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Conserved domains on  [gi|74186313|dbj|BAE42936|]
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unnamed protein product [Mus musculus]

Protein Classification

eIF-2B_gamma_N domain-containing protein( domain architecture ID 10135960)

eIF-2B_gamma_N domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 3.16e-104

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: 299.57  E-value: 3.16e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKM-----KMKLDIVC 77
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313  78 IPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQESIEPVPGqKGKKKPVEQRDF 157
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74186313 158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd04198 160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 3.16e-104

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: 299.57  E-value: 3.16e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKM-----KMKLDIVC 77
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313  78 IPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQESIEPVPGqKGKKKPVEQRDF 157
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74186313 158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd04198 160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-134 5.10e-28

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: 106.01  E-value: 5.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--KDVQKALCAEFKmKMKLDIVCIPDE 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEYFGDGS-RFGVRITYVDEG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 74186313  82 ADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:COG1208  80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVP 133
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-126 1.90e-16

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 75.37  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313     5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNK-PLIWYPLNLLERVGFEEVIVVTTKdvQKALCAEFKM----KMKLDIVCIP 79
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ--EHRFMLNELLgdgsKFGVQITYAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 74186313    80 DEADMGTADSLRHIYPKL---KTDVLVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 4-56 3.16e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 49.67  E-value: 3.16e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74186313    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT 56
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIST 57
 
Name Accession Description Interval E-value
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-212 3.16e-104

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: 299.57  E-value: 3.16e-104
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKM-----KMKLDIVC 77
Cdd:cd04198   1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIVVVPEEEQAEISTYLRSfplnlKQKLDEVT 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313  78 IPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKGQESIEPVPGqKGKKKPVEQRDF 157
Cdd:cd04198  81 IVLDEDMGTADSLRHIRKKIKKDFLVLSCDLITDLPLIELVDLHRSHDASLTVLLYPPPVSSEQKGG-KGKSKKADERDV 159

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74186313 158 IGVDSTGKRLLFMANEADLDEELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd04198 160 IGLDEKTQRLLFITSEEDLDEDLELRKSLLKRHPRVTITTKLLDAHVYIFKRWVL 214
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
 3-212 7.23e-76

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: 227.91  E-value: 7.23e-76
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKALCAEFKMK-------MKLDI 75
Cdd:cd02507   1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLKSKwsslsskMIVDV 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313  76 VCIPDEADMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVV----DLFRAYDASLAMLMRKGQESIEPvpgqkgkKKP 151
Cdd:cd02507  81 ITSDLCESAGDALRLRDIRGLIRSDFLLLSCDLVSNIPLSELLeerrKKDKNAIATLTVLLASPPVSTEQ-------SKK 153

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74186313 152 VEQRDFIGVDSTGKRLLFMANEADLDE--ELVIKGSILQKHPRIHFHTGLVDAHLYCLKKYVV 212
Cdd:cd02507 154 TEEEDVIAVDSKTQRLLLLHYEEDLDEdlELIIRKSLLSKHPNVTIRTDLLDCHIYICSPDVL 216
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
 4-134 5.10e-28

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: 106.01  E-value: 5.10e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--KDVQKALCAEFKmKMKLDIVCIPDE 81
Cdd:COG1208   1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGylAEQIEEYFGDGS-RFGVRITYVDEG 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 74186313  82 ADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:COG1208  80 EPLGTGGALKRALPLLGDEpFLVLNGDILTDLDLAALLAFHREKGADATLALVP 133
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
 5-220 7.57e-26

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: 99.58  E-value: 7.57e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKD---VQKALCAEFKMKMKLDIVciPDE 81
Cdd:cd04181   1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLgeqIEEYFGDGSKFGVNIEYV--VQE 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313  82 ADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMrkgqesiepvpgqkgkkKPVEQRDFIGV 160
Cdd:cd04181  79 EPLGTAGAVRNAEDFLGDDdFLVVNGDVLTDLDLSELLRFHREKGADATIAV-----------------KEVEDPSRYGV 141

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313 161 dstgkrllfmaneADLDEELVIKGsILQKhPRiHFHTGLVDAHLYCLKKYVVDFLMENSE 220
Cdd:cd04181 142 -------------VELDDDGRVTR-FVEK-PT-LPESNLANAGIYIFEPEILDYIPEILP 185
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
4-132 1.36e-17

