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Conserved domains on  [gi|818342831|gb|KKQ24813|]
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Glucose-1-phosphate cytidylyltransferase [Candidatus Roizmanbacteria bacterium GW2011_GWC1_37_12]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may 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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
3-256 3.20e-117

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.


The actual alignment was detected with superfamily member cd02524:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 253  Bit Score: 335.70  E-value: 3.20e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFTSDFTLDTRNHK 82
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 PKFYledRDEVDNFEITFVDTGIETMPGERILRCQKYIpKKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGVHPR 162
Cdd:cd02524   81 IELH---NSDIEDWKVTLVDTGLNTMTGGRLKRVRRYL-GDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 163 SKYGLIKTTKDNFVTKFVEKPVLND-WINGGFMIFDKRAFNYINPGEM--EHDLLKRLALKNELSIYYHNNFWFCMDTYK 239
Cdd:cd02524  157 GRFGELDLDDDGQVTSFTEKPQGDGgWINGGFFVLEPEVFDYIDGDDTvfEREPLERLAKDGELMAYKHTGFWQCMDTLR 236
                        250
                 ....*....|....*..
gi 818342831 240 EVEDLNKMWKEGKAAWK 256
Cdd:cd02524  237 DKQTLEELWNSGKAPWK 253
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-256 3.20e-117

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: 335.70  E-value: 3.20e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFTSDFTLDTRNHK 82
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 PKFYledRDEVDNFEITFVDTGIETMPGERILRCQKYIpKKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGVHPR 162
Cdd:cd02524   81 IELH---NSDIEDWKVTLVDTGLNTMTGGRLKRVRRYL-GDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 163 SKYGLIKTTKDNFVTKFVEKPVLND-WINGGFMIFDKRAFNYINPGEM--EHDLLKRLALKNELSIYYHNNFWFCMDTYK 239
Cdd:cd02524  157 GRFGELDLDDDGQVTSFTEKPQGDGgWINGGFFVLEPEVFDYIDGDDTvfEREPLERLAKDGELMAYKHTGFWQCMDTLR 236
                        250
                 ....*....|....*..
gi 818342831 240 EVEDLNKMWKEGKAAWK 256
Cdd:cd02524  237 DKQTLEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-258 2.39e-84

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 252.37  E-value: 2.39e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831    2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFTSDFTLDTRNH 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   82 KPKFYledRDEVDNFEITFVDTGIETMPGERILRCQKYIpkKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGVHP 161
Cdd:TIGR02623  81 TMEVH---HKRVEPWRVTLVDTGESTQTGGRLKRVREYL--DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  162 RSKYGLIKTTKDNfVTKFVEKPVLND-WINGGFMIFDKRAFNYINpGEM---EHDLLKRLALKNELSIYYHNNFWFCMDT 237
Cdd:TIGR02623 156 PGRFGALDLEGEQ-VTSFQEKPLGDGgWINGGFFVLNPSVLDLID-GDAtvwEQEPLETLAQRGELSAYEHSGFWQPMDT 233
                         250       260
                  ....*....|....*....|.
gi 818342831  238 YKEVEDLNKMWKEGKAAWKIW 258
Cdd:TIGR02623 234 LRDKNYLEELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-258 3.72e-83

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: 248.53  E-value: 3.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFtsdftldtrnh 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  82 kpkfyledrdevdNFEITFVDTGIETMPGERILRCQKYIpkKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGV-- 159
Cdd:COG1208   70 -------------GVRITYVDEGEPLGTGGALKRALPLL--GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpv 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 160 HPRSKYGLIKTTKDNFVTKFVEKP--VLNDWINGGFMIFDKRAFNYINPGEMEH--DLLKRLALKNELSIYYHNNFWFCM 235
Cdd:COG1208  135 PDPSRYGVVELDGDGRVTRFVEKPeePPSNLINAGIYVLEPEIFDYIPEGEPFDleDLLPRLIAEGRVYGYVHDGYWLDI 214
                        250       260
                 ....*....|....*....|...
gi 818342831 236 DTYKEVEDLNKMWKEGKAAWKIW 258
Cdd:COG1208  215 GTPEDLLEANALLLSGKAPVVIW 237
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 4.10e-17

