|
Name |
Accession |
Description |
Interval |
E-value |
| PRK10122 |
PRK10122 |
UTP--glucose-1-phosphate uridylyltransferase GalF; |
1-297 |
0e+00 |
|
UTP--glucose-1-phosphate uridylyltransferase GalF;
Pssm-ID: 182252 [Multi-domain] Cd Length: 297 Bit Score: 629.23 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQR 80
Cdd:PRK10122 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 81 VKRQLLAEVQSICPPGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRS 160
Cdd:PRK10122 81 VKRQLLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTD 240
Cdd:PRK10122 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 238863113 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
Cdd:PRK10122 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
|
|
| galF |
TIGR01105 |
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a ... |
1-297 |
0e+00 |
|
UTP-glucose-1-phosphate uridylyltransferase, non-catalytic GalF subunit; GalF is a non-catalytic subunit of the UTP-glucose pyrophosphorylase modulating the enzyme activity to increase the formation of UDP-glucose [Regulatory functions, Protein interactions]
Pssm-ID: 130175 Cd Length: 297 Bit Score: 596.63 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQR 80
Cdd:TIGR01105 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 81 VKRQLLAEVQSICPPGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRS 160
Cdd:TIGR01105 81 VKRQLLAEVQSICPPGVTIMNVRQAQPLGLGHSILCARPVVGDNPFVVVLPDIIIDDATADPLRYNLAAMIARFNETGRS 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTD 240
Cdd:TIGR01105 161 QVLAKRMPGDLSEYSVIQTKEPLDREGKVSRIVEFIEKPDQPQTLDSDLMAVGRYVLSADIWAELERTEPGAWGRIQLTD 240
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 238863113 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
Cdd:TIGR01105 241 AIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKSIEKLLSE 297
|
|
| GalU |
COG1210 |
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis]; |
5-297 |
6.78e-149 |
|
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440823 [Multi-domain] Cd Length: 288 Bit Score: 418.67 E-value: 6.78e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:COG1210 5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKGKEE 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 LLAEVQSICPPgVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplRYNLAAMIARFNETGRSQVLA 164
Cdd:COG1210 85 LLEEVRSISPL-ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSE-----KPCLKQMIEVYEETGGSVIAV 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 KRMPG-DLSEYSVIQTKEpldREGKVSRIVEFIEKPDqPQTLDSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTDAIA 243
Cdd:COG1210 159 QEVPPeEVSKYGIVDGEE---IEGGVYRVTGLVEKPA-PEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIA 234
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 238863113 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
Cdd:COG1210 235 ALAKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKELLKE 288
|
|
| PRK13389 |
PRK13389 |
UTP--glucose-1-phosphate uridylyltransferase GalU; |
5-297 |
3.93e-128 |
|
UTP--glucose-1-phosphate uridylyltransferase GalU;
Pssm-ID: 184021 [Multi-domain] Cd Length: 302 Bit Score: 366.92 E-value: 3.93e-128
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:PRK13389 10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVKRQ 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 LLAEVQSICPPGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIARFNETGRSQVLA 164
Cdd:PRK13389 90 LLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESDLSQDNLAEMIRRFDETGHSQIMV 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 KRMPgDLSEYSVIQTKEPLDREGKVSRIVEFIEKPdQPQTLDSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTDAIAE 244
Cdd:PRK13389 170 EPVA-DVTAYGVVDCKGVELAPGESVPMVGVVEKP-KADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAIDM 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|...
gi 238863113 245 LAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKLLSE 297
Cdd:PRK13389 248 LIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEEMGI 300
|
|
| UGPase_prokaryotic |
cd02541 |
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ... |
5-279 |
2.49e-124 |
|
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: 355.69 E-value: 2.49e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:cd02541 2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKTD 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 LLaEVQSICPPGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDdaSADPlryNLAAMIARFNETGRSQVLA 164
Cdd:cd02541 82 LL-EEVRIISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID--SKEP---CLKQLIEAYEKTGASVIAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 KRMPG-DLSEYSVIQTKEpldREGKVSRIVEFIEKPDqPQTLDSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTDAIA 243
Cdd:cd02541 156 EEVPPeDVSKYGIVKGEK---IDGDVFKVKGLVEKPK-PEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIA 231
|
250 260 270
....*....|....*....|....*....|....*.