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 78.36  E-value: 1.36e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TKDVQKALCAEFKMKMKldIVCIPDE 81
Cdd:COG1213   1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgyKAELIEEALARPGPDVT--FVYNPDY 78

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 74186313  82 ADMGTADSLRHIYPKLKTDVLVLSCDLITDvalHEVVDLFRAYDASLAMLM 132
Cdd:COG1213  79 DETNNIYSLWLAREALDEDFLLLNGDVVFD---PAILKRLLASDGDIVLLV 126
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
 5-142 1.08e-16

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: 75.73  E-value: 1.08e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TKDVQKALCAEFkmkMKLDIVCIPDEA 82
Cdd:cd02523   1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgyKKEQIEELLKKY---PNIKFVYNPDYA 77

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74186313  83 DMGTADSLRHIYPKLKTDVLVLSCDLITDVA-LHEVVDlfraYDASLAML-MRKGQESIEPV 142
Cdd:cd02523  78 ETNNIYSLYLARDFLDEDFLLLEGDVVFDPSiLERLLS----SPADNAILvDKKTKEWEDEY 135
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
 5-126 1.90e-16

Nucleotidyl transferase; This family includes a wide range of enzymes which transfer nucleotides onto phosphosugars.


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 75.37  E-value: 1.90e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313     5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNK-PLIWYPLNLLERVGFEEVIVVTTKdvQKALCAEFKM----KMKLDIVCIP 79
Cdd:pfam00483   2 AIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREIIVILTQ--EHRFMLNELLgdgsKFGVQITYAL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 74186313    80 DEADMGTADSLRHIYPKL---KTDVLVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:pfam00483  80 QPEGKGTAPAVALAADFLgdeKSDVLVLGGDHIYRMDLEQAVKFHIEKAA 129
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
 5-134 2.35e-15

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: 71.77  E-value: 2.35e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT--KDVQKALCAEFKmKMKLDIVCIPDEA 82
Cdd:cd06426   1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNylAEMIEDYFGDGS-KFGVNISYVREDK 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 74186313  83 DMGTADSLRHIYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:cd06426  80 PLGTAGALSLLPEKPTDPFLVMNGDILTNLNYEHLLDFHKENNADATVCVRE 131
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
 4-148 1.06e-14

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: 70.29  E-value: 1.06e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEFKmkmKLDIVcIPD 80
Cdd:cd06422   1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNThhlADQIEAHLGDSRF---GLRIT-ISD 76

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 74186313  81 EAD--MGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRKgqesiEPVPGQKGK 148
Cdd:cd06422  77 EPDelLETGGGIKKALPLLGDEpFLVVNGDILWDGDLAPLLLLHAWRMDALLLLLPL-----VRNPGHNGV 142
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
 5-134 6.78e-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: 67.96  E-value: 6.78e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIvvttkdvqkaLCAEFKMKM-----------KL 73
Cdd:cd06915   1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIV----------LSVGYLAEQieeyfgdgyrgGI 70

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74186313  74 DIVCIPDEADMGTADSLRHIYPKLKTD-VLVLSCDLITDVALHEVVDLFRAYDASLAMLMRK 134
Cdd:cd06915  71 RIYYVIEPEPLGTGGAIKNALPKLPEDqFLVLNGDTYFDVDLLALLAALRASGADATMALRR 132
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
 5-142 7.52e-14

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: 66.45  E-value: 7.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313     5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTKDVQKALCAEFkmkmklDIVCIPDE-AD 83
Cdd:pfam12804   1 AVILAGGRSSRMGG-----DKALLPLGGKPLLERVLERLRPA-GDEVVVVANDEEVLAALAGL------GVPVVPDPdPG 68

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74186313    84 MGTADSLRHI--YPKLKTDVLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQEsIEPV 142
Cdd:pfam12804  69 QGPLAGLLAAlrAAPGADAVLVLACDmpFLTPELLRRLLAAAEESGADIVVPVYDGGR-GHPL 130
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
 3-205 3.20e-13

