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Conserved domains on  [gi|2732496388|ref|WP_345892768|]
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glycosyltransferase [Bacillus subtilis]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-238 2.28e-52

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 175.18  E-value: 2.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITSIK---IFNKTNEGFAKACNQGLEVA 77
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALAFPRvrvIRNPENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  78 SGDNILFLNNDTVVTNQWLEPMIKLlyqddkigmvgpvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlv 157
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 158 gFCLLVKKKVLDEVGGFDERFvGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFTgnpDLSINQLYEENRQRFIDK 237
Cdd:COG1216   106 -ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFLRK 180


                  .
gi 2732496388 238 W 238
Cdd:COG1216   181 H 181
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 236-360 3.49e-12

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: 63.11  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 236 DKWKVDVTTFfdsqpqLTALVPAEAdSILHIGCGTGAaGTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVE 311
Cdd:COG2227     8 DFWDRRLAAL------LARLLPAGG-RVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARERAAELnvdfVQGDLE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2732496388 312 tcDLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 360
Cdd:COG2227    80 --DLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-238 2.28e-52

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 175.18  E-value: 2.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITSIK---IFNKTNEGFAKACNQGLEVA 77
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALAFPRvrvIRNPENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  78 SGDNILFLNNDTVVTNQWLEPMIKLlyqddkigmvgpvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlv 157
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 158 gFCLLVKKKVLDEVGGFDERFvGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFTgnpDLSINQLYEENRQRFIDK 237
Cdd:COG1216   106 -ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFLRK 180


                  .
gi 2732496388 238 W 238
Cdd:COG1216   181 H 181
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-211 6.28e-48

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: 161.96  E-value: 6.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   6 IIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS--IKIFNKTNEGFAKACNQGLEVASGDNIL 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRELFPevRLIRNGENLGFGAGNNQGIREAKGDYVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  84 FLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlRLVGFCLLV 163
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGP----------------------------------------KVSGAFLLV 119

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2732496388 164 KKKVLDEVGGFDERFVGGsFEDDDLSLRVLQAGYQLKIALDSFVHHHG 211
Cdd:cd04186   120 RREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-170 5.65e-24

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: 97.85  E-value: 5.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS-----IKIFNKTNEGFAKACNQGLEVASG 79
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN-FEIIVVDDGSTDGTVEIAEEYAKkdprvRVIRLPENRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYvsgpQQVPVNYTNVEEIEDFSRLYCLQQRGRSKAVLRLVGF 159
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI----FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 2732496388 160 CLLVKKKVLDE 170
Cdd:pfam00535 156 FALYRREALEE 166
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 236-360 3.49e-12

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: 63.11  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 236 DKWKVDVTTFfdsqpqLTALVPAEAdSILHIGCGTGAaGTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVE 311
Cdd:COG2227     8 DFWDRRLAAL------LARLLPAGG-RVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARERAAELnvdfVQGDLE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2732496388 312 tcDLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 360
Cdd:COG2227    80 --DLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-196 5.46e-12

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 65.23  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIwkHTNNDCIEVIVIDNGSHDGTRDYLKQ-----ITSIKifnktneGFAKACNQGLEVASG 79
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADL--QALRGDAEVIVVDGGSTDGTVEIARSlgakvIHSPK-------GRARQMNAGAALAKG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGmvGPVSNYVSGPqQVPVNYtnveeIEDFSRLyclqqrgRSKavLRLVGF 159
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAIRRALAKPGYVA--GAFDLRFDGP-GLLLRL-----IEWGVNL-------RSR--LTGIPY 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2732496388 160 ---CLLVKKKVLDEVGGFDERFVggsFEDDDLSLRVLQAG 196
Cdd:TIGR04283 136 gdqGLFVRRSLFEQIGGFPDIPL---MEDIELSRRLRRLG 172
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-107 7.58e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.14  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   3 KTSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRD----YLKQITSIKIFNKTNEGFAKACNQGLEVAS 78
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEiakhYAENYPHVRLLHQANAGVSVARNTGLAVAT 85

                          90       100
                  ....*....|....*....|....*....
gi 2732496388  79 GDNILFLNNDTVVTNQWLEPMIKLLYQDD 107
Cdd:PRK10073   86 GKYVAFPDADDVVYPTMYETLMTMALEDD 114
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 264-356 2.12e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.21  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 264 LHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVEtcDLPYPESFFDVILIGDLLNCSKNPRH 339
Cdd:pfam08241   1 LDVGCGTGLL-TELLARLGARVTGVDISPEMLELAREKAPREgltfVVGDAE--DLPFPDNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 2732496388 340 TIETLAVYLKPSGSLIC 356
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
 252-357 1.27e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.55  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 252 LTALVPAEADSILHIGCGTGAAGTELLNR--QSCLLYGIEKDELLQTIASPYYEQ------VISADVEtcDLPYPESFFD 323
Cdd:PRK08317   12 FELLAVQPGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSEAMLALAKERAAGlgpnveFVRGDAD--GLPFPDGSFD 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2732496388 324 VILIGDLLNCSKNPRHTIETLAVYLKPSGSLICS 357
Cdd:PRK08317   90 AVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 263-358 7.80e-06

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: 44.73  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 263 ILHIGCGTGAAGTELLNRQSCLLYGIEKDELLQTIASPYYE-------QVISADVETcDLPYPESFFDVILIGDLLNCSK 335
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAalladnvEVLKGDAEE-LPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 2732496388 336 -NPRHTIETLAVYLKPSGSLICSI 358
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
10-96 4.84e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 45.17  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  10 TYNQLALTKQCLESIWKHTNNDCI--EVIVIDNGSHDGT----RDYLKQ---ITSIKIFNKTNEGFAKACNQGLEVASGD 80
Cdd:NF038302    9 TYNGANRLPEVLERLRSQIGTESLswEIIVVDNNSTDNTaqvvQEYQKNwpsPYPLRYCFEPQQGAAFARQRAIQEAKGE 88

