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Conserved domains on  [gi|1176173506|gb|OQX88828|]
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glucose-1-phosphate thymidylyltransferase [candidate division KSB1 bacterium 4484_87]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
rmlA_long super family cl36843
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-353 2.57e-151

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


The actual alignment was detected with superfamily member TIGR01208:

Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 429.90  E-value: 2.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITN-ADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGpVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVD-SRIVSVEEKPK 159
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDgKRILKLVEKPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 160 HPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGWWKDTGKPIDLLEANRLVLEHTDP 239
Cdd:TIGR01208 161 EPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLILDEVER 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 240 KIEGSINgKSSLAGNVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSSEIEYSIILNKCKVLDIGIR 319
Cdd:TIGR01208 241 EVQGVDD-ESKIRGRVVVGEGAKIVNSVIRGPAVIGEDCIIENSYIGPYTSIGEGVVIRDAEVEHSIVLDESVIEGVQAR 319

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1176173506 320 IESSLLGTDVEIVKSEDKPSTHRFFIGDQSRIEL 353
Cdd:TIGR01208 320 IVDSVIGKKVRIKGNRRRPGDLRLTIGDYSQVEL 353
 
Name Accession Description Interval E-value
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-353 2.57e-151

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 429.90  E-value: 2.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITN-ADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGpVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVD-SRIVSVEEKPK 159
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDgKRILKLVEKPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 160 HPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGWWKDTGKPIDLLEANRLVLEHTDP 239
Cdd:TIGR01208 161 EPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLILDEVER 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 240 KIEGSINgKSSLAGNVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSSEIEYSIILNKCKVLDIGIR 319
Cdd:TIGR01208 241 EVQGVDD-ESKIRGRVVVGEGAKIVNSVIRGPAVIGEDCIIENSYIGPYTSIGEGVVIRDAEVEHSIVLDESVIEGVQAR 319

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1176173506 320 IESSLLGTDVEIVKSEDKPSTHRFFIGDQSRIEL 353
Cdd:TIGR01208 320 IVDSVIGKKVRIKGNRRRPGDLRLTIGDYSQVEL 353
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-236 1.53e-127

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: 364.97  E-value: 1.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDSRIVSVEEKPKH 160
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDGRIVRLVEKPKE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176173506 161 PKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGWWKDTGKPIDLLEANRLVLEH 236
Cdd:cd04189   161 PPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEANRLLLDK 236
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-290 4.45e-118

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 343.23  E-value: 4.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNA-DSDEVPRAIGDGSQWGVKITYIPQ 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPeDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEI-VDSRIVSVEEK 157
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGdGLSELLREAAARESGATIFGYKVEDPERYGVVEFdEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 158 PKHPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITG-WWKDTGKPIDLLEANRLVL-- 234
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGfAWLDTGTHESLLEANRFVLti 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176173506 235 EHTDPKIEGSINGKSSLAGNVSVGKGSKIINSnirgpvvigentvVENSYIGPFTS 290
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANS-------------LEKSGYGPYLL 283
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-234 1.02e-62

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: 200.17  E-value: 1.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANK-PILHYAIETVAAAGIKEIGIITNA-DSDEVPRAIGDGSQWGVKITYIPQ 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQeHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKDPF-IFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLA--KVKDPERFGVPEIVDS-RIVSV 154
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRmDLEQAVKFHIEKAADATVTFGivPVEPPTGYGVVEFDDNgRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 155 EEKPKHPK-SHFAVAGIYIYDYHVFE-AVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGW-WKDTGKPIDLLEANR 231
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYaWLDVGTWDSLWEANL 240


                  ...
gi 1176173506 232 LVL 234
Cdd:pfam00483 241 FLL 243
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-233 1.13e-51

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 173.32  E-value: 1.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGII-TNADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIsTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDS-RIVSVEEKP 158
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGhDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNgTAISLEEKP 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176173506 159 KHPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGW-WKDTGKPIDLLEANRLV 233
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYaWLDTGTHQSLIEASNFI 240
 
Name Accession Description Interval E-value
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-353 2.57e-151

glucose-1-phosphate thymidylylransferase, long form; The family of known and putative glucose-1-phosphate thymidyltransferase (also called dTDP-glucose synthase) shows a deep split into a short form (see TIGR01207) and a long form described by this model. The homotetrameric short form is found in numerous bacterial species that incorporate dTDP-L-rhamnose, which it helps synthesize, into the cell wall. It is subject to feedback inhibition. This form, in contrast, is found in many species for which it serves as a sugar-activating enzyme for antibiotic biosynthesis and or other, unknown pathways, and in which dTDP-L-rhamnose is not necessarily produced. Alternate name: dTDP-D-glucose synthase


Pssm-ID: 273500 [Multi-domain]  Cd Length: 353  Bit Score: 429.90  E-value: 2.57e-151
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITN-ADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGpVTGEEIKEIVGEGERFGAKITYIVQG 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVD-SRIVSVEEKPK 159
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGDDDFVVYLGDNLIQDGISRFVKSFEEKDYDALILLTKVRDPTAFGVAVLEDgKRILKLVEKPK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 160 HPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGWWKDTGKPIDLLEANRLVLEHTDP 239
Cdd:TIGR01208 161 EPPSNLAVVGLYMFRPLIFEAIKNIKPSWRGELEITDAIQWLIEKGYKVGGSKVTGWWKDTGKPEDLLDANRLILDEVER 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 240 KIEGSINgKSSLAGNVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSSEIEYSIILNKCKVLDIGIR 319
Cdd:TIGR01208 241 EVQGVDD-ESKIRGRVVVGEGAKIVNSVIRGPAVIGEDCIIENSYIGPYTSIGEGVVIRDAEVEHSIVLDESVIEGVQAR 319

                         330       340       350
                  ....*....|....*....|....*....|....
gi 1176173506 320 IESSLLGTDVEIVKSEDKPSTHRFFIGDQSRIEL 353
Cdd:TIGR01208 320 IVDSVIGKKVRIKGNRRRPGDLRLTIGDYSQVEL 353
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-236 1.53e-127

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: 364.97  E-value: 1.53e-127
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:cd04189     1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITYILQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDSRIVSVEEKPKH 160
Cdd:cd04189    81 EPLGLAHAVLAARDFLGDEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPRRFGVAVVDDGRIVRLVEKPKE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176173506 161 PKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGWWKDTGKPIDLLEANRLVLEH 236
Cdd:cd04189   161 PPSNLALVGVYAFTPAIFDAISRLKPSWRGELEITDAIQWLIDRGRRVGYSIVTGWWKDTGTPEDLLEANRLLLDK 236
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-290 4.45e-118

