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Conserved domains on  [gi|556474017|ref|WP_023325622|]
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MULTISPECIES: glycosyltransferase family 2 protein [Enterobacteriaceae]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10135474)

glycosyltransferase family 2 protein catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds

CATH:  3.90.550.10
CAZY:  GT2
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3000077

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-237 2.52e-99

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: 289.15  E-value: 2.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   4 IVVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFICQRQHVIDYSLDRYLKEWAPNSEVICIDGI 83
Cdd:cd04183    1 IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLKLLAPNATVVELDGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  84 TEGAACTVMCAEELINNDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDPKWSYAEMNENNHVTRVVEKEVV 163
Cdd:cd04183   81 TLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRWSYVKLDENGRVIETAEKEPI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556474017 164 SDEATVGIYNYKKGADFCRSVKRMIALDQRSNGEFYVAPAYTLMyENEGAKIGIYNIGEeaNGMYGLGIPADLE 237
Cdd:cd04183  161 SDLATAGLYYFKSGSLFVEAAKKMIRKDDSVNGEFYISPLYNEL-ILDGKKVGIYLIDK--DDYHSFGTPEDLE 231
 
Name Accession Description Interval E-value
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-237 2.52e-99

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: 289.15  E-value: 2.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   4 IVVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFICQRQHVIDYSLDRYLKEWAPNSEVICIDGI 83
Cdd:cd04183    1 IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLKLLAPNATVVELDGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  84 TEGAACTVMCAEELINNDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDPKWSYAEMNENNHVTRVVEKEVV 163
Cdd:cd04183   81 TLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRWSYVKLDENGRVIETAEKEPI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556474017 164 SDEATVGIYNYKKGADFCRSVKRMIALDQRSNGEFYVAPAYTLMyENEGAKIGIYNIGEeaNGMYGLGIPADLE 237
Cdd:cd04183  161 SDLATAGLYYFKSGSLFVEAAKKMIRKDDSVNGEFYISPLYNEL-ILDGKKVGIYLIDK--DDYHSFGTPEDLE 231
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
5-172 1.14e-15

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: 73.65  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   5 VVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFIC--QRQHVIDYSLDRYLKEWapnsEVICID- 81
Cdd:COG1208    3 VILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVgyLAEQIEEYFGDGSRFGV----RITYVDe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  82 GITEGAACTVMCAEELINnDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDPK-WSYAEMNENNHVTRVVEK 160
Cdd:COG1208   79 GEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSrYGVVELDGDGRVTRFVEK 157
                        170
                 ....*....|....
gi 556474017 161 --EVVSDEATVGIY 172
Cdd:COG1208  158 peEPPSNLINAGIY 171
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
10-177 7.26e-09

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 54.57  E-value: 7.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   10 GRGSRFAKEGYVDPKPLI-KLKDKRMIQVVINNLTPSIPHRFIFICQRQHVIdySLDRYLKEWAPNSEVICIdgITE--- 85
Cdd:pfam00483   8 GSGTRLWPLTRTLAKPLVpVGGKYPLIDYPLSRLANAGIREIIVILTQEHRF--MLNELLGDGSKFGVQITY--ALQpeg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   86 -GAACTVMCAEELINND-EPLMIANSDQWIDidiNDYLNYMKH-----EDLDGLIMTMKADDP-KWSYAEMNENNHVTRV 157
Cdd:pfam00483  84 kGTAPAVALAADFLGDEkSDVLVLGGDHIYR---MDLEQAVKFhiekaADATVTFGIVPVEPPtGYGVVEFDDNGRVIRF 160
                         170       180
                  ....*....|....*....|...
gi 556474017  158 VEK---EVVSDEATVGIYNYKKG 177
Cdd:pfam00483 161 VEKpklPKASNYASMGIYIFNSG 183
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
86-218 9.66e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 36.73  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  86 GAACTVMCAEELINN----------DEPLMIANSdqwididINDYLNYMKHEDLDGLIMTMKADDPKwSYAEM--NENNH 153
Cdd:PRK14354  77 GTGHAVMQAEEFLADkegttlvicgDTPLITAET-------LKNLIDFHEEHKAAATILTAIAENPT-GYGRIirNENGE 148
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556474017 154 VTRVVE-KEVVSDEATV-----GIYnykkgadfCRSVKRMI-ALDQRSN----GEFYVAPAYTLMyENEGAKIGIY 218
Cdd:PRK14354 149 VEKIVEqKDATEEEKQIkeintGTY--------CFDNKALFeALKKISNdnaqGEYYLTDVIEIL-KNEGEKVGAY 215
 
