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Conserved domains on  [gi|943359088|gb|ALL34869|]
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GalU [Acinetobacter baumannii]

Protein Classification

UTP--glucose-1-phosphate uridylyltransferase( domain architecture ID 10003115)

UTP--glucose-1-phosphate uridylyltransferase catalyzes the formation of UDP-glucose from glucose-1-phosphate and UTP, which is an intermediate step in the biosynthesis of diglucosyl-diacylglycerol (Glc2-DAG)

CATH:  3.90.550.10
EC:  2.7.7.9
Gene Ontology:  GO:0009225|GO:0003983
PubMed:  15020755

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
1-289 4.47e-166

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


:

Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 461.81  E-value: 4.47e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   1 MIKKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKK 80
Cdd:COG1210    2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  81 KFDLLAEISQIVPkHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSGqnDLSRMISRYNSSQAAQIMV 160
Cdd:COG1210   82 KEELLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKP--CLKQMIEVYEETGGSVIAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 161 EAVPDHLVDQYGIVDVKqsPNEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAML 240
Cdd:COG1210  159 QEVPPEEVSKYGIVDGE--EIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAAL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 943359088 241 QDTDTVEAYRMQGQTFDCGSKLGYLKAVLHYGVEHPKLGNDFKQLIQEL 289
Cdd:COG1210  237 AKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
1-289 4.47e-166

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 461.81  E-value: 4.47e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   1 MIKKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKK 80
Cdd:COG1210    2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  81 KFDLLAEISQIVPkHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSGqnDLSRMISRYNSSQAAQIMV 160
Cdd:COG1210   82 KEELLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKP--CLKQMIEVYEETGGSVIAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 161 EAVPDHLVDQYGIVDVKqsPNEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAML 240
Cdd:COG1210  159 QEVPPEEVSKYGIVDGE--EIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAAL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 943359088 241 QDTDTVEAYRMQGQTFDCGSKLGYLKAVLHYGVEHPKLGNDFKQLIQEL 289
Cdd:COG1210  237 AKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-272 8.52e-137

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: 386.89  E-value: 8.52e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKKKF 82
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  83 DLLAEISqIVPKHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKdsSGQNDLSRMISRYNSSQAAQIMVEA 162
Cdd:cd02541   81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID--SKEPCLKQLIEAYEKTGASVIAVEE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 163 VPDHLVDQYGIVDVKQSpnEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAMLQD 242
Cdd:cd02541  158 VPPEDVSKYGIVKGEKI--DGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLE 235

                        250       260       270
                 ....*....|....*....|....*....|
gi 943359088 243 TDTVEAYRMQGQTFDCGSKLGYLKAVLHYG 272
Cdd:cd02541  236 EEPVYAYVFEGKRYDCGNKLGYLKATVEFA 265
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 3-267 2.40e-124

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: 355.51  E-value: 2.40e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088    3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKKKF 82
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   83 DLLAEISQIVPKhVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSGqnDLSRMISRYNSSQAAQIMVEA 162
Cdd:TIGR01099  81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP--ALKQMIKAYEKTGCSIIAVQE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  163 VPDHLVDQYGIVDVKQSpnEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAMLQD 242
Cdd:TIGR01099 158 VPKEEVSKYGVIDGEGI--EKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLE 235

                         250       260
                  ....*....|....*....|....*
gi 943359088  243 TDTVEAYRMQGQTFDCGSKLGYLKA 267
Cdd:TIGR01099 236 NETVLAYKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-289 3.83e-117

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 338.80  E-value: 3.83e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   2 IKKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKKK 81
Cdd:PRK13389   8 VKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  82 FDLLAEISQIVPKHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSG---QNDLSRMISRYNSSQAAQI 158
Cdd:PRK13389  88 RQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESdlsQDNLAEMIRRFDETGHSQI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 159 MVEAVPDhlVDQYGIVDVK-QSPNEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAI 237
Cdd:PRK13389 168 MVEPVAD--VTAYGVVDCKgVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAI 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 943359088 238 AMLQDTDTVEAYRMQGQTFDCGSKLGYLKAVLHYGVEHPKLGNDFKQLIQEL 289
Cdd:PRK13389 246 DMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-271 5.51e-18