gi 238863113 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLR 279
Cdd:cd02541 232 KLLEEEPVYAYVFEGKRYDCGNKLGYLKATVEFALK 267
|
|
| galU |
TIGR01099 |
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ... |
5-272 |
1.45e-119 |
|
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar genes galU and galF [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]
Pssm-ID: 273443 [Multi-domain] Cd Length: 260 Bit Score: 343.57 E-value: 1.45e-119
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQRVKRQ 84
Cdd:TIGR01099 2 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKEE 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 LLAEVQSICPPgVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASAdplryNLAAMIARFNETGRSQVLA 164
Cdd:TIGR01099 82 LLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP-----ALKQMIKAYEKTGCSIIAV 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 KRMPG-DLSEYSVIQTKEpldREGKVSRIVEFIEKPdQPQTLDSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTDAIA 243
Cdd:TIGR01099 156 QEVPKeEVSKYGVIDGEG---IEKDLYKVKNMVEKP-KPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAIN 231
|
250 260
....*....|....*....|....*....
gi 238863113 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:TIGR01099 232 KLLENETVLAYKFNGKRYDCGSKLGYLEA 260
|
|
| NTP_transferase |
cd04181 |
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ... |
6-264 |
6.82e-51 |
|
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.
Pssm-ID: 133024 [Multi-domain] Cd Length: 217 Bit Score: 166.99 E-value: 6.82e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELeslleqrvkrql 85
Cdd:cd04181 1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 86 laevqsicppGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplryNLAAMIARFNETGR-SQVLA 164
Cdd:cd04181 69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL--------DLSELLRFHREKGAdATIAV 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 KRMPgDLSEYSVIQTkeplDREGkvsRIVEFIEKPDQPqtlDSDIMAVGRYVLSADIWPELERTQPGawGRIQLTDAIAE 244
Cdd:cd04181 131 KEVE-DPSRYGVVEL----DDDG---RVTRFVEKPTLP---ESNLANAGIYIFEPEILDYIPEILPR--GEDELTDAIPL 197
|
250 260
....*....|....*....|
gi 238863113 245 LAKKQSVDAMLMTGDSYDCG 264
Cdd:cd04181 198 LIEEGKVYGYPVDGYWLDIG 217
|
|
| G1P_TT_long |
cd04189 |
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ... |
5-272 |
1.80e-41 |
|
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family is the long form of Glucose-1-phosphate thymidylyltransferase. Glucose-1-phosphate thymidylyltransferase catalyses the formation of dTDP-glucose, from dTTP and glucose 1-phosphate. It is the first enzyme in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme.There are two forms of Glucose-1-phosphate thymidylyltransferase in bacteria and archeae; short form and long form. The long form, which has an extra 50 amino acids c-terminal, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced.The long from enzymes also have a left-handed parallel helix domain at the c-terminus, whereas, th eshort form enzymes do not have this domain. The homotetrameric, feedback inhibited short form is found in numerous bacterial species that produce dTDP-L-rhamnose.
Pssm-ID: 133032 [Multi-domain] Cd Length: 236 Bit Score: 143.09 E-value: 1.80e-41
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELeslleqrvkrq 84
Cdd:cd04189 2 KGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRF----------- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 llaevqsicppGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADplrynlaaMIARFNETGRS-QVL 163
Cdd:cd04189 71 -----------GVRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISP--------LVRDFLEEDADaSIL 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 164 AKRMPgDLSEYSVIQTKEpldregkvSRIVEFIEKPDQPQtldSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTDAIA 243
Cdd:cd04189 132 LAEVE-DPRRFGVAVVDD--------GRIVRLVEKPKEPP---SNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQ 199
|
250 260 270
....*....|....*....|....*....|
gi 238863113 244 EL-AKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:cd04189 200 WLiDRGRRVGYSIVTGWWKDTGTPEDLLEA 229
|
|
| RmlA1 |
COG1209 |
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis]; |
5-272 |
1.29e-40 |
|
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 440822 [Multi-domain] Cd Length: 294 Bit Score: 142.54 E-value: 1.29e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVThasknavenhfdTSYELEslleqRVKRq 84
Cdd:COG1209 2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDGP-----QFER- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 LLAEVQSIcppGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMIARFNE-TGRSQVL 163
Cdd:COG1209 64 LLGDGSQL---GIKISYAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG-------DGLSELLREAAArESGATIF 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 164 AKRMPgDLSEYSVIQtkepLDREGKVSRIVefiEKPDQPQtldSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTDAIA 243
Cdd:COG1209 134 GYKVE-DPERYGVVE----FDEDGRVVSLE---EKPKEPK---SNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQ 202
|
250 260 270
....*....|....*....|....*....|.
