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Conserved domains on  [gi|488314916|ref|WP_002384301|]
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glycosyltransferase [Enterococcus faecalis]

Protein Classification

class I SAM-dependent methyltransferase; bifunctional glycosyltransferase/class I SAM-dependent methyltransferase( domain architecture ID 11216564)

class I SAM-dependent methyltransferase catalyzes the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor similar to histamine N-methyltransferase| bifunctional glycosyltransferase/class I SAM-dependent methyltransferase catalyzes the transfer of saccharide moieties from a donor to an acceptor to form glycosidic bonds and/or the methylation of one or more specific substrates using S-adenosyl-L-methionine (SAM or AdoMet) as the methyl donor

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 554-755 1.30e-118

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


:

Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 362.29  E-value: 1.30e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNVEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALS 633
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  634 IATGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTDEDKITENGRRFNAFYKSDWNPELILNHNYITHFVVVKRDL 713
Cdd:cd04184    81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFKPDWSPDLLLSQNYIGHLLVYRRSL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 488314916  714 LEKVGGLNSAYNGAQDYDFVLRATEQAMKIKHIPGMMYHWRA 755
Cdd:cd04184   161 VRQVGGFREGFEGAQDYDLVLRVSEHTDRIAHIPRVLYHWRA 202
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 18-127 2.50e-16

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


:

Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 76.21  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   18 IVAQIKENSDVLEFGPGNGRMTSYLMEeKKCQVSIVELDKELYD----HVSQFSTDAFYGNIDENDwveyFAGKTFDYIV 93
Cdd:COG2227    18 LARLLPAGGRVLDVGCGTGRLALALAR-RGADVTGVDISPEALEiareRAAELNVDFVQGDLEDLP----LEDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488314916   94 FADVLEHLMNPQSALAKVKPFLKPGGQILITFPN 127
Cdd:COG2227    93 CSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
810-1010 1.28e-05

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 47.29  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  810 PMVSLIITndTENMSSYLRQLLE---KTAYTNYEILL------PARFENQINIQNDRLRYVSTETRHGM-------IQAA 873
Cdd:COG1216     3 PKVSVVIP--TYNRPELLRRCLEsllAQTYPPFEVIVvdngstDGTAELLAALAFPRVRVIRNPENLGFaaarnlgLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  874 KGEYVALLNAGLVPTKnDWLKELMNIGqqetsglvtgrvvdaryrvetvgvsvdtdkgrllypekgtpgkslgyyyrial 953
Cdd:COG1216    81 GGDYLLFLDDDTVVEP-DWLERLLAAA----------------------------------------------------- 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488314916  954 prniqaatedCLLFNKQLYLNLEGINESLGKEWMGVDLSLQFASAGKRNVYVSYAIL 1010
Cdd:COG1216   107 ----------CLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVV 153
 
Name Accession Description Interval E-value
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 554-755 1.30e-118

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 362.29  E-value: 1.30e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNVEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALS 633
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  634 IATGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTDEDKITENGRRFNAFYKSDWNPELILNHNYITHFVVVKRDL 713
Cdd:cd04184    81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFKPDWSPDLLLSQNYIGHLLVYRRSL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 488314916  714 LEKVGGLNSAYNGAQDYDFVLRATEQAMKIKHIPGMMYHWRA 755
Cdd:cd04184   161 VRQVGGFREGFEGAQDYDLVLRVSEHTDRIAHIPRVLYHWRA 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 553-762 3.68e-37

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 139.07  E-value: 3.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  553 QPKISVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASP--SEHIkpmLEKYKELDQRIKVIYREENGHISEATNS 630
Cdd:COG0463     1 MPLVSVVIPTYN-EEEYLEEALESLLAQTYPDFEIIVVDDGSTdgTAEI---LRELAAKDPRIRVIRLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  631 ALSIATGDFIGFMDNDDELAPQALYEVVKALNTDPtIDFLYTDEdKITENGRRFNAFYKSDWNPELILN--HNYITHFVV 708
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSR-LIREGESDLRRLGSRLFNLVRLLTnlPDSTSGFRL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488314916  709 VKRDLLEKVgGLNSAYngAQDYDFvLRATEQAMKIKHIPgmmYHWRAIESSTAL 762
Cdd:COG0463   155 FRREVLEEL-GFDEGF--LEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNL 201
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 557-716 1.28e-31

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 121.35  E-value: 1.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   557 SVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPsEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALSIAT 636
Cdd:pfam00535    1 SVIIPTYN-EEKYLLETLESLLNQTYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   637 GDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLY--------TDEDKITENGRRFNAFYKSDWNPELILNHNYITHFVV 708
Cdd:pfam00535   79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGsryvifgeTGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFAL 158


                   ....*...
gi 488314916   709 VKRDLLEK 716
Cdd:pfam00535  159 YRREALEE 166
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 18-127 2.50e-16

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 76.21  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   18 IVAQIKENSDVLEFGPGNGRMTSYLMEeKKCQVSIVELDKELYD----HVSQFSTDAFYGNIDENDwveyFAGKTFDYIV 93
Cdd:COG2227    18 LARLLPAGGRVLDVGCGTGRLALALAR-RGADVTGVDISPEALEiareRAAELNVDFVQGDLEDLP----LEDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488314916   94 FADVLEHLMNPQSALAKVKPFLKPGGQILITFPN 127
Cdd:COG2227    93 CSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 554-656 5.53e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 80.48  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNVEeKWLAACVSSLQNQYYENWELCLADDASpSEHIKPMLEKYKELDQRIKVIYrEENGHISEATNSALS 633
Cdd:PRK10073    6 PKLSIIIPLYNAG-KDFRAFMESLIAQTWTALEIIIVNDGS-TDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLA 82

                          90       100
                  ....*....|....*....|...
gi 488314916  634 IATGDFIGFMDNDDELAPQaLYE 656
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPT-MYE 104
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 22-174 8.07e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 64.37  E-value: 8.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    22 IKENSDVLEFGPGNGRMTSYLmeeKKCQVSIVELDKELYDHVSQFSTDAFYGNIDENDWVEyfaGKTFDYIVFADVLEHL 101
Cdd:pfam13489   20 LPSPGRVLDFGCGTGIFLRLL---RAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVP---AGKFDVIVAREVLEHV 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488314916   102 MNPQSALAKVKPFLKPGGQILITFPNLAhnsvliDLFNNRLTWNETGLLDATHKSFYLQEGFEKVFAEVGLYI 174
Cdd:pfam13489   94 PDPPALLRQIAALLKPGGLLLLSTPLAS------DEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFEV 160
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 27-125 2.05e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 58.98  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   27 DVLEFGPGNGRMTSYLMEEKKCQVSIVELDKELYDHVSQFSTDAFYGNID--ENDWVE--YFAGKTFDYIVFADVLEHLM 102
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEvlKGDAEElpPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 488314916  103 -NPQSALAKVKPFLKPGGQILITF 125
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
810-1010 1.28e-05