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: 81.15  E-value: 5.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088    4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDR-PAIEYVVREAVEAGIEQIILVThsskasieNYFDRnFELETTLEQKKKF 82
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEHR-FMLNELLGDGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   83 DLLAEISQivpkhvsvisvrQPQPLGLGHAVLCAKSVVGQD--DFAVLLPDVLVKDssgqnDLSRMISRY-NSSQAAQIM 159
Cdd:pfam00483  72 GVQITYAL------------QPEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRM-----DLEQAVKFHiEKAADATVT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  160 VEAVPDHLVDQYGIVDVkqspneGESIAMQGIVEKpPVGSAPSNLSVVGRYVLPAKI-MQLLESTPKGAGNEIQLTDAI- 237
Cdd:pfam00483 135 FGIVPVEPPTGYGVVEF------DDNGRVIRFVEK-PKLPKASNYASMGIYIFNSGVlDFLAKYLEELKRGEDEITDILp 207

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 943359088  238 AMLQDTDTVEAYRMQGQT-FDCGSKLGYLKAVLHY 271
Cdd:pfam00483 208 KALEDGKLAYAFIFKGYAwLDVGTWDSLWEANLFL 242
 
Name Accession Description Interval E-value
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
1-289 4.47e-166

UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 461.81  E-value: 4.47e-166
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   1 MIKKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKK 80
Cdd:COG1210    2 KIRKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRGKRAIEDHFDRSYELEATLEAKG 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  81 KFDLLAEISQIVPkHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSGqnDLSRMISRYNSSQAAQIMV 160
Cdd:COG1210   82 KEELLEEVRSISP-LANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKP--CLKQMIEVYEETGGSVIAV 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 161 EAVPDHLVDQYGIVDVKqsPNEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAML 240
Cdd:COG1210  159 QEVPPEEVSKYGIVDGE--EIEGGVYRVTGLVEKPAPEEAPSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAAL 236

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 943359088 241 QDTDTVEAYRMQGQTFDCGSKLGYLKAVLHYGVEHPKLGNDFKQLIQEL 289
Cdd:COG1210  237 AKEEPVYAYEFEGKRYDCGDKLGYLKATVEFALKRPDLGEEFREYLKEL 285
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 3-272 8.52e-137

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: 386.89  E-value: 8.52e-137
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKKKF 82
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRGKRAIEDHFDRSYELEETLEKKGKT 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  83 DLLAEISqIVPKHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKdsSGQNDLSRMISRYNSSQAAQIMVEA 162
Cdd:cd02541   81 DLLEEVR-IISDLANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLID--SKEPCLKQLIEAYEKTGASVIAVEE 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 163 VPDHLVDQYGIVDVKQSpnEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAMLQD 242
Cdd:cd02541  158 VPPEDVSKYGIVKGEKI--DGDVFKVKGLVEKPKPEEAPSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLLE 235

                        250       260       270
                 ....*....|....*....|....*....|
gi 943359088 243 TDTVEAYRMQGQTFDCGSKLGYLKAVLHYG 272
Cdd:cd02541  236 EEPVYAYVFEGKRYDCGNKLGYLKATVEFA 265
galU TIGR01099
UTP--glucose-1-phosphate uridylyltransferase; Built to distinquish between the highly similar ...
 3-267 2.40e-124