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 343.23  E-value: 4.45e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNA-DSDEVPRAIGDGSQWGVKITYIPQ 79
Cdd:COG1209     1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPeDGPQFERLLGDGSQLGIKISYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEI-VDSRIVSVEEK 157
Cdd:COG1209    81 PEPLGLAHAFIIAEDFIGGDPVALVLGDNIFYGdGLSELLREAAARESGATIFGYKVEDPERYGVVEFdEDGRVVSLEEK 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 158 PKHPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITG-WWKDTGKPIDLLEANRLVL-- 234
Cdd:COG1209   161 PKEPKSNLAVTGLYFYDNDVVEIAKNLKPSARGELEITDANQAYLERGKLVVELLGRGfAWLDTGTHESLLEANRFVLti 240

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1176173506 235 EHTDPKIEGSINGKSSLAGNVSVGKGSKIINSnirgpvvigentvVENSYIGPFTS 290
Cdd:COG1209   241 EKRQGLKIACPEEIAYRMGWIDAEQLAKLANS-------------LEKSGYGPYLL 283
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
 1-313 6.44e-87

UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The MJ_1101 protein from Methanococcus jannaschii has been characterized as the GlmU enzyme catalyzing the final two steps of UDP-GlcNAc biosynthesis. Many of the genes identified by this model are in proximity to the GlmS and GlmM genes and are also presumed to be GlmU. However, some archaeal genomes contain multiple closely-related homologs from this family and it is not clear what the substrate specificity is for each of them.


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 267.15  E-value: 6.44e-87
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIEYVVQE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIgKDPFIFYLGDNMV-VGGVKRFVDAFESdqvncYLTLAKVKDPERFGVPEIVDSRIVSVEEKPK 159
Cdd:TIGR03992  81 EQLGTADALGSAKEYV-DDEFLVLNGDVLLdSDLLERLIRAEAP-----AIAVVEVDDPSDYGVVETDGGRVTGIVEKPE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 160 HPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGyQIGFSEITGWWKDTGKPIDLLEANRLVLEHTDP 239
Cdd:TIGR03992 155 NPPSNLINAGIYLFSPEIFELLEKTKLSPRGEYELTDALQLLIDEG-KVKAVELDGFWLDVGRPWDLLDANEALLDNLEP 233

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1176173506 240 KIEGSINGKSSLAGNVSVGKGSKIIN-SNIRGPVVIGENTVV-ENSYIGPFTSIQNDCYV-RSSEIEYSIILNKCKV 313
Cdd:TIGR03992 234 RIEGTVEENVTIKGPVVIGEGAVIRSgTYIEGPVYIGKNCDIgPNAYIRPYTVIGNNVHIgNAVEIKNSIIMEGTKI 310
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-233 3.15e-80

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: 244.79  E-value: 3.15e-80
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITN-ADSDEVPRAIGDGSQWGVKITYIPQ 79
Cdd:cd02538     1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTpEDLPLFKELLGDGSDLGIRITYAVQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEI-VDSRIVSVEEK 157
Cdd:cd02538    81 PKPGGLAQAFIIGEEFIGDDPVCLILGDNIFYGqGLSPILQRAAAQKEGATVFGYEVNDPERYGVVEFdENGRVLSIEEK 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176173506 158 PKHPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGyQIGFSEI--TGWWKDTGKPIDLLEANRLV 233
Cdd:cd02538   161 PKKPKSNYAVTGLYFYDNDVFEIAKQLKPSARGELEITDVNNEYLEKG-KLSVELLgrGFAWLDTGTHESLLEASNFV 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-221 1.21e-64

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: 204.35  E-value: 1.21e-64
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQESP 82
Cdd:cd04181     1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  83 LGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDqvNCYLTLA--KVKDPERFGVPEIVDS-RIVSVEEKPK 159
Cdd:cd04181    81 LGTAGAVRNAEDFLGDDDFLVVNGDVLTDLDLSELLRFHREK--GADATIAvkEVEDPSRYGVVELDDDgRVTRFVEKPT 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176173506 160 HPKSHFAVAGIYIYDYHVFEAVNNIEPsaRGELEISDAHQYLIDHGYQIGFsEITGWWKDTG 221
Cdd:cd04181   159 LPESNLANAGIYIFEPEILDYIPEILP--RGEDELTDAIPLLIEEGKVYGY-PVDGYWLDIG 217
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-234 1.02e-62

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: 200.17  E-value: 1.02e-62
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANK-PILHYAIETVAAAGIKEIGIITNA-DSDEVPRAIGDGSQWGVKITYIPQ 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQeHRFMLNELLGDGSKFGVQITYALQ 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKDPF-IFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLA--KVKDPERFGVPEIVDS-RIVSV 154
Cdd:pfam00483  81 PEGKGTAPAVALAADFLGDEKSdVLVLGGDHIYRmDLEQAVKFHIEKAADATVTFGivPVEPPTGYGVVEFDDNgRVIRF 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 155 EEKPKHPK-SHFAVAGIYIYDYHVFE-AVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGW-WKDTGKPIDLLEANR 231
Cdd:pfam00483 161 VEKPKLPKaSNYASMGIYIFNSGVLDfLAKYLEELKRGEDEITDILPKALEDGKLAYAFIFKGYaWLDVGTWDSLWEANL 240


                  ...
gi 1176173506 232 LVL 234
Cdd:pfam00483 241 FLL 243
rmlA TIGR01207
glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase ...
 2-233 2.25e-61

glucose-1-phosphate thymidylyltransferase, short form; Alternate name: dTDP-D-glucose synthase homotetramer This model describes a tightly conserved but broadly distributed subfamily (here designated as short form) of known and putative bacterial glucose-1-phosphate thymidylyltransferases. It is well characterized in several species as the first of four enzymes involved in the biosynthesis of dTDP-L-rhamnose, a cell wall constituent and a feedback inhibitor of the enzyme. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 130274 [Multi-domain]  Cd Length: 286  Bit Score: 198.39  E-value: 2.25e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNA-DSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:TIGR01207   1 KGIILAGGSGTRLYPITRGVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIISTPeDTPRFQRLLGDGSQWGINLSYAVQP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDS-RIVSVEEKP 158
Cdd:TIGR01207  81 SPDGLAQAFIIGEDFIGGDPSALVLGDNIFYGhDLSDLLRRAAARTEGATVFAYQVSDPERYGVVEFDSNgRAISIEEKP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176173506 159 KHPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQ-YLIDHGYQIgfsEITG---WWKDTGKPIDLLEANRLV 233
Cdd:TIGR01207 161 AQPKSNYAVTGLYFYDNRVVEIARQLKPSARGELEITDLNRvYLEEGRLSV---ELLGrgyAWLDTGTHDSLLEASNFI 236
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-239 3.21e-61

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: 196.14  E-value: 3.21e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQES 81
Cdd:COG1208     1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  82 PLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDS-RIVSVEEKPKH 160
Cdd:COG1208    81 PLGTGGALKRALPLLGDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSRYGVVELDGDgRVTRFVEKPEE 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176173506 161 PKSHFAVAGIYIYDYHVFEAVnniepSARGELEISDAHQYLIDHGyQIGFSEITGWWKDTGKPIDLLEANRLVLEHTDP 239
Cdd:COG1208   161 PPSNLINAGIYVLEPEIFDYI-----PEGEPFDLEDLLPRLIAEG-RVYGYVHDGYWLDIGTPEDLLEANALLLSGKAP 233
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-233 1.13e-51

