
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
5-265 |
1.47e-11 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 63.54 E-value: 1.47e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 5 RKAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFV-----TGRNKRSIEDHFDKAYELEtele 79
Cdd:PRK15480 4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIstpqdTPRFQQLLGDGSQWGLNLQ---- 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 80 mrhkdkllehvrnilppnitclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLI---DAPKgalKQMVEVYGRSGNS 156
Cdd:PRK15480 80 ----------------------YKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFyghDLPK---LMEAAVNKESGAT 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 157 ILGVETVEASQtgsYGIVETEqlkqfQRITGIVEKPKPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDgIAK 236
Cdd:PRK15480 135 VFAYHVNDPER---YGVVEFD-----QNGTAISLEEKPLQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD-INR 205
|
250 260 270
....*....|....*....|....*....|..
gi 488154311 237 LLDHEFVLAHPFEGTRY---DCGSKLGYLEAT 265
Cdd:PRK15480 206 IYMEQGRLSVAMMGRGYawlDTGTHQSLIEAS 237
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
13-264 |
1.95e-11 |
|
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: 62.19 E-value: 1.95e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 13 GMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYeletELEMRHKdkllehvrn 92
Cdd:cd06915 7 GLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGY----RGGIRIY--------- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 93 ilppnitclYIRQAEALGLGHAVLCARAAIGDEPFAVILADDLIDApkgALKQMVEVYGRSG--NSILGVETVEASQtgs 170
Cdd:cd06915 74 ---------YVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFDV---DLLALLAALRASGadATMALRRVPDASR--- 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 171 YGIVETEqlkQFQRITGIVEkpKPEDAPSNLAVVGRYILTPRIFDLLTNLPRGAgneiqLTDGIAKLLDHEFVLAHPFEG 250
Cdd:cd06915 139 YGNVTVD---GDGRVIAFVE--KGPGAAPGLINGGVYLLRKEILAEIPADAFSL-----EADVLPALVKRGRLYGFEVDG 208
|
250
....*....|....
gi 488154311 251 TRYDCGSKLGYLEA 264
Cdd:cd06915 209 YFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-264 |
8.36e-11 |
|
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: 60.28 E-value: 8.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVfvtgrnkrsIEDHFdkayeletelemrHKDK 85
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIV---------VNTHH-------------LADQ 58
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 86 LLEHVRN-ILPPNITclYIR-QAEALGLGHAVLCARAAIGDEPFAVILAD-----DLIDAPKGALKQMvevygrsGNSIL 158
Cdd:cd06422 59 IEAHLGDsRFGLRIT--ISDePDELLETGGGIKKALPLLGDEPFLVVNGDilwdgDLAPLLLLHAWRM-------DALLL 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 159 GVETVEASQTGSYGIVETEQLKQFQRitgivekpKPEDAPSNLAVVGRYILTPRIFDlltNLPRGAGNEIQLTDgiaKLL 238
Cdd:cd06422 130 LLPLVRNPGHNGVGDFSLDADGRLRR--------GGGGAVAPFTFTGIQILSPELFA---GIPPGKFSLNPLWD---RAI 195
|
250 260
....*....|....*....|....*.
gi 488154311 239 DHEFVLAHPFEGTRYDCGSKLGYLEA 264
Cdd:cd06422 196 AAGRLFGLVYDGLWFDVGTPERLLAA 221
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
12-190 |
1.43e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 58.33 E-value: 1.43e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFlpatKAS-PKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRnkrsiedhfdkayeletelemrHKDKLLEHV 90
Cdd:PRK14353 13 AGEGTRM----KSSlPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP----------------------GAEAVAAAA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 91 RNILPPNITCLyirQAEALGLGHAVLCARAAI--GDEPFAVILADD-LIDAPkgALKQMVEvyGRSGNSILGVETVEASQ 167
Cdd:PRK14353 67 AKIAPDAEIFV---QKERLGTAHAVLAAREALagGYGDVLVLYGDTpLITAE--TLARLRE--RLADGADVVVLGFRAAD 139
|
170 180
....*....|....*....|....*
gi 488154311 168 TGSYG--IVETEQLkqfqriTGIVE 190
Cdd:PRK14353 140 PTGYGrlIVKGGRL------VAIVE 158
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-188 |
4.27e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 56.70 E-value: 4.27e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFlpaTKASPKEMLPIVDKPLIQYAVEEAVEAGcTEMVFVTGRNKrsiedhfdkayeletelemrhkdk 85
Cdd:PRK14357 2 RALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEA------------------------ 53
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 86 llEHVRNILPPNITcLYIrQAEALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNS--ILGVETV 163
Cdd:PRK14357 54 --ELVKKLLPEWVK-IFL-QEEQLGTAHAVMCARDFIEPGDDLLILYGDVPLISENTLKRLIEEHNRKGADvtILVADLE 129
|
170 180 190
....*....|....*....|....*....|....*..