gi 238863113 244 E-LAKKQSVDAMLMTGDS-YDCGKKMGYMQA 272
Cdd:COG1209 203 AyLERGKLVVELLGRGFAwLDTGTHESLLEA 233
|
|
| GCD1 |
COG1208 |
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ... |
5-272 |
1.11e-39 |
|
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: 138.75 E-value: 1.11e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELeslleqrvkrq 84
Cdd:COG1208 1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 llaevqsicppGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRS-QVL 163
Cdd:COG1208 70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILTD--------LDLAALLAFHREKGADaTLA 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 164 AKRMPgDLSEYSVIQtkepLDREGkvsRIVEFIEKPDQPqtlDSDIMAVGRYVLSADIWPELERTQPgawgrIQLTDAIA 243
Cdd:COG1208 131 LVPVP-DPSRYGVVE----LDGDG---RVTRFVEKPEEP---PSNLINAGIYVLEPEIFDYIPEGEP-----FDLEDLLP 194
|
250 260
....*....|....*....|....*....
gi 238863113 244 ELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:COG1208 195 RLIAEGRVYGYVHDGYWLDIGTPEDLLEA 223
|
|
| G1P_TT_short |
cd02538 |
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ... |
5-240 |
7.75e-17 |
|
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: 78.00 E-value: 7.75e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVThasknavenhfdTSYELESLleqrvkRQ 84
Cdd:cd02538 2 KGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIS------------TPEDLPLF------KE 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 LLAEVQSIcppGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDasadplrYNLAAMIARFNE-TGRSQVL 163
Cdd:cd02538 64 LLGDGSDL---GIRITYAVQPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYG-------QGLSPILQRAAAqKEGATVF 133
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238863113 164 AKRMPgDLSEYSVIQtkepLDREGKVSRIvefIEKPDQPQtldSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTD 240
Cdd:cd02538 134 GYEVN-DPERYGVVE----FDENGRVLSI---EEKPKKPK---SNYAVTGLYFYDNDVFEIAKQLKPSARGELEITD 199
|
|
| NTP_transferase_like_2 |
cd06426 |
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ... |
6-249 |
1.40e-16 |
|
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: 76.78 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELeslleqrvkrql 85
Cdd:cd06426 1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKF------------ 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 86 laevqsicppGVTIMNVRQGEPLGLGHSILCARPAIgDNPFVVVLPDVVIddasadplRYNLAAMIARFNETGRSQVLAK 165
Cdd:cd06426 69 ----------GVNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILT--------NLNYEHLLDFHKENNADATVCV 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 166 R-----MPgdlseYSVIQTKEpldregkvSRIVEFIEKPDQPQTLDSDImavgrYVLSADIWPELERTQpgawgRIQLTD 240
Cdd:cd06426 130 ReyevqVP-----YGVVETEG--------GRITSIEEKPTHSFLVNAGI-----YVLEPEVLDLIPKNE-----FFDMPD 186
|
....*....
gi 238863113 241 AIAELAKKQ 249
Cdd:cd06426 187 LIEKLIKEG 195
|
|
| NTP_transferase |
pfam00483 |
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ... |
5-221 |
9.55e-16 |
|
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.