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 173.32  E-value: 1.13e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGII-TNADSDEVPRAIGDGSQWGVKITYIPQE 80
Cdd:PRK15480    5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIsTPQDTPRFQQLLGDGSQWGLNLQYKVQP 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG-GVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDS-RIVSVEEKP 158
Cdd:PRK15480   85 SPDGLAQAFIIGEEFIGGDDCALVLGDNIFYGhDLPKLMEAAVNKESGATVFAYHVNDPERYGVVEFDQNgTAISLEEKP 164

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1176173506 159 KHPKSHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITGW-WKDTGKPIDLLEANRLV 233
Cdd:PRK15480  165 LQPKSNYAVTGLYFYDNDVVEMAKNLKPSARGELEITDINRIYMEQGRLSVAMMGRGYaWLDTGTHQSLIEASNFI 240
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-230 4.16e-41

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: 144.98  E-value: 4.16e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNA---------DSD------------- 58
Cdd:cd02541     1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfDRSyeleetlekkgkt 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  59 ---EVPRAIGDGsqwgVKITYIPQESPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVG---GVKRFVDAFESDQVNCyLTL 132
Cdd:cd02541    81 dllEEVRIISDL----ANIHYVRQKEPLGLGHAVLCAKPFIGDEPFAVLLGDDLIDSkepCLKQLIEAYEKTGASV-IAV 155

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 133 AKVKDPE--RFGVPEI--VDSRIVSVE---EKPKhPK---SHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLI 202
Cdd:cd02541   156 EEVPPEDvsKYGIVKGekIDGDVFKVKglvEKPK-PEeapSNLAIVGRYVLTPDIFDILENTKPGKGGEIQLTDAIAKLL 234

                         250       260
                  ....*....|....*....|....*...
gi 1176173506 203 DHGYQIGFsEITGWWKDTGKPIDLLEAN 230
Cdd:cd02541   235 EEEPVYAY-VFEGKRYDCGNKLGYLKAT 261
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-238 3.82e-36

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 132.46  E-value: 3.82e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNA---------DS--------------- 57
Cdd:COG1210     5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGRgkraiedhfDRsyeleatleakgkee 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  58 --DEVpRAIGDGsqwgVKITYIPQESPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGV---KRFVDAFESDQVNcYLTL 132
Cdd:COG1210    85 llEEV-RSISPL----ANIHYVRQKEPLGLGHAVLCARPFVGDEPFAVLLGDDLIDSEKpclKQMIEVYEETGGS-VIAV 158

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 133 AKVKDPE--RFGV--PEIVDSRIVSVE---EKPKHPK--SHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDAHQYLID 203
Cdd:COG1210   159 QEVPPEEvsKYGIvdGEEIEGGVYRVTglvEKPAPEEapSNLAIVGRYILTPEIFDILEKTKPGAGGEIQLTDAIAALAK 238

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1176173506 204 ----HGYqigfsEITGWWKDTGKPIDLLEAN-RLVLEHTD 238
Cdd:COG1210   239 eepvYAY-----EFEGKRYDCGDKLGYLKATvEFALKRPD 273
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-230 4.12e-33

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: 122.62  E-value: 4.12e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQESP 82
Cdd:cd06426     1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVREDKP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  83 LGLAHVIKIAEDFIgKDPFIFYLGD---NMVVGGVKRFVDAFESDqvncyLTLA----KVKDPerFGVPEIVDSRIVSVE 155
Cdd:cd06426    81 LGTAGALSLLPEKP-TDPFLVMNGDiltNLNYEHLLDFHKENNAD-----ATVCvreyEVQVP--YGVVETEGGRITSIE 152

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176173506 156 EKPKHpkSHFAVAGIYIYDYHVFEavnNIEPSARgeLEISDAHQYLIDHGYQIGFSEITGWWKDTGKPIDLLEAN 230
Cdd:cd06426   153 EKPTH--SFLVNAGIYVLEPEVLD---LIPKNEF--FDMPDLIEKLIKEGKKVGVFPIHEYWLDIGRPEDYEKAN 220
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-234 2.68e-32

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: 120.78  E-value: 2.68e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQ-WGVKITYIPQ 79
Cdd:cd06425     1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLKEYEKkLGIKITFSIE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKD--PFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGV--PEIVDSRIVSVE 155
Cdd:cd06425    81 TEPLGTAGPLALARDLLGDDdePFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPSKYGVvvHDENTGRIERFV 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 156 EKPKHPKSHFAVAGIYIYDYHVfeaVNNIEP-SARGELEISDAhqyLIDHGyQIGFSEITGWWKDTGKPIDLLEANRLVL 234
Cdd:cd06425   161 EKPKVFVGNKINAGIYILNPSV---LDRIPLrPTSIEKEIFPK---MASEG-QLYAYELPGFWMDIGQPKDFLKGMSLYL 233
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-187 8.48e-28

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: 108.41  E-value: 8.48e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKITYIPQESP 82
Cdd:cd06915     1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPEP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  83 LGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIV-DSRIVSVEEKPKHP 161
Cdd:cd06915    81 LGTGGAIKNALPKLPEDQFLVLNGDTYFDVDLLALLAALRASGADATMALRRVPDASRYGNVTVDgDGRVIAFVEKGPGA 160

                         170       180
                  ....*....|....*....|....*.
gi 1176173506 162 KSHFAVAGIYIYDYHVFEAVNNIEPS 187
Cdd:cd06915   161 APGLINGGVYLLRKEILAEIPADAFS 186
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-229 6.11e-20

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: 86.86  E-value: 6.11e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDgSQWGVKITYIP-QE 80
Cdd:cd06422     1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHLGD-SRFGLRITISDePD 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAKVKDPERFGVPEIVDSRIVSVEEKPKH 160
Cdd:cd06422    80 ELLETGGGIKKALPLLGDEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPLVRNPGHNGVGDFSLDADGRLRRGGGG 159

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176173506 161 PKSHFAVAGIYIYDYHVFEavnNIEPsarGELEISDAHQYLIDHGyQIGFSEITGWWKDTGKPIDLLEA 229
Cdd:cd06422   160 AVAPFTFTGIQILSPELFA---GIPP---GKFSLNPLWDRAIAAG-RLFGLVYDGLWFDVGTPERLLAA 221
glgC PRK05293
glucose-1-phosphate adenylyltransferase; Provisional
 1-307 1.12e-19