gi 488154311 164 EAS-------QTGSYGIVE----TEQLKQFQRI-TGI 188
Cdd:PRK14357 130 DPTgygriirDGGKYRIVEdkdaPEEEKKIKEInTGI 166
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
15-243 |
1.50e-08 |
|
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: 54.18 E-value: 1.50e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 15 GTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedhfdkaYELETELEmrhkdKLLEHVRNil 94
Cdd:cd06428 11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIG-------------FYPESVFS-----DFISDAQQ-- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 95 PPNITCLYIRQAEALGLGHAVLCARAAI---GDEPFAVILADDLIDAPkgaLKQMVEVYGRSGNS--ILGVEtVEASQTG 169
Cdd:cd06428 71 EFNVPIRYLQEYKPLGTAGGLYHFRDQIlagNPSAFFVLNADVCCDFP---LQELLEFHKKHGASgtILGTE-ASREQAS 146
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 488154311 170 SYG-IVETEQLkqfQRITGIVEKPkpEDAPSNLAVVGRYILTPRIFDLLTNLPRGAGNEIQLTDGIAKLLDHEFV 243
Cdd:cd06428 147 NYGcIVEDPST---GEVLHYVEKP--ETFVSDLINCGVYLFSPEIFDTIKKAFQSRQQEAQLGDDNNREGRAEVI 216
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
8-232 |
8.70e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 53.06 E-value: 8.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 8 VFPVAGMGTRFlpaTKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNkrsiedhfdkAYELETELEMrhkdkll 87
Cdd:PRK14358 11 VILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHG----------AEQVEAALQG------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 88 ehvrnilpPNITclYIRQAEALGLGHAVLCARAAI--GDEPFAVILADDLIDAPKgALKQMVEVYgRSGNSILGVETVEA 165
Cdd:PRK14358 71 --------SGVA--FARQEQQLGTGDAFLSGASALteGDADILVLYGDTPLLRPD-TLRALVADH-RAQGSAMTILTGEL 138
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 488154311 166 SQTGSYGIVETEQLKQFQRitgIVEKPKPEDAPSNLAVV--GRYILTPRIfdllTNLPRGAGN-----EIQLTD 232
Cdd:PRK14358 139 PDATGYGRIVRGADGAVER---IVEQKDATDAEKAIGEFnsGVYVFDARA----PELARRIGNdnkagEYYLTD 205
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
12-158 |
3.86e-07 |
|
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: 49.48 E-value: 3.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFlpatkASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedHfdkayeletelemrHKDKLLEHVR 91
Cdd:cd04182 8 AGRSSRM-----GGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLG--------A--------------EADAVRAALA 60
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 92 NILPPNITCLYirqaEALGLGHAVLCARAAIGDEP--FAVILAD-DLIDApkGALKQMVEVYGRSGNSIL 158
Cdd:cd04182 61 GLPVVVVINPD----WEEGMSSSLAAGLEALPADAdaVLILLADqPLVTA--ETLRALIDAFREDGAGIV 124
|
|
| MocA |
COG2068 |
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism]; |
12-158 |
4.41e-07 |
|
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
Pssm-ID: 441671 [Multi-domain] Cd Length: 195 Bit Score: 49.39 E-value: 4.41e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFlpatkASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDkayeletelemrhkdkllehvr 91
Cdd:COG2068 11 AGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALA---------------------- 63
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 92 nilPPNITCLYIRQAEaLGLGHAVLCARAAIGDEPFAVILAddLIDAP---KGALKQMVEVYGRSGNSIL 158
Cdd:COG2068 64 ---GLGVRVVVNPDWE-EGMSSSLRAGLAALPADADAVLVL--LGDQPlvtAETLRRLLAAFRESPASIV 127
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
6-82 |
4.11e-06 |
|
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: 46.86 E-value: 4.11e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKAYELETELEMRH 82
Cdd:cd02507 2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIV 78
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
6-101 |
4.50e-06 |
|
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: 46.50 E-value: 4.50e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 6 KAVFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTE-MVFVTGRNKRSIEDHFDKAY-----ELETELE 79
Cdd:cd04198 2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDvIVVVPEEEQAEISTYLRSFPlnlkqKLDEVTI 81
|
90 100
....*....|....*....|....*.
