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Conserved domains on  [gi|495112875|ref|WP_007837695|]
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MULTISPECIES: sugar phosphate nucleotidyltransferase [Phocaeicola]

Protein Classification

glycosyltransferase family protein( domain architecture ID 27718)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
2-274 3.68e-55

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


The actual alignment was detected with superfamily member cd06422:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 221  Bit Score: 177.38  E-value: 3.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLeANQNFGIDIQISDETD 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL-GDSRFGLRITISDEPD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  82 CLLDTGGGLERAYYLLhhpedmftkeGETPyelifenlmkgmdeeeiierglgimrkecYLLHNVDILSNCDFESLMYYH 161
Cdd:cd06422   80 ELLETGGGIKKALPLL----------GDEP-----------------------------FLVVNGDILWDGDLAPLLLLH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 162 QNS-SNINATLLVSPrkTSRYLLFNDDNLlrgwvnkdtmetKPAGL--RYKEGEYREYAYSGIQVTTPKILNLLPRGKYS 238
Cdd:cd06422  121 AWRmDALLLLLPLVR--NPGHNGVGDFSL------------DADGRlrRGGGGAVAPFTFTGIQILSPELFAGIPPGKFS 186
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495112875 239 IIDFYLSICHRVDIqCYVEDDLQLLDIGKPENLEKA 274
Cdd:cd06422  187 LNPLWDRAIAAGRL-FGLVYDGLWFDVGTPERLLAA 221
 
Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-274 3.68e-55

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: 177.38  E-value: 3.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLeANQNFGIDIQISDETD 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL-GDSRFGLRITISDEPD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  82 CLLDTGGGLERAYYLLhhpedmftkeGETPyelifenlmkgmdeeeiierglgimrkecYLLHNVDILSNCDFESLMYYH 161
Cdd:cd06422   80 ELLETGGGIKKALPLL----------GDEP-----------------------------FLVVNGDILWDGDLAPLLLLH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 162 QNS-SNINATLLVSPrkTSRYLLFNDDNLlrgwvnkdtmetKPAGL--RYKEGEYREYAYSGIQVTTPKILNLLPRGKYS 238
Cdd:cd06422  121 AWRmDALLLLLPLVR--NPGHNGVGDFSL------------DADGRlrRGGGGAVAPFTFTGIQILSPELFAGIPPGKFS 186
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495112875 239 IIDFYLSICHRVDIqCYVEDDLQLLDIGKPENLEKA 274
Cdd:cd06422  187 LNPLWDRAIAAGRL-FGLVYDGLWFDVGTPERLLAA 221
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-278 1.44e-51

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: 168.79  E-value: 1.44e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQISDETD 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  82 cLLDTGGGLERAYYLLhhPEDMFtkegetpyelifenlmkgmdeeeiierglgimrkecyLLHNVDILSNCDFESLMYYH 161
Cdd:COG1208   81 -PLGTGGALKRALPLL--GDEPF-------------------------------------LVLNGDILTDLDLAALLAFH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 162 QNSSNINATLLVSPRKTSRY--LLFNDDNLLRGWVNKdtmetkpaglryKEGEYREYAYSGIQVTTPKILNLLPRG-KYS 238
Cdd:COG1208  121 REKGADATLALVPVPDPSRYgvVELDGDGRVTRFVEK------------PEEPPSNLINAGIYVLEPEIFDYIPEGePFD 188
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 495112875 239 IIDFYLSICHRVDIQCYVEDDlQLLDIGKPENLEKAEEFL 278
Cdd:COG1208  189 LEDLLPRLIAEGRVYGYVHDG-YWLDIGTPEDLLEANALL 227
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-75 3.28e-20

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


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 89.19  E-value: 3.28e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112875    1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQ 75
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIE 75
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-80 3.70e-12

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: 64.58  E-value: 3.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875    2 KAMIFAAGLGSRLKPLTDTRPKALITVGGK-TMLEHIILKLKAAGFDE-IVINVHHFSNQILAFLEANQNFGIDIQISDE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                  .
gi 495112875   80 T 80
Cdd:pfam00483  81 P 81
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-65 4.58e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.60  E-value: 4.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112875   3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLE 65
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLG 64
 