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: 78.06  E-value: 4.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831    2 KVIILCGGVGTRLKEETEFKPKPMVFIGNK-PILWHIMKIYASYGFNEFILALGYkadYIKEFFLNQKAFTSDFTLdtrn 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ---EHRFMLNELLGDGSKFGV---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   81 hkpkfyledrdevdNFEITFVDTGIETMPGERILRcqKYIPKKDKYFMVTYGDGVSDIDVDALVKFH--KKQKTIGT--I 156
Cdd:pfam00483  74 --------------QITYALQPEGKGTAPAVALAA--DFLGDEKSDVLVLGGDHIYRMDLEQAVKFHieKAADATVTfgI 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  157 TGVHPRSKYGLIKTTKDNFVTKFVEKP---VLNDWINGGFMIFDKRAFN----YINPGEMEH----DLLKRLALKNELSI 225
Cdd:pfam00483 138 VPVEPPTGYGVVEFDDNGRVIRFVEKPklpKASNYASMGIYIFNSGVLDflakYLEELKRGEdeitDILPKALEDGKLAY 217
                         250
                  ....*....|..
gi 818342831  226 YYHNNFWFCMDT 237
Cdd:pfam00483 218 AFIFKGYAWLDV 229
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-63 2.35e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 38.19  E-value: 2.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818342831   3 VIILCGGVGTRLKEEtefKPKPMVFIGNKPILWHIMKIYASYG-FNEFILALGykADYIKEF 63
Cdd:PRK00155   6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP--PDDRPDF 62
 
Name Accession Description Interval E-value
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-256 3.20e-117

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: 335.70  E-value: 3.20e-117
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFTSDFTLDTRNHK 82
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIKEYFLNYFLHNSDVTIDLGTNR 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 PKFYledRDEVDNFEITFVDTGIETMPGERILRCQKYIpKKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGVHPR 162
Cdd:cd02524   81 IELH---NSDIEDWKVTLVDTGLNTMTGGRLKRVRRYL-GDDETFMLTYGDGVSDVNINALIEFHRSHGKLATVTAVHPP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 163 SKYGLIKTTKDNFVTKFVEKPVLND-WINGGFMIFDKRAFNYINPGEM--EHDLLKRLALKNELSIYYHNNFWFCMDTYK 239
Cdd:cd02524  157 GRFGELDLDDDGQVTSFTEKPQGDGgWINGGFFVLEPEVFDYIDGDDTvfEREPLERLAKDGELMAYKHTGFWQCMDTLR 236
                        250
                 ....*....|....*..
gi 818342831 240 EVEDLNKMWKEGKAAWK 256
Cdd:cd02524  237 DKQTLEELWNSGKAPWK 253
G1P_cyt_trans TIGR02623
glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme ...
2-258 2.39e-84

glucose-1-phosphate cytidylyltransferase; Members of this family are the enzyme glucose-1-phosphate cytidylyltransferase, also called CDP-glucose pyrophosphorylase, the product of the rfbF gene. [Cell envelope, Biosynthesis and degradation of surface polysaccharides and lipopolysaccharides]


Pssm-ID: 131672 [Multi-domain]  Cd Length: 254  Bit Score: 252.37  E-value: 2.39e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831    2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFTSDFTLDTRNH 81
Cdd:TIGR02623   1 KAVILAGGLGTRISEETHLRPKPMVEIGGKPILWHIMKIYSHHGINDFIICCGYKGYVIKEYFANYFLHMSDVTFHMADN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   82 KPKFYledRDEVDNFEITFVDTGIETMPGERILRCQKYIpkKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGVHP 161
Cdd:TIGR02623  81 TMEVH---HKRVEPWRVTLVDTGESTQTGGRLKRVREYL--DDEAFCFTYGDGVADIDIKALIAFHRKHGKKATVTAVQP 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  162 RSKYGLIKTTKDNfVTKFVEKPVLND-WINGGFMIFDKRAFNYINpGEM---EHDLLKRLALKNELSIYYHNNFWFCMDT 237
Cdd:TIGR02623 156 PGRFGALDLEGEQ-VTSFQEKPLGDGgWINGGFFVLNPSVLDLID-GDAtvwEQEPLETLAQRGELSAYEHSGFWQPMDT 233
                         250       260
                  ....*....|....*....|.
gi 818342831  238 YKEVEDLNKMWKEGKAAWKIW 258
Cdd:TIGR02623 234 LRDKNYLEELWESGRAPWKVW 254
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-258 3.72e-83