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 47.29  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  810 PMVSLIITndTENMSSYLRQLLE---KTAYTNYEILL------PARFENQINIQNDRLRYVSTETRHGM-------IQAA 873
Cdd:COG1216     3 PKVSVVIP--TYNRPELLRRCLEsllAQTYPPFEVIVvdngstDGTAELLAALAFPRVRVIRNPENLGFaaarnlgLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  874 KGEYVALLNAGLVPTKnDWLKELMNIGqqetsglvtgrvvdaryrvetvgvsvdtdkgrllypekgtpgkslgyyyrial 953
Cdd:COG1216    81 GGDYLLFLDDDTVVEP-DWLERLLAAA----------------------------------------------------- 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488314916  954 prniqaatedCLLFNKQLYLNLEGINESLGKEWMGVDLSLQFASAGKRNVYVSYAIL 1010
Cdd:COG1216   107 ----------CLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVV 153
PRK08317 PRK08317
hypothetical protein; Provisional
 76-143 6.44e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.62  E-value: 6.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488314916   76 DENDWVEY---------FAGKTFDYIVFADVLEHLMNPQSALAKVKPFLKPGGQILITFPNLAhnSVLIDLFNNRLT 143
Cdd:PRK08317   66 GLGPNVEFvrgdadglpFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWD--TLVWHSGDRALM 140
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-59 3.33e-03

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 40.68  E-value: 3.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 488314916    10 DESTsVGKIV--AQIKENSDVLEFGPGNGRMTSYLMEEKKcQVSIVELDKEL 59
Cdd:TIGR00755   14 DENV-IRKIVeaANIQEGDRVLEIGPGLGALTEPLLKRAK-KVTAIEIDPRL 63
 
Name Accession Description Interval E-value
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 554-755 1.30e-118

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which 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. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 362.29  E-value: 1.30e-118
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNVEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALS 633
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKRVLKKYAAQDPRIKVVFREENGGISAATNSALE 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  634 IATGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTDEDKITENGRRFNAFYKSDWNPELILNHNYITHFVVVKRDL 713
Cdd:cd04184    81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEPFFKPDWSPDLLLSQNYIGHLLVYRRSL 160

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 488314916  714 LEKVGGLNSAYNGAQDYDFVLRATEQAMKIKHIPGMMYHWRA 755
Cdd:cd04184   161 VRQVGGFREGFEGAQDYDLVLRVSEHTDRIAHIPRVLYHWRA 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 553-762 3.68e-37

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 139.07  E-value: 3.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  553 QPKISVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASP--SEHIkpmLEKYKELDQRIKVIYREENGHISEATNS 630
Cdd:COG0463     1 MPLVSVVIPTYN-EEEYLEEALESLLAQTYPDFEIIVVDDGSTdgTAEI---LRELAAKDPRIRVIRLERNRGKGAARNA 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  631 ALSIATGDFIGFMDNDDELAPQALYEVVKALNTDPtIDFLYTDEdKITENGRRFNAFYKSDWNPELILN--HNYITHFVV 708
Cdd:COG0463    77 GLAAARGDYIAFLDADDQLDPEKLEELVAALEEGP-ADLVYGSR-LIREGESDLRRLGSRLFNLVRLLTnlPDSTSGFRL 154

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 488314916  709 VKRDLLEKVgGLNSAYngAQDYDFvLRATEQAMKIKHIPgmmYHWRAIESSTAL 762
Cdd:COG0463   155 FRREVLEEL-GFDEGF--LEDTEL-LRALRHGFRIAEVP---VRYRAGESKLNL 201
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 554-762 9.46e-32

Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1,6-N-acetylglucosamine synthase [Cell motility];


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 126.39  E-value: 9.46e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNvEEKWLAACVSSLQNQYY--ENWELCLADDASpSEHIKPMLEKYKELDQRIKVIYREENGHISEATNSA 631
Cdd:COG1215    29 PRVSVIIPAYN-EEAVIEETLRSLLAQDYpkEKLEVIVVDDGS-TDETAEIARELAAEYPRVRVIERPENGGKAAALNAG 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  632 LSIATGDFIGFMDNDDELAPQALYEVVKALNtDPTIDFlytdedkitengrrfnafyksdwnpelilnhnyITHFVVVKR 711
Cdd:COG1215   107 LKAARGDIVVFLDADTVLDPDWLRRLVAAFA-DPGVGA---------------------------------SGANLAFRR 152

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 488314916  712 DLLEKVGGLnSAYNGAQDYDFVLRATEQAMKIKHIPGMMYHWRAIESSTAL 762
Cdd:COG1215   153 EALEEVGGF-DEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRAL 202
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 557-716 1.28e-31

Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, UDP-N-acetyl- galactosamine, GDP-mannose or CDP-abequose, to a range of substrates including cellulose, dolichol phosphate and teichoic acids.


Pssm-ID: 425738 [Multi-domain]  Cd Length: 166  Bit Score: 121.35  E-value: 1.28e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   557 SVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPsEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALSIAT 636
Cdd:pfam00535    1 SVIIPTYN-EEKYLLETLESLLNQTYPNFEIIVVDDGST-DGTVEIAEEYAKKDPRVRVIRLPENRGKAGARNAGLRAAT 78

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   637 GDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLY--------TDEDKITENGRRFNAFYKSDWNPELILNHNYITHFVV 708
Cdd:pfam00535   79 GDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGsryvifgeTGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFAL 158


                   ....*...
gi 488314916   709 VKRDLLEK 716
Cdd:pfam00535  159 YRREALEE 166
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 557-754 9.40e-29

WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella dysenteriae WfeV are glycosyltransferase 2 family enzymes involved in O-antigen biosynthesis. GT-2 enzymes have 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: 133055 [Multi-domain]  Cd Length: 202  Bit Score: 114.56  E-value: 9.40e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  557 SVAVPVYNVEEkWLAACVSSLQNQYYENWELCLADDASP---SEHIKpmleKYKelDQRIKVIYREENGhISEATNSALS 633
Cdd:cd06433     1 SIITPTYNQAE-TLEETIDSVLSQTYPNIEYIVIDGGSTdgtVDIIK----KYE--DKITYWISEPDKG-IYDAMNKGIA 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  634 IATGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTDEDKITENGRRFNAFYKSDWNPELILNHNYITH---FvvVK 710
Cdd:cd06433    73 LATGDIIGFLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRRPPPFLDKFLLYGMPICHqatF--FR 150

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488314916  711 RDLLEKVGGLNSAYNGAQDYDFVLRATEQAMKIKHIPGMMYHWR 754
Cdd:cd06433   151 RSLFEKYGGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFR 194
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 558-746 1.29e-24

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.