Pssm-ID: 425709 [Multi-domain] Cd Length: 243 Bit Score: 74.98 E-value: 9.55e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDK-PMIQYIVDEIVAAGIKEILLVThasknavenhfdTSYELESLLEQrvkr 83
Cdd:pfam00483 1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL------------TQEHRFMLNEL---- 64
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 84 qlLAEVQSIcppGVTIMNVRQGEPLGLGHSILCARPAIGDNPF-VVVLP-DVVIDDAsadplrynLAAMIARFNETGrSQ 161
Cdd:pfam00483 65 --LGDGSKF---GVQITYALQPEGKGTAPAVALAADFLGDEKSdVLVLGgDHIYRMD--------LEQAVKFHIEKA-AD 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 238863113 162 VLAKRMPGDL---SEYSVIQTkeplDREGKVSRiveFIEKPDQPqtLDSDIMAVGRYVLSADI 221
Cdd:pfam00483 131 ATVTFGIVPVeppTGYGVVEF----DDNGRVIR---FVEKPKLP--KASNYASMGIYIFNSGV 184
|
|
| NTP_transferase_WcbM_like |
cd06915 |
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ... |
6-272 |
1.17e-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: 74.13 E-value: 1.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYEleslleqrvkrql 85
Cdd:cd06915 1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYR------------- 67
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 86 laevqsicpPGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRSQVLA- 164
Cdd:cd06915 68 ---------GGIRIYYVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYFD--------VDLLALLAALRASGADATMAl 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 KRMPgDLSEYSVIQtkepLDREGkvsRIVEFIEKP--DQPQTLDSdimavGRYVLSADIWPELERTQPGAwgriqLTDAI 242
Cdd:cd06915 131 RRVP-DASRYGNVT----VDGDG---RVIAFVEKGpgAAPGLING-----GVYLLRKEILAEIPADAFSL-----EADVL 192
|
250 260 270
....*....|....*....|....*....|
gi 238863113 243 AELAKKQSVDAMLMTGDSYDCGKKMGYMQA 272
Cdd:cd06915 193 PALVKRGRLYGFEVDGYFIDIGIPEDYARA 222
|
|
| NTP_transferase_like_1 |
cd06422 |
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ... |
5-152 |
4.80e-15 |
|
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.
Pssm-ID: 133044 [Multi-domain] Cd Length: 221 Bit Score: 72.60 E-value: 4.80e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYEleslleqrvkrq 84
Cdd:cd06422 1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGDSRF------------ 68
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238863113 85 llaevqsicPPGVTIMNVRqGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLRYNLAAMIA 152
Cdd:cd06422 69 ---------GLRITISDEP-DELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDA 126
|
|
| M1P_guanylylT_B_like_N |
cd06425 |
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ... |
4-221 |
1.66e-13 |
|
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: 68.39 E-value: 1.66e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILL-VTHASKNavenhfdtsyeLESLLEQRVK 82
Cdd:cd06425 1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILaVNYRPED-----------MVPFLKEYEK 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 83 RqllaevqsicpPGVTIMNVRQGEPLGLGHSILCARPAIG--DNPFVVVLPDVVIDdasadplrYNLAAMIARFNETGRS 160
Cdd:cd06425 70 K-----------LGIKITFSIETEPLGTAGPLALARDLLGddDEPFFVLNSDVICD--------FPLAELLDFHKKHGAE 130
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 238863113 161 QVLAKRMPGDLSEYSVIQTKEpldREGKVSRiveFIEKPDQPQtldSDIMAVGRYVLSADI 221
Cdd:cd06425 131 GTILVTKVEDPSKYGVVVHDE---NTGRIER---FVEKPKVFV---GNKINAGIYILNPSV 182
|
|
| COG1213 |
COG1213 |
Choline kinase [Lipid transport and metabolism]; |
5-248 |
1.17e-12 |
|
Choline kinase [Lipid transport and metabolism];
Pssm-ID: 440826 [Multi-domain] Cd Length: 236 Bit Score: 66.03 E-value: 1.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 5 KAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVthasknavenhfdTSYELEsLLEQRVKRq 84
Cdd:COG1213 1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVV-------------TGYKAE-LIEEALAR- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 llaevqsiCPPGVTIMNVRQGEPLGLGHSILCARPAIGDnPFVVVLPDVVIDDasadplrynlaAMIARFNETGRSQVLA 164
Cdd:COG1213 66 --------PGPDVTFVYNPDYDETNNIYSLWLAREALDE-DFLLLNGDVVFDP-----------AILKRLLASDGDIVLL 125
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 165 ---KRMPGDLSEYSVIqtkepLDREGkvsRIVEFIEKPDqpqtlDSDIM--AVGRYVLSADIWPELERTQPGAWGRIQ-- 237
Cdd:COG1213 126 vdrKWEKPLDEEVKVR-----VDEDG---RIVEIGKKLP-----PEEADgeYIGIFKFSAEGAAALREALEALIDEGGpn 192
|
250
....*....|...