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: 248.53  E-value: 3.72e-83
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFtsdftldtrnh 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRF----------- 69
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  82 kpkfyledrdevdNFEITFVDTGIETMPGERILRCQKYIpkKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGV-- 159
Cdd:COG1208   70 -------------GVRITYVDEGEPLGTGGALKRALPLL--GDEPFLVLNGDILTDLDLAALLAFHREKGADATLALVpv 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 160 HPRSKYGLIKTTKDNFVTKFVEKP--VLNDWINGGFMIFDKRAFNYINPGEMEH--DLLKRLALKNELSIYYHNNFWFCM 235
Cdd:COG1208  135 PDPSRYGVVELDGDGRVTRFVEKPeePPSNLINAGIYVLEPEIFDYIPEGEPFDleDLLPRLIAEGRVYGYVHDGYWLDI 214
                        250       260
                 ....*....|....*....|...
gi 818342831 236 DTYKEVEDLNKMWKEGKAAWKIW 258
Cdd:COG1208  215 GTPEDLLEANALLLSGKAPVVIW 237
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-233 1.15e-50

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


Pssm-ID: 133024 [Multi-domain]  Cd Length: 217  Bit Score: 165.06  E-value: 1.15e-50
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFtsdftldtrnhk 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKF------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 pkfyledrdevdNFEITFVdtgIETMP---GERILRCQKYIpkKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITG- 158
Cdd:cd04181   69 ------------GVNIEYV---VQEEPlgtAGAVRNAEDFL--GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVk 131
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 159 -VHPRSKYGLIKTTKDNFVTKFVEKPVL--NDWINGGFMIFDKRAFNYINPGE-----MEHDLLKRLALKNELSIYYHNN 230
Cdd:cd04181  132 eVEDPSRYGVVELDDDGRVTRFVEKPTLpeSNLANAGIYIFEPEILDYIPEILprgedELTDAIPLLIEEGKVYGYPVDG 211

                 ...
gi 818342831 231 FWF 233
Cdd:cd04181  212 YWL 214
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-223 6.03e-37

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: 129.98  E-value: 6.03e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEfflnqkaftsdftldtrnhk 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEE-------------------- 60
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 pkfYLEDRDEVDnFEITFVdtgIETMP---GERILRCQKYIPkkDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTITGV 159
Cdd:cd06915   61 ---YFGDGYRGG-IRIYYV---IEPEPlgtGGAIKNALPKLP--EDQFLVLNGDTYFDVDLLALLAALRASGADATMALR 131
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 160 H--PRSKYGLIKTTKDNFVTKFVEKPV--LNDWINGGFMIFDKRAFNYI--NPGEMEHDLLKRLALKNEL 223
Cdd:cd06915  132 RvpDASRYGNVTVDGDGRVIAFVEKGPgaAPGLINGGVYLLRKEILAEIpaDAFSLEADVLPALVKRGRL 201
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-236 3.50e-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: 117.70  E-value: 3.50e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   1 MKVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFlnqkaftsdftldtrn 80
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFL---------------- 64
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 hkpKFYlEDRDEVdnfEITFvdtGIETMP---GERILRCQKYIPKKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTI- 156
Cdd:cd06425   65 ---KEY-EKKLGI---KITF---SIETEPlgtAGPLALARDLLGDDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTIl 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 157 -TGVHPRSKYGLIKTTKDNF-VTKFVEKPV--LNDWINGGFMIFDKRAFNYI--NPGEMEHDLLKRLALKNELSIYYHNN 230
Cdd:cd06425  135 vTKVEDPSKYGVVVHDENTGrIERFVEKPKvfVGNKINAGIYILNPSVLDRIplRPTSIEKEIFPKMASEGQLYAYELPG 214