Pssm-ID: 132997 [Multi-domain]  Cd Length: 156  Bit Score: 101.04  E-value: 1.29e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASpSEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALSIATG 637
Cdd:cd00761     1 VIIPAYN-EEPYLERCLESLLAQTYPNFEVIVVDDGS-TDGTLEILEEYAKKDPRVIRVINEENQGLAAARNAGLKAARG 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  638 DFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTdedkitengrrfnafyksdwnpelilnhnyiTHFVVVKRDLLEKV 717
Cdd:cd00761    79 EYILFLDADDLLLPDWLERLVAELLADPEADAVGG-------------------------------PGNLLFRRELLEEI 127

                         170       180
                  ....*....|....*....|....*....
gi 488314916  718 GGLNSAYNGAQDYDFVLRATEQAMKIKHI 746
Cdd:cd00761   128 GGFDEALLSGEEDDDFLLRLLRGGKVAFR 156
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
553-772 1.51e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 96.60  E-value: 1.51e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  553 QPKISVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKpMLEKYKelDQRIKVIYREENGHISEATNSAL 632
Cdd:COG1216     2 RPKVSVVIPTYN-RPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAE-LLAALA--FPRVRVIRNPENLGFAAARNLGL 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  633 SIATGDFIGFMDNDDELAPQALYEVVKAlntdptidflytdedkitengrrfnafyksdwnpelilnhnyitHFVVVKRD 712
Cdd:COG1216    78 RAAGGDYLLFLDDDTVVEPDWLERLLAA--------------------------------------------ACLLIRRE 113

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488314916  713 LLEKVGGLNSAY-NGAQDYDFVLRATEQAMKIKHIPG-MMYHWRaiesSTALNPESKGYAYV 772
Cdd:COG1216   114 VFEEVGGFDERFfLYGEDVDLCLRLRKAGYRIVYVPDaVVYHLG----GASSGPLLRAYYLG 171
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 558-667 3.51e-17

CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins. Cellulose synthase catalyzes the polymerization reaction of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues in plants, most algae, some bacteria and fungi, and even some animals. In bacteria, algae and lower eukaryotes, there is a second unrelated type of cellulose synthase (Type II), which produces acylated cellulose, a derivative of cellulose. Chitin synthase catalyzes the incorporation of GlcNAc from substrate UDP-GlcNAc into chitin, which is a linear homopolymer of beta-(1,4)-linked GlcNAc residues and Glucan Biosynthesis protein catalyzes the elongation of beta-1,2 polyglucose chains of Glucan.


Pssm-ID: 133045 [Multi-domain]  Cd Length: 180  Bit Score: 80.35  E-value: 3.51e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKYKELDQRIKVIYREENGHISEATNSALSIATG 637
Cdd:cd06423     1 IIVPAYN-EEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAKG 79

                          90       100       110
                  ....*....|....*....|....*....|
gi 488314916  638 DFIGFMDNDDELAPQALYEVVKALNTDPTI 667
Cdd:cd06423    80 DIVVVLDADTILEPDALKRLVVPFFADPKV 109
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 18-127 2.50e-16

2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and metabolism]; 2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase is part of the Pathway/BioSystem: Ubiquinone biosynthesis


Pssm-ID: 441829 [Multi-domain]  Cd Length: 126  Bit Score: 76.21  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   18 IVAQIKENSDVLEFGPGNGRMTSYLMEeKKCQVSIVELDKELYD----HVSQFSTDAFYGNIDENDwveyFAGKTFDYIV 93
Cdd:COG2227    18 LARLLPAGGRVLDVGCGTGRLALALAR-RGADVTGVDISPEALEiareRAAELNVDFVQGDLEDLP----LEDGSFDLVI 92

                          90       100       110
                  ....*....|....*....|....*....|....
gi 488314916   94 FADVLEHLMNPQSALAKVKPFLKPGGQILITFPN 127
Cdd:COG2227    93 CSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 554-656 5.53e-16

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 80.48  E-value: 5.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNVEeKWLAACVSSLQNQYYENWELCLADDASpSEHIKPMLEKYKELDQRIKVIYrEENGHISEATNSALS 633
Cdd:PRK10073    6 PKLSIIIPLYNAG-KDFRAFMESLIAQTWTALEIIIVNDGS-TDNSVEIAKHYAENYPHVRLLH-QANAGVSVARNTGLA 82

                          90       100
                  ....*....|....*....|...
gi 488314916  634 IATGDFIGFMDNDDELAPQaLYE 656
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPT-MYE 104
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 558-752 3.44e-13

Subfamily of Glycosyltransferase Family GT2 of 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: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 68.35  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNVEEkWLAACVSSLQNQYYENWELCLADDASPsehiKPMLEKYKELDQRIKVIYREENGHISEATNSALSIATG 637
Cdd:cd04186     1 IIIVNYNSLE-YLKACLDSLLAQTYPDFEVIVVDNAST----DGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKG 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  638 DFIGFMDNDDELAPQALYEVVKALNTDPTIDFLytdEDKITengrrfnafyksdwnpelilnhnyiTHFVVVKRDLLEKV 717
Cdd:cd04186    76 DYVLLLNPDTVVEPGALLELLDAAEQDPDVGIV---GPKVS-------------------------GAFLLVRREVFEEV 127

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 488314916  718 GGLNSAY-NGAQDYDFVLRATEQAMKIKHIPGM-MYH 752
Cdd:cd04186   128 GGFDEDFfLYYEDVDLCLRARLAGYRVLYVPQAvIYH 164
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 557-717 1.83e-12