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: 66.09  E-value: 3.20e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKAlcAEF-------KMKMKLDI 75
Cdd:cd04197   1 LQAVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQI--KEYiekskwsKPKSSLMI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313  76 V-CIPDEADMGTADSLRHIYPK--LKTDVLVLSCDLITDVALHEVVDLFRAY-----DASLAMLMRKGqesIEPVPGQKG 147
Cdd:cd04197  79 ViIIMSEDCRSLGDALRDLDAKglIRGDFILVSGDVVSNIDLKEILEEHKERrkkdkNAIMTMVLKEA---SPPHRTRRT 155

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313 148 KKKPVeqrdfIGVDSTGKRLLFMANEADLDEE--LVIKGSILQKHPRIHFHTGLVDAHLY 205
Cdd:cd04197 156 GEEFV-----IAVDPKTSRLLHYEELPGSKYRsiTDLPSELLGSNSEVEIRHDLLDCHID 210
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
 5-126 1.94e-12

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: 64.15  E-value: 1.94e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTK--DVQKALCAEFKMKMKLDIVCIPDEA 82
Cdd:cd06425   3 ALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYrpEDMVPFLKEYEKKLGIKITFSIETE 82

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 74186313  83 DMGTADSLRHIYPKLKTDV---LVLSCDLITDVALHEVVDLFRAYDA 126
Cdd:cd06425  83 PLGTAGPLALARDLLGDDDepfFVLNSDVICDFPLAELLDFHKKHGA 129
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
 5-131 2.26e-12

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: 64.07  E-value: 2.26e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCaefkmkmKLDIVCIPDE 81
Cdd:cd02540   1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghgAEQVKKALA-------NPNVEFVLQE 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74186313  82 ADMGTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:cd02540  71 EQLGTGHAVKQALPALKDfegDVLVLYGDvpLITPETLQRLLEAHREAGADVTVL 125
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
1-136 9.60e-12

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 61.72  E-value: 9.60e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   1 MEFQAVVMAVGGGSRMtdltsSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAefkmkMKLDIVC 77
Cdd:COG2068   2 SKVAAIILAAGASSRM-----GRPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLgadAEEVAAALAG-----LGVRVVV 71

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74186313  78 IPD-EADMGTadSLR----HIYPKLkTDVLVLSCD--LITDVALHEVVDLFRAYDASLAMLMRKGQ 136
Cdd:COG2068  72 NPDwEEGMSS--SLRaglaALPADA-DAVLVLLGDqpLVTAETLRRLLAAFRESPASIVAPTYDGR 134
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
 5-128 1.01e-11

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: 62.20  E-value: 1.01e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVV---TTKDVQKALCAEFKMKMKldIVCIPDE 81
Cdd:cd04189   3 GLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVvgpTGEEIKEALGDGSRFGVR--ITYILQE 80

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 74186313  82 ADMGTADSLRHIYPKLKTD--VLVLSCDLITDvALHEVVDLFRA--YDASL 128
Cdd:cd04189  81 EPLGLAHAVLAARDFLGDEpfVVYLGDNLIQE-GISPLVRDFLEedADASI 130
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
5-63 2.66e-11

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 61.64  E-value: 2.66e-11
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKD----VQKAL 63
Cdd:COG1209   3 GIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTPEdgpqFERLL 65
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
 1-131 3.69e-11

Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440820 [Multi-domain]  Cd Length: 457  Bit Score: 61.58  E-value: 3.69e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   1 MEFQAVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEfkmkmklDIVC 77
Cdd:COG1207   1 SPLAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVghgAEQVRAALADL-------DVEF 70

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*....
gi 74186313  78 IPDEADMGTADSLRHIYPKLKTD---VLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:COG1207  71 VLQEEQLGTGHAVQQALPALPGDdgtVLVLYGDvpLIRAETLKALLAAHRAAGAAATVL 129
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
 8-127 4.36e-10

GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP:adenosylcobinamide-phosphate guanylyltransferase is part of the Pathway/BioSystem: Cobalamine/B12 biosynthesis


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 56.82  E-value: 4.36e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   8 MAVGGGSRMTDltssIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQKAlcAEFKMKMKLDIVCIPDE---ADM 84
Cdd:COG2266   1 MAGGKGTRLGG----GEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKT--REYLKERGVEVIETPGEgyvEDL 74