gi 238863113 238 --LTDAIAELAKK 248
Cdd:COG1213 193 lyYEDALQELIDE 205
|
|
| PRK15480 |
PRK15480 |
glucose-1-phosphate thymidylyltransferase RfbA; Provisional |
1-272 |
8.92e-12 |
|
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
Pssm-ID: 185377 [Multi-domain] Cd Length: 292 Bit Score: 64.31 E-value: 8.92e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 1 MTNLKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASknavenhfDTSYeleslleqr 80
Cdd:PRK15480 1 MKTRKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPQ--------DTPR--------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 81 vKRQLLAEVQSIcppGVTIMNVRQGEPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASADPLrynlaaMIARFNETGRS 160
Cdd:PRK15480 64 -FQQLLGDGSQW---GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGHDLPKL------MEAAVNKESGA 133
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 161 QVLAKRMpGDLSEYSVIQtkepLDREGKVsriVEFIEKPDQPQtldSDIMAVGRYVLSADIWPELERTQPGAWGRIQLTD 240
Cdd:PRK15480 134 TVFAYHV-NDPERYGVVE----FDQNGTA---ISLEEKPLQPK---SNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
|
250 260 270
....*....|....*....|....*....|....*
gi 238863113 241 aIAELAKKQSVDAMLMTGDSY---DCGKKMGYMQA 272
Cdd:PRK15480 203 -INRIYMEQGRLSVAMMGRGYawlDTGTHQSLIEA 236
|
|
| GT2_GlmU_N_bac |
cd02540 |
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ... |
6-249 |
1.50e-11 |
|
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: 62.92 E-value: 1.50e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMlpatK-AIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVEnhfdtsyeleslleqrvkrq 84
Cdd:cd02540 1 AVILAAGKGTRM----KsDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVK-------------------- 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 85 llaevQSICPPGVTImnVRQGEPLGLGHSILCARPAI-GDNPFVVVLP-DV-VIDDASadplrynLAAMIARFNETGRSQ 161
Cdd:cd02540 57 -----KALANPNVEF--VLQEEQLGTGHAVKQALPALkDFEGDVLVLYgDVpLITPET-------LQRLLEAHREAGADV 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 162 VLAKRMPGDLSEYS-VIqtkepLDREGKVSRIVEFIEKPDQPQTLD---SDIMAVGryvlSADIWPELERTQP-GAWGRI 236
Cdd:cd02540 123 TVLTAELEDPTGYGrII-----RDGNGKVLRIVEEKDATEEEKAIRevnAGIYAFD----AEFLFEALPKLTNnNAQGEY 193
|
250
....*....|...
gi 238863113 237 QLTDAIaELAKKQ 249
Cdd:cd02540 194 YLTDII-ALAVAD 205
|
|
| GlmU |
COG1207 |
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ... |
2-194 |
8.70e-11 |
|
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: 61.97 E-value: 8.70e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 2 TNLKAVIPVAGLGMHMlpatK-AIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTsyeleslleqr 80
Cdd:COG1207 1 SPLAVVILAAGKGTRM----KsKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD----------- 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 81 vkrqllaevqsicpPGVTImnVRQGEPLGLGHSILCARPAI-GDNPFVVVLP-DVviddasadPL--RYNLAAMIARFNE 156
Cdd:COG1207 66 --------------LDVEF--VLQEEQLGTGHAVQQALPALpGDDGTVLVLYgDV--------PLirAETLKALLAAHRA 121
|
170 180 190
....*....|....*....|....*....|....*....
gi 238863113 157 TGRS-QVLAKRMPgDLSEYSVIQTkeplDREGKVSRIVE 194
Cdd:COG1207 122 AGAAaTVLTAELD-DPTGYGRIVR----DEDGRVLRIVE 155
|
|
| glmU |
PRK14353 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
6-253 |
1.07e-10 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184642 [Multi-domain] Cd Length: 446 Bit Score: 61.80 E-value: 1.07e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVEnhfdtsyeleslleqrvkrql 85
Cdd:PRK14353 8 AIILAAGEGTRM---KSSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA--------------------- 63
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 86 lAEVQSICPPGVTimnVRQGEPLGLGHSILCARPAI-----------GDNPFVvvlpdvviddaSADPLRynlaAMIARF 154
Cdd:PRK14353 64 -AAAAKIAPDAEI---FVQKERLGTAHAVLAAREALaggygdvlvlyGDTPLI-----------TAETLA----RLRERL 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 155 NETGRSQVLAKRmPGDLSEYSVIQTKepldrEGKVSRIVEFIEKPDQPQTLD---SDIMAVGRyvlsADIWPELER-TQP 230
Cdd:PRK14353 125 ADGADVVVLGFR-AADPTGYGRLIVK-----GGRLVAIVEEKDASDEERAITlcnSGVMAADG----ADALALLDRvGND 194
|
250 260
....*....|....*....|...