Subfamily of Glycosyltransferase Family GT2 of 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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 67.66  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  557 SVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKpMLEKYKELDQRIKVIYREEnGHISEATN--SALSI 634
Cdd:cd04196     1 AVLMATYN-GEKYLREQLDSILAQTYKNDELIISDDGSTDGTVE-IIKEYIDKDPFIIILIRNG-KNLGVARNfeSLLQA 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  635 ATGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTDEDKITENGRR------FNAFYKSDWNPELILNHNYITHF-V 707
Cdd:cd04196    78 ADGDYVFFCDQDDIWLPDKLERLLKAFLKDDKPLLVYSDLELVDENGNPigesffEYQKIKPGTSFNNLLFQNVVTGCtM 157

                         170
                  ....*....|
gi 488314916  708 VVKRDLLEKV 717
Cdd:cd04196   158 AFNRELLELA 167
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
553-746 6.86e-12

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 67.32  E-value: 6.86e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  553 QPKISVAVPVYNVEEKWLAAcVSSLQNQYYENWELCLADDASPS-EHIKPMLEKYKelDQRIKVIYREENGHISEATNSA 631
Cdd:PRK10018    4 NPLISIYMPTWNRQQLAIRA-IKSVLRQDYSNWEMIIVDDCSTSwEQLQQYVTALN--DPRITYIHNDINSGACAVRNQA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  632 LSIATGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTD----EDKITENGRRFNAFYKSDWNPELILNHNYITHFV 707
Cdd:PRK10018   81 IMLAQGEYITGIDDDDEWTPNRLSVFLAHKQQLVTHAFLYANdyvcQGEVYSQPASLPLYPKSPYSRRLFYKRNIIGNQV 160

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 488314916  708 VV-----KRDLLEkvgglnSAYNGAQDYDFVLR---------ATEQAMKIKHI 746
Cdd:PRK10018  161 FTwawrfKECLFD------TELKAAQDYDIFLRmvveygepwKVEEATQILHI 207
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 22-174 8.07e-12

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 64.37  E-value: 8.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    22 IKENSDVLEFGPGNGRMTSYLmeeKKCQVSIVELDKELYDHVSQFSTDAFYGNIDENDWVEyfaGKTFDYIVFADVLEHL 101
Cdd:pfam13489   20 LPSPGRVLDFGCGTGIFLRLL---RAQGFSVTGVDPSPIAIERALLNVRFDQFDEQEAAVP---AGKFDVIVAREVLEHV 93

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 488314916   102 MNPQSALAKVKPFLKPGGQILITFPNLAhnsvliDLFNNRLTWNETGLLDATHKSFYLQEGFEKVFAEVGLYI 174
Cdd:pfam13489   94 PDPPALLRQIAALLKPGGLLLLSTPLAS------DEADRLLLEWPYLRPRNGHISLFSARSLKRLLEEAGFEV 160
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 555-747 8.91e-12

ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA catalyzes the formation of a beta-1,3 linkage of the second sugar (glucose) of the succinoglycan with the galactose on the lipid carrie. Succinoglycan is an acidic exopolysaccharide that is important for invasion of the nodules. Succinoglycan is a high-molecular-weight polymer composed of repeating octasaccharide units. These units are synthesized on membrane-bound isoprenoid lipid carriers, beginning with galactose followed by seven glucose molecules, and modified by the addition of acetate, succinate, and pyruvate. ExoA is a membrane protein with a transmembrance domain at c-terminus.


Pssm-ID: 133016 [Multi-domain]  Cd Length: 249  Bit Score: 66.49  E-value: 8.91e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  555 KISVAVPVYNvEEKWLAACVSSLQNQYY--ENWELCLADDASpSEHIKPMLEKYKELDQRIKVIYREEnGHISEATNSAL 632
Cdd:cd02525     1 FVSIIIPVRN-EEKYIEELLESLLNQSYpkDLIEIIVVDGGS-TDGTREIVQEYAAKDPRIRLIDNPK-RIQSAGLNIGI 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  633 SIATGDFIGFMDNDDELAPQALYEVVKAL-NTDPTIDFLYTDEDKITENGRRFNAFYKSDW------NPELILNHNYI-- 703
Cdd:cd02525    78 RNSRGDIIIRVDAHAVYPKDYILELVEALkRTGADNVGGPMETIGESKFQKAIAVAQSSPLgsggsaYRGGAVKIGYVdt 157

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 488314916  704 THFVVVKRDLLEKVGGLNSAYNGAQDYDFVLRATEQAMKIKHIP 747
Cdd:cd02525   158 VHHGAYRREVFEKVGGFDESLVRNEDAELNYRLRKAGYKIWLSP 201
Cfa COG2230
Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport ...
 20-126 2.29e-11

Cyclopropane fatty-acyl-phospholipid synthase and related methyltransferases [Lipid transport and metabolism];


Pssm-ID: 441831 [Multi-domain]  Cd Length: 158  Bit Score: 63.02  E-value: 2.29e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   20 AQIKENSDVLEFGPGNGRMTSYLMEEKKCQVSIVELDKELYDHVSQFSTDAFYGN---IDENDWVEYFAGKTFDYIVFAD 96
Cdd:COG2230    47 LGLKPGMRVLDIGCGWGGLALYLARRYGVRVTGVTLSPEQLEYARERAAEAGLADrveVRLADYRDLPADGQFDAIVSIG 126

                          90       100       110
                  ....*....|....*....|....*....|..
gi 488314916   97 VLEHL--MNPQSALAKVKPFLKPGGQILITFP 126
Cdd:COG2230   127 MFEHVgpENYPAYFAKVARLLKPGGRLLLHTP 158
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 20-138 1.58e-10

Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG is part of the Pathway/BioSystem: Biotin biosynthesis


Pssm-ID: 441828 [Multi-domain]  Cd Length: 143  Bit Score: 60.39  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   20 AQIKENSDVLEFGPGNGRMTSYLMEeKKCQVSIVELDKELYDHVSQFSTDAFYGnidendwVEY---------FAGKTFD 90
Cdd:COG2226    18 LGLRPGARVLDLGCGTGRLALALAE-RGARVTGVDISPEMLELARERAAEAGLN-------VEFvvgdaedlpFPDGSFD 89

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 488314916   91 YIVFADVLEHLMNPQSALAKVKPFLKPGGQILITFPNLAHNSVLIDLF 138
Cdd:COG2226    90 LVISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 27-125 2.05e-10

S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; AdoMet-MTases are enzymes that use S-adenosyl-L-methionine (SAM or AdoMet) as a substrate for methyltransfer, creating the product S-adenosyl-L-homocysteine (AdoHcy). There are at least five structurally distinct families of AdoMet-MTases, class I being the largest and most diverse. Within this class enzymes can be classified by different substrate specificities (small molecules, lipids, nucleic acids, etc.) and different target atoms for methylation (nitrogen, oxygen, carbon, sulfur, etc.).