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 74186313  85 GTAdsLRHIypklKTDVLVLSCDL--ITDVALHEVVDLFRAYDAS 127
Cdd:COG2266  75 NEA--LESI----SGPVLVVPADLplLTPEIIDDIIDAYLESGKP 113
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
 5-57 5.19e-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: 5.19e-10
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|...
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTK 57
Cdd:cd02538   3 GIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILIISTP 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 ...
 5-131 4.89e-09

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


Pssm-ID: 133050 [Multi-domain]  Cd Length: 257  Bit Score: 54.95  E-value: 4.89e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMaVGG---GSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERV-GFEEVIVVT--TKDVQKALCAEFKMKMKLDIVCI 78
Cdd:cd06428   1 AVIL-VGGpqkGTRFRPLSLDVPKPLFPVAGKPMIHHHIEACAKVpDLKEVLLIGfyPESVFSDFISDAQQEFNVPIRYL 79

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 74186313  79 PDEADMGTADSLRH----IYPKLKTDVLVLSCDLITDVALHEVVDLFRAYDASLAML 131
Cdd:cd06428  80 QEYKPLGTAGGLYHfrdqILAGNPSAFFVLNADVCCDFPLQELLEFHKKHGASGTIL 136
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
 1-144 1.55e-08

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: 52.50  E-value: 1.55e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   1 MEFQAVVMAVGGGSRM-TDltssipKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTKDVQKAlcaefkmkmKLDIVCIP 79
Cdd:COG0746   3 MPITGVILAGGRSRRMgQD------KALLPLGGRPLLERVLERLRPQ-VDEVVIVANRPERYA---------ALGVPVVP 66

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74186313  80 DE-ADMG------TAdsLRHIypklKTD-VLVLSCD--LITDvalhEVVD-LFRAYDASLAMLMRKGQESIEPVPG 144
Cdd:COG0746  67 DDpPGAGplagilAA--LEAA----PAEwVLVLACDmpFLPP----DLVRrLLEALEEGADAVVPRSGGRLEPLFA 132
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
 5-129 1.77e-08

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: 52.18  E-value: 1.77e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT--TKDVQKALCAEFkmkmKLDIVCIPDeA 82
Cdd:cd04182   3 AIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLgaEADAVRAALAGL----PVVVVINPD-W 72

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|..
gi 74186313  83 DMGTADSLRHIYPKLKTD---VLVLSCD--LITDVALHEVVDLFRAYDASLA 129
Cdd:cd04182  73 EEGMSSSLAAGLEALPADadaVLILLADqpLVTAETLRALIDAFREDGAGIV 124
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
 5-53 2.43e-08

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: 52.57  E-value: 2.43e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*....
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIV 53
Cdd:cd02524   1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWHIMKIYSHYGHNDFIL 49
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
 5-58 2.97e-08

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: 52.14  E-value: 2.97e-08
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 74186313   5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVTTKD 58
Cdd:cd02516   3 AIILAAGSGSRMG---ADIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVPPD 54
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
 6-77 4.16e-08

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: 51.67  E-value: 4.16e-08
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74186313   6 VVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVTTKDVQ---KALCAEFKMKMKLDIVC 77
Cdd:COG1211   1 IIPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVPPDDIeyfEELLAKYGIDKPVRVVA 73
PRK15480 PRK15480
glucose-1-phosphate thymidylyltransferase RfbA; Provisional
 4-56 3.16e-07

glucose-1-phosphate thymidylyltransferase RfbA; Provisional


Pssm-ID: 185377 [Multi-domain]  Cd Length: 292  Bit Score: 49.67  E-value: 3.16e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74186313    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTT 56
Cdd:PRK15480   5 KGIILAGGSGTRLYPVTMAVSKQLLPIYDKPMIYYPLSTLMLAGIRDILIIST 57
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
 5-108 4.17e-07

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: 48.34  E-value: 4.17e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   5 AVVMAVGGGSRMTDltssiPKPLLPVGNKPLIWYPLNLLERVgFEEVIVVTTKDVQKALcaefkmkmKLDIVCIPDEA-D 83
Cdd:cd02503   3 GVILAGGKSRRMGG-----DKALLELGGKPLLEHVLERLKPL-VDEVVISANRDQERYA--------LLGVPVIPDEPpG 68