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: 355.51  E-value: 2.40e-124
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088    3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKKKF 82
Cdd:TIGR01099   1 RKAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYIVEEAVEAGIEEIVFVTGRGKRAIEDHFDYSYELEHQLEKRGKE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   83 DLLAEISQIVPKhVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSGqnDLSRMISRYNSSQAAQIMVEA 162
Cdd:TIGR01099  81 ELLEEVRKISNL-ATIFYVRQKEQKGLGHAVLCARPFVGDEPFAVILGDDIVVNEEP--ALKQMIKAYEKTGCSIIAVQE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  163 VPDHLVDQYGIVDVKQSpnEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAMLQD 242
Cdd:TIGR01099 158 VPKEEVSKYGVIDGEGI--EKDLYKVKNMVEKPKPEEAPSNLAIVGRYILTPDIFDLLEETPPGKGGEIQLTDAINKLLE 235

                         250       260
                  ....*....|....*....|....*
gi 943359088  243 TDTVEAYRMQGQTFDCGSKLGYLKA 267
Cdd:TIGR01099 236 NETVLAYKFNGKRYDCGSKLGYLEA 260
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-289 3.83e-117

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 338.80  E-value: 3.83e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   2 IKKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQKKK 81
Cdd:PRK13389   8 VKKAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSIENHFDTSFELEAMLEKRVK 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  82 FDLLAEISQIVPKHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSG---QNDLSRMISRYNSSQAAQI 158
Cdd:PRK13389  88 RQLLDEVQSICPPHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVILDEYESdlsQDNLAEMIRRFDETGHSQI 167

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 159 MVEAVPDhlVDQYGIVDVK-QSPNEGESIAMQGIVEKPPVGSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAI 237
Cdd:PRK13389 168 MVEPVAD--VTAYGVVDCKgVELAPGESVPMVGVVEKPKADVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDEIQLTDAI 245

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 943359088 238 AMLQDTDTVEAYRMQGQTFDCGSKLGYLKAVLHYGVEHPKLGNDFKQLIQEL 289
Cdd:PRK13389 246 DMLIEKETVEAYHMKGKSHDCGNKLGYMQAFVEYGIRHNTLGTEFKAWLEEE 297
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-289 5.95e-95

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 282.16  E-value: 5.95e-95
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   1 MIK-KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEQK 79
Cdd:PRK10122   1 MTNlKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELESLLEQR 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  80 KKFDLLAEISQIVPKHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDSSG---QNDLSRMISRYNSSQAA 156
Cdd:PRK10122  81 VKRQLLAEVQSICPPGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDASAdplRYNLAAMIARFNETGRS 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 157 QIMVEAVPDHLvDQYGIVDVKQS-PNEGESIAMQGIVEKPPVGSA-PSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLT 234
Cdd:PRK10122 161 QVLAKRMPGDL-SEYSVIQTKEPlDREGKVSRIVEFIEKPDQPQTlDSDLMAVGRYVLSADIWPELERTEPGAWGRIQLT 239

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 943359088 235 DAIAMLQDTDTVEAYRMQGQTFDCGSKLGYLKAVLHYGVEHPKLGNDFKQLIQEL 289
Cdd:PRK10122 240 DAIAELAKKQSVDAMLMTGDSYDCGKKMGYMQAFVKYGLRNLKEGAKFRKGIEKL 294
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-259 2.69e-50

NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; Nucleotidyltransferases transfer nucleotides onto phosphosugars. The enzyme family includes Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase. The products are activated sugars that are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides.


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 165.06  E-value: 2.69e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   5 AVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELettleqkkkfdl 84
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  85 laeisqivpkHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDssgqnDLSRMISRYNSSQA-AQIMVEAV 163
Cdd:cd04181   69 ----------GVNIEYVVQEEPLGTAGAVRNAEDFLGDDDFLVVNGDVLTDL-----DLSELLRFHREKGAdATIAVKEV 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 164 PDHLvdQYGIVDVKqspNEGESIamqGIVEKPPVGsaPSNLSVVGRYVLPAKIMQLLESTPKgaGNEIQLTDAIAMLQDT 243
Cdd:cd04181  134 EDPS--RYGVVELD---DDGRVT---RFVEKPTLP--ESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEE 201