                 ....*.
gi 818342831 231 FWfcMD 236
Cdd:cd06425  215 FW--MD 218
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-233 1.84e-30

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: 112.99  E-value: 1.84e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFtsdftldtrnhk 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKF------------ 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 pkfyledrdevdNFEITFVDtgiETMP----GERILrcqkyIPKKDK-YFMVTYGDGVSDIDVDALVKFHKKQKTIGTIt 157
Cdd:cd06426   69 ------------GVNISYVR---EDKPlgtaGALSL-----LPEKPTdPFLVMNGDILTNLNYEHLLDFHKENNADATV- 127
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 158 GVHPRS---KYGLIKtTKDNFVTKFVEKPVLNDWINGGFMIFDKRAFNYINPGEMEH--DLLKRLALKNE-LSIYYHNNF 231
Cdd:cd06426  128 CVREYEvqvPYGVVE-TEGGRITSIEEKPTHSFLVNAGIYVLEPEVLDLIPKNEFFDmpDLIEKLIKEGKkVGVFPIHEY 206

                 ..
gi 818342831 232 WF 233
Cdd:cd06426  207 WL 208
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-64 3.78e-17

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 77.97  E-value: 3.78e-17
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 818342831   2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFF 64
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEAL 63
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-237 4.10e-17

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: 78.06  E-value: 4.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831    2 KVIILCGGVGTRLKEETEFKPKPMVFIGNK-PILWHIMKIYASYGFNEFILALGYkadYIKEFFLNQKAFTSDFTLdtrn 80
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ---EHRFMLNELLGDGSKFGV---- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   81 hkpkfyledrdevdNFEITFVDTGIETMPGERILRcqKYIPKKDKYFMVTYGDGVSDIDVDALVKFH--KKQKTIGT--I 156
Cdd:pfam00483  74 --------------QITYALQPEGKGTAPAVALAA--DFLGDEKSDVLVLGGDHIYRMDLEQAVKFHieKAADATVTfgI 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  157 TGVHPRSKYGLIKTTKDNFVTKFVEKP---VLNDWINGGFMIFDKRAFN----YINPGEMEH----DLLKRLALKNELSI 225
Cdd:pfam00483 138 VPVEPPTGYGVVEFDDNGRVIRFVEKPklpKASNYASMGIYIFNSGVLDflakYLEELKRGEdeitDILPKALEDGKLAY 217
                         250
                  ....*....|..
gi 818342831  226 YYHNNFWFCMDT 237
Cdd:pfam00483 218 AFIFKGYAWLDV 229
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
3-232 9.43e-14

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: 68.82  E-value: 9.43e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGV--GTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADyiKEFFLNQKAFTSDFTLDTRn 80
Cdd:cd06428    1 AVILVGGPqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVPDLKEVLLIGFYPE--SVFSDFISDAQQEFNVPIR- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 hkpkfYLEDrdevdnfeitfvDTGIETMPG-----ERILRCQkyiPKKdkyFMVTYGDGVSDIDVDALVKFHKKQKTIGT 155
Cdd:cd06428   78 -----YLQE------------YKPLGTAGGlyhfrDQILAGN---PSA---FFVLNADVCCDFPLQELLEFHKKHGASGT 134
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 156 ITGVHPR----SKYG-LIKTTKDNFVTKFVEKP--VLNDWINGGFMIFDKRAFNYI----------------NPGE---- 208
Cdd:cd06428  135 ILGTEASreqaSNYGcIVEDPSTGEVLHYVEKPetFVSDLINCGVYLFSPEIFDTIkkafqsrqqeaqlgddNNREgrae 214
                        250       260
                 ....*....|....*....|....*..
gi 818342831 209 ---MEHDLLKRLALKNELSIYYHNNFW 232
Cdd:cd06428  215 virLEQDVLTPLAGSGKLYVYKTDDFW 241
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-64 1.08e-13

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


Pssm-ID: 133014 [Multi-domain]  Cd Length: 229  Bit Score: 68.41  E-value: 1.08e-13
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFF 64
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELL 62
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-217 1.46e-13