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 179997 [Multi-domain]  Cd Length: 380  Bit Score: 89.16  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANK-PILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQW-------GV 72
Cdd:PRK05293    4 MLAMILAGGQGTRLGKLTKNIAKPAVPFGGKyRIIDFTLSNCANSGIDTVGVLTQYQPLELNNHIGIGSPWdldringGV 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  73 KI--TYIPQESP---LGLAHVIKIAEDFIGK-DP-FIFYL-GDNMVVGGVKRFVDAFESDQVNcyLTLAKVKDP----ER 140
Cdd:PRK05293   84 TIlpPYSESEGGkwyKGTAHAIYQNIDYIDQyDPeYVLILsGDHIYKMDYDKMLDYHKEKEAD--VTIAVIEVPweeaSR 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 141 FGVPEI-VDSRIVSVEEKPKHPKSHFAVAGIYIYDYHVFEAVnnIEPSARGELEISDAHQ----YLIDHGYQIGFSEITG 215
Cdd:PRK05293  162 FGIMNTdENMRIVEFEEKPKNPKSNLASMGIYIFNWKRLKEY--LIEDEKNPNSSHDFGKnvipLYLEEGEKLYAYPFKG 239

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 216 WWKDTGKPIDLLEAN-RLVLEHT-----DPK-------------------------------IEGSINgKSSLAGNVSVG 258
Cdd:PRK05293  240 YWKDVGTIESLWEANmELLRPENplnlfDRNwriysvnpnlppqyiaenakvknslvvegcvVYGTVE-HSVLFQGVQVG 318

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 1176173506 259 KGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSSEIEYSII 307
Cdd:PRK05293  319 EGSVVKDSVIMPGAKIGENVVIERAIIGENAVIGDGVIIGGGKEVITVI 367
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-197 1.85e-19

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 87.25  E-value: 1.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQW---------- 70
Cdd:PRK10122    4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHASKNAVENHFDTSYELeslleqrvkr 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  71 ------------GVKITYIPQESPLGLAHVIKIAEDFIGKDPFIFYLGDNMVVGG------------VKRFVDAFESdQV 126
Cdd:PRK10122   84 qllaevqsicppGVTIMNVRQGQPLGLGHSILCARPAIGDNPFVVVLPDVVIDDAsadplrynlaamIARFNETGRS-QV 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176173506 127 NCYLTLAKVKDPERFGVPEIVD-----SRIVSVEEKPKHPK---SHFAVAGIYIYDYHVFEAVNNIEPSARGELEISDA 197
Cdd:PRK10122  163 LAKRMPGDLSEYSVIQTKEPLDregkvSRIVEFIEKPDQPQtldSDLMAVGRYVLSADIWPELERTEPGAWGRIQLTDA 241
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-209 3.55e-17

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: 79.48  E-value: 3.55e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLR---PlthtqnKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSqwgvkITYIPQ 79
Cdd:cd02540     1 AVILAAGKGTRMKsdlP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPN-----VEFVLQ 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFIGKDPfifylGDNMVVGG---------VKRFVDAFEsdQVNCYLTL--AKVKDPERFGvpeivd 148
Cdd:cd02540    70 EEQLGTGHAVKQALPALKDFE-----GDVLVLYGdvplitpetLQRLLEAHR--EAGADVTVltAELEDPTGYG------ 136

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176173506 149 sRIVS---------VEEK---PKHPKSHFAVAGIYIYD-YHVFEAVNNIEPS-ARGELEISDAHQYLIDHGYQIG 209
Cdd:cd02540   137 -RIIRdgngkvlriVEEKdatEEEKAIREVNAGIYAFDaEFLFEALPKLTNNnAQGEYYLTDIIALAVADGLKVA 210
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-313 4.89e-17

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: 81.61  E-value: 4.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLR---PlthtqnKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDgsqwgVKITYI 77
Cdd:COG1207     3 LAVVILAAGKGTRMKsklP------KVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALAD-----LDVEFV 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  78 PQESPLGLAHVIKIAEDFIGKDPfifylGDNMVVGG---------VKRFVDAFESDQVNCYLTLAKVKDPERFGvpeivd 148
Cdd:COG1207    72 LQEEQLGTGHAVQQALPALPGDD-----GTVLVLYGdvpliraetLKALLAAHRAAGAAATVLTAELDDPTGYG------ 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 149 sRIVS---------VEEK---PKHPKSHFAVAGIYIYD-YHVFEAVNNIEPS-ARGELEISDAHQYLIDHGYQIG----- 209
Cdd:COG1207   141 -RIVRdedgrvlriVEEKdatEEQRAIREINTGIYAFDaAALREALPKLSNDnAQGEYYLTDVIAIARADGLKVAavqpe 219

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 210 -FSEITGwwkdTGKPIDLLEANRL----VLEH--------TDPK---IEgsingksslaGNVSVGKGSKI-INSNIRGPV 272
Cdd:COG1207   220 dPWEVLG----VNDRVQLAEAERIlqrrIAERlmragvtiIDPAttyID----------GDVEIGRDVVIdPNVILEGKT 285

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1176173506 273 VIGENTVvensyIGPFTSIQN-----DCYVRSSEIEYSIILNKCKV 313
Cdd:COG1207   286 VIGEGVV-----IGPNCTLKDstigdGVVIKYSVIEDAVVGAGATV 326
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-347 8.82e-14

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 72.17  E-value: 8.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHtqnKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQwgvkitYIPQESP 82
Cdd:PRK14354    5 AIILAAGKGTRMKSKLP---KVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLGDRSE------FALQEEQ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  83 LGLAHVIKIAEDFI-GKDpfifylGDNMVVGG---------VKRFVDAFESDQ-VNCYLTlAKVKDPERFG--------- 142
Cdd:PRK14354   76 LGTGHAVMQAEEFLaDKE------GTTLVICGdtplitaetLKNLIDFHEEHKaAATILT-AIAENPTGYGriirnenge 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 143 VPEIVDSRIVSVEEKPKHPKShfavAGIYIYDYHV-FEAVNNIEP-SARGELEISDAHQYLIDHGYQIG------FSEIT 214
Cdd:PRK14354  149 VEKIVEQKDATEEEKQIKEIN----TGTYCFDNKAlFEALKKISNdNAQGEYYLTDVIEILKNEGEKVGayqtedFEESL 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 215 GwwkdTGKPIDLLEA-----NRLVLEHTdpkIEGS--INGKSS-LAGNVSVGKGSKII-NSNIRGPVVIGENTVV-ENSY 284
Cdd:PRK14354  225 G----VNDRVALAEAekvmrRRINEKHM---VNGVtiIDPESTyIDADVEIGSDTVIEpGVVIKGNTVIGEDCVIgPGSR 297

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1176173506 285 IGPfTSIQNDCYVRSSEIEYSIILNKCKvldIG----IRIESSL-----LGTDVEIVKSEDKPST---HRFFIGD 347
Cdd:PRK14354  298 IVD-STIGDGVTITNSVIEESKVGDNVT---VGpfahLRPGSVIgeevkIGNFVEIKKSTIGEGTkvsHLTYIGD 368
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-233 3.30e-13