Name Accession Description Interval E-value
NTP_transferase_like_1 cd06422
NTP_transferase_like_1 is a member of the nucleotidyl transferase family; This is a subfamily ...
2-274 3.68e-55

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: 177.38  E-value: 3.68e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLeANQNFGIDIQISDETD 81
Cdd:cd06422    1 KAMILAAGLGTRMRPLTDTRPKPLVPVAGKPLIDHALDRLAAAGIRRIVVNTHHLADQIEAHL-GDSRFGLRITISDEPD 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  82 CLLDTGGGLERAYYLLhhpedmftkeGETPyelifenlmkgmdeeeiierglgimrkecYLLHNVDILSNCDFESLMYYH 161
Cdd:cd06422   80 ELLETGGGIKKALPLL----------GDEP-----------------------------FLVVNGDILWDGDLAPLLLLH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 162 QNS-SNINATLLVSPrkTSRYLLFNDDNLlrgwvnkdtmetKPAGL--RYKEGEYREYAYSGIQVTTPKILNLLPRGKYS 238
Cdd:cd06422  121 AWRmDALLLLLPLVR--NPGHNGVGDFSL------------DADGRlrRGGGGAVAPFTFTGIQILSPELFAGIPPGKFS 186
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495112875 239 IIDFYLSICHRVDIqCYVEDDLQLLDIGKPENLEKA 274
Cdd:cd06422  187 LNPLWDRAIAAGRL-FGLVYDGLWFDVGTPERLLAA 221
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
2-278 1.44e-51

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: 168.79  E-value: 1.44e-51
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQISDETD 81
Cdd:COG1208    1 KAVILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVGYLAEQIEEYFGDGSRFGVRITYVDEGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  82 cLLDTGGGLERAYYLLhhPEDMFtkegetpyelifenlmkgmdeeeiierglgimrkecyLLHNVDILSNCDFESLMYYH 161
Cdd:COG1208   81 -PLGTGGALKRALPLL--GDEPF-------------------------------------LVLNGDILTDLDLAALLAFH 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 162 QNSSNINATLLVSPRKTSRY--LLFNDDNLLRGWVNKdtmetkpaglryKEGEYREYAYSGIQVTTPKILNLLPRG-KYS 238
Cdd:COG1208  121 REKGADATLALVPVPDPSRYgvVELDGDGRVTRFVEK------------PEEPPSNLINAGIYVLEPEIFDYIPEGePFD 188
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 495112875 239 IIDFYLSICHRVDIQCYVEDDlQLLDIGKPENLEKAEEFL 278
Cdd:COG1208  189 LEDLLPRLIAEGRVYGYVHDG-YWLDIGTPEDLLEANALL 227
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
3-242 9.28e-39

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: 135.02  E-value: 9.28e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQISDETDc 82
Cdd:cd04181    1 AVILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGEQIEEYFGDGSKFGVNIEYVVQEE- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  83 LLDTGGGLERAYYLLhhPEDMFtkegetpyelifenlmkgmdeeeiierglgimrkecyLLHNVDILSNCDFESLMYYHQ 162
Cdd:cd04181   80 PLGTAGAVRNAEDFL--GDDDF-------------------------------------LVVNGDVLTDLDLSELLRFHR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 163 NSSNInATLLVSPRK-TSRY--LLFNDDNLLRGWVNKDTmetkpaglrykeGEYREYAYSGIQVTTPKILNLLPRGKYSI 239
Cdd:cd04181  121 EKGAD-ATIAVKEVEdPSRYgvVELDDDGRVTRFVEKPT------------LPESNLANAGIYIFEPEILDYIPEILPRG 187

                 ...
gi 495112875 240 IDF 242
Cdd:cd04181  188 EDE 190
NTP_transferase_like_2 cd06426
NTP_trnasferase_like_2 is a member of the nucleotidyl transferase family; This is a subfamily ...
3-274 6.89e-28