gi 238863113 231 GAWGRIQLTDaIAELAKKQSVDA 253
Cdd:PRK14353 195 NAKGEYYLTD-IVAIARAEGLRV 216
|
|
| eIF-2B_gamma_N |
cd04198 |
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-72 |
1.19e-10 |
|
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133041 [Multi-domain] Cd Length: 214 Bit Score: 59.98 E-value: 1.19e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVT-HASKNAVENHFDTSYE 72
Cdd:cd04198 1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpEEEQAEISTYLRSFPL 70
|
|
| eIF-2B_gamma_N_like |
cd02507 |
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ... |
4-81 |
3.04e-10 |
|
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; N-terminal domain of eEIF-2B epsilon and gamma, subunits of eukaryotic translation initiators, is a subfamily of glycosyltranferase 2 and is predicted to have glycosyltranferase activity. eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133001 [Multi-domain] Cd Length: 216 Bit Score: 58.80 E-value: 3.04e-10
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 238863113 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLEQRV 81
Cdd:cd02507 1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKWSSLSSKMIV 78
|
|
| glmU |
PRK14355 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
1-220 |
2.46e-09 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237685 [Multi-domain] Cd Length: 459 Bit Score: 57.83 E-value: 2.46e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 1 MTNLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELESLLeqr 80
Cdd:PRK14355 1 MNNLAAIILAAGKGTRM---KSDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGDVSFAL--- 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 81 vkrqllaevqsicppgvtimnvrQGEPLGLGHSILCARPAI-GDNPFVVVL-PDV-VIDDASadplrynLAAMIARFNET 157
Cdd:PRK14355 75 -----------------------QEEQLGTGHAVACAAPALdGFSGTVLILcGDVpLLRAET-------LQGMLAAHRAT 124
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238863113 158 GRS-QVLAKRMPGDLSEYSVIQtkeplDREGKVSRIVEfiEKPDQPQTLDSDIMAVGRYVLSAD 220
Cdd:PRK14355 125 GAAvTVLTARLENPFGYGRIVR-----DADGRVLRIVE--EKDATPEERSIREVNSGIYCVEAA 181
|
|
| PC_cytidylyltransferase |
cd02523 |
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ... |
6-253 |
6.52e-09 |
|
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: 55.32 E-value: 6.52e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTSYELEslleqrvkrql 85
Cdd:cd02523 1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIK----------- 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 86 laevqsicppgvTIMNVRQGEPlGLGHSILCARPAIGDNpFVVVLPDVVIDDASADPL----RYNLAAMIARFNEtgrsq 161
Cdd:cd02523 70 ------------FVYNPDYAET-NNIYSLYLARDFLDED-FLLLEGDVVFDPSILERLlsspADNAILVDKKTKE----- 130
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 162 vlakrmpgdlseySVIQTKEPLDREGKVSRIVEFIEKPDQPQtldsdimavGRYV----LSADIWPEL--------ERTQ 229
Cdd:cd02523 131 -------------WEDEYVKDLDDAGVLLGIISKAKNLEEIQ---------GEYVgiskFSPEDADRLaealeeliEAGR 188
|
250 260
....*....|....*....|....
gi 238863113 230 PGAWgriqLTDAIAELAKKQSVDA 253
Cdd:cd02523 189 VNLY----YEDALQRLISEEGVKV 208
|
|
| glmU |
PRK14358 |
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ... |
4-240 |
1.47e-08 |
|
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional
Pssm-ID: 237688 [Multi-domain] Cd Length: 481 Bit Score: 55.37 E-value: 1.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 4 LKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVT-HASKnavenhfdtsyELESLLEQrvk 82
Cdd:PRK14358 8 LDVVILAAGQGTRM---KSALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTgHGAE-----------QVEAALQG--- 70
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 83 rqllaevqsicpPGVTImnVRQGEPLGLGHSILCARPAIGDNPfvvvlPDVVIDDASADPLR-YNLAAMIARFNETGRS- 160
Cdd:PRK14358 71 ------------SGVAF--ARQEQQLGTGDAFLSGASALTEGD-----ADILVLYGDTPLLRpDTLRALVADHRAQGSAm 131
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 161 QVLAKRMPgDLSEYSVIQTkeplDREGKVSRIVEfiEKPDQPQTLDSDIMAVGRYVLSADIwPELER--TQPGAWGRIQL 238
Cdd:PRK14358 132 TILTGELP-DATGYGRIVR----GADGAVERIVE--QKDATDAEKAIGEFNSGVYVFDARA-PELARriGNDNKAGEYYL 203
|
..