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 68.34  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGdgsQWGVKITYIpqES 81
Cdd:COG1213     1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALA---RPGPDVTFV--YN 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  82 PL----GLAHVIKIAEDFIGKDPFIFYlGDnmVV---GGVKRFVDAFESDQVNC-YLTLAKVKDPERFGVPEivDSRIVS 153
Cdd:COG1213    76 PDydetNNIYSLWLAREALDEDFLLLN-GD--VVfdpAILKRLLASDGDIVLLVdRKWEKPLDEEVKVRVDE--DGRIVE 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 154 VEekpKHPKSHFAVA---GIYIYDY----HVFEAVNNIEPSARGELEISDAHQYLIDHGYQIGFSEITG-WWK--DTgkP 223
Cdd:COG1213   151 IG---KKLPPEEADGeyiGIFKFSAegaaALREALEALIDEGGPNLYYEDALQELIDEGGPVKAVDIGGlPWVeiDT--P 225

                         250
                  ....*....|
gi 1176173506 224 IDLLEANRLV 233
Cdd:COG1213   226 EDLERAEELF 235
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-347 7.50e-13

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 69.02  E-value: 7.50e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPlthTQNKHLIPIANKPILHYAIETVAAAGiKEIGIITNADSDEVPRAIgdgSQWgVKITYipQE 80
Cdd:PRK14357    1 MRALVLAAGKGTRMKS---KIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLL---PEW-VKIFL--QE 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFI--GKDPFIFYlGDNMVV--GGVKRFVDAFESDQVNCYLTLAKVKDPERFG--VPEIVDSRIVSV 154
Cdd:PRK14357   71 EQLGTAHAVMCARDFIepGDDLLILY-GDVPLIseNTLKRLIEEHNRKGADVTILVADLEDPTGYGriIRDGGKYRIVED 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 155 EEKPKHPKSHFAV-AGIYIYD-YHVFEAVNNIEP-SARGELEISDAhqylidhgyqIGFSEITGwwkdTGKPIDLLEA-- 229
Cdd:PRK14357  150 KDAPEEEKKIKEInTGIYVFSgDFLLEVLPKIKNeNAKGEYYLTDA----------VNFAEKVR----VVKTEDLLEItg 215

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 230 --NRLVLEHTDPKIEGSINGKSSLAGNVSVGKGSKIINSNIR-GPVVI--------GENTVVENSYIGPFTSIQnDCYVR 298
Cdd:PRK14357  216 vnTRIQLAWLEKQLRMRILEELMENGVTILDPNTTYIHYDVEiGMDTIiypmtfieGKTRIGEDCEIGPMTRIV-DCEIG 294

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1176173506 299 S------SEIEYSIILNKCKV-----LDIGIRI-ESSLLGTDVEIVKS---EDKPSTHRFFIGD 347
Cdd:PRK14357  295 NnvkiirSECEKSVIEDDVSVgpfsrLREGTVLkKSVKIGNFVEIKKStigENTKAQHLTYLGD 358
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-168 3.50e-12

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: 64.99  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWGVKIT----Y 76
Cdd:cd04198     1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSFPLNLKQKldevT 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  77 IPQESPLGLAHVIKIAEDFIGKDpFIFYLGDNMVVGGVKRFVDAFESDQVNCYLTLAkvkdperfgvPEIVDSRIVSVEE 156
Cdd:cd04198    81 IVLDEDMGTADSLRHIRKKIKKD-FLVLSCDLITDLPLIELVDLHRSHDASLTVLLY----------PPPVSSEQKGGKG 149

                         170
                  ....*....|..
gi 1176173506 157 KPKHPKSHFAVA 168
Cdd:cd04198   150 KSKKADERDVIG 161
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 1-96 8.33e-12

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 63.81  E-value: 8.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAI--GDGSQWGVK----- 73
Cdd:cd02507     1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLlkSKWSSLSSKmivdv 80

                          90       100
                  ....*....|....*....|....*...
gi 1176173506  74 ITYIPQESpLGLAHVI-----KIAEDFI 96
Cdd:cd02507    81 ITSDLCES-AGDALRLrdirgLIRSDFL 107
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-203 9.64e-12

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 64.93  E-value: 9.64e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   2 KALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSD------------------EVPRA 63
Cdd:PRK13389   10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNsienhfdtsfeleamlekRVKRQ 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  64 IGDGSQW----GVKITYIPQESPLGLAHVIKIAEDFIGKDPFIFYLGDNMvvggvkrfVDAFESD--QVNCYLTLAK--- 134
Cdd:PRK13389   90 LLDEVQSicppHVTIMQVRQGLAKGLGHAVLCAHPVVGDEPVAVILPDVI--------LDEYESDlsQDNLAEMIRRfde 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 135 ----------VKDPERFGVpeiVDSR-----------IVSVEEKPK--HPKSHFAVAGIYIYDYHVFEAVNNIEPSARGE 191
Cdd:PRK13389  162 tghsqimvepVADVTAYGV---VDCKgvelapgesvpMVGVVEKPKadVAPSNLAIVGRYVLSADIWPLLAKTPPGAGDE 238

                         250
                  ....*....|..
gi 1176173506 192 LEISDAHQYLID 203
Cdd:PRK13389  239 IQLTDAIDMLIE 250
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-54 2.26e-11

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 63.02  E-value: 2.26e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1176173506   3 ALITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITN 54
Cdd:cd02523     1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTG 52
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
 3-294 7.23e-11

Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate transport and metabolism];


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 62.79  E-value: 7.23e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHTQNKHLIPIANKpilhY-----AIETVAAAGIKEIGIITNADSDEVPRAIGDGSQWgvkityi 77
Cdd:COG0448     4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK----YriidfPLSNCVNSGIRRVGVLTQYKSHSLNDHIGSGKPW------- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  78 pqesplglahvikiaeDFIGKDPFIF-------------YLGD------NMvvggvkRFVDAFESDQV------NCY--- 129
Cdd:COG0448    73 ----------------DLDRKRGGVFilppyqqregedwYQGTadavyqNL------DFIERSDPDYVlilsgdHIYkmd 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 130 --------------LTLA----KVKDPERFGVPEI-VDSRIVSVEEKPKHPKSHFAVAGIYIYDYHVF-EAVNNIEPSAR 189
Cdd:COG0448   131 yrqmldfhiesgadITVAcievPREEASRFGVMEVdEDGRITEFEEKPKDPKSALASMGIYVFNKDVLiELLEEDAPNSS 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 190 GELeISDAHQYLIDHGyQIGFSEITGWWKDTGKPIDLLEANRLVLE--------------HTDPK--------------- 240
Cdd:COG0448   211 HDF-GKDIIPRLLDRG-KVYAYEFDGYWRDVGTIDSYYEANMDLLDpepefnlydpewpiYTKQKdlppakfvrggkvkn 288

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176173506 241 --------IEGSINgKSSLAGNVSVGKGSKIINSNIRGPVVIGENTVVENS------YIGPFTSIQND 294
Cdd:COG0448   289 slvsngciISGTVE-NSVLFRGVRVESGAVVENSVIMPGVVIGEGAVIENAiidknvVIPPGVVIGED 355
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-86 1.07e-09