                        250
                 ....*....|....*.
gi 943359088 244 DTVEAYRMQGQTFDCG 259
Cdd:cd04181  202 GKVYGYPVDGYWLDIG 217
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 3-268 6.54e-42

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: 144.25  E-value: 6.54e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNfelettleqkKKF 82
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDG----------SRF 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  83 DllaeisqivpkhVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVkdssgQNDLSRMISRYNSSQA-AQIMVE 161
Cdd:cd04189   71 G------------VRITYILQEEPLGLAHAVLAARDFLGDEPFVVYLGDNLI-----QEGISPLVRDFLEEDAdASILLA 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 162 AVPDhlVDQYGIVDVkqspnEGESIamQGIVEKP--PvgsaPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAIAM 239
Cdd:cd04189  134 EVED--PRRFGVAVV-----DDGRI--VRLVEKPkeP----PSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQW 200

                        250       260       270
                 ....*....|....*....|....*....|
gi 943359088 240 LQDTD-TVEAYRMQGQTFDCGSKLGYLKAV 268
Cdd:cd04189  201 LIDRGrRVGYSIVTGWWKDTGTPEDLLEAN 230
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-267 2.29e-33

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: 122.18  E-value: 2.29e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELettleqkkkfd 83
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  84 llaeisqivpkHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVkDSsgqnDLSRMISRYNSSQA-AQIMVEA 162
Cdd:COG1208   70 -----------GVRITYVDEGEPLGTGGALKRALPLLGDEPFLVLNGDILT-DL----DLAALLAFHREKGAdATLALVP 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 163 VPDHlvDQYGIVDVkqspNEGESIamQGIVEKPPvgSAPSNLSVVGRYVLPAKIMQLLEstpkgAGNEIQLTDAIAMLQD 242
Cdd:COG1208  134 VPDP--SRYGVVEL----DGDGRV--TRFVEKPE--EPPSNLINAGIYVLEPEIFDYIP-----EGEPFDLEDLLPRLIA 198

                        250       260
                 ....*....|....*....|....*
gi 943359088 243 TDTVEAYRMQGQTFDCGSKLGYLKA 267
Cdd:COG1208  199 EGRVYGYVHDGYWLDIGTPEDLLEA 223
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
4-261 5.71e-33

dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 122.51  E-value: 5.71e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVthsskasienyfdrnfeleTTLEQKKKF- 82
Cdd:COG1209    2 KGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILII-------------------STPEDGPQFe 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  83 DLLAEISQIVPKhvsvIS-VRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDssgqNDLSRMISRYNSSQA-AQIMV 160
Cdd:COG1209   63 RLLGDGSQLGIK----ISyAVQPEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYG----DGLSELLREAAARESgATIFG 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 161 EAVPDHlvDQYGIVDVKqspNEGESIamqGIVEKP--PvgsaPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTDAI- 237
Cdd:COG1209  135 YKVEDP--ERYGVVEFD---EDGRVV---SLEEKPkeP----KSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANq 202

                        250       260
                 ....*....|....*....|....*
gi 943359088 238 AMLQDTDTVEAYRMQGQT-FDCGSK 261
Cdd:COG1209  203 AYLERGKLVVELLGRGFAwLDTGTH 227
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 4-271 5.51e-18

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: 81.15  E-value: 5.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088    4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDR-PAIEYVVREAVEAGIEQIILVThsskasieNYFDRnFELETTLEQKKKF 82
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVIL--------TQEHR-FMLNELLGDGSKF 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   83 DLLAEISQivpkhvsvisvrQPQPLGLGHAVLCAKSVVGQD--DFAVLLPDVLVKDssgqnDLSRMISRY-NSSQAAQIM 159
Cdd:pfam00483  72 GVQITYAL------------QPEGKGTAPAVALAADFLGDEksDVLVLGGDHIYRM-----DLEQAVKFHiEKAADATVT 134