                          90
                  ....*....|....*.
gi 2732496388  81 NILFLNNDTVVTNQWL 96
Cdd:NF038302   89 LIGFLDDDNLPAPNWV 104
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 261-358 3.54e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.81  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 261 DSILHIGCGTGAAgTELLNRQscllygIEKDELLQT-IASPYYEQV----------ISADVETCDLpyPESFFDVILIGD 329
Cdd:TIGR02072  36 ASVLDIGCGTGYL-TRALLKR------FPQAEFIALdISAGMLAQAktklsenvqfICGDAEKLPL--EDSSFDLIVSNL 106

                          90       100
                  ....*....|....*....|....*....
gi 2732496388 330 LLNCSKNPRHTIETLAVYLKPSGSLICSI 358
Cdd:TIGR02072 107 ALQWCDDLSQALSELARVLKPGGLLAFST 135
rADc smart00650
Ribosomal RNA adenine dimethylases;
252-316 8.84e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 8.84e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  252 LTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKD----ELLQTIASPYYE-QVISADVETCDLP 316
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGAL-TEELLERAKRVTAIEIDprlaPRLREKFAAADNlTVIHGDALKFDLP 74
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-238 2.28e-52

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 175.18  E-value: 2.28e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITSIK---IFNKTNEGFAKACNQGLEVA 77
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALAFPRvrvIRNPENLGFAAARNLGLRAA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  78 SGDNILFLNNDTVVTNQWLEPMIKLlyqddkigmvgpvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlv 157
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------------- 105

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 158 gFCLLVKKKVLDEVGGFDERFvGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFTgnpDLSINQLYEENRQRFIDK 237
Cdd:COG1216   106 -ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFLRK 180


                  .
gi 2732496388 238 W 238
Cdd:COG1216   181 H 181
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 6-211 6.28e-48

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: 161.96  E-value: 6.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   6 IIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS--IKIFNKTNEGFAKACNQGLEVASGDNIL 83
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRELFPevRLIRNGENLGFGAGNNQGIREAKGDYVL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  84 FLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlRLVGFCLLV 163
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGP----------------------------------------KVSGAFLLV 119

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2732496388 164 KKKVLDEVGGFDERFVGGsFEDDDLSLRVLQAGYQLKIALDSFVHHHG 211
Cdd:cd04186   120 RREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
 3-215 1.05e-27

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: 112.14  E-value: 1.05e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   3 KTSIIVLTYNQLALTKQCLESIWKHT-NNDCIEVIVIDNGSHDGTRDYLKQI----TSIK-IFNKTNEGFAKACNQGLEV 76
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQDyPKEKLEVIVVDDGSTDETAEIARELaaeyPRVRvIERPENGGKAAALNAGLKA 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  77 ASGDNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVGPvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrl 156
Cdd:COG1215   110 ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGA------------------------------------------ 146

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2732496388 157 vgfCLLVKKKVLDEVGGFDERFVGgsfEDDDLSLRVLQAGYQLKIALDSFVHHHGHATF 215
Cdd:COG1215   147 ---NLAFRREALEEVGGFDEDTLG---EDLDLSLRLLRAGYRIVYVPDAVVYEEAPETL 199
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
 6-197 7.61e-27

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: 105.67  E-value: 7.61e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   6 IIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS-----IKIFNKTNEGFAKACNQGLEVASGD 80
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPN-FEVIVVDDGSTDGTLEILEEYAKkdprvIRVINEENQGLAAARNAGLKAARGE 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  81 NILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlvgfc 160
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL------------------------------------------ 117

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2732496388 161 lLVKKKVLDEVGGFDERFVGGsFEDDDLSLRVLQAGY 197
Cdd:cd00761   118 -LFRRELLEEIGGFDEALLSG-EEDDDFLLRLLRGGK 152
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 1-216 1.24e-24

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.93  E-value: 1.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS----IKIF-NKTNEGFAKACNQGLE 75
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPD-FEIIVVDDGSTDGTAEILRELAAkdprIRVIrLERNRGKGAARNAGLA 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  76 VASGDNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVgpvsnyvsgpqqvpVNYTNVEEIEDFSRLYCLQQRGRSKAVLR 155
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAAL-EEGPADLV--------------YGSRLIREGESDLRRLGSRLFNLVRLLTN 144

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2732496388 156 L---VGFCLLVKKKVLDEVgGFDERFvggsFEDDDLsLRVLQAGYqlKIALDSFVHHHGHATFT 216
Cdd:COG0463   145 LpdsTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGF--RIAEVPVRYRAGESKLN 200
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
 5-204 4.96e-24

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: 100.38  E-value: 4.96e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIWKHT-NNDCIEVIVIDNGSHDGTRDYLKQITS----IKIFNKTNEGFAKACNQGLEVASG 79
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNQSyPKDLIEIIVVDGGSTDGTREIVQEYAAkdprIRLIDNPKRIQSAGLNIGIRNSRG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYVSGPQQvpvnyTNVEEIEDfSRLY---CLQQRGRSKAVLRL 156
Cdd:cd02525    83 DIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQ-----KAIAVAQS-SPLGsggSAYRGGAVKIGYVD 156

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2732496388 157 VGFCLLVKKKVLDEVGGFDERFVGGsfEDDDLSLRVLQAGYqlKIALD 204
Cdd:cd02525   157 TVHHGAYRREVFEKVGGFDESLVRN--EDAELNYRLRKAGY--KIWLS 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
 5-170 5.65e-24

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: 97.85  E-value: 5.65e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS-----IKIFNKTNEGFAKACNQGLEVASG 79
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN-FEIIVVDDGSTDGTVEIAEEYAKkdprvRVIRLPENRGKAGARNAGLRAATG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYvsgpQQVPVNYTNVEEIEDFSRLYCLQQRGRSKAVLRLVGF 159
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI----FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155

                         170
                  ....*....|.
gi 2732496388 160 CLLVKKKVLDE 170
Cdd:pfam00535 156 FALYRREALEE 166
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
 6-185 8.31e-20

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: 86.51  E-value: 8.31e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   6 IIVLTYNQLALTKQCLESIwKHTNNDCIEVIVIDNGSHDGTRDYLKQITSIKIFN------KTNEGFAKACNQGLEVASG 79
Cdd:cd06423     1 IIVPAYNEEAVIERTIESL-LALDYPKLEVIVVDDGSTDDTLEILEELAALYIRRvlvvrdKENGGKAGALNAGLRHAKG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVG-------PVSNYVsgpqqvpvnyTNVEEIEdFSRLYCLQQRGRS-- 150
Cdd:cd06423    80 DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQgrvrvrnGSENLL----------TRLQAIE-YLSIFRLGRRAQSal 148

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2732496388 151 KAVLRLVGFCLLVKKKVLDEVGGFDERFVGgsfED 185
Cdd:cd06423   149 GGVLVLSGAFGAFRREALREVGGWDEDTLT---ED 180
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
 5-197 1.57e-17

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: 80.67  E-value: 1.57e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS--IKIFNKTNEGFAKACNQGLEVASGDNI 82
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPN-IEYIVIDGGSTDGTVDIIKKYEDkiTYWISEPDKGIYDAMNKGIALATGDII 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  83 LFLNNDTVvtnqwlepmikllYQDDKIGMVGpvsNYVSGPQQVPVNYTNVEEI-EDFSRLYCLQQRGRSKAVLRLVGFC- 160
Cdd:cd06433    80 GFLNSDDT-------------LLPGALLAVV---AAFAEHPEVDVVYGDVLLVdENGRVIGRRRPPPFLDKFLLYGMPIc 143

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2732496388 161 ---LLVKKKVLDEVGGFDE--RFVGgsfeDDDLSLRVLQAGY 197
Cdd:cd06433   144 hqaTFFRRSLFEKYGGFDEsyRIAA----DYDLLLRLLLAGK 181
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
 7-210 5.40e-15

RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative dTDP-rhamnosyl transferase. dTDP rhamnosyl transferases of Shigella flexneri add rhamnose sugars to N-acetyl-glucosamine in the O-antigen tetrasaccharide repeat. Lipopolysaccharide O antigens are important virulence determinants for many bacteria. The variations of sugar composition, the sequence of the sugars and the linkages in the O antigen provide structural diversity of the O antigen.


Pssm-ID: 133017 [Multi-domain]  Cd Length: 237  Bit Score: 74.24  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   7 IVLTYN-QLALTKQCLESIwkhtNNDCIEVIVIDNGSH-DGTRDYLKQITSIK-IFNKTNEGFAKACNQGLEVASGDN-- 81
Cdd:cd02526     2 VVVTYNpDLSKLKELLAAL----AEQVDKVVVVDNSSGnDIELRLRLNSEKIElIHLGENLGIAKALNIGIKAALENGad 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  82 -ILFLNNDTVVTNQWLEPMI---KLLYQDDKIGMVGPVSNYVSGPQQVPvnytnveeiEDFSRLYCLQQRGRSKAVLRLV 157
Cdd:cd02526    78 yVLLFDQDSVPPPDMVEKLLaykILSDKNSNIGAVGPRIIDRRTGENSP---------GVRKSGYKLRIQKEGEEGLKEV 148

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 158 GFCL----LVKKKVLDEVGGFDERFvggsFEDD---DLSLRVLQAGYQLKIALDSFVHHH 210
Cdd:cd02526   149 DFLItsgsLISLEALEKVGGFDEDL----FIDYvdtEWCLRARSKGYKIYVVPDAVLKHE 204
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
 5-121 2.11e-14

UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of lipooligosaccharide; UDP-glucose: lipooligosaccharide (LOS) beta-1-4-glucosyltransferase catalyzes the addition of the first residue, glucose, of the lacto-N-neotetrase structure to HepI of the LOS inner core. LOS is the major constituent of the outer leaflet of the outer membrane of gram-positive bacteria. It consists of a short oligosaccharide chain of variable composition (alpha chain) attached to a branched inner core which is lined in turn to lipid A. Beta 1,4 glucosyltransferase is required to attach the alpha chain to the inner core.


Pssm-ID: 133005 [Multi-domain]  Cd Length: 229  Bit Score: 72.32  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIwkhtNNDCIEVIVIDNGSHDGTRDYLKQITsIKIFNKTNEGFAKACNQGLEVASGDNILF 84
Cdd:cd02511     3 SVVIITKNEERNIERCLESV----KWAVDEIIVVDSGSTDRTVEIAKEYG-AKVYQRWWDGFGAQRNFALELATNDWVLS 77

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2732496388  85 LNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYVSG 121
Cdd:cd02511    78 LDADERLTPELADEILALLATDDYDGYYVPRRNFFLG 114
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 20-197 7.23e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 67.70  E-value: 7.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  20 CLESIWKHT-NNDCIEVIVIDNGSHDGTRDYLKQITSIKIFN--------KTNEGFAKACNQGLEVASGDNILFLNNDTV 90
Cdd:cd04192    15 LLQSLSALDyPKEKFEVILVDDHSTDGTVQILEFAAAKPNFQlkilnnsrVSISGKKNALTTAIKAAKGDWIVTTDADCV 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  91 VTNQWLEPMIKlLYQDDKIGMV-GPVSNYvsgpqqvpVNYTNVEEIEDFSRLYCLqqrGRSKAVLRL------VGFCLLV 163
Cdd:cd04192    95 VPSNWLLTFVA-FIQKEQIGLVaGPVIYF--------KGKSLLAKFQRLDWLSLL---GLIAGSFGLgkpfmcNGANMAY 162

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2732496388 164 KKKVLDEVGGFDerfvGGSF---EDDDLSLRVLQAGY 197
Cdd:cd04192   163 RKEAFFEVGGFE----GNDHiasGDDELLLAKVASKY 195
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
 5-196 3.40e-12

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: 65.30  E-value: 3.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYN-QLALTKQCLESIWKHTNnDCIEVIVIDNGS-HDGTRDYLKQITS----IKI-FNKTNEGFAKACNQGLEVA 77
Cdd:cd04184     4 SIVMPVYNtPEKYLREAIESVRAQTY-PNWELCIADDAStDPEVKRVLKKYAAqdprIKVvFREENGGISAATNSALELA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  78 SGDNILFLNNDTVVTNQWL---------EPMIKLLYQD-DKIGMVGPVSNYVSGPqqvpvnytnveeieDFSRLYCLQQr 147
Cdd:cd04184    83 TGEFVALLDHDDELAPHALyevvkalneHPDADLIYSDeDKIDEGGKRSEPFFKP--------------DWSPDLLLSQ- 147

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2732496388 148 grskavlRLVGFCLLVKKKVLDEVGGFDERFVGGsfEDDDLSLRVLQAG 196
Cdd:cd04184   148 -------NYIGHLLVYRRSLVRQVGGFREGFEGA--QDYDLVLRVSEHT 187
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
 236-360 3.49e-12

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: 63.11  E-value: 3.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 236 DKWKVDVTTFfdsqpqLTALVPAEAdSILHIGCGTGAaGTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVE 311
Cdd:COG2227     8 DFWDRRLAAL------LARLLPAGG-RVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARERAAELnvdfVQGDLE 79

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2732496388 312 tcDLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 360
Cdd:COG2227    80 --DLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
 5-196 5.46e-12

transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it sugar moiety, as part of a biosynthetic pathway. Other proposed members of the pathway include another transferase (TIGR04282), a phosphoesterase, and a radical SAM enzyme (TIGR04167) whose C-terminal domain (pfam12345) frequently contains a selenocysteine. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 275103 [Multi-domain]  Cd Length: 220  Bit Score: 65.23  E-value: 5.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIwkHTNNDCIEVIVIDNGSHDGTRDYLKQ-----ITSIKifnktneGFAKACNQGLEVASG 79
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADL--QALRGDAEVIVVDGGSTDGTVEIARSlgakvIHSPK-------GRARQMNAGAALAKG 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGmvGPVSNYVSGPqQVPVNYtnveeIEDFSRLyclqqrgRSKavLRLVGF 159
Cdd:TIGR04283  73 DILLFLHADTRLPKDFLEAIRRALAKPGYVA--GAFDLRFDGP-GLLLRL-----IEWGVNL-------RSR--LTGIPY 135

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2732496388 160 ---CLLVKKKVLDEVGGFDERFVggsFEDDDLSLRVLQAG 196
Cdd:TIGR04283 136 gdqGLFVRRSLFEQIGGFPDIPL---MEDIELSRRLRRLG 172
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
 6-210 1.03e-11

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: 63.37  E-value: 1.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   6 IIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITSIKIFN-----KTNEGF--AKACNQGLEVAS 78
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILP-FEVIIADDGSTEETKELIEEFKSQFPIPikhvwQEDEGFrkAKIRNKAIAAAK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  79 GDNILFLNNDTVVTNQWLEPMIKLLyqDDKIgmvgpvsnYVSGpqqvpvnytnveeiedfSRLY----CLQQRGRSkavl 154
Cdd:cd06420    80 GDYLIFIDGDCIPHPDFIADHIELA--EPGV--------FLSG-----------------SRVLlnekLTERGIRG---- 128

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2732496388 155 rlvgfC-LLVKKKVLDEVGGFDERFVGGSFEDDDLSLRVLQAGYQLKIALDSFVHHH 210
Cdd:cd06420   129 -----CnMSFWKKDLLAVNGFDEEFTGWGGEDSELVARLLNSGIKFRKLKFAAIVFH 180
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 7-235 2.35e-11

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: 133028 [Multi-domain]  Cd Length: 202  Bit Score: 62.65  E-value: 2.35e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   7 IVLTYNQLALTKQCLESIWKHT-NNDciEVIVIDNGSHDGTRDYLKQITSIKIF----NKTNEGFAKACNQGLEVASGDN 81
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTrPPD--HIIVIDNASTDGTAEWLTSLGDLDNIvylrLPENLGGAGGFYEGVRRAYELG 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  82 ---ILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVGPVSNYVSGPqqvpvnytnveeiedFsrlyclqqrgrskavlrlVG 158
Cdd:cd04185    80 ydwIWLMDDDAIPDPDALEKLLAYA-DKDNPQFLAPLVLDPDGS---------------F------------------VG 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 159 FclLVKKKVLDEVGGFDERFvggsF--EDD-DLSLRVLQAGYqlKIALDSFVHHHGHA----TFTGNPDLSINQLYEENR 231
Cdd:cd04185   126 V--LISRRVVEKIGLPDKEF----FiwGDDtEYTLRASKAGP--GIYVPDAVVVHKTAinkgSSAVVNIDPPWKLYYGVR 197


                  ....
gi 2732496388 232 QRFI 235
Cdd:cd04185   198 NRIY 201
PRK10073 PRK10073
putative glycosyl transferase; Provisional
 3-107 7.58e-11

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 63.14  E-value: 7.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   3 KTSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRD----YLKQITSIKIFNKTNEGFAKACNQGLEVAS 78
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEiakhYAENYPHVRLLHQANAGVSVARNTGLAVAT 85

                          90       100
                  ....*....|....*....|....*....
gi 2732496388  79 GDNILFLNNDTVVTNQWLEPMIKLLYQDD 107
Cdd:PRK10073   86 GKYVAFPDADDVVYPTMYETLMTMALEDD 114
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
 30-198 1.40e-10

CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of proteins related to Agrobacterium tumefaciens CelA and Gluconacetobacter xylinus BscA. These proteins are involved in the elongation of the glucan chain of cellulose, an aggregate of unbranched polymers of beta-1,4-linked glucose residues. They are putative catalytic subunit of cellulose synthase, which is a glycosyltransferase using UDP-glucose as the substrate. The catalytic subunit is an integral membrane protein with 6 transmembrane segments and it is postulated that the protein is anchored in the membrane at the N-terminal end.


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 61.05  E-value: 1.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  30 NDCIEVIVIDNGSHDGTRDYLKQITSIKIFN----KTNEGfAKA--CNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLL 103
Cdd:cd06421    31 HDKLRVYVLDDGRRPELRALAAELGVEYGYRyltrPDNRH-AKAgnLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYF 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 104 YQDDKIGMVGPVSNYVSGPQQVPVNYTNVEEIEDFsrlYCLQQRGRSkavLRLVGFCL----LVKKKVLDEVGGFDERFV 179
Cdd:cd06421   110 LDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELF---YGVIQPGRD---RWGAAFCCgsgaVVRREALDEIGGFPTDSV 183

                         170
                  ....*....|....*....
gi 2732496388 180 GgsfEDDDLSLRVLQAGYQ 198
Cdd:cd06421   184 T---EDLATSLRLHAKGWR 199
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 33-195 2.17e-10

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


Pssm-ID: 313356 [Multi-domain]  Cd Length: 276  Bit Score: 61.14  E-value: 2.17e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  33 IEVIVIDNGShdgTRDYLKQITSIKIFN---------KTNEGFAKACNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLL 103
Cdd:pfam10111  30 FELIIINDGS---TDKTLEEVSSIKDHNlqvyypnapDTTYSLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIA 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 104 yqddkigMVGPVSNYVSGPQQVPVNYTNVEEIEDFSRLYCLQQRGRskaVLR--------LVGFCL------LVKKKVLD 169
Cdd:pfam10111 107 -------TSLALQENIQAAVVLPVTDLNDESSNFLRRGGDLTASGD---VLRdllvfyspLAIFFApnssnaLINRQAFI 176

                         170       180
                  ....*....|....*....|....*.
gi 2732496388 170 EVGGFDERFVGGSFEDDDLSLRVLQA 195
Cdd:pfam10111 177 EVGGFDESFRGHGAEDFDIFLRLAAR 202
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
 5-191 8.84e-10

GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; Glycosyltransferase family 2 (GT-2) subfamily 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: 133013 [Multi-domain]  Cd Length: 221  Bit Score: 58.74  E-value: 8.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESIwKHTNNDCIEVIVIDNGSHDGTRDYLKQITSIKIfnKTNEGFAKACNQGLEVASGDNILF 84
Cdd:cd02522     2 SIIIPTLNEAENLPRLLASL-RRLNPLPLEIIVVDGGSTDGTVAIARSAGVVVI--SSPKGRARQMNAGAAAARGDWLLF 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  85 LNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSnyvsgpqqvpvnytnveeIEDFSRLYclqqRGRSKAV-LRLVGF---- 159
Cdd:cd02522    79 LHADTRLPPDWDAAIIETLRADGAVAGAFRLR------------------FDDPGPRL----RLLELGAnLRSRLFglpy 136

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2732496388 160 ---CLLVKKKVLDEVGGFDERFVggsFEDDDLSLR 191
Cdd:cd02522   137 gdqGLFIRRELFEELGGFPELPL---MEDVELVRR 168
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
 252-371 8.87e-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: 56.93  E-value: 8.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 252 LTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYE------QVISADVEtcDLPYPESFFDVI 325
Cdd:COG2226    15 LAALGLRPGARVLDLGCGTGRL-ALALAERGARVTGVDISPEMLELARERAAeaglnvEFVVGDAE--DLPFPDGSFDLV 91

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2732496388 326 LIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPNTAYADTFFSLL 371
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
 4-236 1.50e-09

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: 58.15  E-value: 1.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   4 TSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQI------TSIKIFNKTNE----GFAKACNQG 73
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPP-VEVVVVVNPSDAETLDVAEEIaarfpdVRLRVIRNARLlgptGKSRGLNHG 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  74 LEVASGDNILFLNNDTVV---TNQWLEPmiklLYQDDKIGMVGpVSNYVSGPQQVPVNYTNVEEIEDFSRLYCLQQRGRs 150
Cdd:pfam13641  83 FRAVKSDLVVLHDDDSVLhpgTLKKYVQ----YFDSPKVGAVG-TPVFSLNRSTMLSALGALEFALRHLRMMSLRLALG- 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 151 kaVLRLVGFCLLVKKKVLDEVGGFDERFVGGsfEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFtgnpdlsinQLYEEN 230
Cdd:pfam13641 157 --VLPLSGAGSAIRREVLKELGLFDPFFLLG--DDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYL---------AASIKQ 223


                  ....*.
gi 2732496388 231 RQRFID 236
Cdd:pfam13641 224 RARWVY 229
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 264-356 2.12e-09

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


Pssm-ID: 462406 [Multi-domain]  Cd Length: 94  Bit Score: 54.21  E-value: 2.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 264 LHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVEtcDLPYPESFFDVILIGDLLNCSKNPRH 339
Cdd:pfam08241   1 LDVGCGTGLL-TELLARLGARVTGVDISPEMLELAREKAPREgltfVVGDAE--DLPFPDNSFDLVLSSEVLHHVEDPER 77

                          90
                  ....*....|....*..
gi 2732496388 340 TIETLAVYLKPSGSLIC 356
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
 5-112 1.43e-08

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: 54.94  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYN-QLALTKQcLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS------IKIFNKTNEGFAKACNQGLEVA 77
Cdd:cd04196     1 AVLMATYNgEKYLREQ-LDSILAQTYKND-ELIISDDGSTDGTVEIIKEYIDkdpfiiILIRNGKNLGVARNFESLLQAA 78

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2732496388  78 SGDNILFLNNDTVvtnqW----LEPMIKLLYQDDKIGMV 112
Cdd:cd04196    79 DGDYVFFCDQDDI----WlpdkLERLLKAFLKDDKPLLV 113
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
 34-208 2.04e-08

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: 54.71  E-value: 2.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  34 EVIVIDNGSHDGT-----RDYLKQI-TSIKIFN-KTNEGF-AKACNQGLEVASGDN--ILFLNNDTVVTNQWLEPMIKLl 103
Cdd:cd06435    30 EVIVIDNNTKDEAlwkpvEAHCAQLgERFRFFHvEPLPGAkAGALNYALERTAPDAeiIAVIDADYQVEPDWLKRLVPI- 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 104 YQDDKIGMVgpvsnyvsgpqQVPVNYTNVEEIEDFSRLYC---------LQQRGRSKAVLRlVGFCLLVKKKVLDEVGGF 174
Cdd:cd06435   109 FDDPRVGFV-----------QAPQDYRDGEESLFKRMCYAeykgffdigMVSRNERNAIIQ-HGTMCLIRRSALDDVGGW 176

                         170       180       190
                  ....*....|....*....|....*....|....
gi 2732496388 175 DERFVggsFEDDDLSLRVLQAGYQLKIALDSFVH 208
Cdd:cd06435   177 DEWCI---TEDSELGLRMHEAGYIGVYVAQSYGH 207
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
 82-208 5.47e-08

Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include putative glucosyltransferases, which are involved in bacterial capsule biosynthesis.


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 52.72  E-value: 5.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  82 ILFLNNDTVVTNQWLEpMIKLLYQDDKIGMVgpvsnyvSGPQQVPVNYTNVEEIEDFSRLY----CLQQRGRSKAVLRLV 157
Cdd:pfam13632   2 ILLLDADTVLPPDCLL-GIANEMASPEVAII-------QGPILPMNVGNYLEELAALFFADdhgkSIPVRMALGRVLPFV 73

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2732496388 158 GFCLLVKKKVLDEVGGFDERFVGgsfEDDDLSLRVLQAGYQLKIALDSFVH 208
Cdd:pfam13632  74 GSGAFLRRSALQEVGGWDDGSVS---EDFDFGLRLQRAGYRVRFAPYSAVY 121
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
249-369 2.78e-07

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


Pssm-ID: 444001 [Multi-domain]  Cd Length: 181  Bit Score: 50.38  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 249 QPQLTALVPAEADSILHIGCGTGAAGTELLNRQSCLLyGIEKDE--LLQTIASPYYEQVISADVetCDLPYPESFFDVIL 326
Cdd:COG4976    36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLT-GVDLSEemLAKAREKGVYDRLLVADL--ADLAEPDGRFDLIV 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2732496388 327 IGDLLNCSKNPRHTIETLAVYLKPSGSLICSIpNTAYADTFFS 369
Cdd:COG4976   113 AADVLTYLGDLAAVFAGVARALKPGGLFIFSV-EDADGSGRYA 154
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
 5-142 4.33e-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: 51.04  E-value: 4.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   5 SIIVLTYNQLALTKQCLESI----WKhtnNDCIEVIVIDNGSHDGT----RDYLKQItSIKIFNKTNEGFAKACNQGLEV 76
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLlaldYP---RDRLEIIVVSDGSTDGTaeiaREYADKG-VKLLRFPERRGKAAALNRALAL 107

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2732496388  77 ASGDNILFlnndTVVTNQWLEPMIKLL---YQDDKIGmvgpvsnYVSGpQQVPVNYTNVEEIEDFSRLY 142
Cdd:cd06439   108 ATGEIVVF----TDANALLDPDALRLLvrhFADPSVG-------AVSG-ELVIVDGGGSGSGEGLYWKY 164
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
 34-238 7.46e-07

pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide alpha-N-acetylgalactosaminyltransferases (pp-GalNAc-T) initiate the formation of mucin-type, O-linked glycans by catalyzing the transfer of alpha-N-acetylgalactosamine (GalNAc) from UDP-GalNAc to hydroxyl groups of Ser or Thr residues of core proteins to form the Tn antigen (GalNAc-a-1-O-Ser/Thr). These enzymes are type II membrane proteins with a GT-A type catalytic domain and a lectin domain located on the lumen side of the Golgi apparatus. In human, there are 15 isozymes of pp-GalNAc-Ts, representing the largest of all glycosyltransferase families. Each isozyme has unique but partially redundant substrate specificity for glycosylation sites on acceptor proteins.


Pssm-ID: 133004 [Multi-domain]  Cd Length: 299  Bit Score: 50.67  E-value: 7.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  34 EVIVIDNGShdgTRDYLKQ---------ITSIKIF-NKTNEGFAKACNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLL 103
Cdd:cd02510    32 EIILVDDFS---DKPELKLlleeyykkyLPKVKVLrLKKREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARI 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 104 YQDDKIgMVGPVSNyvsgpqqvPVNYTNVEEIE-------------DFSRLYCLQQ-RGRSKAVL-----RLVGFCLLVK 164
Cdd:cd02510   109 AENRKT-VVCPIID--------VIDADTFEYRGssgdarggfdwslHFKWLPLPEEeRRRESPTApirspTMAGGLFAID 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 165 KKVLDEVGGFDE--RFVGG-SFEdddLSLRVLQAGYQLKIALDSFVHH---HGHATFTGNPDlsiNQLYEENRQRFIDKW 238
Cdd:cd02510   180 REWFLELGGYDEgmDIWGGeNLE---LSFKVWQCGGSIEIVPCSRVGHifrRKRKPYTFPGG---SGTVLRNYKRVAEVW 253
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
259-357 8.39e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.13  E-value: 8.39e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 259 EADSILHIGCGTGAAGTELLNR-QSCLLYGIEKDELLQTIASPYYEQV--ISADVETCDLPYPesfFDVILIGDLLNCSK 335
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfPGARVTGVDLSPEMLARARARLPNVrfVVADLRDLDPPEP---FDLVVSNAALHWLP 77

                          90       100
                  ....*....|....*....|..
gi 2732496388 336 NPRHTIETLAVYLKPSGSLICS 357
Cdd:COG4106    78 DHAALLARLAAALAPGGVLAVQ 99
Glyco_tranf_2_5 pfam13712
Glycosyltransferase like family; Members of this family of prokaryotic proteins include ...
 67-238 9.53e-07

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


Pssm-ID: 463964 [Multi-domain]  Cd Length: 210  Bit Score: 49.54  E-value: 9.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  67 AKACNQGLEVASGDNILFLNNDTVVTN-QWLEPMIKLLYQDDKIGMVGpvsnyVSGPQQVPVN---------YTNVEEIE 136
Cdd:pfam13712  42 AAAYNEAMSASDAKYKVYIHQDVFIINkDFIEDLLSIFKKDPSIGMIG-----VVGAQSLPDSgvwwessykVGKVYVPS 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 137 DFSRLYCLQQRGRSK--AVLRLVGFCLLVKKKVldevgGFDE-RFVGGSFEDDDLSLRVLQAGYQLKIALDS---FVHHH 210
Cdd:pfam13712 117 KDESYLLRQGEAEGKyeEVEAIDGLFMATQYDI-----PWREdLFDGWHFYDVSQSLEFRRAGYKVVVPYQEkpwCIHDC 191

                         170       180
                  ....*....|....*....|....*...
gi 2732496388 211 GHATFTGnpdlsinqlYEENRQRFIDKW 238
Cdd:pfam13712 192 GFLNLDN---------YEKYRKIFLKEY 210
PRK08317 PRK08317
hypothetical protein; Provisional
 252-357 1.27e-06

hypothetical protein; Provisional


Pssm-ID: 181382 [Multi-domain]  Cd Length: 241  Bit Score: 49.55  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 252 LTALVPAEADSILHIGCGTGAAGTELLNR--QSCLLYGIEKDELLQTIASPYYEQ------VISADVEtcDLPYPESFFD 323
Cdd:PRK08317   12 FELLAVQPGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSEAMLALAKERAAGlgpnveFVRGDAD--GLPFPDGSFD 89

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2732496388 324 VILIGDLLNCSKNPRHTIETLAVYLKPSGSLICS 357
Cdd:PRK08317   90 AVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
 263-352 4.81e-06

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


Pssm-ID: 463945 [Multi-domain]  Cd Length: 96  Bit Score: 44.86  E-value: 4.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 263 ILHIGCGTGAAGTELLNRQSCLLYGIEKDELLQTIASPYYE------QVISADVEtcDLPYPESFFDVILIGDLLNC--S 334
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAeaglnvEFVQGDAE--DLPFPDGSFDLVVSSGVLHHlpD 78

                          90
                  ....*....|....*...
gi 2732496388 335 KNPRHTIETLAVYLKPSG 352
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
 4-205 6.08e-06

Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are bi-functional glycosyltransferases that catalyze polymerization of hyaluronan. HASs transfer both GlcUA and GlcNAc in beta-(1,3) and beta-(1,4) linkages, respectively to the hyaluronan chain using UDP-GlcNAc and UDP-GlcUA as substrates. HA is made as a free glycan, not attached to a protein or lipid. HASs do not need a primer for HA synthesis; they initiate HA biosynthesis de novo with only UDP-GlcNAc, UDP-GlcUA, and Mg2+. Hyaluronan (HA) is a linear heteropolysaccharide composed of (1-3)-linked beta-D-GlcUA-beta-D-GlcNAc disaccharide repeats. It can be found in vertebrates and a few microbes and is typically on the cell surface or in the extracellular space, but is also found inside mammalian cells. Hyaluronan has several physiochemical and biological functions such as space filling, lubrication, and providing a hydrated matrix through which cells can migrate.


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 47.25  E-value: 6.08e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   4 TSIIVLTYNQ-LALTKQCLESIWKhtnNDCIEVIVIDNGSHDGTRDYLKQI---TSIKIFNKTNEGFAKACNQGLEVASG 79
Cdd:cd06434     2 VTVIIPVYDEdPDVFRECLRSILR---QKPLEIIVVTDGDDEPYLSILSQTvkyGGIFVITVPHPGKRRALAEGIRHVTT 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  80 DNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVGPVSNyVSGPQQVPVNYTNVEEIEdfsRLYCLQQRGRSK--AVLRLV 157
Cdd:cd06434    79 DIVVLLDSDTVWPPNALPEMLKPF-EDPKVGGVGTNQR-ILRPRDSKWSFLAAEYLE---RRNEEIRAAMSYdgGVPCLS 153

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2732496388 158 GFCLLVKKKVLDEV----GGFDERFVGGSFE-DDDLSL--RVLQAGYQLKIALDS 205
Cdd:cd06434   154 GRTAAYRTEILKDFlfleEFTNETFMGRRLNaGDDRFLtrYVLSHGYKTVYQYTS 208
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
 263-358 7.80e-06

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: 44.73  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 263 ILHIGCGTGAAGTELLNRQSCLLYGIEKDELLQTIASPYYE-------QVISADVETcDLPYPESFFDVILIGDLLNCSK 335
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAalladnvEVLKGDAEE-LPPEADESFDVIISDPPLHHLV 80

                          90       100
                  ....*....|....*....|....
gi 2732496388 336 -NPRHTIETLAVYLKPSGSLICSI 358
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
 263-383 1.24e-05

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: 45.91  E-value: 1.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 263 ILHIGCGTGAAGTELLNRQSCLLYGIEKDE--LLQTIASPYYeqVISADVETCDLPYPESFFDVILIGDLLNCSKNPRHT 340
Cdd:pfam07021  17 VLDLGCGDGTLLYLLKEEKGVDGYGIELDAagVAECVAKGLY--VIQGDLDEGLEHFPDKSFDYVILSQTLQATRNPREV 94

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2732496388 341 IETLavyLKPSGSLICSIPNTAYADTFFSLLCGAST-------YTHFITP 383
Cdd:pfam07021  95 LDEM---LRIGRRCIVSFPNFGHWRVRWSLLSRGRMpvtdllpYTWYNTP 141
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
 264-354 1.32e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.90  E-value: 1.32e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 264 LHIGCGTGAAGTELLNRQSCL-LYGIEKDELLQTIASPYYEQVISADVETCDLPYPESF------FDVILIGDLLNCSKN 336
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGeldpgsFDVVVASNVLHHLAD 80

                          90
                  ....*....|....*...
gi 2732496388 337 PRHTIETLAVYLKPSGSL 354
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
 227-360 1.58e-05

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


Pssm-ID: 404385 [Multi-domain]  Cd Length: 162  Bit Score: 45.11  E-value: 1.58e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 227 YEENRQRFIDKWKvdvttffdsqpQLTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYEQVI 306
Cdd:pfam13489   1 YAHQRERLLADLL-----------LRLLPKLPSPGRVLDFGCGTGIF-LRLLRAQGFSVTGVDPSPIAIERALLNVRFDQ 68

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2732496388 307 SADVEtcdLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 360
Cdd:pfam13489  69 FDEQE---AAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPL 119
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
 1-88 1.66e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 46.23  E-value: 1.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   1 MVKTSIIVLTYNQ---LALTKQCLESIWKHTNNdcIEVIVIDNGSHDGTRDYLKQItsIKIFNKTN---------EGFAK 68
Cdd:PLN02726    8 AMKYSIIVPTYNErlnIALIVYLIFKALQDVKD--FEIIVVDDGSPDGTQDVVKQL--QKVYGEDRillrprpgkLGLGT 83

                          90       100
                  ....*....|....*....|
gi 2732496388  69 ACNQGLEVASGDNILFLNND 88
Cdd:PLN02726   84 AYIHGLKHASGDFVVIMDAD 103
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
 34-85 1.97e-05

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: 45.26  E-value: 1.97e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2732496388  34 EVIVIDNGSHDGTRDYLKQI-----TSIKIFNKTNEGFAKACNQGLEVASGDNILFL 85
Cdd:cd04179    30 EIIVVDDGSTDGTAEIARELaarvpRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
 68-212 3.11e-05

Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2.4.1.80.


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 44.20  E-value: 3.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  68 KACN--QGLEVASGDNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMV-GPVsnYVSGPQQVPVNYTNVEeIEDFSRLYCL 144
Cdd:pfam13506  18 KVNNllQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVtSPP--VGSDPKGLAAALEAAF-FNTLAGVLQA 93

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2732496388 145 QQRGRSKAVlrlvGFCLLVKKKVLDEVGGFdERFVGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGH 212
Cdd:pfam13506  94 ALSGIGFAV----GMSMAFRRADLERIGGF-EALADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGP 156
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
10-96 4.84e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 45.17  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  10 TYNQLALTKQCLESIWKHTNNDCI--EVIVIDNGSHDGT----RDYLKQ---ITSIKIFNKTNEGFAKACNQGLEVASGD 80
Cdd:NF038302    9 TYNGANRLPEVLERLRSQIGTESLswEIIVVDNNSTDNTaqvvQEYQKNwpsPYPLRYCFEPQQGAAFARQRAIQEAKGE 88

                          90
                  ....*....|....*.
gi 2732496388  81 NILFLNNDTVVTNQWL 96
Cdd:NF038302   89 LIGFLDDDNLPAPNWV 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
 259-360 1.14e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.40  E-value: 1.14e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 259 EADSILHIGCGTGAAGTEL--LNRQSCLLYGIEKDELL-----QTIASPYYEQV--ISADVETCDLPYPESFFDVILIGD 329
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELaeELGPNAEVVGIDISEEAiekarENAQKLGFDNVefEQGDIEELPELLEDDKFDVVISNC 82

                          90       100       110
                  ....*....|....*....|....*....|.
gi 2732496388 330 LLNCSKNPRHTIETLAVYLKPSGSLICSIPN 360
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
 6-94 1.42e-04

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: 43.22  E-value: 1.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388   6 IIVLTYNQLALTKQCLESIWKHTNNDCIEVIVIDNGSHDGTRDYLKQ---------ITSIKIFNKTNE----GFAKacNQ 72
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSAEIIEKwrkkledsgVIVLVGSHNSPSpkgvGYAK--NQ 78

                          90       100
                  ....*....|....*....|..
gi 2732496388  73 GLEVASGDNILFLNNDTVVTNQ 94
Cdd:cd06913    79 AIAQSSGRYLCFLDSDDVMMPQ 100
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
 34-88 9.14e-04

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: 40.63  E-value: 9.14e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2732496388  34 EVIVIDNGSHDGTRDYLKQI-----TSIKIF-NKTNEGFAKACNQGLEVASGDNILFLNND 88
Cdd:cd04188    32 EIIVVDDGSKDGTAEVARKLarknpALIRVLtLPKNRGKGGAVRAGMLAARGDYILFADAD 92
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
 252-326 1.31e-03

tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) A37 N6-methylase TrmN6 is part of the Pathway/BioSystem: tRNA modification


Pssm-ID: 443299 [Multi-domain]  Cd Length: 238  Bit Score: 40.13  E-value: 1.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 252 LTALVPAE-ADSILHIGCGTGAAGTELLNR-QSCLLYGIEKDELLQTIA------SPYYEQ--VISADVETCDLPYPESF 321
Cdd:COG4123    29 LAAFAPVKkGGRVLDLGTGTGVIALMLAQRsPGARITGVEIQPEAAELArrnvalNGLEDRitVIHGDLKEFAAELPPGS 108


                  ....*
gi 2732496388 322 FDVIL 326
Cdd:COG4123   109 FDLVV 113
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
 261-358 3.54e-03

malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin biosynthetic gene clusters in proteobacteria, firmicutes, green-sulfur bacteria, fusobacterium and bacteroides, carries out an enzymatic step prior to the formation of pimeloyl-CoA, namely O-methylation of the malonyl group preferentially while on acyl carrier protein. The enzyme is recognizable as a methyltransferase by homology. [Biosynthesis of cofactors, prosthetic groups, and carriers, Biotin]


Pssm-ID: 273953 [Multi-domain]  Cd Length: 240  Bit Score: 38.81  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388 261 DSILHIGCGTGAAgTELLNRQscllygIEKDELLQT-IASPYYEQV----------ISADVETCDLpyPESFFDVILIGD 329
Cdd:TIGR02072  36 ASVLDIGCGTGYL-TRALLKR------FPQAEFIALdISAGMLAQAktklsenvqfICGDAEKLPL--EDSSFDLIVSNL 106

                          90       100
                  ....*....|....*....|....*....
gi 2732496388 330 LLNCSKNPRHTIETLAVYLKPSGSLICSI 358
Cdd:TIGR02072 107 ALQWCDDLSQALSELARVLKPGGLLAFST 135
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
 34-85 8.41e-03

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: 37.07  E-value: 8.41e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2732496388  34 EVIVIDNGSHDGTRDYLKQIT----SIKIFNKT-NEGFAKACNQGLEVASGDNILFL 85
Cdd:cd04187    31 EIIFVDDGSTDRTLEILRELAardpRVKVIRLSrNFGQQAALLAGLDHARGDAVITM 87
rADc smart00650
Ribosomal RNA adenine dimethylases;
252-316 8.84e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 8.84e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2732496388  252 LTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKD----ELLQTIASPYYE-QVISADVETCDLP 316
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGAL-TEELLERAKRVTAIEIDprlaPRLREKFAAADNlTVIHGDALKFDLP 74
 
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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