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: 58.42  E-value: 1.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGG--KGTRLRPLTHTQNKHLIPIANKPILHYAIETVAA-AGIKEIGIITNADSDEVPRAIGDGSQ-WGVKITYIP 78
Cdd:cd06428     1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKvPDLKEVLLIGFYPESVFSDFISDAQQeFNVPIRYLQ 80


                  ....*...
gi 1176173506  79 QESPLGLA 86
Cdd:cd06428    81 EYKPLGTA 88
LbH_G1P_TT_C_like cd05636
Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix ...
 239-313 1.21e-09

Putative glucose-1-phosphate thymidylyltransferase, C-terminal Left-handed parallel beta-Helix (LbH) domain: Proteins in this family show simlarity to glucose-1-phosphate adenylyltransferases in that they contain N-terminal catalytic domains that resemble a dinucleotide-binding Rossmann fold and C-terminal LbH fold domains. Members in this family are predicted to be glucose-1-phosphate thymidylyltransferases, which are involved in the dTDP-L-rhamnose biosynthetic pathway. Glucose-1-phosphate thymidylyltransferase catalyzes the synthesis of deoxy-thymidine di-phosphate (dTDP)-L-rhamnose, an important component of the cell wall of many microorganisms. The C-terminal LbH domain contains multiple turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100060 [Multi-domain]  Cd Length: 163  Bit Score: 56.44  E-value: 1.21e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176173506 239 PKIEGSINGKSSLAGNVSVGKGSKII-NSNIRGPVVIGENTVV-ENSYIGPFTSIQNDCYV-RSSEIEYSIILNKCKV 313
Cdd:cd05636     2 DEIEGTVEEGVTIKGPVWIGEGAIVRsGAYIEGPVIIGKGCEIgPNAYIRGYTVLGDGCVVgNSVEVKNSIIMDGTKV 79
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-331 7.26e-09

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 57.06  E-value: 7.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPlthTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGSQwgvkITYIPQESP 82
Cdd:PRK14355    6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVREHFAGDGD----VSFALQEEQ 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  83 LGLAHVIKIAEDFIgkDPF----IFYLGDNMVV--GGVKRFVDAFESDQVNCYLTLAKVKDPerFGVPEIV---DSRIVS 153
Cdd:PRK14355   79 LGTGHAVACAAPAL--DGFsgtvLILCGDVPLLraETLQGMLAAHRATGAAVTVLTARLENP--FGYGRIVrdaDGRVLR 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 154 -VEEKPKHPKSHFAV---AGIYIYDY-HVFEAVNNI-EPSARGELEISDAHQYLIDHGYQIGFSEITgwwkdtgKPIDLL 227
Cdd:PRK14355  155 iVEEKDATPEERSIRevnSGIYCVEAaFLFDAIGRLgNDNAQGEYYLTDIVAMAAAEGLRCLAFPVA-------DPDEIM 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 228 EAN-RLVLEHTDPKIEGSINGKSSLAGNVSVGKGSKIINsniRGpVVIGENTVVE-NSYIGPFTSIQNDCyvrssEIEYS 305
Cdd:PRK14355  228 GVNdRAQLAEAARVLRRRINRELMLAGVTLIDPETTYID---RG-VVIGRDTTIYpGVCISGDTRIGEGC-----TIEQG 298

                         330       340       350
                  ....*....|....*....|....*....|.
gi 1176173506 306 IILNKCKVLD-----IGIRIESSLLGTDVEI 331
Cdd:PRK14355  299 VVIKGCRIGDdvtvkAGSVLEDSVVGDDVAI 329
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-113 1.58e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 52.56  E-value: 1.58e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHtqnKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGsqwGVKITYIPQESP 82
Cdd:PRK14353    8 AIILAAGEGTRMKSSLP---KVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAEAVAAAAAKI---APDAEIFVQKER 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1176173506  83 LGLAHVIKIAEDFIGKdpfiFYlGDNMVVGG 113
Cdd:PRK14353   82 LGTAHAVLAAREALAG----GY-GDVLVLYG 107
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-56 3.03e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 50.52  E-value: 3.03e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1176173506   3 ALITSGGKGTRLRPlthTQNKHLIPIANKPILHYAIETVAAAG-IKEIGIITNAD 56
Cdd:PRK00155    6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPPD 57
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 11-70 6.94e-07

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 49.53  E-value: 6.94e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  11 GTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIgDGSQW 70
Cdd:cd04197    11 NRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYI-EKSKW 69
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-150 2.80e-06

GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133025 [Multi-domain]  Cd Length: 186  Bit Score: 47.17  E-value: 2.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRplthtQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDGsqwGVKITYIPQESp 82
Cdd:cd04182     3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGL---PVVVVINPDWE- 73

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1176173506  83 LGLAHVIKIAEDFIGKDP--FIFYLGDnMV---VGGVKRFVDAFESDqvNCYLTLAKVKDpeRFGVPEIVDSR 150
Cdd:cd04182    74 EGMSSSLAAGLEALPADAdaVLILLAD-QPlvtAETLRALIDAFRED--GAGIVAPVYQG--RRGHPVLFPRS 141
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-303 2.89e-06

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 48.95  E-value: 2.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRL---RPlthtqnKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGDgsqwgVKITYIPQ 79
Cdd:PRK14356    8 ALILAAGKGTRMhsdKP------KVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVRAAFPD-----EDARFVLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  80 ESPLGLAHVIKIAEDFI---GKDPFIFYLGDNMVV--GGVKRFVDAFESDQVnCYLTLaKVKDPERFG--------VPEI 146
Cdd:PRK14356   77 EQQLGTGHALQCAWPSLtaaGLDRVLVVNGDTPLVttDTIDDFLKEAAGADL-AFMTL-TLPDPGAYGrvvrrnghVAAI 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 147 VDSRivSVEEKPKHPKSHFAVAGIYIYDyhvFEAVNNIEP-----SARGELEISDahqyLIDHGYQIGFSeITGwwKDTG 221
Cdd:PRK14356  155 VEAK--DYDEALHGPETGEVNAGIYYLR---LDAVESLLPrltnaNKSGEYYITD----LVGLAVAEGMN-VLG--VNCG 222

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 222 KPIDLLEAN--------------RLVLEHtdpkIEGSINGKSslAGNVSVGKGSKI-INSNIRGPVvigenTVVENSYIG 286
Cdd:PRK14356  223 EDPNLLGVNtpaelvrseellraRIVEKH----LESGVLIHA--PESVRIGPRATIePGAEIYGPC-----EIYGASRIA 291

                         330
                  ....*....|....*..
gi 1176173506 287 PFTSIQNDCYVRSSEIE 303
Cdd:PRK14356  292 RGAVIHSHCWLRDAVVS 308
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-88 7.88e-06

MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine dinucleotide biosynthesis protein A). The family also includes a wide range of other NTP transferase domain.