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  160 VEAVPDHLVDQYGIVDVkqspneGESIAMQGIVEKpPVGSAPSNLSVVGRYVLPAKI-MQLLESTPKGAGNEIQLTDAI- 237
Cdd:pfam00483 135 FGIVPVEPPTGYGVVEF------DDNGRVIRFVEK-PKLPKASNYASMGIYIFNSGVlDFLAKYLEELKRGEDEITDILp 207

                         250       260       270
                  ....*....|....*....|....*....|....*
gi 943359088  238 AMLQDTDTVEAYRMQGQT-FDCGSKLGYLKAVLHY 271
Cdd:pfam00483 208 KALEDGKLAYAFIFKGYAwLDVGTWDSLWEANLFL 242
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 3-235 2.34e-13

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: 67.99  E-value: 2.34e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVthsskasienyfdrnfeleTTLEQKKKF 82
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILII-------------------STPEDLPLF 61

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  83 -DLLAEISQIvPKHVSVISvrQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDssgqNDLSRMISRYNSSQA-AQIMV 160
Cdd:cd02538   62 kELLGDGSDL-GIRITYAV--QPKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYG----QGLSPILQRAAAQKEgATVFG 134

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 943359088 161 EAVPDhlVDQYGIVDVKQSPNegesiaMQGIVEKPPVgsAPSNLSVVGRYVLPAKIMQLLES-TPKGAGnEIQLTD 235
Cdd:cd02538  135 YEVND--PERYGVVEFDENGR------VLSIEEKPKK--PKSNYAVTGLYFYDNDVFEIAKQlKPSARG-ELEITD 199
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-267 3.52e-12

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: 64.46  E-value: 3.52e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   5 AVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFdrnfelettlEQKKKFDl 84
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYF----------GDGSKFG- 69

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  85 laeisqivpkhVSVISVRQPQPLGLGHAVLCAKSVVgQDDFAVLLPDVLVKDssgqnDLSRMISRYNSSQAAQIMVEAVP 164
Cdd:cd06426   70 -----------VNISYVREDKPLGTAGALSLLPEKP-TDPFLVMNGDILTNL-----NYEHLLDFHKENNADATVCVREY 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 165 DHLVdQYGIVdvkqspnEGESIAMQGIVEKPPVgsapSNLSVVGRYVL-PakimQLLESTPKGAgnEIQLTDAI-AMLQD 242
Cdd:cd06426  133 EVQV-PYGVV-------ETEGGRITSIEEKPTH----SFLVNAGIYVLeP----EVLDLIPKNE--FFDMPDLIeKLIKE 194

                        250       260
                 ....*....|....*....|....*
gi 943359088 243 TDTVEAYRMQGQTFDCGSKLGYLKA 267
Cdd:cd06426  195 GKKVGVFPIHEYWLDIGRPEDYEKA 219
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 10-240 1.42e-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: 1.42e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  10 AGLGTRFlpasKS-IPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNfelettleqkkkfdllaei 88
Cdd:cd02540    6 AGKGTRM----KSdLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANP------------------- 62

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  89 sqivpkhvSVISVRQPQPLGLGHAVLCAKSVVGQ--DDFAVLLPDV-LVKDSSgqndLSRMISRYNSSQAAQIMVEAVPD 165
Cdd:cd02540   63 --------NVEFVLQEEQLGTGHAVKQALPALKDfeGDVLVLYGDVpLITPET----LQRLLEAHREAGADVTVLTAELE 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 166 HlVDQYG-IVdvkqsPNEGESIamQGIVEKPPVGSAPSNLSVV--GRYVLPAKIM-QLLES-TPKGAGNEIQLTDAIAML 240
Cdd:cd02540  131 D-PTGYGrII-----RDGNGKV--LRIVEEKDATEEEKAIREVnaGIYAFDAEFLfEALPKlTNNNAQGEYYLTDIIALA 202
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-176 6.19e-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: 61.03  E-value: 6.19e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   5 AVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELETTLEqkkkfdl 84
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIY------- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  85 laeisqivpkhvsviSVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVkdssgQNDLSRMISRYNSSQAAQIM-VEAV 163
Cdd:cd06915   74 ---------------YVIEPEPLGTGGAIKNALPKLPEDQFLVLNGDTYF-----DVDLLALLAALRASGADATMaLRRV 133

