NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|816130583|gb|AKE80720|]
View 

nucleotidyl transferase family protein [Streptococcus suis]

Protein Classification

LicC family protein( domain architecture ID 10790888)

LicC family protein

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-221 8.33e-99

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


:

Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 286.73  E-value: 8.33e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDKYDTY 80
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  81 NNFYSMYLVRDFLSDAYVIDADNYLHTNFLDSDVTISTYFSAYKDNFEDEWLLKCDDNGQVKEIVIDSGEGSILSGVSYW 160
Cdd:COG4750   81 NNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSAVYKEGETDEWCVKTNRDGRITKIEIGGKDGWIMLGHSYW 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816130583 161 DAKSGQVLNKLIEEVLESNDFCNLYWDNLVKDNLDKLTVYKRDIPSNVIFEIDNLDDLGQL 221
Cdd:COG4750  161 DKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIYEFDSLDELREF 221
 
Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-221 8.33e-99

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 286.73  E-value: 8.33e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDKYDTY 80
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  81 NNFYSMYLVRDFLSDAYVIDADNYLHTNFLDSDVTISTYFSAYKDNFEDEWLLKCDDNGQVKEIVIDSGEGSILSGVSYW 160
Cdd:COG4750   81 NNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSAVYKEGETDEWCVKTNRDGRITKIEIGGKDGWIMLGHSYW 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816130583 161 DAKSGQVLNKLIEEVLESNDFCNLYWDNLVKDNLDKLTVYKRDIPSNVIFEIDNLDDLGQL 221
Cdd:COG4750  161 DKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIYEFDSLDELREF 221
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-218 5.67e-66

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: 203.62  E-value: 5.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFD-FLESKYGVRLIHNDKYDTYN 81
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEeLLKKYPNIKFVYNPDYAETN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  82 NFYSMYLVRDFLS-DAYVIDADNYLHTNFLDSDVTISTYFSAYKDNFEDEWLLK----CDDNGQVKEIVIDSGEGS---- 152
Cdd:cd02523   81 NIYSLYLARDFLDeDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEyvkdLDDAGVLLGIISKAKNLEeiqg 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816130583 153 ILSGVSYWDAKSGQVLNKLIEEVLESNdFCNLYWDNLVKDNLDKLTVYKRDIPSNVIFEIDNLDDL 218
Cdd:cd02523  161 EYVGISKFSPEDADRLAEALEELIEAG-RVNLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDL 225
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-95 1.46e-13

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: 68.58  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583    2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLS-EKFDFL---ESKYGVRLIHNDKY 77
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTgEEIKEIvgeGERFGAKITYIVQG 80

                          90
                  ....*....|....*...
gi 816130583   78 DTYNNFYSMYLVRDFLSD 95
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGD 98
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-79 6.43e-10

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: 56.05  E-value: 6.43e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583    3 AIILAAGMGTRLRpltftTPKSLIEVGDQTLIERQILFLNEIGiSEIIIVTGYlSEKFDFLEsKYGVRLIHNDKYDT 79
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND-EEVLAALA-GLGVPVVPDPDPGQ 69
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-53 7.13e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.51  E-value: 7.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQIL-FLNEIGISEIIIVT 53
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEaFLAHPRIDEIIVVV 54
 
Name Accession Description Interval E-value
LicC COG4750
CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid ...
 1-221 8.33e-99

CTP:phosphocholine cytidylyltransferase LicC [Cell wall/membrane/envelope biogenesis, Lipid transport and metabolism];


Pssm-ID: 443784 [Multi-domain]  Cd Length: 228  Bit Score: 286.73  E-value: 8.33e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDKYDTY 80
Cdd:COG4750    1 MNAIILAAGLGSRFAPITYETPKGLLKVNGEPLIERQIRQLHEAGITDITVVVGYLKEQFEYLEDKYGVKLIYNPDYAEY 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  81 NNFYSMYLVRDFLSDAYVIDADNYLHTNFLDSDVTISTYFSAYKDNFEDEWLLKCDDNGQVKEIVIDSGEGSILSGVSYW 160
Cdd:COG4750   81 NNISSLYLVRDKLGNTYICSSDNYLTENPFEKYEYKSYYSAVYKEGETDEWCVKTNRDGRITKIEIGGKDGWIMLGHSYW 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 816130583 161 DAKSGQVLNKLIEEVLESNDFCNLYWDNLVKDNLDKLTVYKRDIPSNVIFEIDNLDDLGQL 221
Cdd:COG4750  161 DKEDSKKFKEILEEEYEDPETRDLYWEDIYMDHIDELDMYARKYPAGDIYEFDSLDELREF 221
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 3-218 5.67e-66