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: 67.98  E-value: 1.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   1 MKVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNQKAFTSDFTLdTRN 80
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRITY-ILQ 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 HKPKfyledrdevdnfeitfvdtGIetmpGERILRCQKYIpkKDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTI--TG 158
Cdd:cd04189   80 EEPL-------------------GL----AHAVLAARDFL--GDEPFVVYLGDNLIQEGISPLVRDFLEEDADASIllAE 134
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 159 VHPRSKYGLIKtTKDNFVTKFVEKP---VLNDWINGGFM----IFDkrAFNYINP---GEME-HDLLKRL 217
Cdd:cd04189  135 VEDPRRFGVAV-VDDGRIVRLVEKPkepPSNLALVGVYAftpaIFD--AISRLKPswrGELEiTDAIQWL 201
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-147 4.76e-10

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 57.67  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   1 MKVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFIL-------ALgyKADYIKEFFLNQKaftsd 73
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVvvpeeeqAE--ISTYLRSFPLNLK----- 73
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818342831  74 ftldtrnhkpkfyledrdeVDNFEITFVDtgIETMPGERILRcqKYIPKKDKYFMVTYGDGVSDIDVDALVKFH 147
Cdd:cd04198   74 -------------------QKLDEVTIVL--DEDMGTADSLR--HIRKKIKKDFLVLSCDLITDLPLIELVDLH 124
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
2-183 4.77e-10

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: 58.95  E-value: 4.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831    2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYK-ADYIKEFFLNQKAFTSDFTLdTRN 80
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVtGEEIKEIVGEGERFGAKITY-IVQ 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   81 HKPKfyledrdevdnfeitfvdtGIetmpGERILRCQKYIPKKDkyFMVTYGDGVSDIDVDALVK-FHKKQKTIGT-ITG 158
Cdd:TIGR01208  80 GEPL-------------------GL----AHAVYTARDFLGDDD--FVVYLGDNLIQDGISRFVKsFEEKDYDALIlLTK 134
                         170       180
                  ....*....|....*....|....*
gi 818342831  159 VHPRSKYGLIKTTKDNFVTKFVEKP 183
Cdd:TIGR01208 135 VRDPTAFGVAVLEDGKRILKLVEKP 159
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-204 1.34e-09

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 57.41  E-value: 1.34e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   1 MKVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMkiyasygfnEFILALGykadyIKEFflnqkAFTSdftldTRN 80
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPL---------STLMLAG-----IREI-----LIIS-----TPE 56
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 HKPKF--YLEDRDEVDnFEITFVdtgIETMP---GERILRCQKYIpKKDKYFMV-----TYGDGVSDidvdaLVKFHKKQ 150
Cdd:COG1209   57 DGPQFerLLGDGSQLG-IKISYA---VQPEPlglAHAFIIAEDFI-GGDPVALVlgdniFYGDGLSE-----LLREAAAR 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 818342831 151 KTIGTITGVH---PRSkYGLIKTTKDNFVTKFVEKPVL--NDWINGGFMIFDKRAFNYI 204
Cdd:COG1209  127 ESGATIFGYKvedPER-YGVVEFDEDGRVVSLEEKPKEpkSNLAVTGLYFYDNDVVEIA 184
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-233 2.09e-09

NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133044 [Multi-domain]  Cd Length: 221  Bit Score: 56.04  E-value: 2.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   2 KVIILCGGVGTRLKEETEFKPKPMVFIGNKP-ILWHIMKIyASYGFNEFILALGYKADYIKEFFlnqkaftsdftldtrn 80
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPlIDHALDRL-AAAGIRRIVVNTHHLADQIEAHL---------------- 63
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 hkpkfyledRDEVDNFEITFVD---TGIETMPGerILRCQKYIPkkDKYFMVTYGDGVSDIDVDALVKFHKKQKTIGTIT 157
Cdd:cd06422   64 ---------GDSRFGLRITISDepdELLETGGG--IKKALPLLG--DEPFLVVNGDILWDGDLAPLLLLHAWRMDALLLL 130
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 158 -------GVHPRSKYGLiktTKDNFVTKFVEKPVlNDWINGGFMIFDKRAFNYINPGEME-HDLLKRLALKNELSIYYHN 229
Cdd:cd06422  131 lplvrnpGHNGVGDFSL---DADGRLRRGGGGAV-APFTFTGIQILSPELFAGIPPGKFSlNPLWDRAIAAGRLFGLVYD 206