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: 106.83  E-value: 6.89e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQISDEtDC 82
Cdd:cd06426    1 VVIMAGGKGTRLRPLTENTPKPMLKVGGKPILETIIDRFIAQGFRNFYISVNYLAEMIEDYFGDGSKFGVNISYVRE-DK 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  83 LLDTGGGLerayyllhhpedmftkegetpyelifeNLMKGMDEEEIIerglgIMrkecyllhNVDILSNCDFESLMYYHQ 162
Cdd:cd06426   80 PLGTAGAL---------------------------SLLPEKPTDPFL-----VM--------NGDILTNLNYEHLLDFHK 119
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 163 NSSNInATLLVSPRKTS-RYLLFN-DDNLLRGwvnkdtMETKPaglrykegEYREYAYSGIQVTTPKILNLLPRGKY--- 237
Cdd:cd06426  120 ENNAD-ATVCVREYEVQvPYGVVEtEGGRITS------IEEKP--------THSFLVNAGIYVLEPEVLDLIPKNEFfdm 184
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 495112875 238 -SIIDFYLSICHRVdiQCYVEDDlQLLDIGKPENLEKA 274
Cdd:cd06426  185 pDLIEKLIKEGKKV--GVFPIHE-YWLDIGRPEDYEKA 219
NTP_transferase_WcbM_like cd06915
WcbM_like is a subfamily of nucleotidyl transferases; WcbM protein of Burkholderia mallei is ...
3-275 3.54e-27

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: 104.94  E-value: 3.54e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQISDETDc 82
Cdd:cd06915    1 AVILAGGLGTRLRSVVKDLPKPLAPVAGRPFLEYLLEYLARQGISRIVLSVGYLAEQIEEYFGDGYRGGIRIYYVIEPE- 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  83 LLDTGGGLERAyyLLHHPEDMFtkegetpyelifenlmkgmdeeeiierglgimrkecyLLHNVDILSNCDFESLMYYHQ 162
Cdd:cd06915   80 PLGTGGAIKNA--LPKLPEDQF-------------------------------------LVLNGDTYFDVDLLALLAALR 120
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875 163 NSSNINATLLVSPRKTSRY--LLFNDDNLLRGWVNKDtmetkpaglrykEGEYREYAYSGIQVTTPKILNLLPRGKYSII 240
Cdd:cd06915  121 ASGADATMALRRVPDASRYgnVTVDGDGRVIAFVEKG------------PGAAPGLINGGVYLLRKEILAEIPADAFSLE 188
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 495112875 241 -DFYLSICHRVDIQCYVEDDlQLLDIGKPENLEKAE 275
Cdd:cd06915  189 aDVLPALVKRGRLYGFEVDG-YFIDIGIPEDYARAQ 223
Arch_glmU TIGR03992
UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate N-acetyltransferase; The ...
1-75 3.28e-20

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


Pssm-ID: 274908 [Multi-domain]  Cd Length: 393  Bit Score: 89.19  E-value: 3.28e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112875    1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDIQ 75
Cdd:TIGR03992   1 MKAVILAAGKGTRMRPLTETRPKPMLPVAGKPLLEHIIEALRDAGIDDFVFVVGYGKEKVREYFGDGSRGGVPIE 75
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
1-74 1.37e-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: 84.93  E-value: 1.37e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNFGIDI 74
Cdd:cd04189    1 MKGLILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDLREAGIEDIGIVVGPTGEEIKEALGDGSRFGVRI 74
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
2-76 7.40e-19

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 82.98  E-value: 7.40e-19
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANqnfGIDIQI 76
Cdd:COG1213    1 KAVILAAGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTGYKAELIEEALARP---GPDVTF 72
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
3-70 5.81e-18

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: 80.35  E-value: 5.81e-18
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQNF 70
Cdd:cd02523    1 AIILAAGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTGYKKEQIEELLKKYPNI 68
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
1-104 2.82e-17

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: 78.79  E-value: 2.82e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFL-EANQNFGIDIQISDE 79
Cdd:cd06425    1 MKALILVGGYGTRLRPLTLTVPKPLVEFCNKPMIEHQIEALAKAGVKEIILAVNYRPEDMVPFLkEYEKKLGIKITFSIE 80
                         90       100
                 ....*....|....*....|....*
gi 495112875  80 TDClLDTGGGLERAYYLLHHPEDMF 104
Cdd:cd06425   81 TEP-LGTAGPLALARDLLGDDDEPF 104
RmlA1 COG1209
dTDP-glucose pyrophosphorylase [Cell wall/membrane/envelope biogenesis];
1-76 2.53e-15