                        90       100
                ....*....|....*....|....*.
gi 74186313  84 MGTADSLRHIYPKLKTD-VLVLSCDL 108
Cdd:cd02503  69 KGPLAGILAALRAAPADwVLVLACDM 94
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 4.78e-07

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 49.48  E-value: 4.78e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313    5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDVQkALCAEFKMKMKLDIVCIPDEaDM 84
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGPGAE-AVAAAAAKIAPDAEIFVQKE-RL 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74186313   85 GTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLfRAYDASLAML 131
Cdd:PRK14353  83 GTAHAVLAAREALAGgygDVLVLYGDtpLITAETLARLRER-LADGADVVVL 133
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
 4-96 4.88e-07

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: 49.07  E-value: 4.88e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTK---------DVQKALCAEFKMKMKLD 74
Cdd:cd02541   2 KAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTGRgkraiedhfDRSYELEETLEKKGKTD 81

                        90       100
                ....*....|....*....|...
gi 74186313  75 IVCIPDE-ADMGTADSLRHIYPK 96
Cdd:cd02541  82 LLEEVRIiSDLANIHYVRQKEPL 104
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
5-77 2.98e-06

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 46.28  E-value: 2.98e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74186313    5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVG-FEEVIVVT----TKDVQKALCAEFKmkmKLDIVC 77
Cdd:PRK00155   6 AIIPAAGKGSRMG---ADRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVppddRPDFAELLLAKDP---KVTVVA 77
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
4-55 7.54e-06

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 45.67  E-value: 7.54e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74186313    4 QAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVT 61
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-216 1.62e-05

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 45.10  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313    5 AVVMAVGGGSRMtdlTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEfkmkmklDIVCIPDE 81
Cdd:PRK14356   8 ALILAAGKGTRM---HSDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVghrADMVRAAFPDE-------DARFVLQE 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   82 ADMGTADSLRHIYPKLK----TDVLVLSCD--LITDVALHEVVDlfRAYDASLAMLmrkgqeSIE-PVPGQKGKkkpveq 154
Cdd:PRK14356  78 QQLGTGHALQCAWPSLTaaglDRVLVVNGDtpLVTTDTIDDFLK--EAAGADLAFM------TLTlPDPGAYGR------ 143

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74186313  155 rdfigVDSTGKRLLFMANEADLDEELvikgsilqKHPRihfhTGLVDAHLYCLKKYVVDFLM 216
Cdd:PRK14356 144 -----VVRRNGHVAAIVEAKDYDEAL--------HGPE----TGEVNAGIYYLRLDAVESLL 188
glmU PRK14358
bifunctional N-acetylglucosamine-1-phosphate uridyltransferase/glucosamine-1-phosphate ...
 6-131 3.59e-05

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


Pssm-ID: 237688 [Multi-domain]  Cd Length: 481  Bit Score: 43.81  E-value: 3.59e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313    6 VVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALCAEfkmkmklDIVCIPDEA 82
Cdd:PRK14358  11 VILAAGQGTRMK---SALPKVLHPVAGRPMVAWAVKAARDLGARKIVVVTghgAEQVEAALQGS-------GVAFARQEQ 80

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74186313   83 DMGTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:PRK14358  81 QLGTGDAFLSGASALTEgdaDILVLYGDtpLLRPDTLRALVADHRAQGSAMTIL 134
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-110 4.41e-05

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 43.67  E-value: 4.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313    1 MEFQAVVMAVGGGSRMtdlTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT---TKDVQKALC--AEFKMKmkldi 75
Cdd:PRK14354   1 MNRYAIILAAGKGTRM---KSKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVghgAEEVKEVLGdrSEFALQ----- 72

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 74186313   76 vcipdEADMGTADSLRHIYPKLKT---DVLVLSCD--LIT 110
Cdd:PRK14354  73 -----EEQLGTGHAVMQAEEFLADkegTTLVICGDtpLIT 107
ispDF PRK09382
bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol ...
 1-58 5.03e-05

bifunctional 2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase/2-C-methyl-D-erythritol 2,4-cyclodiphosphate synthase protein; Provisional