Name Accession Description Interval E-value
GT2_BcE_like cd04183
GT2_BcbE_like is likely involved in the biosynthesis of the polysaccharide capsule; ...
4-237 2.52e-99

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: 289.15  E-value: 2.52e-99
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   4 IVVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFICQRQHVIDYSLDRYLKEWAPNSEVICIDGI 83
Cdd:cd04183    1 IIIPMAGLGSRFKKAGYTYPKPLIEVDGKPMIEWVIESLAKIFDSRFIFICRDEHNTKFHLDESLKLLAPNATVVELDGE 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  84 TEGAACTVMCAEELINNDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDPKWSYAEMNENNHVTRVVEKEVV 163
Cdd:cd04183   81 TLGAACTVLLAADLIDNDDPLLIFNCDQIVESDLLAFLAAFRERDLDGGVLTFFSSHPRWSYVKLDENGRVIETAEKEPI 160
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 556474017 164 SDEATVGIYNYKKGADFCRSVKRMIALDQRSNGEFYVAPAYTLMyENEGAKIGIYNIGEeaNGMYGLGIPADLE 237
Cdd:cd04183  161 SDLATAGLYYFKSGSLFVEAAKKMIRKDDSVNGEFYISPLYNEL-ILDGKKVGIYLIDK--DDYHSFGTPEDLE 231
NTP_transferase cd04181
NTP_transferases catalyze the transfer of nucleotides onto phosphosugars; ...
5-172 6.62e-20

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: 84.94  E-value: 6.62e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   5 VVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFICQRQH--VIDYSLDRYlkEWAPNSEvICIDG 82
Cdd:cd04181    2 VILAAGKGTRLRPLTDTRPKPLLPIAGKPILEYIIERLARAGIDEIILVVGYLGeqIEEYFGDGS--KFGVNIE-YVVQE 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  83 ITEGAACTVMCAEELInNDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDP-KWSYAEMNENNHVTRVVEK- 160
Cdd:cd04181   79 EPLGTAGAVRNAEDFL-GDDDFLVVNGDVLTDLDLSELLRFHREKGADATIAVKEVEDPsRYGVVELDDDGRVTRFVEKp 157
                        170
                 ....*....|...
gi 556474017 161 -EVVSDEATVGIY 172
Cdd:cd04181  158 tLPESNLANAGIY 170
GCD1 COG1208
NDP-sugar pyrophosphorylase, includes eIF-2Bgamma, eIF-2Bepsilon, and LPS biosynthesis protein ...
5-172 1.14e-15

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: 73.65  E-value: 1.14e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   5 VVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFIC--QRQHVIDYSLDRYLKEWapnsEVICID- 81
Cdd:COG1208    3 VILAGGLGTRLRPLTDTRPKPLLPVGGKPLLEHILERLAAAGITEIVINVgyLAEQIEEYFGDGSRFGV----RITYVDe 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  82 GITEGAACTVMCAEELINnDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDPK-WSYAEMNENNHVTRVVEK 160
Cdd:COG1208   79 GEPLGTGGALKRALPLLG-DEPFLVLNGDILTDLDLAALLAFHREKGADATLALVPVPDPSrYGVVELDGDGRVTRFVEK 157
                        170
                 ....*....|....
gi 556474017 161 --EVVSDEATVGIY 172
Cdd:COG1208  158 peEPPSNLINAGIY 171
NTP_transferase pfam00483
Nucleotidyl transferase; This family includes a wide range of enzymes which transfer ...
10-177 7.26e-09