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


Pssm-ID: 440822 [Multi-domain]  Cd Length: 294  Bit Score: 74.36  E-value: 2.53e-15
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINV-HHFSNQILAFLEANQNFGIDIQI 76
Cdd:COG1209    1 MKGIILAGGSGTRLRPLTLTVSKQLLPVYDKPMIYYPLSTLMLAGIREILIIStPEDGPQFERLLGDGSQLGIKISY 77
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
2-80 3.70e-12

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: 64.58  E-value: 3.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875    2 KAMIFAAGLGSRLKPLTDTRPKALITVGGK-TMLEHIILKLKAAGFDE-IVINVHHFSNQILAFLEANQNFGIDIQISDE 79
Cdd:pfam00483   1 KAIILAGGSGTRLWPLTRTLAKPLVPVGGKyPLIDYPLSRLANAGIREiIVILTQEHRFMLNELLGDGSKFGVQITYALQ 80

                  .
gi 495112875   80 T 80
Cdd:pfam00483  81 P 81
eIF-2B_gamma_N_like cd02507
The N-terminal of eIF-2B_gamma_like is predicted to have glycosyltransferase activity; ...
1-82 8.15e-11

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: 60.34  E-value: 8.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLE----ANQNFGIDIQI 76
Cdd:cd02507    1 FQAVVLADGFGSRFLPLTSDIPKALLPVANVPLIDYTLEWLEKAGVEEVFVVCCEHSQAIIEHLLkskwSSLSSKMIVDV 80

                 ....*.
gi 495112875  77 SDETDC 82
Cdd:cd02507   81 ITSDLC 86
MocA COG2068
CTP:molybdopterin cytidylyltransferase MocA [Coenzyme transport and metabolism];
3-66 7.49e-10

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


Pssm-ID: 441671 [Multi-domain]  Cd Length: 195  Bit Score: 57.09  E-value: 7.49e-10
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112875   3 AMIFAAGLGSRLKpltdtRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEA 66
Cdd:COG2068    6 AIILAAGASSRMG-----RPKLLLPLGGKPLLERAVEAALAAGLDPVVVVLGADAEEVAAALAG 64
eIF-2B_gamma_N cd04198
The N-terminal domain of gamma subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
1-51 1.09e-09

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: 56.90  E-value: 1.09e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVI 51
Cdd:cd04198    1 FQAVILAGGGGSRLYPLTDNIPKALLPVANKPMIWYPLDWLEKAGFEDVIV 51
GT2_GlmU_N_bac cd02540
N-terminal domain of bacterial GlmU; The N-terminal domain of N-Acetylglucosamine-1-phosphate ...
3-102 1.21e-09

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: 57.14  E-value: 1.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLeanQNFGIDIQISDETdc 82
Cdd:cd02540    1 AVILAAGKGTRMK---SDLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVKKAL---ANPNVEFVLQEEQ-- 72
                         90       100
                 ....*....|....*....|
gi 495112875  83 lLDTGGGLERAYYLLHHPED 102
Cdd:cd02540   73 -LGTGHAVKQALPALKDFEG 91
NTP_transf_3 pfam12804
MobA-like NTP transferase domain; This family includes the MobA protein (Molybdopterin-guanine ...
3-79 2.47e-09

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: 54.89  E-value: 2.47e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112875    3 AMIFAAGLGSRLKpltdtRPKALITVGGKTMLEHIILKLKAAgFDEIVINVHHfsNQILAFLEAnqnFGIDIqISDE 79
Cdd:pfam12804   1 AVILAGGRSSRMG-----GDKALLPLGGKPLLERVLERLRPA-GDEVVVVAND--EEVLAALAG---LGVPV-VPDP 65
GlmU COG1207
Bifunctional protein GlmU, N-acetylglucosamine-1-phosphate-uridyltransferase ...
1-68 3.09e-08