Pssm-ID: 100107 [Multi-domain]  Cd Length: 107  Bit Score: 58.98  E-value: 2.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   27 DVLEFGPGNGRMTSYLMEEKKCQVSIVELDKELYDHVSQFSTDAFYGNID--ENDWVE--YFAGKTFDYIVFADVLEHLM 102
Cdd:cd02440     1 RVLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAALLADNVEvlKGDAEElpPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 488314916  103 -NPQSALAKVKPFLKPGGQILITF 125
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
SmtA COG0500
SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, ...
 18-129 8.96e-10

SAM-dependent methyltransferase [Secondary metabolites biosynthesis, transport and catabolism, General function prediction only];


Pssm-ID: 440266 [Multi-domain]  Cd Length: 199  Bit Score: 59.54  E-value: 8.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   18 IVAQIKENSDVLEFGPGNGRMTSYLMEEKKCQVSIVELDKELYDHVSQFSTDAFYGNI-----DENDWVEYFAGKtFDYI 92
Cdd:COG0500    20 LLERLPKGGRVLDLGCGTGRNLLALAARFGGRVIGIDLSPEAIALARARAAKAGLGNVeflvaDLAELDPLPAES-FDLV 98

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 488314916   93 VFADVLEHLmNP---QSALAKVKPFLKPGGQILITFPNLA 129
Cdd:COG0500    99 VAFGVLHHL-PPeerEALLRELARALKPGGVLLLSASDAA 137
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 29-123 4.31e-09

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.59  E-value: 4.31e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    29 LEFGPGNGRMTSYLMEeKKCQVSIVELDKELYDHVSQFSTDAFYGNIDENdwVEY--FAGKTFDYIVFADVLEHLMNPQS 106
Cdd:pfam08241    1 LDVGCGTGLLTELLAR-LGARVTGVDISPEMLELAREKAPREGLTFVVGD--AEDlpFPDNSFDLVLSSEVLHHVEDPER 77

                           90
                   ....*....|....*..
gi 488314916   107 ALAKVKPFLKPGGQILI 123
Cdd:pfam08241   78 ALREIARVLKPGGILII 94
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 558-661 4.82e-08

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 54.12  E-value: 4.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSSLQN--QYYENWELCLADDASP--SEHIkpmLEKYKELDQRIKVIYREEN-GHISeATNSAL 632
Cdd:cd04179     1 VVIPAYN-EEENIPELVERLLAvlEEGYDYEIIVVDDGSTdgTAEI---ARELAARVPRVRVIRLSRNfGKGA-AVRAGF 75

                          90       100
                  ....*....|....*....|....*....
gi 488314916  633 SIATGDFIGFMDNDDELAPQALYEVVKAL 661
Cdd:cd04179    76 KAARGDIVVTMDADLQHPPEDIPKLLEKL 104
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 18-130 5.91e-08

Methionine biosynthesis protein MetW; This family consists of several bacterial and one archaeal methionine biosynthesis MetW proteins. Biosynthesis of methionine from homoserine in Pseudomonas putida takes place in three steps. The first step is the acylation of homoserine to yield an acyl-L-homoserine. This reaction is catalyzed by the products of the metXW genes and is equivalent to the first step in enterobacteria, gram-positive bacteria and fungi, except that in these microorganizms the reaction is catalyzed by a single polypeptide (the product of the metA gene in Escherichia coli and the met5 gene product in Neurospora crassa). In Pseudomonas putida, as in gram-positive bacteria and certain fungi, the second and third steps are a direct sulfhydrylation that converts the O-acyl-L-homoserine into homocysteine and further methylation to yield methionine. The latter reaction can be mediated by either of the two methionine synthetases present in the cells.


Pssm-ID: 399779  Cd Length: 193  Bit Score: 54.00  E-value: 5.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    18 IVAQIKENSDVLEFGPGNGRMTSYLMEEKKCQVSIVELDKELYDHVSQFSTDAFYGNIDENdwVEYFAGKTFDYIVFADV 97
Cdd:pfam07021    7 ILEWIPPGSRVLDLGCGDGTLLYLLKEEKGVDGYGIELDAAGVAECVAKGLYVIQGDLDEG--LEHFPDKSFDYVILSQT 84

                           90       100       110
                   ....*....|....*....|....*....|...
gi 488314916    98 LEHLMNPQSALakvKPFLKPGGQILITFPNLAH 130
Cdd:pfam07021   85 LQATRNPREVL---DEMLRIGRRCIVSFPNFGH 114
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 28-119 3.32e-07

Methyltransferase domain; This family appears to be a methyltransferase domain.


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 49.10  E-value: 3.32e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    28 VLEFGPGNGRMTSYLMEEKKCQVSIVELDKELYDHVSQ------FSTDAFYGNIDENDwveyFAGKTFDYIVFADVLEHL 101
Cdd:pfam13649    1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERAREraaeagLNVEFVQGDAEDLP----FPDGSFDLVVSSGVLHHL 76

                           90       100
                   ....*....|....*....|
gi 488314916   102 MNPQ--SALAKVKPFLKPGG 119
Cdd:pfam13649   77 PDPDleAALREIARVLKPGG 96
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 552-667 3.51e-07

CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of cellulose synthase (CESA) superfamily. CESA superfamily includes a wide variety of glycosyltransferase family 2 enzymes that share the common characteristic of catalyzing the elongation of polysaccharide chains. The members of the superfamily include cellulose synthase catalytic subunit, chitin synthase, glucan biosynthesis protein and other families of CESA-like proteins.