gi 238863113 239 TD 240
Cdd:PRK14358 204 TD 205
|
|
| glmU |
PRK14354 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
2-123 |
1.06e-06 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 184643 [Multi-domain] Cd Length: 458 Bit Score: 49.44 E-value: 1.06e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 2 TNLKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIllVTHASKNAvenhfdtsyeleslleQRV 81
Cdd:PRK14354 1 MNRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKI--VTVVGHGA----------------EEV 59
|
90 100 110 120
....*....|....*....|....*....|....*....|..
gi 238863113 82 KRQLLAEVQSicppgvtimnVRQGEPLGLGHSILCARPAIGD 123
Cdd:PRK14354 60 KEVLGDRSEF----------ALQEEQLGTGHAVMQAEEFLAD 91
|
|
| M1P_guanylylT_A_like_N |
cd06428 |
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ... |
6-229 |
9.52e-06 |
|
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: 46.09 E-value: 9.52e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAG--LGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVA-AGIKEILLVThasknavenhFDTSYELESLLEqRVK 82
Cdd:cd06428 1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIG----------FYPESVFSDFIS-DAQ 69
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 83 RQllaevqsicpPGVTIMNVRQGEPLGLGHSILCARPAI-GDNP--FVVVLPDVVIDdasadplrYNLAAMIARFNETGR 159
Cdd:cd06428 70 QE----------FNVPIRYLQEYKPLGTAGGLYHFRDQIlAGNPsaFFVLNADVCCD--------FPLQELLEFHKKHGA 131
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 238863113 160 SQVL----AKRMpgDLSEYSVIQTKEpldregKVSRIVEFIEKpdqPQTLDSDIMAVGRYVLSADIWPELERTQ 229
Cdd:cd06428 132 SGTIlgteASRE--QASNYGCIVEDP------STGEVLHYVEK---PETFVSDLINCGVYLFSPEIFDTIKKAF 194
|
|
| glmU |
PRK14357 |
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ... |
4-130 |
1.51e-05 |
|
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;
Pssm-ID: 237687 [Multi-domain] Cd Length: 448 Bit Score: 45.91 E-value: 1.51e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 4 LKAVIPVAGLGMHMlpaTKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHasknavenhfdtSYELeslleqrvkr 83
Cdd:PRK14357 1 MRALVLAAGKGTRM---KSKIPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGH------------EAEL---------- 55
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 238863113 84 qllaeVQSICPPGVTImnVRQGEPLGLGHSILCARPAIGDNPFVVVL 130
Cdd:PRK14357 56 -----VKKLLPEWVKI--FLQEEQLGTAHAVMCARDFIEPGDDLLIL 95
|
|
| eIF-2B_epsilon_N |
cd04197 |
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ... |
4-70 |
1.94e-05 |
|
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of epsilon subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit epsilon shares sequence similarity with gamma subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.
Pssm-ID: 133040 [Multi-domain] Cd Length: 217 Bit Score: 44.91 E-value: 1.94e-05
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 238863113 4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVENHFDTS 70
Cdd:cd04197 1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKS 67
|
|
| GT_2_like_f |
cd04182 |
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ... |
6-164 |
1.16e-03 |
|
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.
Pssm-ID: 133025 [Multi-domain] Cd Length: 186 Bit Score: 39.08 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLG--MHMlpatkaiPKEMLPIVDKPMIQYIVDEIVAAGIKEILLVTHASKNAVenhfdtsyeleslleqrvkR 83
Cdd:cd04182 3 AIILAAGRSsrMGG-------NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAV-------------------R 56
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 84 QLLAevqsicPPGVTIMNVRQGEpLGLGHSILCARPAIGDNP--FVVVL---PDVVIDDasadplrynLAAMIARFNETG 158
Cdd:cd04182 57 AALA------GLPVVVVINPDWE-EGMSSSLAAGLEALPADAdaVLILLadqPLVTAET---------LRALIDAFREDG 120
|
....*.