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: 54.26  E-value: 3.09e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112875   1 MKAMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANQ 68
Cdd:COG1207    3 LAVVILAAGKGTRMK---SKLPKVLHPLAGKPMLEHVLDAARALGPDRIVVVVGHGAEQVRAALADLD 67
UGPase_prokaryotic cd02541
Prokaryotic UGPase catalyses the synthesis of UDP-glucose; Prokaryotic UDP-Glucose ...
1-54 5.40e-08

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: 52.53  E-value: 5.40e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVH 54
Cdd:cd02541    1 RKAVIPAAGLGTRFLPATKAIPKEMLPIVDKPVIQYIVEEAVAAGIEDIIIVTG 54
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
3-51 7.61e-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: 51.41  E-value: 7.61e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 495112875   3 AMIFAAGLGSRLKpltdtRPKALITVGGKTMLEHIILKLKAAGFDEIVI 51
Cdd:cd04182    3 AIILAAGRSSRMG-----GNKLLLPLDGKPLLRHALDAALAAGLSRVIV 46
MobA COG0746
Molybdopterin-guanine dinucleotide biosynthesis protein A [Coenzyme transport and metabolism]; ...
1-64 7.91e-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: 51.35  E-value: 7.91e-08
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 495112875   1 MKAMIFAAGLGSRLKpltdtRPKALITVGGKTMLEHIILKLKAAgFDEIVINVHHfsNQILAFL 64
Cdd:COG0746    5 ITGVILAGGRSRRMG-----QDKALLPLGGRPLLERVLERLRPQ-VDEVVIVANR--PERYAAL 60
MobA cd02503
MobA catalyzes the formation of molybdopterin guanine dinucleotide; The prokaryotic enzyme ...
1-55 2.50e-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: 49.88  E-value: 2.50e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 495112875   1 MKAMIFAAGLGSRLKpltdtRPKALITVGGKTMLEHIILKLKAAgFDEIVINVHH 55
Cdd:cd02503    1 ITGVILAGGKSRRMG-----GDKALLELGGKPLLEHVLERLKPL-VDEVVISANR 49
IspD COG1211
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase [Lipid transport and metabolism]; ...
5-54 3.41e-07

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: 49.74  E-value: 3.41e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112875   5 IFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAG-FDEIVINVH 54
Cdd:COG1211    2 IPAAGSGSRMG---AGIPKQFLPLGGKPVLEHTLEAFLAHPrIDEIVVVVP 49
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-65 4.58e-07

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 50.60  E-value: 4.58e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 495112875   3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLE 65
Cdd:PRK14354   5 AIILAAGKGTRMK---SKLPKVLHKVCGKPMVEHVVDSVKKAGIDKIVTVVGHGAEEVKEVLG 64
CDP-ME_synthetase cd02516
CDP-ME synthetase is involved in mevalonate-independent isoprenoid production; ...
3-54 5.20e-07

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: 49.44  E-value: 5.20e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495112875   3 AMIFAAGLGSRLKPltdTRPKALITVGGKTMLEHIILKLKAAG-FDEIVINVH 54
Cdd:cd02516    3 AIILAAGSGSRMGA---DIPKQFLELGGKPVLEHTLEAFLAHPaIDEIVVVVP 52
G1P_cytidylyltransferase cd02524
G1P_cytidylyltransferase catalyzes the production of CDP-D-Glucose; ...
3-51 6.88e-07

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: 49.11  E-value: 6.88e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHiILKLKAA-GFDEIVI 51
Cdd:cd02524    1 VVILAGGLGTRLSEETELKPKPMVEIGGRPILWH-IMKIYSHyGHNDFIL 49
ispD PRK00155
D-ribitol-5-phosphate cytidylyltransferase;
3-62 8.67e-07

D-ribitol-5-phosphate cytidylyltransferase;


Pssm-ID: 234670  Cd Length: 227  Bit Score: 48.59  E-value: 8.67e-07
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495112875   3 AMIFAAGLGSRLKPltdTRPKALITVGGKTMLEHIILKLKAAG-FDEIVINVH-----HFSNQILA 62
Cdd:PRK00155   6 AIIPAAGKGSRMGA---DRPKQYLPLGGKPILEHTLEAFLAHPrIDEIIVVVPpddrpDFAELLLA 68
PRK10122 PRK10122
UTP--glucose-1-phosphate uridylyltransferase GalF;
1-66 3.35e-06