                 ....
gi 818342831 230 NFWF 233
Cdd:cd06422  207 GLWF 210
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-157 5.40e-09

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 54.95  E-value: 5.40e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   1 MKVIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFFLNqkaftsdftldtrn 80
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLK-------------- 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 hkpKFYLEDRDEVDNFEITFVDTgiETM-PGERILRCQKyipKKDKYFMVTYGDGVSDIDVDALVKFHKKQ--KTIGTIT 157
Cdd:cd02507   67 ---SKWSSLSSKMIVDVITSDLC--ESAgDALRLRDIRG---LIRSDFLLLSCDLVSNIPLSELLEERRKKdkNAIATLT 138
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-200 8.97e-07

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: 49.25  E-value: 8.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   1 MKVIILCGGVGTRLKEETefkPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEfflnqkaftsdftldtrn 80
Cdd:COG1207    3 LAVVILAAGKGTRMKSKL---PKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRA------------------ 61
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  81 hkpkfYLEDRDevdnfeITFVD------TGietmpgeRILRC-QKYIPKKDKYFMVTYGDgVSDIDVD---ALVKFHKKQ 150
Cdd:COG1207   62 -----ALADLD------VEFVLqeeqlgTG-------HAVQQaLPALPGDDGTVLVLYGD-VPLIRAEtlkALLAAHRAA 122
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818342831 151 KTIGTI--------TGvhprskYGLIKTTKDNFVTKFVE--------KPVlnDWINGGFMIFDKRA 200
Cdd:COG1207  123 GAAATVltaelddpTG------YGRIVRDEDGRVLRIVEekdateeqRAI--REINTGIYAFDAAA 180
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-205 6.47e-06

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: 45.97  E-value: 6.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEEtefKPKPMVFIGNKPILWHIMKIYASYGFNEFILALGYKADYIKEFflnqkaftsdftldtrnhk 82
Cdd:cd02540    1 AVILAAGKGTRMKSD---LPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKA------------------- 58
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  83 pkfyledrdeVDNFEITFVDTgiETMPG--ERILRCQKYIPKKDKYFMVTYGDG--VSDIDVDALVKFHKKQKTIGTITG 158
Cdd:cd02540   59 ----------LANPNVEFVLQ--EEQLGtgHAVKQALPALKDFEGDVLVLYGDVplITPETLQRLLEAHREAGADVTVLT 126
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 818342831 159 VHPR--SKYGLIKTTKDNFVTKFVE---------KPVLndwINGGFMIFDKRA-FNYIN 205
Cdd:cd02540  127 AELEdpTGYGRIIRDGNGKVLRIVEekdateeekAIRE---VNAGIYAFDAEFlFEALP 182
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-53 2.78e-05

CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; 4-diphosphocytidyl-2-methyl-D-erythritol synthase (CDP-ME), also called 2C-methyl-d-erythritol 4-phosphate cytidylyltransferase catalyzes the third step in the alternative (non-mevalonate) pathway of Isopentenyl diphosphate (IPP) biosynthesis: the formation of 4-diphosphocytidyl-2C-methyl-D-erythritol from CTP and 2C-methyl-D-erythritol 4-phosphate. This mevalonate independent pathway that utilizes pyruvate and glyceraldehydes 3-phosphate as starting materials for production of IPP occurs in a variety of bacteria, archaea and plant cells, but is absent in mammals. Thus, CDP-ME synthetase is an attractive targets for the structure-based design of selective antibacterial, herbicidal and antimalarial drugs.