Pssm-ID: 133061 [Multi-domain]  Cd Length: 251  Bit Score: 52.58  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  552 FQPKISVAVPVYNvEEKWLAACVSSLQNQYY--ENWELCLADDASP--SEHIkpmLEKYkeLDQRIKVIYREENGHISEA 627
Cdd:cd06439    27 YLPTVTIIIPAYN-EEAVIEAKLENLLALDYprDRLEIIVVSDGSTdgTAEI---AREY--ADKGVKLLRFPERRGKAAA 100

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 488314916  628 TNSALSIATGDFIGFMDNDDELAPQALYEVVKALNtDPTI 667
Cdd:cd06439   101 LNRALALATGEIVVFTDANALLDPDALRLLVRHFA-DPSV 139
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 558-646 4.96e-07

N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin polymerase is a two domain, bi-functional protein. The N-terminal domain functions as a GalNAc transferase. The bacterial chondroitin polymerase catalyzes elongation of the chondroitin chain by alternatively transferring the GlcUA and GalNAc moiety from UDP-GlcUA and UDP-GalNAc to the non-reducing ends of the chondroitin chain. The enzyme consists of N-terminal and C-terminal domains in which the two active sites catalyze the addition of GalNAc and GlcUA, respectively. Chondroitin chains range from 40 to over 100 repeating units of the disaccharide. Sulfated chondroitins are involved in the regulation of various biological functions such as central nervous system development, wound repair, infection, growth factor signaling, and morphogenesis, in addition to its conventional structural roles. In Caenorhabditis elegans, chondroitin is an essential factor for the worm to undergo cytokinesis and cell division. Chondroitin is synthesized as proteoglycans, sulfated and secreted to the cell surface or extracellular matrix.


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 51.04  E-value: 4.96e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPSEhIKPMLEKYKELDQ-RIKVIYREENG-HISEATNSALSIA 635
Cdd:cd06420     1 LIITTYN-RPEALELVLKSVLNQSILPFEVIIADDGSTEE-TKELIEEFKSQFPiPIKHVWQEDEGfRKAKIRNKAIAAA 78

                          90
                  ....*....|.
gi 488314916  636 TGDFIGFMDND 646
Cdd:cd06420    79 KGDYLIFIDGD 89
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 557-722 6.36e-07

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 51.63  E-value: 6.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  557 SVAVPVYNVEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKY-KELDQRIKVIYREE-NGHISEATNSALSI 634
Cdd:cd06435     1 SIHVPCYEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEALWKPVEAHcAQLGERFRFFHVEPlPGAKAGALNYALER 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  635 ATGD--FIGFMDNDDELAPQALYEVVKALnTDPTIDFLYTDEDKITENG----RRFNAFYKSDWNPELILNHNY---ITH 705
Cdd:cd06435    81 TAPDaeIIAVIDADYQVEPDWLKRLVPIF-DDPRVGFVQAPQDYRDGEEslfkRMCYAEYKGFFDIGMVSRNERnaiIQH 159

                         170
                  ....*....|....*....
gi 488314916  706 --FVVVKRDLLEKVGGLNS 722
Cdd:cd06435   160 gtMCLIRRSALDDVGGWDE 178
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 29-121 7.43e-07

Methyltransferase domain; Members of this family are SAM dependent methyltransferases.


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 48.52  E-value: 7.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    29 LEFGPGNGRMTSYLmEEKKCQVSIVELD---------KELYDHVSQFSTDAFYGNIDEndwVEYFAGKTFDYIVFADVLE 99
Cdd:pfam08242    1 LEIGCGTGTLLRAL-LEALPGLEYTGLDispaaleaaRERLAALGLLNAVRVELFQLD---LGELDPGSFDVVVASNVLH 76

                           90       100
                   ....*....|....*....|..
gi 488314916   100 HLMNPQSALAKVKPFLKPGGQI 121
Cdd:pfam08242   77 HLADPRAVLRNIRRLLKPGGVL 98
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
 557-747 1.40e-06

GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a glycosyltransferase involved in exopolysaccharide amylovora biosynthesis in Erwinia amylovora. Amylovara is one of the three exopolysaccharide produced by E. amylovora. Amylovara-deficient mutants are non-pathogenic. 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: 133038 [Multi-domain]  Cd Length: 201  Bit Score: 50.01  E-value: 1.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  557 SVAVPVYNVEE-KWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKYKeLDQRIKVIYREENGHISEATNSALSIA 635
Cdd:cd04195     1 SVLMSVYIKEKpEFLREALESILKQTLPPDEVVLVKDGPVTQSLNEVLEEFK-RKLPLKVVPLEKNRGLGKALNEGLKHC 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  636 TGDFIGFMDNDDELAPQALYEVVKALNTDPTIDFLYTDEDKITENGRRFNAFYKSDWNPELIL---NHNYITHFVVV-KR 711
Cdd:cd04195    80 TYDWVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRLPTSHDDILKfarRRSPFNHPTVMfRK 159

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 488314916  712 DLLEKVGGLNSAYNGaQDYDFVLRATEQAMKIKHIP 747
Cdd:cd04195   160 SKVLAVGGYQDLPLV-EDYALWARMLANGARFANLP 194
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
28-125 2.66e-06

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 46.74  E-value: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   28 VLEFGPGNGRMTSYLMEE-KKCQVSIVELDKELYDHVSQFSTDAFYGNIDENDWVeyfAGKTFDYIVFADVLEHLMNPQS 106
Cdd:COG4106     5 VLDLGCGTGRLTALLAERfPGARVTGVDLSPEMLARARARLPNVRFVVADLRDLD---PPEPFDLVVSNAALHWLPDHAA 81

                          90
                  ....*....|....*....
gi 488314916  107 ALAKVKPFLKPGGQILITF 125
Cdd:COG4106    82 LLARLAAALAPGGVLAVQV 100
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
810-1010 1.28e-05

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 47.29  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  810 PMVSLIITndTENMSSYLRQLLE---KTAYTNYEILL------PARFENQINIQNDRLRYVSTETRHGM-------IQAA 873
Cdd:COG1216     3 PKVSVVIP--TYNRPELLRRCLEsllAQTYPPFEVIVvdngstDGTAELLAALAFPRVRVIRNPENLGFaaarnlgLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  874 KGEYVALLNAGLVPTKnDWLKELMNIGqqetsglvtgrvvdaryrvetvgvsvdtdkgrllypekgtpgkslgyyyrial 953
Cdd:COG1216    81 GGDYLLFLDDDTVVEP-DWLERLLAAA----------------------------------------------------- 106

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488314916  954 prniqaatedCLLFNKQLYLNLEGINESLGKEWMGVDLSLQFASAGKRNVYVSYAIL 1010
Cdd:COG1216   107 ----------CLLIRREVFEEVGGFDERFFLYGEDVDLCLRLRKAGYRIVYVPDAVV 153
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 558-646 2.14e-05

DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate.