UTP--glucose-1-phosphate uridylyltransferase GalF;


Pssm-ID: 182252 [Multi-domain]  Cd Length: 297  Bit Score: 47.58  E-value: 3.35e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVH--------HF--SNQILAFLEA 66
Cdd:PRK10122   4 LKAVIPVAGLGMHMLPATKAIPKEMLPIVDKPMIQYIVDEIVAAGIKEIVLVTHasknavenHFdtSYELESLLEQ 79
G1P_TT_short cd02538
G1P_TT_short is the short form of glucose-1-phosphate thymidylyltransferase; This family is ...
1-51 3.39e-06

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: 47.18  E-value: 3.39e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112875   1 MKAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVI 51
Cdd:cd02538    1 MKGIILAGGSGTRLYPLTKVVSKQLLPVYDKPMIYYPLSTLMLAGIREILI 51
GalU COG1210
UTP-glucose-1-phosphate uridylyltransferase [Cell wall/membrane/envelope biogenesis];
2-67 7.75e-06

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


Pssm-ID: 440823 [Multi-domain]  Cd Length: 288  Bit Score: 46.18  E-value: 7.75e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVH--------HF--SNQILAFLEAN 67
Cdd:COG1210    5 KAVIPVAGLGTRFLPATKAIPKEMLPIVDKPLIQYVVEEAVAAGIEEIIFVTGrgkraiedHFdrSYELEATLEAK 80
eIF-2B_epsilon_N cd04197
The N-terminal domain of epsilon subunit of the eIF-2B is a subfamily of glycosyltransferase 2; ...
3-85 1.01e-05

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: 45.29  E-value: 1.01e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEA-------NQNFGIDIQ 75
Cdd:cd04197    3 AVVLADSFNRRFRPLTKEKPRCLLPLANVPLIDYTLEFLALNGVEEVFVFCCSHSDQIKEYIEKskwskpkSSLMIVIII 82
                         90
                 ....*....|
gi 495112875  76 ISDETDCLLD 85
Cdd:cd04197   83 MSEDCRSLGD 92
glmU PRK14353
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-55 1.17e-05

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


Pssm-ID: 184642 [Multi-domain]  Cd Length: 446  Bit Score: 46.01  E-value: 1.17e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 495112875   3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHH 55
Cdd:PRK14353   8 AIILAAGEGTRMK---SSLPKVLHPVAGRPMLAHVLAAAASLGPSRVAVVVGP 57
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
7-74 1.56e-05

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: 44.49  E-value: 1.56e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 495112875   7 AAGLGSRLkpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEANqnfGIDI 74
Cdd:COG2266    2 AGGKGTRL----GGGEKPLLEICGKPMIDRVIDALEESCIDKIYVAVSPNTPKTREYLKER---GVEV 62
PRK13389 PRK13389
UTP--glucose-1-phosphate uridylyltransferase GalU;
2-60 1.88e-05

UTP--glucose-1-phosphate uridylyltransferase GalU;


Pssm-ID: 184021 [Multi-domain]  Cd Length: 302  Bit Score: 45.28  E-value: 1.88e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 495112875   2 KAMIFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQI 60
Cdd:PRK13389  10 KAVIPVAGLGTRMLPATKAIPKEMLPLVDKPLIQYVVNECIAAGITEIVLVTHSSKNSI 68
mobA PRK00317
molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed
1-52 2.04e-05

molybdopterin-guanine dinucleotide biosynthesis protein MobA; Reviewed


Pssm-ID: 234725 [Multi-domain]  Cd Length: 193  Bit Score: 44.41  E-value: 2.04e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 495112875   1 MKAMIFAAGLGSRLkpltDTRPKALITVGGKTMLEHIILKLkAAGFDEIVIN 52
Cdd:PRK00317   4 ITGVILAGGRSRRM----GGVDKGLQELNGKPLIQHVIERL-APQVDEIVIN 50
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
5-101 4.13e-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: 43.78  E-value: 4.13e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   5 IFAAGLGSRLKPLTDTRPKALITVGGKTMLEHIILKLKAAGFDEIvinvhhfsnqILAFL-EANQNFGIDIQISD-ETDC 82
Cdd:cd04183    3 IPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRF----------IFICRdEHNTKFHLDESLKLlAPNA 72
                         90       100
                 ....*....|....*....|....
gi 495112875  83 ---LLD--TGGGLERAYYLLHHPE 101
Cdd:cd04183   73 tvvELDgeTLGAACTVLLAADLID 96
glgC PRK00725
glucose-1-phosphate adenylyltransferase; Provisional
3-31 6.07e-05