gi 238863113 159 RSQVLA 164
Cdd:cd04182 121 AGIVAP 126
|
|
| ispD |
PRK00155 |
D-ribitol-5-phosphate cytidylyltransferase; |
6-129 |
1.30e-03 |
|
D-ribitol-5-phosphate cytidylyltransferase;
Pssm-ID: 234670 Cd Length: 227 Bit Score: 39.35 E-value: 1.30e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 238863113 6 AVIPVAGLGMHMlpatKA-IPKEMLPIVDKPMIQYIVDEIVAAG-IKEILLVTHASknavenhfDTSYELESLLEQRVKR 83
Cdd:PRK00155 6 AIIPAAGKGSRM----GAdRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPD--------DRPDFAELLLAKDPKV 73
|
90 100 110 120
....*....|....*....|....*....|....*....|....*.
gi 238863113 84 QllaevqsICPPGVTimnvRQgeplglgHSILCARPAIGDNPFVVV 129
Cdd:PRK00155 74 T-------VVAGGAE----RQ-------DSVLNGLQALPDDDWVLV 101
|
|
| COG2266 |
COG2266 |
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ... |
26-62 |
2.00e-03 |
|
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis
Pssm-ID: 441867 [Multi-domain] Cd Length: 185 Bit Score: 38.33 E-value: 2.00e-03
10 20 30
....*....|....*....|....*....|....*..
gi 238863113 26 KEMLPIVDKPMIQYIVDEIVAAGIKEILLVThaSKNA 62
Cdd:COG2266 14 KPLLEICGKPMIDRVIDALEESCIDKIYVAV--SPNT 48
|
|
| MPP_Mre11_N |
cd00840 |
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia ... |
240-283 |
3.75e-03 |
|
Mre11 nuclease, N-terminal metallophosphatase domain; Mre11 (also known as SbcD in Escherichia coli) is a subunit of the MRX protein complex. This complex includes: Mre11, Rad50, and Xrs2/Nbs1, and plays a vital role in several nuclear processes including DNA double-strand break repair, telomere length maintenance, cell cycle checkpoint control, and meiotic recombination, in eukaryotes. During double-strand break repair, the MRX complex is required to hold the two ends of a broken chromosome together. In vitro studies show that Mre11 has 3'-5' exonuclease activity on dsDNA templates and endonuclease activity on dsDNA and ssDNA templates. In addition to the N-terminal phosphatase domain, the eukaryotic MRE11 members of this family have a C-terminal DNA binding domain (not included in this alignment model). MRE11-like proteins are found in prokaryotes and archaea was well as in eukaryotes. Mre11 belongs to the metallophosphatase (MPP) superfamily. MPPs are functionally diverse, but all share a conserved domain with an active site consisting of two metal ions (usually manganese, iron, or zinc) coordinated with octahedral geometry by a cage of histidine, aspartate, and asparagine residues. The MPP superfamily includes: Mre11/SbcD-like exonucleases, Dbr1-like RNA lariat debranching enzymes, YfcE-like phosphodiesterases, purple acid phosphatases (PAPs), YbbF-like UDP-2,3-diacylglucosamine hydrolases, and acid sphingomyelinases (ASMases). The conserved domain is a double beta-sheet sandwich with a di-metal active site made up of residues located at the C-terminal side of the sheets. This domain is thought to allow for productive metal coordination.
Pssm-ID: 277319 [Multi-domain] Cd Length: 186 Bit Score: 37.63 E-value: 3.75e-03
10 20 30 40
....*....|....*....|....*....|....*....|....
gi 238863113 240 DAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKE 283
Cdd:cd00840 29 EEIVDLAIEEKVDFVLIAGDLFDSNNPSPEALKLAIEGLRRLCE 72
|
|
| glgC |
PRK00844 |
glucose-1-phosphate adenylyltransferase; Provisional |
162-221 |
8.17e-03 |
|
glucose-1-phosphate adenylyltransferase; Provisional
Pssm-ID: 234846 [Multi-domain] Cd Length: 407 Bit Score: 37.50 E-value: 8.17e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 238863113 162 VLAKRMP-GDLSEYSVIQTkeplDREGkvsRIVEFIEKPDQPQTLDSD---IMA-VGRYVLSADI 221
Cdd:PRK00844 149 VAAIRVPrEEASAFGVIEV----DPDG---RIRGFLEKPADPPGLPDDpdeALAsMGNYVFTTDA 206
|
|
| |