Pssm-ID: 463715 [Multi-domain]  Cd Length: 159  Bit Score: 45.26  E-value: 7.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRplthtQNKHLIPIANKPILHYAIETVAAAGiKEIGIITNAdsDEVPRAIgdgSQWGVKITY--IPQE 80
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND--EEVLAAL---AGLGVPVVPdpDPGQ 69

                          90
                  ....*....|...
gi 1176173506  81 SPL-----GLAHV 88
Cdd:pfam12804  70 GPLagllaALRAA 82
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-163 1.65e-05

G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; Alpha-D-Glucose-1-phosphate Cytidylyltransferase catalyzes the production of CDP-D-Glucose from alpha-D-Glucose-1-phosphate and MgCTP as substrate. CDP-D-Glucose is the precursor for synthesizing four of the five naturally occurring 3,6-dideoxy sugars-abequose (3,6-dideoxy-D-Xylo-hexose), ascarylose (3,6-dideoxy-L-arabino-hexose), paratose (3,6-dideoxy-D-ribohexose), and tyvelose (3,6-dideoxy-D-arabino-hexose. Deoxysugars are ubiquitous in nature where they function in a variety of biological processes, including cell adhesion, immune response, determination of ABO blood groups, fertilization, antibiotic function, and microbial pathogenicity.


Pssm-ID: 133015 [Multi-domain]  Cd Length: 253  Bit Score: 45.64  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   3 ALITSGGKGTRLRPLTHTQNKHLIPIANKPIL--------HYAI-ETVAAAG-----IKE-----------IGIITNADS 57
Cdd:cd02524     1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILwhimkiysHYGHnDFILCLGykghvIKEyflnyflhnsdVTIDLGTNR 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  58 DEV-PRAIGDgsqWGVKITYIPQESPLGlaHVIKIAEDFIGKD-PFIFYLGDnmvvgGV-----KRFVDAFESDQVNCyl 130
Cdd:cd02524    81 IELhNSDIED---WKVTLVDTGLNTMTG--GRLKRVRRYLGDDeTFMLTYGD-----GVsdvniNALIEFHRSHGKLA-- 148

                         170       180       190
                  ....*....|....*....|....*....|....
gi 1176173506 131 TLAKVKDPERFGVPEIV-DSRIVSVEEKPKHPKS 163
Cdd:cd02524   149 TVTAVHPPGRFGELDLDdDGQVTSFTEKPQGDGG 182
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 25-131 2.98e-05

Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a common GT-A type structural fold; Glycosyltransferases (GTs) are enzymes that synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein. Based on the stereochemistry of the donor and acceptor molecules, GTs are classified as either retaining or inverting enzymes. To date, all GT structures adopt one of two possible folds, termed GT-A fold and GT-B fold. This hierarchy includes diverse families of glycosyl transferases 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. The majority of the proteins in this superfamily are Glycosyltransferase family 2 (GT-2) proteins. But it also includes families GT-43, GT-6, GT-8, GT13 and GT-7; which are evolutionarily related to GT-2 and share structure similarities.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 43.65  E-value: 2.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  25 LIPIAN-KPILHYAIETVAAAGIK--EIGIITNADSDEVPRAIGDGSQWGVKITYIPQESPLGLAHVIKIAEDFIGKDPF 101
Cdd:cd00761     2 IIPAYNeEPYLERCLESLLAQTYPnfEVIVVDDGSTDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGEYI 81

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1176173506 102 IFYLGDNMVVGG-VKRFVDAFESDQVNCYLT 131
Cdd:cd00761    82 LFLDADDLLLPDwLERLVAELLADPEADAVG 112
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 244-302 1.57e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 43.44  E-value: 1.57e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1176173506 244 SINGKSSLAGNVSVGKGSKIINSNIRGPVVIgENTVVENSYIGPFTSIQNDCYVRSSEI 302
Cdd:PRK14359  261 EFEGECELEEGVRILGKSKIENSHIKAHSVI-EESIIENSDVGPLAHIRPKSEIKNTHI 318
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-213 1.74e-04

GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; GT2_BcbE_like: The bcbE gene is one of the genes in the capsule biosynthetic locus of Pasteurella multocida. Its deducted product is likely involved in the biosynthesis of the polysaccharide capsule, which is found on surface of a wide range of bacteria. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 42.24  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   4 LITSGGKGTRLRPLTHTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNAD---SDEVPRAIGDGSQwGVKITYIPQE 80
Cdd:cd04183     2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEhntKFHLDESLKLLAP-NATVVELDGE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SpLGLAHVIKIAEDFI-GKDPFIFYLGDNMVVGGVKRFVDAF-ESDQVNCYLTLAKVKDpeRFGVPEIVDSRIVsVEEKP 158
Cdd:cd04183    81 T-LGAACTVLLAADLIdNDDPLLIFNCDQIVESDLLAFLAAFrERDLDGGVLTFFSSHP--RWSYVKLDENGRV-IETAE 156

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1176173506 159 KHPKSHFAVAGIYIY----DYhvFEAVNN-IEPSAR--GELEISDAHQYLIDHGYQIGFSEI 213
Cdd:cd04183   157 KEPISDLATAGLYYFksgsLF--VEAAKKmIRKDDSvnGEFYISPLYNELILDGKKVGIYLI 216
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-292 1.90e-04

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.04  E-value: 1.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRPlthTQNKHLIPIANKPILHYAIETVAAAGIKEIGIITNADSDEVPRAIGdgsqwGVKITYIPQE 80
Cdd:PRK14358    8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQ-----GSGVAFARQE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506  81 SPLGLAHVIKIAEDFIGK---DPFIFYlGDNMVV--GGVKRFVDAFESDqvNCYLTLAKVKDPERFGVPEIVDS------ 149
Cdd:PRK14358   80 QQLGTGDAFLSGASALTEgdaDILVLY-GDTPLLrpDTLRALVADHRAQ--GSAMTILTGELPDATGYGRIVRGadgave 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 150 RIvsVEEKPKHPKSHfAV----AGIYIYDYHVFEAVNNI-EPSARGELEISDAHQYLIDHGYQIGFSEITgwwkdtgKPI 224
Cdd:PRK14358  157 RI--VEQKDATDAEK-AIgefnSGVYVFDARAPELARRIgNDNKAGEYYLTDLLGLYRAGGAQVRAFKLS-------DPD 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 225 DLLEAN--------------RLVLEH-------TDP---KIEGSIN--------------GKSSLAGNVSVGKGSKIINS 266
Cdd:PRK14358  227 EVLGANdraglaqleatlrrRINEAHmkagvtlQDPgtiLIEDTVTlgrdvtiepgvllrGQTRVADGVTIGAYSVVTDS 306

                         330       340       350
                  ....*....|....*....|....*....|..
gi 1176173506 267 NIRGPVVIGENTVVEN------SYIGPFTSIQ 292
Cdd:PRK14358  307 VLHEGAVIKPHSVLEGaevgagSDVGPFARLR 338
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-88 3.07e-04

Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; Molybdopterin-guanine dinucleotide biosynthesis protein A is part of the Pathway/BioSystem: Molybdopterin biosynthesis


Pssm-ID: 440509 [Multi-domain]  Cd Length: 188  Bit Score: 41.33  E-value: 3.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLRplthtQNKHLIPIANKPILHYAIETVAAAgIKEIGIITNADSDEvpraigdgSQWGVKITY--IP 78
Cdd:COG0746     5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPERY--------AALGVPVVPddPP 70

                          90
                  ....*....|....*
gi 1176173506  79 QESPL-----GLAHV 88
Cdd:COG0746    71 GAGPLagilaALEAA 85
Fucokinase pfam07959
L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated ...
 249-303 4.29e-04

L-fucokinase; In the salvage pathway of GDP-L-fucose, free cytosolic fucose is phosphorylated by L-fucokinase to form L-fucose-L-phosphate, which is then further converted to GDP-L-fucose in the reaction catalyzed by GDP-L-fucose pyrophosphorylase.