                        170
                 ....*....|...
gi 943359088 164 PDhlVDQYGIVDV 176
Cdd:cd06915  134 PD--ASRYGNVTV 144
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 3-235 8.45e-11

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 61.23  E-value: 8.45e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   3 KKAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVthsskasienyfdrnfeleTTLEQKKKF 82
Cdd:PRK15480   4 RKGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILII-------------------STPQDTPRF 64

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  83 -DLLAEISQIvpkHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLLPDVLVKDssgqNDLSRMI-SRYNSSQAAQIMV 160
Cdd:PRK15480  65 qQLLGDGSQW---GLNLQYKVQPSPDGLAQAFIIGEEFIGGDDCALVLGDNIFYG----HDLPKLMeAAVNKESGATVFA 137

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 943359088 161 EAVPDHlvDQYGIVDVKqspNEGESIAMQgivEKPPvgSAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEIQLTD 235
Cdd:PRK15480 138 YHVNDP--ERYGVVEFD---QNGTAISLE---EKPL--QPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITD 202
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-74 5.80e-10

Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family contains proteins similar to prokaryotic phosphocholine (P-cho) cytidylyltransferases. Phosphocholine (PC) cytidylyltransferases catalyze the transfer of a cytidine monophosphate from CTP to phosphocholine to form CDP-choline. PC is the most abundant phospholipid in eukaryotic membranes and it is also important in prokaryotic membranes. For pathogenic prokaryotes, the cell surface PC facilitates the interaction with host surface and induces attachment and invasion. In addition cell wall PC serves as scaffold for a group of choline-binding proteins that are secreted from the cells. Phosphocholine (PC) cytidylyltransferase is a key enzyme in the prokaryotic choline metabolism pathway. It has been hypothesized to consist of a choline transport system, a choline kinase, CTP:phosphocholine cytidylyltransferase, and a choline phosphotransferase that transfers P-Cho from CDP-Cho to either lipoteichoic acid or lipopolysaccharide.


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 58.01  E-value: 5.80e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   5 AVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDRNFELET 74
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNIKF 70
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 10-252 7.71e-10

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: 59.27  E-value: 7.71e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  10 AGLGTRFlpasKS-IPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFdrnfelettleqkkkfdllaei 88
Cdd:COG1207   10 AGKGTRM----KSkLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAAL---------------------- 63

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  89 sqivpKHVSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVL-LP-DV-LVKDSSgqndLSRMISRYNSSQAAQIMVEAVPD 165
Cdd:COG1207   64 -----ADLDVEFVLQEEQLGTGHAVQQALPALPGDDGTVLvLYgDVpLIRAET----LKALLAAHRAAGAAATVLTAELD 134

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 166 hlvD--QYG-IVdvkqspnEGESIAMQGIVE-KppvgSA-PSNLSV----VGRYVLPAKimQLLES----TPKGAGNEIQ 232
Cdd:COG1207  135 ---DptGYGrIV-------RDEDGRVLRIVEeK----DAtEEQRAIreinTGIYAFDAA--ALREAlpklSNDNAQGEYY 198

                        250       260
                 ....*....|....*....|.
gi 943359088 233 LTDAIAML-QDTDTVEAYRMQ 252
Cdd:COG1207  199 LTDVIAIArADGLKVAAVQPE 219
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-56 2.55e-09