Pssm-ID: 236492 [Multi-domain]  Cd Length: 378  Bit Score: 43.30  E-value: 5.03e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 74186313    1 MEFQAVVMAVGGGSRmtdLTSSIPKPLLPVGNKPLIWYPL-NLLERVGFEEVIVVTTKD 58
Cdd:PRK09382   4 SDISLVIVAAGRSTR---FSAEVKKQWLRIGGKPLWLHVLeNLSSAPAFKEIVVVIHPD 59
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
 8-122 5.04e-05

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


Pssm-ID: 133026 [Multi-domain]  Cd Length: 231  Bit Score: 43.01  E-value: 5.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313   8 MAvGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVttkdVQKALCAEFKMKMKL-------DIVCIPD 80
Cdd:cd04183   5 MA-GLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFI----CRDEHNTKFHLDESLkllapnaTVVELDG 79

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....
gi 74186313  81 EADmGTADSLRHIYPKLKTD--VLVLSCDLITDVALHEVVDLFR 122
Cdd:cd04183  80 ETL-GAACTVLLAADLIDNDdpLLIFNCDQIVESDLLAFLAAFR 122
glmU PRK14355
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 5-131 5.33e-05

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


Pssm-ID: 237685 [Multi-domain]  Cd Length: 459  Bit Score: 43.58  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313    5 AVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVTTKDvQKALCAEFKMKMklDIVCIPDEADM 84
Cdd:PRK14355   6 AIILAAGKGTRMK---SDLVKVMHPLAGRPMVSWPVAAAREAGAGRIVLVVGHQ-AEKVREHFAGDG--DVSFALQEEQL 79

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 74186313   85 GTADSLRHIYPKLKT---DVLVLSCD--LITDVALHEVVDLFRAYDASLAML 131
Cdd:PRK14355  80 GTGHAVACAAPALDGfsgTVLILCGDvpLLRAETLQGMLAAHRATGAAVTVL 131
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
3-55 1.37e-04

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 41.80  E-value: 1.37e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74186313    3 FQAVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVT 56
CTP_transf_3 pfam02348
Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) ...
 5-69 7.11e-04

Cytidylyltransferase; This family consists of two main Cytidylyltransferase activities: 1) 3-deoxy-manno-octulosonate cytidylyltransferase,, EC:2.7.7.38 catalysing the reaction:- CTP + 3-deoxy-D-manno-octulosonate <=> diphosphate + CMP-3-deoxy-D-manno-octulosonate, 2) acylneuraminate cytidylyltransferase EC:2.7.7.43,, catalysing the reaction:- CTP + N-acylneuraminate <=> diphosphate + CMP-N-acylneuraminate. NeuAc cytydilyltransferase of Mannheimia haemolytica has been characterized describing kinetics and regulation by substrate charge, energetic charge and amino-sugar demand.


Pssm-ID: 396773  Cd Length: 217  Bit Score: 39.24  E-value: 7.11e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313     5 AVVMAVGGGSRMTDltssipKPLLPVGNKPLIWYPL-NLLERVGFEEVIVVT----TKDVQKALCAEFKM 69
Cdd:pfam02348   2 AIIPARLGSKRLPG------KNLLDLGGKPLIHHVLeAALKSGAFEKVIVATdseeIADVAKEFGAGVVM 65
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
5-55 4.90e-03

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 37.32  E-value: 4.90e-03
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|.
gi 74186313   5 AVVMAVGGGSRMTDLTSSIPKPLLPVGNKPLIWYPLNLLERVGFEEVIVVT 55
Cdd:COG1210   6 AVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVT 56
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
 1-108 6.35e-03

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 36.89  E-value: 6.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74186313    1 MEFQAVVMAVGGGSRMTdltSSIPKPLLPVGNKPLIWYPLNLLERVGfEEVIVVTTKD---VQKALCAEFKmkmKLDIVc 77
Cdd:PRK14359   1 MKLSIIILAAGKGTRMK---SSLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQkerIKEAVLEYFP---GVIFH- 72

                         90       100       110
                 ....*....|....*....|....*....|..
gi 74186313   78 IPDEADM-GTADSLRHIYPKLKtDVLVLSCDL 108
Cdd:PRK14359  73 TQDLENYpGTGGALMGIEPKHE-RVLILNGDM 103
 
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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