Pssm-ID: 462323  Cd Length: 405  Bit Score: 41.87  E-value: 4.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1176173506 249 SSLAGNVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSSEIE 303
Cdd:pfam07959 261 SVIANARQLKAGASVINSVLEPGVSVGPGSVIEYCHLGGPVSIGSGCILSGLDLS 315
LbH_eIF2B_epsilon cd05787
eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 254-331 4.36e-04

eIF-2B epsilon subunit, central Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B epsilon subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold, a central LbH domain containing 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X), and a C-terminal domain of unknown function that is present in eIF-4 gamma, eIF-5, and eIF-2B epsilon. The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100061 [Multi-domain]  Cd Length: 79  Bit Score: 38.33  E-value: 4.36e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1176173506 254 NVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCyvrssEIEYSIILNKCKVLDiGIRIE-SSLLGTDVEI 331
Cdd:cd05787     5 GTSIGEGTTIKNSVIGRNCKIGKNVVIDNSYIWDDVTIEDGC-----TIHHSIVADGAVIGK-GCTIPpGSLISFGVVI 77
LbH_G1P_AT_C_like cd03356
Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to ...
 253-331 1.49e-03

Left-handed parallel beta-Helix (LbH) domain of a group of proteins with similarity to glucose-1-phosphate adenylyltransferase: Included in this family are glucose-1-phosphate adenylyltransferase, mannose-1-phosphate guanylyltransferase, and the eukaryotic translation initiation factor eIF-2B subunits, epsilon and gamma. Most members of this family contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold, followed by a LbH fold domain with at least 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). eIF-2B epsilon contains an additional domain of unknown function at the C-terminus. Proteins containing hexapeptide repeats are often enzymes showing acyltransferase activity.


Pssm-ID: 100046 [Multi-domain]  Cd Length: 79  Bit Score: 36.84  E-value: 1.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506 253 GNVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSseieySIILNKCKVLDiGIRIES-SLLGTDVEI 331
Cdd:cd03356     4 ESTVIGENAIIKNSVIGDNVRIGDGVTITNSILMDNVTIGANSVIVD-----SIIGDNAVIGE-NVRVVNlCIIGDDVVV 77
LbH_eIF2B_gamma_C cd04652
eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a ...
 226-303 1.68e-03

eIF-2B gamma subunit, C-terminal Left-handed parallel beta-Helix (LbH) domain: eIF-2B is a eukaryotic translation initiator, a guanine nucleotide exchange factor (GEF) composed of five different subunits (alpha, beta, gamma, delta and epsilon). eIF2B is important for regenerating GTP-bound eIF2 during the initiation process. This event is obligatory for eIF2 to bind initiator methionyl-tRNA, forming the ternary initiation complex. The eIF-2B gamma subunit contains an N-terminal domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH domain with 4 turns, each containing three imperfect tandem repeats of a hexapeptide repeat motif (X-[STAV]-X-[LIV]-[GAED]-X). The epsilon and gamma subunits form the catalytic subcomplex of eIF-2B, which binds eIF2 and catalyzes guanine nucleotide exchange.


Pssm-ID: 100057 [Multi-domain]  Cd Length: 81  Bit Score: 36.79  E-value: 1.68e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1176173506 226 LLEANRLVLEHTdpkiegSINgKSSLAGNVSVGKGSKIINSNIRGPVVIGENTVVENSYIGPFTSIQNDCYVRSSEIE 303
Cdd:cd04652     1 LVGENTQVGEKT------SIK-RSVIGANCKIGKRVKITNCVIMDNVTIEDGCTLENCIIGNGAVIGEKCKLKDCLVG 71
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-84 3.71e-03

MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme molybdopterin-guanine dinucleotide biosynthesis protein A (MobA). All mononuclear molybdoenzymes bind molybdenum in complex with an organic cofactor termed molybdopterin (MPT). In many bacteria, including Escherichia coli, molybdopterin can be further modified by attachment of a GMP group to the terminal phosphate of molybdopterin to form molybdopterin guanine dinucleotide (MGD). This GMP attachment step is catalyzed by MobA, by linking a guanosine 5'-phosphate to MPT forming molybdopterin guanine dinucleotide. This reaction requires GTP, MgCl2, and the MPT form of the cofactor. It is a reaction unique to prokaryotes, and therefore may represent a potential drug target.


Pssm-ID: 133000 [Multi-domain]  Cd Length: 181  Bit Score: 37.94  E-value: 3.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1176173506   1 MKALITSGGKGTRLrplthTQNKHLIPIANKPILHYAIETVAAAgIKEIGIITNADSDEVPRaigdgsqWGVKITY--IP 78
Cdd:cd02503     1 ITGVILAGGKSRRM-----GGDKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERYAL-------LGVPVIPdePP 67


                  ....*.
gi 1176173506  79 QESPLG 84
Cdd:cd02503    68 GKGPLA 73
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-54 5.79e-03

GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate guanylyltransferase, also called GDP-mannose pyrophosphorylase (GDP-MP), catalyzes the formation of GDP-Mannose from mannose-1-phosphate and GTP. Mannose is a key monosaccharide for glycosylation of proteins and lipids. GDP-Mannose is the activated donor for mannosylation of various biomolecules. This enzyme is known to be bifunctional, as both mannose-6-phosphate isomerase and mannose-1-phosphate guanylyltransferase. This CD covers the N-terminal GDP-mannose-1-phosphate guanylyltransferase domain, whereas the isomerase function is located at the C-terminal half. GDP-MP is a member of the nucleotidyltransferase family of enzymes.


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 37.94  E-value: 5.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1176173506   1 MKALITSGGKGTRLRPLTHTQN-KHLIPIA-NKPILHYAIETVA-AAGIKEIGIITN 54
Cdd:cd02509     1 IYPVILAGGSGTRLWPLSRESYpKQFLKLFgDKSLLQQTLDRLKgLVPPDRILVVTN 57
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-53 9.60e-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: 36.79  E-value: 9.60e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1176173506   8 GGKGTRLRPLthtqNKHLIPIANKPILHYAIETVAAAGIKEIGIIT 53
Cdd:COG2266     3 GGKGTRLGGG----EKPLLEICGKPMIDRVIDALEESCIDKIYVAV 44
 
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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