gi 488154311 80 MRHKDK----LLEHVRNILPPNITCL 101
Cdd:cd04198 82 VLDEDMgtadSLRHIRKKIKKDFLVL 107
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
5-191 |
5.28e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 47.52 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 5 RKAVFPVAGMGTRFlpatKAS-PKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDKayeletelemrhk 83
Cdd:PRK14354 3 RYAIILAAGKGTRM----KSKlPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGD------------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 84 dkllehvrnilppniTCLYIRQAEALGLGHAVLCARAAIGDEPFAV-ILADD--LIDApkGALKQMVEvYGRSGNSILGV 160
Cdd:PRK14354 66 ---------------RSEFALQEEQLGTGHAVMQAEEFLADKEGTTlVICGDtpLITA--ETLKNLID-FHEEHKAAATI 127
|
170 180 190
....*....|....*....|....*....|..
gi 488154311 161 ETVEASQTGSYG-IVETEQlkqfqritGIVEK 191
Cdd:PRK14354 128 LTAIAENPTGYGrIIRNEN--------GEVEK 151
|
|
| GlgC |
COG0448 |
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ... |
124-250 |
3.71e-05 |
|
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];
Pssm-ID: 440217 [Multi-domain] Cd Length: 377 Bit Score: 44.68 E-value: 3.71e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 124 DEPFAVILADDLI---DapkgaLKQMVEVYGRSGNSI-LGVETVEASQTGSYGIVET-EQlkqfQRITGIVEKPKpeDAP 198
Cdd:COG0448 114 DPDYVLILSGDHIykmD-----YRQMLDFHIESGADItVACIEVPREEASRFGVMEVdED----GRITEFEEKPK--DPK 182
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 488154311 199 SNLAVVGRYILTPRIF-DLLT-NLPRGA---GNEIqltdgIAKLLDHEFVLAHPFEG 250
Cdd:COG0448 183 SALASMGIYVFNKDVLiELLEeDAPNSShdfGKDI-----IPRLLDRGKVYAYEFDG 234
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
15-70 |
7.71e-05 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 42.98 E-value: 7.71e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 488154311 15 GTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGRNKRSIEDHFDK 70
Cdd:cd04197 11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEK 66
|
|
| NTP_transf_3 |
pfam12804 |
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ... |
12-158 |
1.69e-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: 41.03 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFlpatkASPKEMLPIVDKPLIQYAVEEAveAGCTEMVFVTGRNKrsiedhfdkayelETELEMRHKDklLEHVR 91
Cdd:pfam12804 6 GGRSSRM-----GGDKALLPLGGKPLLERVLERL--RPAGDEVVVVANDE-------------EVLAALAGLG--VPVVP 63
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488154311 92 NILPpnitclyirqaeALGLGHAVLCARAAIGDEPFAVILADDLIDAPKGALKQMVEVYGRSGNSIL 158
Cdd:pfam12804 64 DPDP------------GQGPLAGLLAALRAAPGADAVLVLACDMPFLTPELLRRLLAAAEESGADIV 118
|
|
| GT2_BcE_like |
cd04183 |
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ... |
8-137 |
4.10e-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: 40.70 E-value: 4.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 8 VFPVAGMGTRFLPATKASPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTgrnkrsIEDHFDKaYELETELEMRHKdkll 87
Cdd:cd04183 2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC------RDEHNTK-FHLDESLKLLAP---- 70
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|.
gi 488154311 88 eHVRNILPPNITclyirqaeaLGLGHAVLCARAAI-GDEPFAVILADDLID 137
Cdd:cd04183 71 -NATVVELDGET---------LGAACTVLLAADLIdNDDPLLIFNCDQIVE 111
|
|
| glmU |
PRK14352 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
12-203 |
8.13e-04 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184641 [Multi-domain] Cd Length: 482 Bit Score: 40.69 E-value: 8.13e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 12 AGMGTRFLPATkasPKEMLPIVDKPLIQYAVEEAVEAGCTEMVFVTGrnkrsiedHfdkayeletelemrHKDKLLEHVR 91
Cdd:PRK14352 12 AGAGTRMRSDT---PKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVG--------H--------------DRERVAPAVA 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488154311 92 NILPPNITCLyirQAEALGLGHAVLCARAAIGDEPFA--VILADD--LIDApkGALKQMVEVYGRSGNSILGVETVEASQ 167
Cdd:PRK14352 67 ELAPEVDIAV---QDEQPGTGHAVQCALEALPADFDGtvVVTAGDvpLLDG--ETLADLVATHTAEGNAVTVLTTTLDDP 141
|
170 180 190
....*....|....*....|....*....|....*...
gi 488154311 168 TGsYG-IVETEQlkqfQRITGIVEKpkpEDA-PSNLAV 203
Cdd:PRK14352 142 TG-YGrILRDQD----GEVTAIVEQ---KDAtPSQRAI 171
|
|
| |