glucose-1-phosphate adenylyltransferase; Provisional


Pssm-ID: 234824 [Multi-domain]  Cd Length: 425  Bit Score: 44.06  E-value: 6.07e-05
                         10        20
                 ....*....|....*....|....*....
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGK 31
Cdd:PRK00725  18 ALILAGGRGSRLKELTDKRAKPAVYFGGK 46
GlgC COG0448
Glucose-1-phosphate adenylyltransferase (ADP-glucose pyrophosphorylase) [Carbohydrate ...
3-31 9.22e-05

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


Pssm-ID: 440217 [Multi-domain]  Cd Length: 377  Bit Score: 43.14  E-value: 9.22e-05
                         10        20
                 ....*....|....*....|....*....
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGK 31
Cdd:COG0448    4 AIILAGGRGSRLGPLTKDRAKPAVPFGGK 32
PRK14489 PRK14489
putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; ...
3-53 1.01e-04

putative bifunctional molybdopterin-guanine dinucleotide biosynthesis protein MobA/MobB; Provisional


Pssm-ID: 237727 [Multi-domain]  Cd Length: 366  Bit Score: 43.20  E-value: 1.01e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 495112875   3 AMIFAAGLGSRLkpltDTRPKALITVGGKTMLEHIILKLKAAgFDEIVINV 53
Cdd:PRK14489   8 GVILAGGLSRRM----NGRDKALILLGGKPLIERVVDRLRPQ-FARIHLNI 53
glmU PRK14352
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-79 1.61e-04

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


Pssm-ID: 184641 [Multi-domain]  Cd Length: 482  Bit Score: 42.62  E-value: 1.61e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 495112875   3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQILAFLEAnQNFGIDIQISDE 79
Cdd:PRK14352   7 VIVLAAGAGTRMR---SDTPKVLHTLAGRSMLGHVLHAAAGLAPQHLVVVVGHDRERVAPAVAE-LAPEVDIAVQDE 79
glmU PRK14359
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
5-66 1.69e-04

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


Pssm-ID: 237689 [Multi-domain]  Cd Length: 430  Bit Score: 42.67  E-value: 1.69e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 495112875   5 IFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGfDEIVINVHHFSNQILAFLEA 66
Cdd:PRK14359   7 ILAAGKGTRMK---SSLPKVLHTICGKPMLFYILKEAFAIS-DDVHVVLHHQKERIKEAVLE 64
M1P_guanylylT_A_like_N cd06428
N-terminal domain of M1P_guanylyl_A_ like proteins are likely to be a isoform of GDP-mannose ...
11-104 1.81e-04

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: 41.86  E-value: 1.81e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875  11 GSRLKPLTDTRPKALITVGGKTMLEHIILKL-KAAGFDEIVINVHHFSNQILAFL-EANQNFGIDIQISDEtDCLLDTGG 88
Cdd:cd06428   11 GTRFRPLSLDVPKPLFPVAGKPMIHHHIEACaKVPDLKEVLLIGFYPESVFSDFIsDAQQEFNVPIRYLQE-YKPLGTAG 89
                         90       100
                 ....*....|....*....|.
gi 495112875  89 GLeraYY-----LLHHPEDMF 104
Cdd:cd06428   90 GL---YHfrdqiLAGNPSAFF 107
ADP_Glucose_PP cd02508
ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ...
3-31 6.78e-04

ADP-glucose pyrophosphorylase is involved in the biosynthesis of glycogen or starch; ADP-glucose pyrophosphorylase (glucose-1-phosphate adenylyltransferase) catalyzes a very important step in the biosynthesis of alpha 1,4-glucans (glycogen or starch) in bacteria and plants: synthesis of the activated glucosyl donor, ADP-glucose, from glucose-1-phosphate and ATP. ADP-glucose pyrophosphorylase is a tetrameric allosterically regulated enzyme. While a homotetramer in bacteria, in plant chloroplasts and amyloplasts, it is a heterotetramer of two different, yet evolutionary related, subunits. There are a number of conserved regions in the sequence of bacterial and plant ADP-glucose pyrophosphorylase subunits. It is a subfamily of a very diverse glycosy transferase family 2.