Pssm-ID: 133009 [Multi-domain]  Cd Length: 218  Bit Score: 44.05  E-value: 2.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818342831   3 VIILCGGVGTRLKEETefkPKPMVFIGNKPILWHIMKI-YASYGFNEFILAL 53
Cdd:cd02516    3 AIILAAGSGSRMGADI---PKQFLELGGKPVLEHTLEAfLAHPAIDEIVVVV 51
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
4-63 1.05e-04

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase is part of the Pathway/BioSystem: Isoprenoid biosynthesis


Pssm-ID: 440824  Cd Length: 224  Bit Score: 42.42  E-value: 1.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818342831   4 IILCGGVGTRLKEETefkPKPMVFIGNKPILWH-IMKIYASYGFNEFILALGykADYIKEF 63
Cdd:COG1211    1 IIPAAGSGSRMGAGI---PKQFLPLGGKPVLEHtLEAFLAHPRIDEIVVVVP--PDDIEYF 56
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
4-228 6.90e-04

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 40.44  E-value: 6.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   4 IILCGGVGTRLKEETEFKPKPMVFIG--------------NKpilwHIMKIYasygfnefILAlGYKA----DYIKEffl 65
Cdd:COG0448    5 IILAGGRGSRLGPLTKDRAKPAVPFGgkyriidfplsncvNS----GIRRVG--------VLT-QYKShslnDHIGS--- 68
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  66 nqkafTSDFTLDTRNHkpkfyledrdevdnfeitFVDT--GIETMPGER--------ILRCQKYIPKKD-KYFMVTYGDG 134
Cdd:COG0448   69 -----GKPWDLDRKRG------------------GVFIlpPYQQREGEDwyqgtadaVYQNLDFIERSDpDYVLILSGDH 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831 135 VSDIDVDALVKFHKKQK---TIGTITgVHPR--SKYGLIKTTKDNFVTKFVEKPVLNDWING--GFMIFDKRAF-----N 202
Cdd:COG0448  126 IYKMDYRQMLDFHIESGadiTVACIE-VPREeaSRFGVMEVDEDGRITEFEEKPKDPKSALAsmGIYVFNKDVLielleE 204
                        250       260
                 ....*....|....*....|....*...
gi 818342831 203 YINPGemEHDLLKRL--ALKNELSIYYH 228
Cdd:COG0448  205 DAPNS--SHDFGKDIipRLLDRGKVYAY 230
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-63 2.35e-03

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 38.19  E-value: 2.35e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818342831   3 VIILCGGVGTRLKEEtefKPKPMVFIGNKPILWHIMKIYASYG-FNEFILALGykADYIKEF 63
Cdd:PRK00155   6 AIIPAAGKGSRMGAD---RPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVP--PDDRPDF 62
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
3-183 3.08e-03

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 38.28  E-value: 3.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKpilWHIMKIYASYGFNEFILALG----YKAD----YIKE--FFLNQKaFTS 72
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGK---FRIIDFALSNCINSGIRRIGvltqYKAHslirHIQRgwSFFREE-LGE 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818342831  73 DFTL---DTRNHKPKFYLEDRDEV-DNFEItfvdtgIETmpgerilrcqkYIPkkdKYFMVTYGDGVSDIDVDALVKFHK 148
Cdd:PRK00725  94 FVDLlpaQQRVDEENWYRGTADAVyQNLDI------IRR-----------YDP---KYVVILAGDHIYKMDYSRMLADHV 153
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 818342831 149 KQK---TIGTITgVhPR---SKYGLIKTTKDNFVTKFVEKP 183
Cdd:PRK00725 154 ESGadcTVACLE-V-PReeaSAFGVMAVDENDRITAFVEKP 192
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-66 7.47e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 37.28  E-value: 7.47e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818342831   3 VIILCGGVGTRLKEETefkPKPMVFIGNKPILWHIMKiyASYGFNEFI-LALGYKADYIKEFFLN 66
Cdd:PRK14359   5 IIILAAGKGTRMKSSL---PKVLHTICGKPMLFYILK--EAFAISDDVhVVLHHQKERIKEAVLE 64
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
3-68 8.88e-03

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: 36.46  E-value: 8.88e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818342831   3 VIILCGGVGTRLKEETEFKPKPMVFIGNKPILWHIMKIYASYGFNEFILAlgYKADYIKEFFLNQK 68
Cdd:cd04183    1 IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFI--CRDEHNTKFHLDES 64
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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