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


Pssm-ID: 425709 [Multi-domain]  Cd Length: 243  Bit Score: 54.57  E-value: 7.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   10 GRGSRFAKEGYVDPKPLI-KLKDKRMIQVVINNLTPSIPHRFIFICQRQHVIdySLDRYLKEWAPNSEVICIdgITE--- 85
Cdd:pfam00483   8 GSGTRLWPLTRTLAKPLVpVGGKYPLIDYPLSRLANAGIREIIVILTQEHRF--MLNELLGDGSKFGVQITY--ALQpeg 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   86 -GAACTVMCAEELINND-EPLMIANSDQWIDidiNDYLNYMKH-----EDLDGLIMTMKADDP-KWSYAEMNENNHVTRV 157
Cdd:pfam00483  84 kGTAPAVALAADFLGDEkSDVLVLGGDHIYR---MDLEQAVKFhiekaADATVTFGIVPVEPPtGYGVVEFDDNGRVIRF 160
                         170       180
                  ....*....|....*....|...
gi 556474017  158 VEK---EVVSDEATVGIYNYKKG 177
Cdd:pfam00483 161 VEKpklPKASNYASMGIYIFNSG 183
G1P_TT_long cd04189
G1P_TT_long represents the long form of glucose-1-phosphate thymidylyltransferase; This family ...
5-172 3.51e-07

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: 49.49  E-value: 3.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   5 VVPMAGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLtpsiphRFIFICQRQHVIDYS---LDRYLKE---WAPNSEVI 78
Cdd:cd04189    4 LILAGGKGTRLRPLTYTRPKQLIPVAGKPIIQYAIEDL------REAGIEDIGIVVGPTgeeIKEALGDgsrFGVRITYI 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  79 cIDGITEGAACTVMCAEELINnDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDP-KWSYAEMnENNHVTRV 157
Cdd:cd04189   78 -LQEEPLGLAHAVLAARDFLG-DEPFVVYLGDNLIQEGISPLVRDFLEEDADASILLAEVEDPrRFGVAVV-DDGRIVRL 154
                        170
                 ....*....|....*..
gi 556474017 158 VEK--EVVSDEATVGIY 172
Cdd:cd04189  155 VEKpkEPPSNLALVGVY 171
M1P_guanylylT_B_like_N cd06425
N-terminal domain of the M1P-guanylyltransferase B-isoform like proteins; GDP-mannose ...
23-172 9.40e-05

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: 42.58  E-value: 9.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  23 PKPLIKLKDKRMIQVVINNLTPS-IPHRFIFICQRQHVidysLDRYLKEWA--PNSEVIC-IDGITEGAACTVMCAEELI 98
Cdd:cd06425   22 PKPLVEFCNKPMIEHQIEALAKAgVKEIILAVNYRPED----MVPFLKEYEkkLGIKITFsIETEPLGTAGPLALARDLL 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 556474017  99 N-NDEPLMIANSDQWIDIDINDYLNYMKHEDLDGLIMTMKADDP-KWSYAEMNENN-HVTRVVEK--EVVSDEATVGIY 172
Cdd:cd06425   98 GdDDEPFFVLNSDVICDFPLAELLDFHKKHGAEGTILVTKVEDPsKYGVVVHDENTgRIERFVEKpkVFVGNKINAGIY 176
PC_cytidylyltransferase cd02523
Phosphocholine cytidylyltransferases catalyze the synthesis of CDP-choline; This family ...
9-199 3.60e-04

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: 40.68  E-value: 3.60e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   9 AGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFIC-QRQHVIDYSLDRYLK-------EWApnsevici 80
Cdd:cd02523    6 AGRGSRLRPLTEDRPKCLLEINGKPLLERQIETLKEAGIDDIVIVTgYKKEQIEELLKKYPNikfvynpDYA-------- 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  81 dgiTEGAACTVMCAEELInnDEPLMIANSDQWIDIDIndyLNYMKHEDLDGLImtmkADDPKWSYAEM------NENNHV 154
Cdd:cd02523   78 ---ETNNIYSLYLARDFL--DEDFLLLEGDVVFDPSI---LERLLSSPADNAI----LVDKKTKEWEDeyvkdlDDAGVL 145
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 556474017 155 TRVVEKEVVSDEA---TVGIYNYKKgADFCRSVKRMIALDQRSNGEFY 199
Cdd:cd02523  146 LGIISKAKNLEEIqgeYVGISKFSP-EDADRLAEALEELIEAGRVNLY 192
COG1213 COG1213
Choline kinase [Lipid transport and metabolism];
9-192 4.84e-04