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 46.79  E-value: 2.14e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSS----LQNQYYENWELCLADDASPSEHIKpMLEKY-KELDQRIKVIYREENGHISEATNSAL 632
Cdd:cd04188     1 VVIPAYN-EEKRLPPTLEEaveyLEERPSFSYEIIVVDDGSKDGTAE-VARKLaRKNPALIRVLTLPKNRGKGGAVRAGM 78

                          90
                  ....*....|....
gi 488314916  633 SIATGDFIGFMDND 646
Cdd:cd04188    79 LAARGDYILFADAD 92
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 553-748 3.56e-05

Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include putative glucosyltransferase, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 46.21  E-value: 3.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   553 QPKISVAVPVYNvEEKWLAACVSSLQNQYYENWELCLADDASPSEHIKPMLEKYKEL-DQRIKVIYREENGHI---SEAT 628
Cdd:pfam13641    1 PPDVSVVVPAFN-EDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEEIAARFpDVRLRVIRNARLLGPtgkSRGL 79

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   629 NSALSIATGDFIGFMDNDDELAPQALYEVVKALnTDPTIDFLYTDEDkiTENGRRF----NAFYKSDWNPELILNHNYI- 703
Cdd:pfam13641   80 NHGFRAVKSDLVVLHDDDSVLHPGTLKKYVQYF-DSPKVGAVGTPVF--SLNRSTMlsalGALEFALRHLRMMSLRLALg 156

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 488314916   704 -----THFVVVKRDLLEKVGGLNSAYNGAQDYDFVLRATEQAMKIKHIPG 748
Cdd:pfam13641  157 vlplsGAGSAIRREVLKELGLFDPFFLLGDDKSLGRRLRRHGWRVAYAPD 206
RsmA COG0030
16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase ...
 9-114 7.45e-05

16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) [Translation, ribosomal structure and biogenesis]; 16S rRNA A1518 and A1519 N6-dimethyltransferase RsmA/KsgA/DIM1 (may also have DNA glycosylase/AP lyase activity) is part of the Pathway/BioSystem: 16S rRNA modification


Pssm-ID: 439801 [Multi-domain]  Cd Length: 270  Bit Score: 45.89  E-value: 7.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    9 TDESTsVGKIV--AQIKENSDVLEFGPGNGRMTSYLMEEKKcQVSIVELDKELYDHVSQfsTDAFYGNIDendwveyfag 86
Cdd:COG0030    21 IDPNI-IRRIVdaAGITPGDTVLEIGPGLGALTRALLERAA-RVTAVEIDRRLAAILRE--TFAAYPNLT---------- 86

                          90       100
                  ....*....|....*....|....*...
gi 488314916   87 ktfdyIVFADVLEHlmnPQSALAKVKPF 114
Cdd:COG0030    87 -----VIEGDALKV---DLPALAAGEPL 106
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
15-128 9.57e-05

Predicted methyltransferase, contains TPR repeat [General function prediction only];


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 44.22  E-value: 9.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916   15 VGKIVAQIKENSD--VLEFGPGNGRMTSYLMEEKKCQVSI------VEL--DKELYDHVSQFSTDAFYgnidendwveyF 84
Cdd:COG4976    35 AEELLARLPPGPFgrVLDLGCGTGLLGEALRPRGYRLTGVdlseemLAKarEKGVYDRLLVADLADLA-----------E 103

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 488314916   85 AGKTFDYIVFADVLEHLMNPQSALAKVKPFLKPGGQILITFPNL 128
Cdd:COG4976   104 PDGRFDLIVAADVLTYLGDLAAVFAGVARALKPGGLFIFSVEDA 147
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 558-652 9.67e-05

Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of poly-N-acetyllactosamine ; This family includes human Beta3GnTL1 and related eukaryotic proteins. Human Beta3GnTL1 is a putative beta-1,3-N-acetylglucosaminyltransferase. Beta3GnTL1 is expressed at various levels in most of tissues examined. Beta 1, 3-N-acetylglucosaminyltransferase has been found to be essential for the formation of poly-N-acetyllactosamine. Poly-N-acetyllactosamine is a unique carbohydrate composed of N-acetyllactosamine repeats. It is often an important part of cell-type-specific oligosaccharide structures and some functional oligosaccharides. It has been shown that the structure and biosynthesis of poly-N-acetyllactosamine display a dramatic change during development and oncogenesis. Several members of beta-1, 3-N-acetylglucosaminyltransferase have been identified.


Pssm-ID: 133063 [Multi-domain]  Cd Length: 219  Bit Score: 44.76  E-value: 9.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNVEEkWLAACVSSLQNQYYEN-WELCLADDASpSEHIKPMLEKYKELDQRIKVIYREENGH------ISEATNS 630
Cdd:cd06913     1 IILPVHNGEQ-WLDECLESVLQQDFEGtLELSVFNDAS-TDKSAEIIEKWRKKLEDSGVIVLVGSHNspspkgVGYAKNQ 78

                          90       100
                  ....*....|....*....|..
gi 488314916  631 ALSIATGDFIGFMDNDDELAPQ 652
Cdd:cd06913    79 AIAQSSGRYLCFLDSDDVMMPQ 100
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 560-658 1.48e-04

Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes related to eukaryotic DPM1; Although the mechanism of eukaryotic enzyme is well studied, the mechanism of the bacterial enzymes is not well understood. The eukaryotic DPM1 is the catalytic subunit of eukaryotic Dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. The enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133030 [Multi-domain]  Cd Length: 181  Bit Score: 43.62  E-value: 1.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  560 VPVYNvEEKWLAACVSSLQN---QYYENWELCLADDASP--SEHIkpmLEKYKELDQRIKVIYREEN-GHISeATNSALS 633
Cdd:cd04187     3 VPVYN-EEENLPELYERLKAvleSLGYDYEIIFVDDGSTdrTLEI---LRELAARDPRVKVIRLSRNfGQQA-ALLAGLD 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488314916  634 IATGDFIGFMD----NDDELAPQAL------YEVV 658
Cdd:cd04187    78 HARGDAVITMDadlqDPPELIPEMLakweegYDVV 112
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 810-1007 1.87e-04

Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis];