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: 203.62  E-value: 5.67e-66
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFD-FLESKYGVRLIHNDKYDTYN 81
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEeLLKKYPNIKFVYNPDYAETN 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  82 NFYSMYLVRDFLS-DAYVIDADNYLHTNFLDSDVTISTYFSAYKDNFEDEWLLK----CDDNGQVKEIVIDSGEGS---- 152
Cdd:cd02523   81 NIYSLYLARDFLDeDFLLLEGDVVFDPSILERLLSSPADNAILVDKKTKEWEDEyvkdLDDAGVLLGIISKAKNLEeiqg 160

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816130583 153 ILSGVSYWDAKSGQVLNKLIEEVLESNdFCNLYWDNLVKDNLDKLTVYKRDIPSNVIFEIDNLDDL 218
Cdd:cd02523  161 EYVGISKFSPEDADRLAEALEELIEAG-RVNLYYEDALQRLISEEGVKVKDISDGFWYEIDDLEDL 225
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-226 5.59e-42

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 142.30  E-value: 5.59e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFLESKY-GVRLIHNDKYDT 79
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIeEALARPGpDVTFVYNPDYDE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  80 YNNFYSMYLVRDFLS-DAYVIDADNYLHTNFL----DSD----VTISTYFsayKDNFEDEWLLKCDDNGQVKEI--VIDS 148
Cdd:COG1213   81 TNNIYSLWLAREALDeDFLLLNGDVVFDPAILkrllASDgdivLLVDRKW---EKPLDEEVKVRVDEDGRIVEIgkKLPP 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583 149 GEGS-ILSGVSYWDAKSGQVLNKLIEEvLESNDFCNLYWDNLVKDNLDK-LTVYKRDIPSNVIFEIDNLDDLGQLQEFLN 226
Cdd:COG1213  158 EEADgEYIGIFKFSAEGAAALREALEA-LIDEGGPNLYYEDALQELIDEgGPVKAVDIGGLPWVEIDTPEDLERAEELFA 236
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 2-227 1.36e-26

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: 102.54  E-value: 1.36e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFLE--SKYGVRL--IHNDK 76
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIeEYFGdgSRFGVRItyVDEGE 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  77 -YDTynnFYSMYLVRDFLSDA--YVIDADNYLHTNFL---------DSDVTISTYFSAYKDNFEDewlLKCDDNGQVKEI 144
Cdd:COG1208   81 pLGT---GGALKRALPLLGDEpfLVLNGDILTDLDLAallafhrekGADATLALVPVPDPSRYGV---VELDGDGRVTRF 154

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583 145 VIDSGEGS---ILSGVsywdaksgQVLNKLIEEVLESNDFCNL--YWDNLVKDNldKLTVYKRDipsNVIFEIDNLDDLG 219
Cdd:COG1208  155 VEKPEEPPsnlINAGI--------YVLEPEIFDYIPEGEPFDLedLLPRLIAEG--RVYGYVHD---GYWLDIGTPEDLL 221


                 ....*...
gi 816130583 220 QLQEFLNS 227
Cdd:COG1208  222 EANALLLS 229
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 3-145 8.82e-24

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: 94.57  E-value: 8.82e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFLE--SKYGVRLihndkydT 79
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIeEYFGdgSKFGVNI-------E 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  80 YnnFY---------SMYLVRDFLSDAY--VIDADNYLHTNFL---------DSDVTISTYfsaYKDNFEDEWLLKCDDNG 139
Cdd:cd04181   74 Y--VVqeeplgtagAVRNAEDFLGDDDflVVNGDVLTDLDLSellrfhrekGADATIAVK---EVEDPSRYGVVELDDDG 148


                 ....*.
gi 816130583 140 QVKEIV 145
Cdd:cd04181  149 RVTRFV 154
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 2-72 4.19e-22