Choline kinase [Lipid transport and metabolism];


Pssm-ID: 440826 [Multi-domain]  Cd Length: 236  Bit Score: 40.22  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   9 AGRGSRFAKEGYVDPKPLIKLKDKRMIQVVINNLTPSIPHRFIFIC-QRQHVIdyslDRYLKEWAPNSEVICID--GITE 85
Cdd:COG1213    7 AGRGSRLGPLTDDIPKCLVEIGGKTLLERQLEALAAAGIKDIVVVTgYKAELI----EEALARPGPDVTFVYNPdyDETN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  86 GAAcTVMCAEELInnDEPLMIANSDQWIDIDINDYLNYMKHEDLdgliMTMkadDPKWS-------YAEMNENNHVTRVV 158
Cdd:COG1213   83 NIY-SLWLAREAL--DEDFLLLNGDVVFDPAILKRLLASDGDIV----LLV---DRKWEkpldeevKVRVDEDGRIVEIG 152
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 556474017 159 eKEVVSDEA---TVGIY--NYKKGADFCRSVKRMIALDQ 192
Cdd:COG1213  153 -KKLPPEEAdgeYIGIFkfSAEGAAALREALEALIDEGG 190
GT_2_like_f cd04182
GT_2_like_f is a subfamily of the glycosyltransferase family 2 (GT-2) with unknown function; ...
2-117 2.58e-03

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: 37.92  E-value: 2.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017   2 LNIVVPMAGRGSRFAKegyvdPKPLIKLKDKRMIQVVINNLTPSIPHRFIFICQ-RQHVIDYSLDRYLKEWAPNSEVici 80
Cdd:cd04182    1 IAAIILAAGRSSRMGG-----NKLLLPLDGKPLLRHALDAALAAGLSRVIVVLGaEADAVRAALAGLPVVVVINPDW--- 72
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 556474017  81 dgiTEGAACTVMCA-EELINNDEPLMIANSDQ-WIDIDI 117
Cdd:cd04182   73 ---EEGMSSSLAAGlEALPADADAVLILLADQpLVTAET 108
COG2266 COG2266
GTP:adenosylcobinamide-phosphate guanylyltransferase [Coenzyme transport and metabolism]; GTP: ...
8-45 9.24e-03

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


Pssm-ID: 441867 [Multi-domain]  Cd Length: 185  Bit Score: 36.02  E-value: 9.24e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 556474017   8 MAG-RGSRFakeGYVDpKPLIKLKDKRMIQVVINNLTPS 45
Cdd:COG2266    1 MAGgKGTRL---GGGE-KPLLEICGKPMIDRVIDALEES 35
glmU PRK14354
bifunctional UDP-N-acetylglucosamine diphosphorylase/glucosamine-1-phosphate ...
86-218 9.66e-03

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


Pssm-ID: 184643 [Multi-domain]  Cd Length: 458  Bit Score: 36.73  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 556474017  86 GAACTVMCAEELINN----------DEPLMIANSdqwididINDYLNYMKHEDLDGLIMTMKADDPKwSYAEM--NENNH 153
Cdd:PRK14354  77 GTGHAVMQAEEFLADkegttlvicgDTPLITAET-------LKNLIDFHEEHKAAATILTAIAENPT-GYGRIirNENGE 148
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 556474017 154 VTRVVE-KEVVSDEATV-----GIYnykkgadfCRSVKRMI-ALDQRSN----GEFYVAPAYTLMyENEGAKIGIY 218
Cdd:PRK14354 149 VEKIVEqKDATEEEKQIkeintGTY--------CFDNKALFeALKKISNdnaqGEYYLTDVIEIL-KNEGEKVGAY 215
 
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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