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 43.92  E-value: 1.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  810 PMVSLIITndTENMSSYLRQLLE---KTAYTNYEILL---------PARFEnQINIQNDRLRYVSTETRHG-------MI 870
Cdd:COG0463     2 PLVSVVIP--TYNEEEYLEEALEsllAQTYPDFEIIVvddgstdgtAEILR-ELAAKDPRIRVIRLERNRGkgaarnaGL 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  871 QAAKGEYVALLNAGLVPTkNDWLKELMNIGQQETSGLVTGRVVDaryrvetvgvsvdtDKGRLLYPEKGTPGkslgyYYR 950
Cdd:COG0463    79 AAARGDYIAFLDADDQLD-PEKLEELVAALEEGPADLVYGSRLI--------------REGESDLRRLGSRL-----FNL 138

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 488314916  951 IALPRNIQAATEDCLLFNKQLYLNLeGINESLGKEWmgvDLsLQFASAGKRNVYVSY 1007
Cdd:COG0463   139 VRLLTNLPDSTSGFRLFRREVLEEL-GFDEGFLEDT---EL-LRALRHGFRIAEVPV 190
PRK08317 PRK08317
hypothetical protein; Provisional
 76-143 6.44e-04

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 42.62  E-value: 6.44e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 488314916   76 DENDWVEY---------FAGKTFDYIVFADVLEHLMNPQSALAKVKPFLKPGGQILITFPNLAhnSVLIDLFNNRLT 143
Cdd:PRK08317   66 GLGPNVEFvrgdadglpFPDGSFDAVRSDRVLQHLEDPARALAEIARVLRPGGRVVVLDTDWD--TLVWHSGDRALM 140
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
 558-661 9.10e-04

DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to eukaryotic DPM1, including enzymes from bacteria and archaea; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133062 [Multi-domain]  Cd Length: 224  Bit Score: 42.14  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSSLQNQYYE-NWELCLADDASPSEHIKpMLEKYKELDQRIKVIYREENGHISEATNSALSIAT 636
Cdd:cd06442     1 IIIPTYN-ERENIPELIERLDAALKGiDYEIIVVDDNSPDGTAE-IVRELAKEYPRVRLIVRPGKRGLGSAYIEGFKAAR 78

                          90       100
                  ....*....|....*....|....*
gi 488314916  637 GDFIGFMDNDDELAPQALYEVVKAL 661
Cdd:cd06442    79 GDVIVVMDADLSHPPEYIPELLEAQ 103
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 22-127 1.36e-03

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 40.48  E-value: 1.36e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916    22 IKENSDVLEFGPGNGRMTSYLMEEKKCQVSIVELDKElyDHVSQFST----DAFYGNI-----DENDWVEYFAGKTFDYI 92
Cdd:pfam13847    1 IDKGMRVLDLGCGTGHLSFELAEELGPNAEVVGIDIS--EEAIEKARenaqKLGFDNVefeqgDIEELPELLEDDKFDVV 78

                           90       100       110
                   ....*....|....*....|....*....|....*
gi 488314916    93 VFADVLEHLMNPQSALAKVKPFLKPGGQILITFPN 127
Cdd:pfam13847   79 ISNCVLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 558-666 2.13e-03

Subfamily of Glycosyltransferase Family GT2 of 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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 40.73  E-value: 2.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  558 VAVPVYNvEEKWLAACVSSLQNQYY--ENWELCLADDASpSEHIKPMLEK-YKELDQRIKVIyREENGHIS---EATNSA 631
Cdd:cd04192     1 VVIAARN-EAENLPRLLQSLSALDYpkEKFEVILVDDHS-TDGTVQILEFaAAKPNFQLKIL-NNSRVSISgkkNALTTA 77

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 488314916  632 LSIATGDFIGFMDNDDELAPQALYEVVKALNTDPT 666
Cdd:cd04192    78 IKAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQI 112
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 554-660 2.41e-03

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 40.84  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 488314916  554 PKISVAVPVYNvEEKWLAACVSSLQN--QYYENWELCLADDASP---SEHIKPMLEKYKelDQRIKVIYREENGHISEAT 628
Cdd:PLN02726    9 MKYSIIVPTYN-ERLNIALIVYLIFKalQDVKDFEIIVVDDGSPdgtQDVVKQLQKVYG--EDRILLRPRPGKLGLGTAY 85

                          90       100       110
                  ....*....|....*....|....*....|..
gi 488314916  629 NSALSIATGDFIGFMDNDDELAPQALYEVVKA 660
Cdd:PLN02726   86 IHGLKHASGDFVVIMDADLSHHPKYLPSFIKK 117
ksgA TIGR00755
ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, ...
 10-59 3.33e-03

ribosomal RNA small subunit methyltransferase A; In both E. coli and Saccharomyces cerevisiae, this protein is responsible for the dimethylation of two adjacent adenosine residues in a conserved hairpin of 16S rRNA in bacteria, 18S rRNA in eukaryotes. This adjacent dimethylation is the only rRNA modification shared by bacteria and eukaryotes. A single member of this family is present in each of the first 20 completed microbial genomes. This protein is essential in yeast, but not in E. coli, where its deletion leads to resistance to the antibiotic kasugamycin. Alternate name: S-adenosylmethionine--6-N',N'-adenosyl (rRNA) dimethyltransferase [Protein synthesis, tRNA and rRNA base modification]


Pssm-ID: 273252 [Multi-domain]  Cd Length: 254  Bit Score: 40.68  E-value: 3.33e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 488314916    10 DESTsVGKIV--AQIKENSDVLEFGPGNGRMTSYLMEEKKcQVSIVELDKEL 59
Cdd:TIGR00755   14 DENV-IRKIVeaANIQEGDRVLEIGPGLGALTEPLLKRAK-KVTAIEIDPRL 63
ksgA PRK14896
16S ribosomal RNA methyltransferase A;
17-76 8.21e-03

16S ribosomal RNA methyltransferase A;


Pssm-ID: 237852 [Multi-domain]  Cd Length: 258  Bit Score: 39.11  E-value: 8.21e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 488314916   17 KIV--AQIKENSDVLEFGPGNGRMTSYLMEEKKcQVSIVELDKELYDHVSQFSTDafYGNID 76
Cdd:PRK14896   20 RIVeyAEDTDGDPVLEIGPGKGALTDELAKRAK-KVYAIELDPRLAEFLRDDEIA--AGNVE 78
 
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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