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: 56.04  E-value: 2.55e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTH 56
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTH 53
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-68 1.50e-08

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 54.09  E-value: 1.50e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDR 68
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALAR 65
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 4-100 2.22e-08

The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; N-terminal domain of gamma subunit of the eukaryotic translation initiation factor 2B (eIF-2B): eIF-2B is a guanine nucleotide-exchange factor which mediates the exchange of GDP (bound to initiation factor eIF2) for GTP, generating active eIF2.GTP complex. EIF2B is a complex multimeric protein consisting of five subunits named alpha, beta, gamma, delta and epsilon. Subunit gamma shares sequence similarity with epsilon subunit, and with a family of bifunctional nucleotide-binding enzymes such as ADP-glucose pyrophosphorylase, suggesting that epsilon subunit may play roles in nucleotide binding activity. In yeast, eIF2B gamma enhances the activity of eIF2B-epsilon leading to the idea that these subunits form the catalytic subcomplex.


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 53.43  E-value: 2.22e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVT---------HSSKASIENYFDRNFELET 74
Cdd:cd04198    2 QAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVpeeeqaeisTYLRSFPLNLKQKLDEVTI 81

                         90       100
                 ....*....|....*....|....*..
gi 943359088  75 TLEQKKK-FDLLAEISQIVPKHVSVIS 100
Cdd:cd04198   82 VLDEDMGtADSLRHIRKKIKKDFLVLS 108
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-128 3.89e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 54.07  E-value: 3.89e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   1 MIKKAVLPVAGLGTRFlpasKS-IPKEMVTVVDRPAIEYVVREAVEAGIEQIILVT-HSSKasienyfdrnfELETTLEQ 78
Cdd:PRK14354   1 MNRYAIILAAGKGTRM----KSkLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVgHGAE-----------EVKEVLGD 65

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 943359088  79 KKKFdllaeisqivpkhvsvisVRQPQPLGLGHAVLCAKSVVGQDDFAVL 128
Cdd:PRK14354  66 RSEF------------------ALQEEQLGTGHAVMQAEEFLADKEGTTL 97
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 4-246 5.12e-08

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 53.61  E-value: 5.12e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   4 KAVLPVAGLGTRFlpASKsIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHsskasienyfdrnfelettleqkkKFD 83
Cdd:PRK14357   2 RALVLAAGKGTRM--KSK-IPKVLHKISGKPMINWVIDTAKKVAQKVGVVLGH------------------------EAE 54

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  84 LlaeISQIVPKHVSVisVRQPQPLGLGHAVLCAKSVVGQ-DDFAVLLPDV-LVKdssgQNDLSRMISRYNSSQAAQIMVE 161
Cdd:PRK14357  55 L---VKKLLPEWVKI--FLQEEQLGTAHAVMCARDFIEPgDDLLILYGDVpLIS----ENTLKRLIEEHNRKGADVTILV 125

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 162 AVPDHLV---------DQYGIVDVKQSPNEgesiaMQGIVEkppVGSapsnlsvvGRYVLPAKimQLLESTPK----GAG 228
Cdd:PRK14357 126 ADLEDPTgygriirdgGKYRIVEDKDAPEE-----EKKIKE---INT--------GIYVFSGD--FLLEVLPKikneNAK 187

                        250
                 ....*....|....*...
gi 943359088 229 NEIQLTDAIAMLQDTDTV 246
Cdd:PRK14357 188 GEYYLTDAVNFAEKVRVV 205
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-132 2.42e-07

bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase GlmU;


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 51.40  E-value: 2.42e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   5 AVLPVAGLGTRFlpasKS-IPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIEnyfdrnfelettleqkkkfd 83
Cdd:PRK14353   8 AIILAAGEGTRM----KSsLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVA-------------------- 63