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: 90.32  E-value: 4.19e-22
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816130583   2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFL-ESKYGVRLI 72
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIeAHLgDSRFGLRIT 73
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 1-106 2.06e-19

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: 83.39  E-value: 2.06e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFL--ESKYGVRL--IHND 75
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIkEALgdGSRFGVRItyILQE 80

                         90       100       110
                 ....*....|....*....|....*....|...
gi 816130583  76 KYDTYNNfySMYLVRDFL--SDAYVIDADNYLH 106
Cdd:cd04189   81 EPLGLAH--AVLAARDFLgdEPFVVYLGDNLIQ 111
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 1-72 4.03e-18

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: 79.95  E-value: 4.03e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF----DFLESKYGVRLI 72
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMvpflKEYEKKLGIKIT 76
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-71 8.36e-18

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 80.13  E-value: 8.36e-18
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEI-IIVTGYLSEKF-DFLE--SKYGVRL 71
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREIlIISTPEDGPQFeRLLGdgSQLGIKI 75
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 3-77 3.13e-14

NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily of nucleotidyl transferases. Nucleotidyl transferases transfer nucleotides onto phosphosugars. The activated sugars are precursors for synthesis of lipopolysaccharide, glycolipids and polysaccharides. Other subfamilies of nucleotidyl transferases include Alpha-D-Glucose-1-Phosphate Cytidylyltransferase, Mannose-1-phosphate guanyltransferase, and Glucose-1-phosphate thymidylyltransferase.


Pssm-ID: 133048 [Multi-domain]  Cd Length: 220  Bit Score: 69.08  E-value: 3.13e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFLE--SKYGVRL--IHNDKY 77
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIeDYFGdgSKFGVNIsyVREDKP 80
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 3-59 4.06e-14

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: 68.73  E-value: 4.06e-14
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEK 59
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQ 57
rmlA_long TIGR01208
glucose-1-phosphate thymidylylransferase, long form; The family of known and putative ...
 2-95 1.46e-13

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: 68.58  E-value: 1.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583    2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLS-EKFDFL---ESKYGVRLIHNDKY 77
Cdd:TIGR01208   1 KALILAAGKGTRLRPLTFTRPKQLIPVANKPILQYAIEDLAEAGITDIGIVVGPVTgEEIKEIvgeGERFGAKITYIVQG 80

                          90
                  ....*....|....*...
gi 816130583   78 DTYNNFYSMYLVRDFLSD 95
Cdd:TIGR01208  81 EPLGLAHAVYTARDFLGD 98
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 3-79 3.10e-12

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: 62.96  E-value: 3.10e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRlrpltFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDKYDT 79
Cdd:cd04182    3 AIILAAGRSSR-----MGGNKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGAEADAVRAALAGLPVVVVINPDWEE 74
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-79 3.99e-12

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 62.87  E-value: 3.99e-12
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRlrpltFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDKYDT 79
Cdd:COG2068    6 AIILAAGASSR-----MGRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAGLGVRVVVNPDWEE 77
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 1-54 5.47e-10

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: 57.58  E-value: 5.47e-10
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTG 54
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIST 54
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 3-79 6.43e-10

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: 56.05  E-value: 6.43e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583    3 AIILAAGMGTRLRpltftTPKSLIEVGDQTLIERQILFLNEIGiSEIIIVTGYlSEKFDFLEsKYGVRLIHNDKYDT 79
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPAG-DEVVVVAND-EEVLAALA-GLGVPVVPDPDPGQ 69
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 2-71 1.02e-09

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: 56.88  E-value: 1.02e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 816130583    2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQ-TLIERQILFLNEIGISEIIIVTG-YLSEKFDFL---ESKYGVRL 71
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTqEHRFMLNELlgdGSKFGVQI 75
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 1-55 2.45e-09

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: 56.00  E-value: 2.45e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGY 55
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGR 55
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
 3-65 2.68e-08

N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose pyrophosphorylase; N-terminal domain of the M1P-guanylyltransferase A-isoform like proteins: The proteins of this family are likely to be a isoform of GDP-mannose pyrophosphorylase. Their sequences are highly conserved with mannose-1-phosphate guanyltransferase, but generally about 40-60 bases longer. GDP-mannose pyrophosphorylase (GTP: alpha-d-mannose-1-phosphate guanyltransferase) catalyzes the formation of GDP-d-mannose from GTP and alpha-d-mannose-1-Phosphate. It contains an N-terminal catalytic domain that resembles a dinucleotide-binding Rossmann fold and a C-terminal LbH fold domain. GDP-d-mannose is the activated form of mannose for formation of cell wall lipoarabinomannan and various mannose-containing glycolipids and polysaccharides. The function of GDP-mannose pyrophosphorylase is essential for cell wall integrity, morphogenesis and viability. Repression of GDP-mannose pyrophosphorylase in yeast leads to phenotypes including cell lysis, defective cell wall, and failure of polarized growth and cell separation.