Pssm-ID: 133002 [Multi-domain]  Cd Length: 200  Bit Score: 39.83  E-value: 6.78e-04
                         10        20
                 ....*....|....*....|....*....
gi 495112875   3 AMIFAAGLGSRLKPLTDTRPKALITVGGK 31
Cdd:cd02508    1 AIILAGGEGTRLSPLTKKRAKPAVPFGGR 29
glmU PRK14357
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
1-128 1.10e-03

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


Pssm-ID: 237687 [Multi-domain]  Cd Length: 448  Bit Score: 40.13  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 495112875   1 MKAMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGfDEIVINVHHFSNQILAFLEANqnfgIDIQISDET 80
Cdd:PRK14357   1 MRALVLAAGKGTRMK---SKIPKVLHKISGKPMINWVIDTAKKVA-QKVGVVLGHEAELVKKLLPEW----VKIFLQEEQ 72
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 495112875  81 dclLDTGGGLERAYYLLHHPEDMFTKEGETPyeLIFENLMKGMDEEEI 128
Cdd:PRK14357  73 ---LGTAHAVMCARDFIEPGDDLLILYGDVP--LISENTLKRLIEEHN 115
GDP-M1P_Guanylyltransferase cd02509
GDP-M1P_Guanylyltransferase catalyzes the formation of GDP-Mannose; GDP-mannose-1-phosphate ...
1-51 2.17e-03

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


Pssm-ID: 133003 [Multi-domain]  Cd Length: 274  Bit Score: 38.71  E-value: 2.17e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 495112875   1 MKAMIFAAGLGSRLKPL-TDTRPKALITV-GGKTMLEHIILKLK-AAGFDEIVI 51
Cdd:cd02509    1 IYPVILAGGSGTRLWPLsRESYPKQFLKLfGDKSLLQQTLDRLKgLVPPDRILV 54
QRI1 COG4284
UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];
7-73 2.60e-03

UDP-N-acetylglucosamine pyrophosphorylase [Carbohydrate transport and metabolism];


Pssm-ID: 443425  Cd Length: 402  Bit Score: 38.71  E-value: 2.60e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 495112875   7 AAGLGSRLKPltdTRPKALITVG---GKTMLEHIILKLKAAG------FDEIVINVHHFSNQILAFLEANQNFGID 73
Cdd:COG4284  102 AGGQGTRLGF---DGPKGLLPVRpvkGKSLFDLIAEQVLAARrrygvpLPLYIMTSFRTHEDTLAFLEEHDYFGLD 174
IspD pfam01128
2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes ...
3-54 3.12e-03

2-C-methyl-D-erythritol 4-phosphate cytidylyltransferase; Members of this family are enzymes which catalyze the formation of 4-diphosphocytidyl-2-C-methyl-D-erythritol from cytidine triphosphate and 2-C-methyl-D-erythritol 4-phosphate (MEP).


Pssm-ID: 460075  Cd Length: 219  Bit Score: 38.20  E-value: 3.12e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 495112875    3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAG-FDEIVINVH 54
Cdd:pfam01128   1 AVIPAAGSGKRMG---AGVPKQFLQLLGQPLLEHTVDAFLASPvVDRIVVAVS 50
glmU PRK14356
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
3-70 4.07e-03

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


Pssm-ID: 237686 [Multi-domain]  Cd Length: 456  Bit Score: 38.17  E-value: 4.07e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 495112875   3 AMIFAAGLGSRLKpltDTRPKALITVGGKTMLEHIILKLKAAGFDEIVINVHHFSNQI-LAFLEANQNF 70
Cdd:PRK14356   8 ALILAAGKGTRMH---SDKPKVLQTLLGEPMLRFVYRALRPLFGDNVWTVVGHRADMVrAAFPDEDARF 73
 
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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