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 943359088  84 llAEISQIVPkhvSVISVRQPQPLGLGHAVLCAKSVV--GQDDFAVLLPDV 132
Cdd:PRK14353  64 --AAAAKIAP---DAEIFVQKERLGTAHAVLAAREALagGYGDVLVLYGDT 109
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 4-100 9.66e-07

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: 48.40  E-value: 9.66e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVrEAVE-AGIEQIILVT-----------HSSKASIENYFDRNFE 71
Cdd:cd02507    2 QAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTL-EWLEkAGVEEVFVVCcehsqaiiehlLKSKWSSLSSKMIVDV 80

                         90       100       110
                 ....*....|....*....|....*....|
gi 943359088  72 LETTLEQKKK-FDLLAEISQIVPKHVSVIS 100
Cdd:cd02507   81 ITSDLCESAGdALRLRDIRGLIRSDFLLLS 110
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 4-231 1.27e-06

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: 48.36  E-value: 1.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   4 KAVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVThsskasieNYFDRNFELETTLEQKKkfd 83
Cdd:cd06425    2 KALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAV--------NYRPEDMVPFLKEYEKK--- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  84 LLAEIsqivpkHVSVisvrQPQPLGLGHAVLCAKSVVGQDD--FAVLLPDVLVkdssgQNDLSRMIS-RYNSSQAAQIMV 160
Cdd:cd06425   71 LGIKI------TFSI----ETEPLGTAGPLALARDLLGDDDepFFVLNSDVIC-----DFPLAELLDfHKKHGAEGTILV 135

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 943359088 161 EAVPDhlVDQYGIVDVKQSPNEgesiaMQGIVEKPPVgsAPSNLSVVGRYVLPAKIMQLLESTPKGAGNEI 231
Cdd:cd06425  136 TKVED--PSKYGVVVHDENTGR-----IERFVEKPKV--FVGNKINAGIYILNPSVLDRIPLRPTSIEKEI 197
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-251 5.15e-06

bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate acetyltransferase; Provisional


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 47.67  E-value: 5.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088   6 VLPVAGLGTRFLPAsksIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVT-HSSKasienyfdrnfELETTLEQKkkfdl 84
Cdd:PRK14358  11 VILAAGQGTRMKSA---LPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTgHGAE-----------QVEAALQGS----- 71

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088  85 laeisqivpkhvSVISVRQPQPLGLGHAVLCAKSVVGQDDFAVLlpdVLVKDSS--GQNDLSRMISRYNSSQAA-QIMVE 161
Cdd:PRK14358  72 ------------GVAFARQEQQLGTGDAFLSGASALTEGDADIL---VLYGDTPllRPDTLRALVADHRAQGSAmTILTG 136

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 943359088 162 AVPDhlVDQYG-IVdvkqspnEGESIAMQGIVEKPPVGSAPSNLSVV--GRYVLPAKIMQLLES-TPKGAGNEIQLTDAI 237
Cdd:PRK14358 137 ELPD--ATGYGrIV-------RGADGAVERIVEQKDATDAEKAIGEFnsGVYVFDARAPELARRiGNDNKAGEYYLTDLL 207

                        250
                 ....*....|....*
gi 943359088 238 AML-QDTDTVEAYRM 251
Cdd:PRK14358 208 GLYrAGGAQVRAFKL 222
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 6-69 8.86e-05

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: 43.01  E-value: 8.86e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 943359088   6 VLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVThsSKASIENYFDRN 69
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFIC--RDEHNTKFHLDE 63
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 5-66 1.51e-04

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: 42.21  E-value: 1.51e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 943359088   5 AVLPVAGLGTRFLPASKSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYF 66
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI 64
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
5-68 2.27e-03

CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 38.22  E-value: 2.27e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 943359088   5 AVLPVAGLGTRFlpaskSIPKEMVTVVDRPAIEYVVREAVEAGIEQIILVTHSSKASIENYFDR 68
Cdd:COG2068    6 AIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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