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 52.64  E-value: 2.68e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAG--MGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEI-GISEIIIVTGYLSEKF-DFLES 65
Cdd:cd06428    1 AVILVGGpqKGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGFYPESVFsDFISD 67
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 1-53 4.74e-08

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


Pssm-ID: 133041 [Multi-domain]  Cd Length: 214  Bit Score: 51.51  E-value: 4.74e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVT 53
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVV 53
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 3-76 2.55e-07

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: 49.82  E-value: 2.55e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 816130583   3 AIILAAGMGTRLRpltFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDK 76
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKALANPNVEFVLQEE 71
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-53 3.27e-07

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


Pssm-ID: 133001 [Multi-domain]  Cd Length: 216  Bit Score: 49.17  E-value: 3.27e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVT 53
Cdd:cd02507    3 AVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVC 53
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 3-59 9.65e-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: 48.87  E-value: 9.65e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEK 59
Cdd:COG1207    5 VVILAAGKGTRMKS---KLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQ 58
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 3-53 1.64e-06

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: 47.13  E-value: 1.64e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   3 AIILAAGMGTRLRpltFTTPKSLIEVGDQTLIERQIL-FLNEIGISEIIIVT 53
Cdd:cd02516    3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEaFLAHPAIDEIVVVV 51
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
3-54 3.20e-06

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 46.95  E-value: 3.20e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTG 54
Cdd:COG1210    6 AVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTG 57
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-53 7.13e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 45.51  E-value: 7.13e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQIL-FLNEIGISEIIIVT 53
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEaFLAHPRIDEIIVVV 54
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 1-53 1.73e-05

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: 43.72  E-value: 1.73e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 816130583   1 MRAIILAAGMGTRlrpltFTTPKSLIEVGDQTLIERQILFLNEIgISEIIIVT 53
Cdd:cd02503    1 ITGVILAGGKSRR-----MGGDKALLELGGKPLLEHVLERLKPL-VDEVVISA 47
glmU PRK14360
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-59 2.55e-05

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


Pssm-ID: 184646 [Multi-domain]  Cd Length: 450  Bit Score: 44.53  E-value: 2.55e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   1 MRAI-ILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEK 59
Cdd:PRK14360   1 MLAVaILAAGKGTRMKS---SLPKVLHPLGGKSLVERVLDSCEELKPDRRLVIVGHQAEE 57
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
 1-54 2.62e-05

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: 44.10  E-value: 2.62e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   1 MRAIILAAGMGTRLRPL-TFTTPKSLIEV-GDQTLIERQIL-FLNEIGISEIIIVTG 54
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDrLKGLVPPDRILVVTN 57
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 3-72 3.93e-05

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: 42.87  E-value: 3.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   3 AIILAAGMGTRlrpltFTTPKSLIEVGDQTLIERQILFLNEIgISEIIIVTGYlSEKFDFLeskyGVRLI 72
Cdd:COG0746    7 GVILAGGRSRR-----MGQDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR-PERYAAL----GVPVV 65
ispD TIGR00453
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are ...
 3-53 5.51e-05

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this protein family are 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase, the IspD protein of the deoxyxylulose pathway of IPP biosynthesis. In about twenty percent of bacterial genomes, this protein occurs as IspDF, a bifunctional fusion protein. [Biosynthesis of cofactors, prosthetic groups, and carriers, Other]


Pssm-ID: 213532  Cd Length: 217  Bit Score: 42.66  E-value: 5.51e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 816130583    3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQI-LFLNEIGISEIIIVT 53
Cdd:TIGR00453   2 AVIPAAGRGTRFGS---GVPKQYLELGGRPLLEHALdAFLAHPAIDEVVVVV 50
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 4-53 7.43e-05

