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Conserved domains on  [gi|2242663361|gb|UQZ73062|]
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methyltransferase domain-containing protein [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];
1-239 3.01e-53

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 177.49  E-value: 3.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS--IKAIFNKTNEGFAKACNQGLEVA 78
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALAFprVRVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLlyqddkigmvgpvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlv 158
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 159 gFCLLVKKKVLDEVGGFDERFvGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFTgnpDLSISQLYEENRQRFIDK 238
Cdd:COG1216   106 -ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFLRK 180

                  .
gi 2242663361 239 W 239
Cdd:COG1216   181 H 181
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
237-361 3.50e-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: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 237 DKWKVDVTTFfdsqpqLTALVPAEAdSILHIGCGTGAaGTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVE 312
Cdd:COG2227     8 DFWDRRLAAL------LARLLPAGG-RVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARERAAELnvdfVQGDLE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2242663361 313 tcDLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 361
Cdd:COG2227    80 --DLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-239 3.01e-53

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 177.49  E-value: 3.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS--IKAIFNKTNEGFAKACNQGLEVA 78
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALAFprVRVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLlyqddkigmvgpvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlv 158
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 159 gFCLLVKKKVLDEVGGFDERFvGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFTgnpDLSISQLYEENRQRFIDK 238
Cdd:COG1216   106 -ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFLRK 180

                  .
gi 2242663361 239 W 239
Cdd:COG1216   181 H 181
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-212 7.90e-49

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: 164.65  E-value: 7.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQ-ITSIKAIFNKTNEGFAKACNQGLEVASGDNIL 84
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRElFPEVRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  85 FLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlRLVGFCLLV 164
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGP----------------------------------------KVSGAFLLV 119
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2242663361 165 KKKVLDEVGGFDERFVGGsFEDDDLSLRVLQAGYQLKIALDSFVHHHG 212
Cdd:cd04186   120 RREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-171 2.78e-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: 98.62  E-value: 2.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS----IKAIFNKTNEGFAKACNQGLEVASG 80
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN-FEIIVVDDGSTDGTVEIAEEYAKkdprVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  81 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYvsgpQQVPVNYTNVEEIEDFSRLYCLQQRGRSKAVLRLVGF 160
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI----FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155
                         170
                  ....*....|.
gi 2242663361 161 CLLVKKKVLDE 171
Cdd:pfam00535 156 FALYRREALEE 166
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
237-361 3.50e-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: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 237 DKWKVDVTTFfdsqpqLTALVPAEAdSILHIGCGTGAaGTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVE 312
Cdd:COG2227     8 DFWDRRLAAL------LARLLPAGG-RVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARERAAELnvdfVQGDLE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2242663361 313 tcDLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 361
Cdd:COG2227    80 --DLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
5-197 7.41e-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: 64.84  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIwkHTNNDCIEVIVIDNGSHDGTRDYLKQ-----ITSIKaifnktneGFAKACNQGLEVAS 79
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADL--QALRGDAEVIVVDGGSTDGTVEIARSlgakvIHSPK--------GRARQMNAGAALAK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  80 GDNILFLNNDTVVTNQWLEPMIKLLYQDDKIGmvGPVSNYVSGPqQVPVNYtnveeIEDFSRLyclqqrgRSKavLRLVG 159
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLEAIRRALAKPGYVA--GAFDLRFDGP-GLLLRL-----IEWGVNL-------RSR--LTGIP 134
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2242663361 160 F---CLLVKKKVLDEVGGFDERFVggsFEDDDLSLRVLQAG 197
Cdd:TIGR04283 135 YgdqGLFVRRSLFEQIGGFPDIPL---MEDIELSRRLRRLG 172
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-108 1.92e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 58.90  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   3 KTSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRD----YLKQITSIKAIfNKTNEGFAKACNQGLEVA 78
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEiakhYAENYPHVRLL-HQANAGVSVARNTGLAVA 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLLYQDD 108
Cdd:PRK10073   85 TGKYVAFPDADDVVYPTMYETLMTMALEDD 114
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
265-357 2.25e-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: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 265 LHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVEtcDLPYPESFFDVILIGDLLNCSKNPRH 340
Cdd:pfam08241   1 LDVGCGTGLL-TELLARLGARVTGVDISPEMLELAREKAPREgltfVVGDAE--DLPFPDNSFDLVLSSEVLHHVEDPER 77
                          90
                  ....*....|....*..
gi 2242663361 341 TIETLAVYLKPSGSLIC 357
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
PRK08317 PRK08317
hypothetical protein; Provisional
253-358 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 2242663361 253 LTALVPAEADSILHIGCGTGAAGTELLNR--QSCLLYGIEKDELLQTIASPYYEQ------VISADVEtcDLPYPESFFD 324
Cdd:PRK08317   12 FELLAVQPGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSEAMLALAKERAAGlgpnveFVRGDAD--GLPFPDGSFD 89
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2242663361 325 VILIGDLLNCSKNPRHTIETLAVYLKPSGSLICS 358
Cdd:PRK08317   90 AVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
264-359 8.62e-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: 44.34  E-value: 8.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 264 ILHIGCGTGAAGTELLNRQSCLLYGIEKDELLQTIASPYYE-------QVISADVETcDLPYPESFFDVILIGDLLNCSK 336
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAalladnvEVLKGDAEE-LPPEADESFDVIISDPPLHHLV 80
                          90       100
                  ....*....|....*....|....
gi 2242663361 337 -NPRHTIETLAVYLKPSGSLICSI 359
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
10-97 8.01e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 44.40  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  10 TYNQLALTKQCLESIWKHTNNDCI--EVIVIDNGSHDGT----RDYLKQ---ITSIKAIFnKTNEGFAKACNQGLEVASG 80
Cdd:NF038302    9 TYNGANRLPEVLERLRSQIGTESLswEIIVVDNNSTDNTaqvvQEYQKNwpsPYPLRYCF-EPQQGAAFARQRAIQEAKG 87
                          90
                  ....*....|....*..
gi 2242663361  81 DNILFLNNDTVVTNQWL 97
Cdd:NF038302   88 ELIGFLDDDNLPAPNWV 104
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
262-419 2.52e-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: 39.58  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 262 DSILHIGCGTGAAgTELLNRQscllygIEKDELLQT-IASPYYEQV----------ISADVETCDLpyPESFFDVILIGD 330
Cdd:TIGR02072  36 ASVLDIGCGTGYL-TRALLKR------FPQAEFIALdISAGMLAQAktklsenvqfICGDAEKLPL--EDSSFDLIVSNL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 331 LLNCSKNPRHTIETLAVYLKPSGSLICSIPNtayADTFFSLLcgASTYTH---FITPRNVNTLFPEYLYDIKSITSHSSD 407
Cdd:TIGR02072 107 ALQWCDDLSQALSELARVLKPGGLLAFSTFG---PGTLHELR--QSFGQHglrYLSLDELKALLKNSFELLTLEEELITL 181
                         170
                  ....*....|..
gi 2242663361 408 TESNIQLFLKEL 419
Cdd:TIGR02072 182 SFDDPLDVLRHL 193
rADc smart00650
Ribosomal RNA adenine dimethylases;
253-317 8.87e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 8.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  253 LTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKD----ELLQTIASPYYE-QVISADVETCDLP 317
Cdd:smart00650   6 VRAANLRPGDTVLEIGPGKGAL-TEELLERAKRVTAIEIDprlaPRLREKFAAADNlTVIHGDALKFDLP 74
 
Name Accession Description Interval E-value
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
1-239 3.01e-53

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 177.49  E-value: 3.01e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS--IKAIFNKTNEGFAKACNQGLEVA 78
Cdd:COG1216     2 RPKVSVVIPTYNRPELLRRCLESLLAQTYPPF-EVIVVDNGSTDGTAELLAALAFprVRVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLlyqddkigmvgpvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlv 158
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------------------------------------------------------- 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 159 gFCLLVKKKVLDEVGGFDERFvGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFTgnpDLSISQLYEENRQRFIDK 238
Cdd:COG1216   106 -ACLLIRREVFEEVGGFDERF-FLYGEDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSG---PLLRAYYLGRNRLLFLRK 180

                  .
gi 2242663361 239 W 239
Cdd:COG1216   181 H 181
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
6-212 7.90e-49

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: 164.65  E-value: 7.90e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQ-ITSIKAIFNKTNEGFAKACNQGLEVASGDNIL 84
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDF-EVIVVDNASTDGSVELLRElFPEVRLIRNGENLGFGAGNNQGIREAKGDYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  85 FLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlRLVGFCLLV 164
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAEQDPDVGIVGP----------------------------------------KVSGAFLLV 119
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2242663361 165 KKKVLDEVGGFDERFVGGsFEDDDLSLRVLQAGYQLKIALDSFVHHHG 212
Cdd:cd04186   120 RREVFEEVGGFDEDFFLY-YEDVDLCLRARLAGYRVLYVPQAVIYHHG 166
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
3-216 6.10e-29

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: 115.61  E-value: 6.10e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   3 KTSIIVLTYNQLALTKQCLESIWKHT-NNDCIEVIVIDNGSHDGTRDYLKQI----TSIKAIFNKTNEGFAKACNQGLEV 77
Cdd:COG1215    30 RVSVIIPAYNEEAVIEETLRSLLAQDyPKEKLEVIVVDDGSTDETAEIARELaaeyPRVRVIERPENGGKAAALNAGLKA 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  78 ASGDNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVGPvsnyvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrl 157
Cdd:COG1215   110 ARGDIVVFLDADTVLDPDWLRRLVAAF-ADPGVGASGA------------------------------------------ 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2242663361 158 vgfCLLVKKKVLDEVGGFDERFVGgsfEDDDLSLRVLQAGYQLKIALDSFVHHHGHATF 216
Cdd:COG1215   147 ---NLAFRREALEEVGGFDEDTLG---EDLDLSLRLLRAGYRIVYVPDAVVYEEAPETL 199
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
6-198 8.76e-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: 105.28  E-value: 8.76e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGT----RDYLKQITSIKAIFNKTNEGFAKACNQGLEVASGD 81
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPN-FEVIVVDDGSTDGTleilEEYAKKDPRVIRVINEENQGLAAARNAGLKAARGE 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  82 NILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYvsgpqqvpvnytnveeiedfsrlyclqqrgrskavlrlvgfc 161
Cdd:cd00761    80 YILFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL------------------------------------------ 117
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2242663361 162 lLVKKKVLDEVGGFDERFVGGsFEDDDLSLRVLQAGY 198
Cdd:cd00761   118 -LFRRELLEEIGGFDEALLSG-EEDDDFLLRLLRGGK 152
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
1-217 6.90e-26

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.40  E-value: 6.90e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   1 MVKTSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS----IKAIFNKTNEGFAKACNQGLE 76
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPD-FEIIVVDDGSTDGTAEILRELAAkdprIRVIRLERNRGKGAARNAGLA 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  77 VASGDNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVgpvsnyvsgpqqvpVNYTNVEEIEDFSRLYCLQQRGRSKAVLR 156
Cdd:COG0463    80 AARGDYIAFLDADDQLDPEKLEELVAAL-EEGPADLV--------------YGSRLIREGESDLRRLGSRLFNLVRLLTN 144
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2242663361 157 L---VGFCLLVKKKVLDEVgGFDERFvggsFEDDDLsLRVLQAGYqlKIALDSFVHHHGHATFT 217
Cdd:COG0463   145 LpdsTSGFRLFRREVLEEL-GFDEGF----LEDTEL-LRALRHGF--RIAEVPVRYRAGESKLN 200
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
5-171 2.78e-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: 98.62  E-value: 2.78e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITS----IKAIFNKTNEGFAKACNQGLEVASG 80
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPN-FEIIVVDDGSTDGTVEIAEEYAKkdprVRVIRLPENRGKAGARNAGLRAATG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  81 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYvsgpQQVPVNYTNVEEIEDFSRLYCLQQRGRSKAVLRLVGF 160
Cdd:pfam00535  80 DYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVI----FGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGG 155
                         170
                  ....*....|.
gi 2242663361 161 CLLVKKKVLDE 171
Cdd:pfam00535 156 FALYRREALEE 166
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
5-205 5.16e-23

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: 97.69  E-value: 5.16e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIWKHT-NNDCIEVIVIDNGSHDGTRDYLKQITS----IKAIFN-KTNEgfAKACNQGLEVA 78
Cdd:cd02525     3 SIIIPVRNEEKYIEELLESLLNQSyPKDLIEIIVVDGGSTDGTREIVQEYAAkdprIRLIDNpKRIQ--SAGLNIGIRNS 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYVSGPQQvpvnyTNVEEIEDfSRLY---CLQQRGRSKAVL 155
Cdd:cd02525    81 RGDIIIRVDAHAVYPKDYILELVEALKRTGADNVGGPMETIGESKFQ-----KAIAVAQS-SPLGsggSAYRGGAVKIGY 154
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 2242663361 156 RLVGFCLLVKKKVLDEVGGFDERFVGGsfEDDDLSLRVLQAGYqlKIALD 205
Cdd:cd02525   155 VDTVHHGAYRREVFEKVGGFDESLVRN--EDAELNYRLRKAGY--KIWLS 200
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
6-186 1.46e-19

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: 85.74  E-value: 1.46e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIwKHTNNDCIEVIVIDNGSHDGTRDYL-----KQITSIKAIFNKTNEGFAKACNQGLEVASG 80
Cdd:cd06423     1 IIVPAYNEEAVIERTIESL-LALDYPKLEVIVVDDGSTDDTLEILeelaaLYIRRVLVVRDKENGGKAGALNAGLRHAKG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  81 DNILFLNNDTVVTNQWLEPMIKLLYQDDKIGMVG-------PVSNYVsgpqqvpvnyTNVEEIEdFSRLYCLQQRGRS-- 151
Cdd:cd06423    80 DIVVVLDADTILEPDALKRLVVPFFADPKVGAVQgrvrvrnGSENLL----------TRLQAIE-YLSIFRLGRRAQSal 148
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2242663361 152 KAVLRLVGFCLLVKKKVLDEVGGFDERFVGgsfED 186
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 ...
5-198 5.64e-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: 79.13  E-value: 5.64e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQITSIKA-IFNKTNEGFAKACNQGLEVASGDNI 83
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPN-IEYIVIDGGSTDGTVDIIKKYEDKITyWISEPDKGIYDAMNKGIALATGDII 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  84 LFLNNDTVvtnqwlepmikllYQDDKIGMVGpvsNYVSGPQQVPVNYTNVEEI-EDFSRLYCLQQRGRSKAVLRLVGFC- 161
Cdd:cd06433    80 GFLNSDDT-------------LLPGALLAVV---AAFAEHPEVDVVYGDVLLVdENGRVIGRRRPPPFLDKFLLYGMPIc 143
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2242663361 162 ---LLVKKKVLDEVGGFDE--RFVGgsfeDDDLSLRVLQAGY 198
Cdd:cd06433   144 hqaTFFRRSLFEKYGGFDEsyRIAA----DYDLLLRLLLAGK 181
GT2_RfbF_like cd02526
RfbF is a putative dTDP-rhamnosyl transferase; Shigella flexneri RfbF protein is a putative ...
7-211 2.53e-16

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: 78.09  E-value: 2.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   7 IVLTYN-QLALTKQCLESIwkhtNNDCIEVIVIDNGSH-DGTRDYLKQITSIKAIFNKTNEGFAKACNQGLEVASGDN-- 82
Cdd:cd02526     2 VVVTYNpDLSKLKELLAAL----AEQVDKVVVVDNSSGnDIELRLRLNSEKIELIHLGENLGIAKALNIGIKAALENGad 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  83 -ILFLNNDTVVTNQWLEPMI---KLLYQDDKIGMVGPVSNYVSGPQQVPvnytnveeiEDFSRLYCLQQRGRSKAVLRLV 158
Cdd:cd02526    78 yVLLFDQDSVPPPDMVEKLLaykILSDKNSNIGAVGPRIIDRRTGENSP---------GVRKSGYKLRIQKEGEEGLKEV 148
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 159 GFCL----LVKKKVLDEVGGFDERFvggsFEDD---DLSLRVLQAGYQLKIALDSFVHHH 211
Cdd:cd02526   149 DFLItsgsLISLEALEKVGGFDEDL----FIDYvdtEWCLRARSKGYKIYVVPDAVLKHE 204
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
5-122 2.02e-13

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: 69.62  E-value: 2.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIwkhtNNDCIEVIVIDNGSHDGTRDYLKQITsIKAIFNKtNEGFAKACNQGLEVASGDNIL 84
Cdd:cd02511     3 SVVIITKNEERNIERCLESV----KWAVDEIIVVDSGSTDRTVEIAKEYG-AKVYQRW-WDGFGAQRNFALELATNDWVL 76
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2242663361  85 FLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSNYVSG 122
Cdd:cd02511    77 SLDADERLTPELADEILALLATDDYDGYYVPRRNFFLG 114
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
5-197 2.04e-13

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: 68.77  E-value: 2.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYN-QLALTKQCLESIWKHTNnDCIEVIVIDNGS-HDGTRDYLKQITS----IKAIFNKTNEGFAKACNQGLEVA 78
Cdd:cd04184     4 SIVMPVYNtPEKYLREAIESVRAQTY-PNWELCIADDAStDPEVKRVLKKYAAqdprIKVVFREENGGISAATNSALELA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWL---------EPMIKLLYQD-DKIGMVGPVSNYVSGPqqvpvnytnveeieDFSRLYCLQQr 148
Cdd:cd04184    83 TGEFVALLDHDDELAPHALyevvkalneHPDADLIYSDeDKIDEGGKRSEPFFKP--------------DWSPDLLLSQ- 147
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2242663361 149 grskavlRLVGFCLLVKKKVLDEVGGFDERFVGGsfEDDDLSLRVLQAG 197
Cdd:cd04184   148 -------NYIGHLLVYRRSLVRQVGGFREGFEGA--QDYDLVLRVSEHT 187
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
20-198 2.67e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 66.16  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  20 CLESIWKHT-NNDCIEVIVIDNGSHDGTRDYL-----KQITSIKAIFN--KTNEGFAKACNQGLEVASGDNILFLNNDTV 91
Cdd:cd04192    15 LLQSLSALDyPKEKFEVILVDDHSTDGTVQILefaaaKPNFQLKILNNsrVSISGKKNALTTAIKAAKGDWIVTTDADCV 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  92 VTNQWLEPMIKlLYQDDKIGMV-GPVSNYvsgpqqvpVNYTNVEEIEDFSRLYCLqqrGRSKAVLRL------VGFCLLV 164
Cdd:cd04192    95 VPSNWLLTFVA-FIQKEQIGLVaGPVIYF--------KGKSLLAKFQRLDWLSLL---GLIAGSFGLgkpfmcNGANMAY 162
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2242663361 165 KKKVLDEVGGFDerfvGGSF---EDDDLSLRVLQAGY 198
Cdd:cd04192   163 RKEAFFEVGGFE----GNDHiasGDDELLLAKVASKY 195
UbiG COG2227
2-polyprenyl-3-methyl-5-hydroxy-6-metoxy-1,4-benzoquinol methylase [Coenzyme transport and ...
237-361 3.50e-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: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 237 DKWKVDVTTFfdsqpqLTALVPAEAdSILHIGCGTGAaGTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVE 312
Cdd:COG2227     8 DFWDRRLAAL------LARLLPAGG-RVLDVGCGTGR-LALALARRGADVTGVDISPEALEIARERAAELnvdfVQGDLE 79
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2242663361 313 tcDLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 361
Cdd:COG2227    80 --DLPLEDGSFDLVICSEVLEHLPDPAALLRELARLLKPGGLLLLSTPN 126
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
6-211 4.03e-12

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: 64.52  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQ-----ITSIKAIFNKtNEGF--AKACNQGLEVA 78
Cdd:cd06420     1 LIITTYNRPEALELVLKSVLNQSILP-FEVIIADDGSTEETKELIEEfksqfPIPIKHVWQE-DEGFrkAKIRNKAIAAA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLLyqDDKIgmvgpvsnYVSGpqqvpvnytnveeiedfSRLY----CLQQRGRSkav 154
Cdd:cd06420    79 KGDYLIFIDGDCIPHPDFIADHIELA--EPGV--------FLSG-----------------SRVLlnekLTERGIRG--- 128
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2242663361 155 lrlvgfC-LLVKKKVLDEVGGFDERFVGGSFEDDDLSLRVLQAGYQLKIALDSFVHHH 211
Cdd:cd06420   129 ------CnMSFWKKDLLAVNGFDEEFTGWGGEDSELVARLLNSGIKFRKLKFAAIVFH 180
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
5-197 7.41e-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: 64.84  E-value: 7.41e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIwkHTNNDCIEVIVIDNGSHDGTRDYLKQ-----ITSIKaifnktneGFAKACNQGLEVAS 79
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADL--QALRGDAEVIVVDGGSTDGTVEIARSlgakvIHSPK--------GRARQMNAGAALAK 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  80 GDNILFLNNDTVVTNQWLEPMIKLLYQDDKIGmvGPVSNYVSGPqQVPVNYtnveeIEDFSRLyclqqrgRSKavLRLVG 159
Cdd:TIGR04283  72 GDILLFLHADTRLPKDFLEAIRRALAKPGYVA--GAFDLRFDGP-GLLLRL-----IEWGVNL-------RSR--LTGIP 134
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2242663361 160 F---CLLVKKKVLDEVGGFDERFVggsFEDDDLSLRVLQAG 197
Cdd:TIGR04283 135 YgdqGLFVRRSLFEQIGGFPDIPL---MEDIELSRRLRRLG 172
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
30-199 2.06e-11

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: 63.75  E-value: 2.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  30 NDCIEVIVIDNGSHDGTRDYLKQI---TSIKAIFNKTNEGfAKA--CNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLL 104
Cdd:cd06421    31 HDKLRVYVLDDGRRPELRALAAELgveYGYRYLTRPDNRH-AKAgnLNNALAHTTGDFVAILDADHVPTPDFLRRTLGYF 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 105 YQDDKIGMVGPVSNYVSGPQQVPVNYTNVEEIEDFsrlYCLQQRGRSkavLRLVGFCL----LVKKKVLDEVGGFDERFV 180
Cdd:cd06421   110 LDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELF---YGVIQPGRD---RWGAAFCCgsgaVVRREALDEIGGFPTDSV 183
                         170
                  ....*....|....*....
gi 2242663361 181 GgsfEDDDLSLRVLQAGYQ 199
Cdd:cd06421   184 T---EDLATSLRLHAKGWR 199
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
7-210 5.70e-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: 61.88  E-value: 5.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   7 IVLTYNQLALTKQCLESIWKHT-NNDciEVIVIDNGSHDGTRDYLKQITSIKAIF---NKTNEGFAKACNQGLEVASGDN 82
Cdd:cd04185     2 VVVTYNRLDLLKECLDALLAQTrPPD--HIIVIDNASTDGTAEWLTSLGDLDNIVylrLPENLGGAGGFYEGVRRAYELG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  83 ---ILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVGPVSNYVSGPqqvpvnytnveeiedFsrlyclqqrgrskavlrlVG 159
Cdd:cd04185    80 ydwIWLMDDDAIPDPDALEKLLAYA-DKDNPQFLAPLVLDPDGS---------------F------------------VG 125
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2242663361 160 FclLVKKKVLDEVGGFDERFvggsF--EDD-DLSLRVLQAGYQLKIaLDSFVHH 210
Cdd:cd04185   126 V--LISRRVVEKIGLPDKEF----FiwGDDtEYTLRASKAGPGIYV-PDAVVVH 172
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
33-196 3.13e-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: 60.75  E-value: 3.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  33 IEVIVIDNGShdgTRDYLKQITSIKAI--------FNKTNEGFAKACNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLL 104
Cdd:pfam10111  30 FELIIINDGS---TDKTLEEVSSIKDHnlqvyypnAPDTTYSLAASRNRGTSHAIGEYISFIDGDCLWSPDKFEKQLKIA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 105 yqddkigMVGPVSNYVSGPQQVPVNYTNVEEIEDFSRLYCLQQRGRskaVLR--------LVGFCL------LVKKKVLD 170
Cdd:pfam10111 107 -------TSLALQENIQAAVVLPVTDLNDESSNFLRRGGDLTASGD---VLRdllvfyspLAIFFApnssnaLINRQAFI 176
                         170       180
                  ....*....|....*....|....*.
gi 2242663361 171 EVGGFDERFVGGSFEDDDLSLRVLQA 196
Cdd:pfam10111 177 EVGGFDESFRGHGAEDFDIFLRLAAR 202
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
4-237 4.23e-10

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: 59.69  E-value: 4.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   4 TSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRDYLKQI------TSIKAIFNKTNEG---FAKACNQG 74
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYPP-VEVVVVVNPSDAETLDVAEEIaarfpdVRLRVIRNARLLGptgKSRGLNHG 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  75 LEVASGDNILFLNNDTVV---TNQWLEPmiklLYQDDKIGMVGpVSNYVSGPQQVPVNYTNVEEIEDFSRLYCLQQRGRs 151
Cdd:pfam13641  83 FRAVKSDLVVLHDDDSVLhpgTLKKYVQ----YFDSPKVGAVG-TPVFSLNRSTMLSALGALEFALRHLRMMSLRLALG- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 152 kaVLRLVGFCLLVKKKVLDEVGGFDERFVGGsfEDDDLSLRVLQAGYQLKIALDSFVHHHGHATFtgnpdlsisQLYEEN 231
Cdd:pfam13641 157 --VLPLSGAGSAIRREVLKELGLFDPFFLLG--DDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYL---------AASIKQ 223

                  ....*.
gi 2242663361 232 RQRFID 237
Cdd:pfam13641 224 RARWVY 229
UbiE COG2226
Ubiquinone/menaquinone biosynthesis C-methylase UbiE/MenG [Coenzyme transport and metabolism]; ...
253-372 8.90e-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: 8.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 253 LTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYE------QVISADVEtcDLPYPESFFDVI 326
Cdd:COG2226    15 LAALGLRPGARVLDLGCGTGRL-ALALAERGARVTGVDISPEMLELARERAAeaglnvEFVVGDAE--DLPFPDGSFDLV 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2242663361 327 LIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPNTAYADTFFSLL 372
Cdd:COG2226    92 ISSFVLHHLPDPERALAEIARVLKPGGRLVVVDFSPPDLAELEELL 137
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
5-192 9.38e-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: 58.35  E-value: 9.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIwKHTNNDCIEVIVIDNGSHDGTRDylkQITSIKAIFNKTNEGFAKACNQGLEVASGDNIL 84
Cdd:cd02522     2 SIIIPTLNEAENLPRLLASL-RRLNPLPLEIIVVDGGSTDGTVA---IARSAGVVVISSPKGRARQMNAGAAAARGDWLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  85 FLNNDTVVTNQWLEPMIKLLYQDDKIGMVGPVSnyvsgpqqvpvnytnveeIEDFSRLYclqqRGRSKAV-LRLVGF--- 160
Cdd:cd02522    78 FLHADTRLPPDWDAAIIETLRADGAVAGAFRLR------------------FDDPGPRL----RLLELGAnLRSRLFglp 135
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2242663361 161 ----CLLVKKKVLDEVGGFDERFVggsFEDDDLSLR 192
Cdd:cd02522   136 ygdqGLFIRRELFEELGGFPELPL---MEDVELVRR 168
PRK10073 PRK10073
putative glycosyl transferase; Provisional
3-108 1.92e-09

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 58.90  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   3 KTSIIVLTYNQLALTKQCLESIWKHTNNDcIEVIVIDNGSHDGTRD----YLKQITSIKAIfNKTNEGFAKACNQGLEVA 78
Cdd:PRK10073    7 KLSIIIPLYNAGKDFRAFMESLIAQTWTA-LEIIIVNDGSTDNSVEiakhYAENYPHVRLL-HQANAGVSVARNTGLAVA 84
                          90       100       110
                  ....*....|....*....|....*....|
gi 2242663361  79 SGDNILFLNNDTVVTNQWLEPMIKLLYQDD 108
Cdd:PRK10073   85 TGKYVAFPDADDVVYPTMYETLMTMALEDD 114
Methyltransf_11 pfam08241
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
265-357 2.25e-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: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 265 LHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYEQV----ISADVEtcDLPYPESFFDVILIGDLLNCSKNPRH 340
Cdd:pfam08241   1 LDVGCGTGLL-TELLARLGARVTGVDISPEMLELAREKAPREgltfVVGDAE--DLPFPDNSFDLVLSSEVLHHVEDPER 77
                          90
                  ....*....|....*..
gi 2242663361 341 TIETLAVYLKPSGSLIC 357
Cdd:pfam08241  78 ALREIARVLKPGGILII 94
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
34-209 9.49e-09

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: 55.87  E-value: 9.49e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  34 EVIVIDNGSHDgtrDYLKQitSIKAIFNKTNEGF------------AKACNQGLEVASGDN--ILFLNNDTVVTNQWLEP 99
Cdd:cd06435    30 EVIVIDNNTKD---EALWK--PVEAHCAQLGERFrffhveplpgakAGALNYALERTAPDAeiIAVIDADYQVEPDWLKR 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 100 MIKLlYQDDKIGMVgpvsnyvsgpqQVPVNYTNVEEIEDFSRLYC---------LQQRGRSKAVLRlVGFCLLVKKKVLD 170
Cdd:cd06435   105 LVPI-FDDPRVGFV-----------QAPQDYRDGEESLFKRMCYAeykgffdigMVSRNERNAIIQ-HGTMCLIRRSALD 171
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2242663361 171 EVGGFDERFVggsFEDDDLSLRVLQAGYQLKIALDSFVH 209
Cdd:cd06435   172 DVGGWDEWCI---TEDSELGLRMHEAGYIGVYVAQSYGH 207
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
5-113 2.14e-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: 54.56  E-value: 2.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYN-QLALTKQcLESIWKHTNNDCiEVIVIDNGSHDGTRDYLKQITS-----IKAIFNKTNEGFAKACNQGLEVA 78
Cdd:cd04196     1 AVLMATYNgEKYLREQ-LDSILAQTYKND-ELIISDDGSTDGTVEIIKEYIDkdpfiIILIRNGKNLGVARNFESLLQAA 78
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2242663361  79 SGDNILFLNNDTVvtnqW----LEPMIKLLYQDDKIGMV 113
Cdd:cd04196    79 DGDYVFFCDQDDI----WlpdkLERLLKAFLKDDKPLLV 113
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
5-143 3.91e-08

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: 54.13  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESI----WKhtnNDCIEVIVIDNGSHDGT----RDYLKQitSIKAIFNKTNEGFAKACNQGLE 76
Cdd:cd06439    32 TIIIPAYNEEAVIEAKLENLlaldYP---RDRLEIIVVSDGSTDGTaeiaREYADK--GVKLLRFPERRGKAAALNRALA 106
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  77 VASGDNILFlnndTVVTNQWLEPMIKLL---YQDDKIGmvgpvsnYVSGpQQVPVNYTNVEEIEDFSRLY 143
Cdd:cd06439   107 LATGEIVVF----TDANALLDPDALRLLvrhFADPSVG-------AVSG-ELVIVDGGGSGSGEGLYWKY 164
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
83-209 5.48e-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: 5.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  83 ILFLNNDTVVTNQWLEpMIKLLYQDDKIGMVgpvsnyvSGPQQVPVNYTNVEEIEDFSRLY----CLQQRGRSKAVLRLV 158
Cdd:pfam13632   2 ILLLDADTVLPPDCLL-GIANEMASPEVAII-------QGPILPMNVGNYLEELAALFFADdhgkSIPVRMALGRVLPFV 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2242663361 159 GFCLLVKKKVLDEVGGFDERFVGgsfEDDDLSLRVLQAGYQLKIALDSFVH 209
Cdd:pfam13632  74 GSGAFLRRSALQEVGGWDDGSVS---EDFDFGLRLQRAGYRVRFAPYSAVY 121
COG4976 COG4976
Predicted methyltransferase, contains TPR repeat [General function prediction only];
250-370 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 2242663361 250 QPQLTALVPAEADSILHIGCGTGAAGTELLNRQSCLLyGIEKDE--LLQTIASPYYEQVISADVetCDLPYPESFFDVIL 327
Cdd:COG4976    36 EELLARLPPGPFGRVLDLGCGTGLLGEALRPRGYRLT-GVDLSEemLAKAREKGVYDRLLVADL--ADLAEPDGRFDLIV 112
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2242663361 328 IGDLLNCSKNPRHTIETLAVYLKPSGSLICSIpNTAYADTFFS 370
Cdd:COG4976   113 AADVLTYLGDLAAVFAGVARALKPGGLFIFSV-EDADGSGRYA 154
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
34-239 3.42e-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: 51.82  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  34 EVIVIDNGShdgTRDYLKQ---------ITSIKAIFNKTNEGFAKACNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLL 104
Cdd:cd02510    32 EIILVDDFS---DKPELKLlleeyykkyLPKVKVLRLKKREGLIRARIAGARAATGDVLVFLDSHCEVNVGWLEPLLARI 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 105 YQDDKIgMVGPVSNyvsgpqqvPVNYTNVEEIE-------------DFSRLYCLQQ-RGRSKAVL-----RLVGFCLLVK 165
Cdd:cd02510   109 AENRKT-VVCPIID--------VIDADTFEYRGssgdarggfdwslHFKWLPLPEEeRRRESPTApirspTMAGGLFAID 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 166 KKVLDEVGGFDE--RFVGG-SFEdddLSLRVLQAGYQLKIALDSFVHH---HGHATFTGNPDlsiSQLYEENRQRFIDKW 239
Cdd:cd02510   180 REWFLELGGYDEgmDIWGGeNLE---LSFKVWQCGGSIEIVPCSRVGHifrRKRKPYTFPGG---SGTVLRNYKRVAEVW 253
Tam COG4106
Trans-aconitate methyltransferase [Energy production and conversion];
260-358 8.41e-07

Trans-aconitate methyltransferase [Energy production and conversion];


Pssm-ID: 443282 [Multi-domain]  Cd Length: 100  Bit Score: 47.13  E-value: 8.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 260 EADSILHIGCGTGAAGTELLNR-QSCLLYGIEKDELLQTIASPYYEQV--ISADVETCDLPYPesfFDVILIGDLLNCSK 336
Cdd:COG4106     1 PPRRVLDLGCGTGRLTALLAERfPGARVTGVDLSPEMLARARARLPNVrfVVADLRDLDPPEP---FDLVVSNAALHWLP 77
                          90       100
                  ....*....|....*....|..
gi 2242663361 337 NPRHTIETLAVYLKPSGSLICS 358
Cdd:COG4106    78 DHAALLARLAAALAPGGVLAVQ 99
Glyco_tranf_2_5 pfam13712
Glycosyltransferase like family; Members of this family of prokaryotic proteins include ...
68-239 9.21e-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: 9.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  68 AKACNQGLEVASGDNILFLNNDTVVTN-QWLEPMIKLLYQDDKIGMVGpvsnyVSGPQQVPVN---------YTNVEEIE 137
Cdd:pfam13712  42 AAAYNEAMSASDAKYKVYIHQDVFIINkDFIEDLLSIFKKDPSIGMIG-----VVGAQSLPDSgvwwessykVGKVYVPS 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 138 DFSRLYCLQQRGRSK--AVLRLVGFCLLVKKKVldevgGFDE-RFVGGSFEDDDLSLRVLQAGYQLKIALDS---FVHHH 211
Cdd:pfam13712 117 KDESYLLRQGEAEGKyeEVEAIDGLFMATQYDI-----PWREdLFDGWHFYDVSQSLEFRRAGYKVVVPYQEkpwCIHDC 191
                         170       180
                  ....*....|....*....|....*...
gi 2242663361 212 GHATFTGnpdlsisqlYEENRQRFIDKW 239
Cdd:pfam13712 192 GFLNLDN---------YEKYRKIFLKEY 210
PRK08317 PRK08317
hypothetical protein; Provisional
253-358 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 2242663361 253 LTALVPAEADSILHIGCGTGAAGTELLNR--QSCLLYGIEKDELLQTIASPYYEQ------VISADVEtcDLPYPESFFD 324
Cdd:PRK08317   12 FELLAVQPGDRVLDVGCGPGNDARELARRvgPEGRVVGIDRSEAMLALAKERAAGlgpnveFVRGDAD--GLPFPDGSFD 89
                          90       100       110
                  ....*....|....*....|....*....|....
gi 2242663361 325 VILIGDLLNCSKNPRHTIETLAVYLKPSGSLICS 358
Cdd:PRK08317   90 AVRSDRVLQHLEDPARALAEIARVLRPGGRVVVL 123
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
34-86 1.51e-06

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: 48.34  E-value: 1.51e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2242663361  34 EVIVIDNGSHDGTRDYLKQI----TSIKAIFNKTNEGFAKACNQGLEVASGDNILFL 86
Cdd:cd04179    30 EIIVVDDGSTDGTAEIARELaarvPRVRVIRLSRNFGKGAAVRAGFKAARGDIVVTM 86
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
4-206 3.15e-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: 48.02  E-value: 3.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   4 TSIIVLTYNQ-LALTKQCLESIWKhtnNDCIEVIVIDNGSHDGTRDYLKQITSIKAIFNKT--NEGFAKACNQGLEVASG 80
Cdd:cd06434     2 VTVIIPVYDEdPDVFRECLRSILR---QKPLEIIVVTDGDDEPYLSILSQTVKYGGIFVITvpHPGKRRALAEGIRHVTT 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  81 DNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMVGPVSNyVSGPQQVPVNYTNVEEIEdfsRLYCLQQRGRSK--AVLRLV 158
Cdd:cd06434    79 DIVVLLDSDTVWPPNALPEMLKPF-EDPKVGGVGTNQR-ILRPRDSKWSFLAAEYLE---RRNEEIRAAMSYdgGVPCLS 153
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2242663361 159 GFCLLVKKKVLDEV----GGFDERFVGGSFE-DDDLSL--RVLQAGYQLKIALDS 206
Cdd:cd06434   154 GRTAAYRTEILKDFlfleEFTNETFMGRRLNaGDDRFLtrYVLSHGYKTVYQYTS 208
Methyltransf_25 pfam13649
Methyltransferase domain; This family appears to be a methyltransferase domain.
264-353 4.82e-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: 4.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 264 ILHIGCGTGAAGTELLNRQSCLLYGIEKDELLQTIASPYYE------QVISADVEtcDLPYPESFFDVILIGDLLNC--S 335
Cdd:pfam13649   1 VLDLGCGTGRLTLALARRGGARVTGVDLSPEMLERARERAAeaglnvEFVQGDAE--DLPFPDGSFDLVVSSGVLHHlpD 78
                          90
                  ....*....|....*...
gi 2242663361 336 KNPRHTIETLAVYLKPSG 353
Cdd:pfam13649  79 PDLEAALREIARVLKPGG 96
AdoMet_MTases cd02440
S-adenosylmethionine-dependent methyltransferases (SAM or AdoMet-MTase), class I; ...
264-359 8.62e-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: 44.34  E-value: 8.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 264 ILHIGCGTGAAGTELLNRQSCLLYGIEKDELLQTIASPYYE-------QVISADVETcDLPYPESFFDVILIGDLLNCSK 336
Cdd:cd02440     2 VLDLGCGTGALALALASGPGARVTGVDISPVALELARKAAAalladnvEVLKGDAEE-LPPEADESFDVIISDPPLHHLV 80
                          90       100
                  ....*....|....*....|....
gi 2242663361 337 -NPRHTIETLAVYLKPSGSLICSI 359
Cdd:cd02440    81 eDLARFLEEARRLLKPGGVLVLTL 104
MetW pfam07021
Methionine biosynthesis protein MetW; This family consists of several bacterial and one ...
264-384 1.25e-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: 1.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 264 ILHIGCGTGAAGTELLNRQSCLLYGIEKDE--LLQTIASPYYeqVISADVETCDLPYPESFFDVILIGDLLNCSKNPRHT 341
Cdd:pfam07021  17 VLDLGCGDGTLLYLLKEEKGVDGYGIELDAagVAECVAKGLY--VIQGDLDEGLEHFPDKSFDYVILSQTLQATRNPREV 94
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2242663361 342 IETLavyLKPSGSLICSIPNTAYADTFFSLLCGAST-------YTHFITP 384
Cdd:pfam07021  95 LDEM---LRIGRRCIVSFPNFGHWRVRWSLLSRGRMpvtdllpYTWYNTP 141
Methyltransf_12 pfam08242
Methyltransferase domain; Members of this family are SAM dependent methyltransferases.
265-355 1.34e-05

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


Pssm-ID: 400515 [Multi-domain]  Cd Length: 98  Bit Score: 43.51  E-value: 1.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 265 LHIGCGTGAAGTELLNRQSCL-LYGIEKDELLQTIASPYYEQVISADVETCDLPYPESF------FDVILIGDLLNCSKN 337
Cdd:pfam08242   1 LEIGCGTGTLLRALLEALPGLeYTGLDISPAALEAARERLAALGLLNAVRVELFQLDLGeldpgsFDVVVASNVLHHLAD 80
                          90
                  ....*....|....*...
gi 2242663361 338 PRHTIETLAVYLKPSGSL 355
Cdd:pfam08242  81 PRAVLRNIRRLLKPGGVL 98
Methyltransf_23 pfam13489
Methyltransferase domain; This family appears to be a methyltransferase domain.
228-361 1.59e-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: 1.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 228 YEENRQRFIDKWKvdvttffdsqpQLTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKDELLQTIASPYYEQVI 307
Cdd:pfam13489   1 YAHQRERLLADLL-----------LRLLPKLPSPGRVLDFGCGTGIF-LRLLRAQGFSVTGVDPSPIAIERALLNVRFDQ 68
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2242663361 308 SADVEtcdLPYPESFFDVILIGDLLNCSKNPRHTIETLAVYLKPSGSLICSIPN 361
Cdd:pfam13489  69 FDEQE---AAVPAGKFDVIVAREVLEHVPDPPALLRQIAALLKPGGLLLLSTPL 119
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
69-213 3.12e-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: 3.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  69 KACN--QGLEVASGDNILFLNNDTVVTNQWLEPMIKLLyQDDKIGMV-GPVsnYVSGPQQVPVNYTNVEeIEDFSRLYCL 145
Cdd:pfam13506  18 KVNNllQGLEAAKYDLLVISDSDIRVPPDYLRDLLAPL-ADPKVGLVtSPP--VGSDPKGLAAALEAAF-FNTLAGVLQA 93
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2242663361 146 QQRGRSKAVlrlvGFCLLVKKKVLDEVGGFdERFVGGSFEDDDLSLRVLQAGYQLKIALDSFVHHHGH 213
Cdd:pfam13506  94 ALSGIGFAV----GMSMAFRRADLERIGGF-EALADYLAEDYALGKLLRAAGLKVVLSPRPILQTSGP 156
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
1-89 7.49e-05

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 44.30  E-value: 7.49e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   1 MVKTSIIVLTYNQ---LALTKQCLESIWKHTNNdcIEVIVIDNGSHDGTRDYLKQitsIKAIFNKTN---------EGFA 68
Cdd:PLN02726    8 AMKYSIIVPTYNErlnIALIVYLIFKALQDVKD--FEIIVVDDGSPDGTQDVVKQ---LQKVYGEDRillrprpgkLGLG 82
                          90       100
                  ....*....|....*....|.
gi 2242663361  69 KACNQGLEVASGDNILFLNND 89
Cdd:PLN02726   83 TAYIHGLKHASGDFVVIMDAD 103
EPS_HpsE NF038302
hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;
10-97 8.01e-05

hormogonium polysaccharide biosynthesis glycosyltransferase HpsE;


Pssm-ID: 439602 [Multi-domain]  Cd Length: 307  Bit Score: 44.40  E-value: 8.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  10 TYNQLALTKQCLESIWKHTNNDCI--EVIVIDNGSHDGT----RDYLKQ---ITSIKAIFnKTNEGFAKACNQGLEVASG 80
Cdd:NF038302    9 TYNGANRLPEVLERLRSQIGTESLswEIIVVDNNSTDNTaqvvQEYQKNwpsPYPLRYCF-EPQQGAAFARQRAIQEAKG 87
                          90
                  ....*....|....*..
gi 2242663361  81 DNILFLNNDTVVTNQWL 97
Cdd:NF038302   88 ELIGFLDDDNLPAPNWV 104
Methyltransf_31 pfam13847
Methyltransferase domain; This family appears to have methyltransferase activity.
260-361 1.11e-04

Methyltransferase domain; This family appears to have methyltransferase activity.


Pssm-ID: 463998 [Multi-domain]  Cd Length: 150  Bit Score: 42.40  E-value: 1.11e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 260 EADSILHIGCGTGAAGTEL--LNRQSCLLYGIEKDELL-----QTIASPYYEQV--ISADVETCDLPYPESFFDVILIGD 330
Cdd:pfam13847   3 KGMRVLDLGCGTGHLSFELaeELGPNAEVVGIDISEEAiekarENAQKLGFDNVefEQGDIEELPELLEDDKFDVVISNC 82
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2242663361 331 LLNCSKNPRHTIETLAVYLKPSGSLICSIPN 361
Cdd:pfam13847  83 VLNHIPDPDKVLQEILRVLKPGGRLIISDPD 113
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
34-89 1.36e-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: 42.94  E-value: 1.36e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2242663361  34 EVIVIDNGSHDGTRDYLKQI-----TSIKAIFNKTNEGFAKACNQGLEVASGDNILFLNND 89
Cdd:cd04188    32 EIIVVDDGSKDGTAEVARKLarknpALIRVLTLPKNRGKGGAVRAGMLAARGDYILFADAD 92
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
6-95 1.88e-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: 42.83  E-value: 1.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIWKHTNNDCIEVIVIDNGSHDGT-------RDYLKQITSIKAIFNKTNE-----GFAKacNQ 73
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGTLELSVFNDASTDKSaeiiekwRKKLEDSGVIVLVGSHNSPspkgvGYAK--NQ 78
                          90       100
                  ....*....|....*....|..
gi 2242663361  74 GLEVASGDNILFLNNDTVVTNQ 95
Cdd:cd06913    79 AIAQSSGRYLCFLDSDDVMMPQ 100
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
34-86 2.04e-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: 42.08  E-value: 2.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2242663361  34 EVIVIDNGSHDGTRDYLKQIT----SIKAIFNKTNEGFAKACNQGLEVASGDNILFL 86
Cdd:cd04187    31 EIIFVDDGSTDRTLEILRELAardpRVKVIRLSRNFGQQAALLAGLDHARGDAVITM 87
TrmN6 COG4123
tRNA1(Val) A37 N6-methylase TrmN6 [Translation, ribosomal structure and biogenesis]; tRNA1(Val) ...
253-327 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 2242663361 253 LTALVPAE-ADSILHIGCGTGAAGTELLNR-QSCLLYGIEKDELLQTIA------SPYYEQ--VISADVETCDLPYPESF 322
Cdd:COG4123    29 LAAFAPVKkGGRVLDLGTGTGVIALMLAQRsPGARITGVEIQPEAAELArrnvalNGLEDRitVIHGDLKEFAAELPPGS 108

                  ....*
gi 2242663361 323 FDVIL 327
Cdd:COG4123   109 FDLVV 113
BioC TIGR02072
malonyl-acyl carrier protein O-methyltransferase BioC; This enzyme, which is found in biotin ...
262-419 2.52e-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: 39.58  E-value: 2.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 262 DSILHIGCGTGAAgTELLNRQscllygIEKDELLQT-IASPYYEQV----------ISADVETCDLpyPESFFDVILIGD 330
Cdd:TIGR02072  36 ASVLDIGCGTGYL-TRALLKR------FPQAEFIALdISAGMLAQAktklsenvqfICGDAEKLPL--EDSSFDLIVSNL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361 331 LLNCSKNPRHTIETLAVYLKPSGSLICSIPNtayADTFFSLLcgASTYTH---FITPRNVNTLFPEYLYDIKSITSHSSD 407
Cdd:TIGR02072 107 ALQWCDDLSQALSELARVLKPGGLLAFSTFG---PGTLHELR--QSFGQHglrYLSLDELKALLKNSFELLTLEEELITL 181
                         170
                  ....*....|..
gi 2242663361 408 TESNIQLFLKEL 419
Cdd:TIGR02072 182 SFDDPLDVLRHL 193
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
5-113 2.77e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 39.75  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   5 SIIVLTYNQLALTKQCLESIWKHTNNDC-------IEVIVIDNGSHDGT--------RDYLKQITSIKAIFNKTNEGFAK 69
Cdd:PTZ00260   73 SIVIPAYNEEDRLPKMLKETIKYLESRSrkdpkfkYEIIIVNDGSKDKTlkvakdfwRQNINPNIDIRLLSLLRNKGKGG 152
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2242663361  70 ACNQGLEVASGDNILFLNNDTVVTNQWLEPMIKLLYQDDK--IGMV 113
Cdd:PTZ00260  153 AVRIGMLASRGKYILMVDADGATDIDDFDKLEDIMLKIEQngLGIV 198
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
6-81 6.44e-03

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: 37.90  E-value: 6.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361   6 IIVLTYNQLALTKQCLESIWKHTNNDCIEVIVIDNGSHDGTRDYLKQITS----IKAIFNKTNEGFAKACNQGLEVASGD 81
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKGIDYEIIVVDDNSPDGTAEIVRELAKeyprVRLIVRPGKRGLGSAYIEGFKAARGD 80
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
18-198 8.65e-03

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: 37.29  E-value: 8.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  18 KQCLESIWKHT-NNDciEVIVIDNG----SHDGTRDYLKQITSIKAIFNKTNEGFAKACNQGLEVASGDNILFLNNDTVV 92
Cdd:cd04195    16 REALESILKQTlPPD--EVVLVKDGpvtqSLNEVLEEFKRKLPLKVVPLEKNRGLGKALNEGLKHCTYDWVARMDTDDIS 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  93 TNQWLEPMIKLLYQDDKIGMVGP-VSNYVSGPQQVpVNYTNVE---EIEDFSRLYCLQQRGrskavlrlvgfCLLVKKKV 168
Cdd:cd04195    94 LPDRFEKQLDFIEKNPEIDIVGGgVLEFDSDGNDI-GKRRLPTshdDILKFARRRSPFNHP-----------TVMFRKSK 161
                         170       180       190
                  ....*....|....*....|....*....|.
gi 2242663361 169 LDEVGGF-DERFVggsfEDDDLSLRVLQAGY 198
Cdd:cd04195   162 VLAVGGYqDLPLV----EDYALWARMLANGA 188
rADc smart00650
Ribosomal RNA adenine dimethylases;
253-317 8.87e-03

Ribosomal RNA adenine dimethylases;


Pssm-ID: 128898  Cd Length: 169  Bit Score: 37.11  E-value: 8.87e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2242663361  253 LTALVPAEADSILHIGCGTGAAgTELLNRQSCLLYGIEKD----ELLQTIASPYYE-QVISADVETCDLP 317
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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