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: 7.43e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 816130583   4 IILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQI-LFLNEIGISEIIIVT 53
Cdd:COG1211    1 IIPAAGSGSRMGA---GIPKQFLPLGGKPVLEHTLeAFLAHPRIDEIVVVV 48
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 3-75 8.52e-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: 42.56  E-value: 8.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFLeSKYgvRLIHND 75
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFILCLGYKGHVIkEYF-LNY--FLHNSD 71
CpsB COG0836
Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];
1-54 1.18e-04

Mannose-1-phosphate guanylyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440598 [Multi-domain]  Cd Length: 347  Bit Score: 42.36  E-value: 1.18e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   1 MRAIILAAGMGTRLRPL-TFTTPKSLIE-VGDQTLIERQIL-FLNEIGISEIIIVTG 54
Cdd:COG0836    3 IYPVILAGGSGTRLWPLsRESYPKQFLPlLGEKSLLQQTVErLAGLVPPENILVVTN 59
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-53 1.29e-04

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 42.20  E-value: 1.29e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVT 53
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-54 1.66e-04

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 42.16  E-value: 1.66e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTG 54
Cdd:PRK14353   8 AIILAAGEGTRMKS---SLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVG 56
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-59 3.05e-04

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


Pssm-ID: 133040 [Multi-domain]  Cd Length: 217  Bit Score: 40.67  E-value: 3.05e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEK 59
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQ 59
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 4-195 3.15e-04

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 40.70  E-value: 3.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   4 IILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVT--GYLSEKFDFLESKygvRLIHNDKYDTYN 81
Cdd:cd04183    2 IIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICrdEHNTKFHLDESLK---LLAPNATVVELD 78

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583  82 NF-----YSMYLVRDFL----------SDAYV-IDADNYL-HTNFLDSDVTISTYFSaykdnFEDEWL-LKCDDNGQVKE 143
Cdd:cd04183   79 GEtlgaaCTVLLAADLIdnddpllifnCDQIVeSDLLAFLaAFRERDLDGGVLTFFS-----SHPRWSyVKLDENGRVIE 153

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 816130583 144 I----VIdSGEGSilSGVSYWdaKSGQVLNKLIEEVLESNDFCN-------LYwDNLVKDNLD 195
Cdd:cd04183  154 TaekePI-SDLAT--AGLYYF--KSGSLFVEAAKKMIRKDDSVNgefyispLY-NELILDGKK 210
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 2-53 7.49e-04

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 39.66  E-value: 7.49e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 816130583   2 RAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVT 53
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIS 56
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-59 1.65e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 39.04  E-value: 1.65e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEK 59
Cdd:PRK14354   5 AIILAAGKGTRMKS---KLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEE 58
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 1-76 2.78e-03

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 38.42  E-value: 2.78e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 816130583   1 MRAIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKFDFLESKYGVRLIHNDK 76
Cdd:PRK14358   8 LDVVILAAGQGTRMKS---ALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTGHGAEQVEAALQGSGVAFARQEQ 80
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-53 3.35e-03

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 37.95  E-value: 3.35e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 816130583   1 MRAIILAAGMGTRLRPLTFTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVT 53
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT 56
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-59 3.48e-03

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 37.99  E-value: 3.48e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEK 59
Cdd:PRK14352   7 VIVLAAGAGTRMRS---DTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRER 60
PTZ00339 PTZ00339
UDP-N-acetylglucosamine pyrophosphorylase; Provisional
 4-40 7.54e-03

UDP-N-acetylglucosamine pyrophosphorylase; Provisional


Pssm-ID: 240368  Cd Length: 482  Bit Score: 37.03  E-value: 7.54e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 816130583   4 IILAAGMGTRLRpltFTTPKSLIEVgdqTLIERQILF 40
Cdd:PTZ00339 110 LILAGGLGTRLG---SDKPKGLLEC---TPVKKKTLF 140
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 3-71 9.13e-03

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 36.65  E-value: 9.13e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 816130583   3 AIILAAGMGTRLRPltfTTPKSLIEVGDQTLIERQILFLNEIGISEIIIVTGYLSEKF-DFLESKYGVRL 71
Cdd:PRK14355   6 AIILAAGKGTRMKS---DLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQAEKVrEHFAGDGDVSF 72
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH