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Conserved domains on  [gi|983222625|gb|KWU62838|]
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glycosyl transferase family 2 [Bacillus cereus]

Protein Classification

glycosyltransferase( domain architecture ID 11440269)

glycosyltransferase catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
17-197 9.10e-32

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


:

Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 118.31  E-value: 9.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASevY-KEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDKNLSKI--RNAGA 89
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQD--YpKEKLEVIVVDDGSTDETAEIARELaaeyPRVRVIERPENGGKAaaLNAGL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  90 EIASGEIIVTIDADTIMTESVLSNVDKYLSSGKYIGGGVNGklermsfgiffsamliiipllfkygavsvgifwCYRKD- 168
Cdd:COG1215  108 KAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL---------------------------------AFRREa 154
                        170       180
                 ....*....|....*....|....*....
gi 983222625 169 FMAINGFNENMLmAEDADFAKRLKEWGKR 197
Cdd:COG1215  155 LEEVGGFDEDTL-GEDLDLSLRLLRAGYR 182
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
17-197 9.10e-32

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 118.31  E-value: 9.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASevY-KEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDKNLSKI--RNAGA 89
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQD--YpKEKLEVIVVDDGSTDETAEIARELaaeyPRVRVIERPENGGKAaaLNAGL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  90 EIASGEIIVTIDADTIMTESVLSNVDKYLSSGKYIGGGVNGklermsfgiffsamliiipllfkygavsvgifwCYRKD- 168
Cdd:COG1215  108 KAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL---------------------------------AFRREa 154
                        170       180
                 ....*....|....*....|....*....
gi 983222625 169 FMAINGFNENMLmAEDADFAKRLKEWGKR 197
Cdd:COG1215  155 LEEVGGFDEDTL-GEDLDLSLRLLRAGYR 182
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
17-197 1.90e-29

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: 110.78  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAkASEVYKEQTEVIVVLNRCTDQTEEIAKSY----NCITL-KNDDKNLSKIRNAGAEI 91
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLL-NQSYPKDLIEIIVVDGGSTDGTREIVQEYaakdPRIRLiDNPKRIQSAGLNIGIRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  92 ASGEIIVTIDADTIMTES-VLSNVDKYLSSGKYIGGGVN-----GKLERmSFGIFFSAMLIIIPLLFKYGA-----VSVG 160
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDyILELVEALKRTGADNVGGPMetigeSKFQK-AIAVAQSSPLGSGGSAYRGGAvkigyVDTV 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 983222625 161 IFWCYRKD-FMAINGFNENMLMAEDADFAKRLKEWGKR 197
Cdd:cd02525  159 HHGAYRREvFEKVGGFDESLVRNEDAELNYRLRKAGYK 196
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
19-247 3.69e-25

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: 98.74  E-value: 3.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   19 SIIIPAHNEEKYIRKCLDSIAkaseVYKEQTEVIVVLNRCTDQTEEIAKSYNCITLKNDdKNLSKIRNAGAEIASGEIIV 98
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADLQ----ALRGDAEVIVVDGGSTDGTVEIARSLGAKVIHSP-KGRARQMNAGAALAKGDILL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   99 TIDADTIMTESVLSNVDKYLSSGKYIGGG----VNGKLERMSFGIFFSAM---LIIIPllfkYGavSVGIFwCYRKDFMA 171
Cdd:TIGR04283  77 FLHADTRLPKDFLEAIRRALAKPGYVAGAfdlrFDGPGLLLRLIEWGVNLrsrLTGIP----YG--DQGLF-VRRSLFEQ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983222625  172 INGFNENMLMaEDADFAKRLKEWGkrnnkKFGTIKNGMITSCRRFDTYGDWAL-LKNPKVILAYLKGNDQKYADKTY 247
Cdd:TIGR04283 150 IGGFPDIPLM-EDIELSRRLRRLG-----RLAILPAPVVTSARRWEKNGILRTiLLNWRLRLLYRLGVSPEELARLY 220
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
19-168 4.32e-19

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: 81.29  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   19 SIIIPAHNEEKYIRKCLDSIAKAsevYKEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDKNLSKI--RNAGAEIA 92
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQ---TYPNFEIIVVDDGSTDGTVEIAEEYakkdPRVRVIRLPENRGKAgaRNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   93 SGEIIVTIDADTIMTESVLSNV-------DKYLSSGKYIGGGVNGKLERMSFGIFFSAMLIIIPLLFKYGAVSVGIFWC- 164
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLvealeedGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFa 157

                  ....*
gi 983222625  165 -YRKD 168
Cdd:pfam00535 158 lYRRE 162
PRK10073 PRK10073
putative glycosyl transferase; Provisional
17-106 2.51e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 53.51  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASEvykEQTEVIVVLNRCTDQTEEIAKSY-----NCITLKNDDKNLSKIRNAGAEI 91
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTW---TALEIIIVNDGSTDNSVEIAKHYaenypHVRLLHQANAGVSVARNTGLAV 83
                         90
                 ....*....|....*
gi 983222625  92 ASGEIIVTIDADTIM 106
Cdd:PRK10073  84 ATGKYVAFPDADDVV 98
 
Name Accession Description Interval E-value
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
17-197 9.10e-32

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


Pssm-ID: 440828 [Multi-domain]  Cd Length: 303  Bit Score: 118.31  E-value: 9.10e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASevY-KEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDKNLSKI--RNAGA 89
Cdd:COG1215   30 RVSVIIPAYNEEAVIEETLRSLLAQD--YpKEKLEVIVVDDGSTDETAEIARELaaeyPRVRVIERPENGGKAaaLNAGL 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  90 EIASGEIIVTIDADTIMTESVLSNVDKYLSSGKYIGGGVNGklermsfgiffsamliiipllfkygavsvgifwCYRKD- 168
Cdd:COG1215  108 KAARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGASGANL---------------------------------AFRREa 154
                        170       180
                 ....*....|....*....|....*....
gi 983222625 169 FMAINGFNENMLmAEDADFAKRLKEWGKR 197
Cdd:COG1215  155 LEEVGGFDEDTL-GEDLDLSLRLLRAGYR 182
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
17-197 1.90e-29

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: 110.78  E-value: 1.90e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAkASEVYKEQTEVIVVLNRCTDQTEEIAKSY----NCITL-KNDDKNLSKIRNAGAEI 91
Cdd:cd02525    1 FVSIIIPVRNEEKYIEELLESLL-NQSYPKDLIEIIVVDGGSTDGTREIVQEYaakdPRIRLiDNPKRIQSAGLNIGIRN 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  92 ASGEIIVTIDADTIMTES-VLSNVDKYLSSGKYIGGGVN-----GKLERmSFGIFFSAMLIIIPLLFKYGA-----VSVG 160
Cdd:cd02525   80 SRGDIIIRVDAHAVYPKDyILELVEALKRTGADNVGGPMetigeSKFQK-AIAVAQSSPLGSGGSAYRGGAvkigyVDTV 158
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 983222625 161 IFWCYRKD-FMAINGFNENMLMAEDADFAKRLKEWGKR 197
Cdd:cd02525  159 HHGAYRREvFEKVGGFDESLVRNEDAELNYRLRKAGYK 196
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
19-247 1.46e-27

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: 105.35  E-value: 1.46e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  19 SIIIPAHNEEKYIRKCLDSIAKASEVykeQTEVIVVLNRCTDQTEEIAKSYNCITLkNDDKNLSKIRNAGAEIASGEIIV 98
Cdd:cd02522    2 SIIIPTLNEAENLPRLLASLRRLNPL---PLEIIVVDGGSTDGTVAIARSAGVVVI-SSPKGRARQMNAGAAAARGDWLL 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  99 TIDADTIMTESVLSNVDKYLSSGKYIGGGVNGKLER-------MSFGIFFSAMLIIIPllfkYGavSVGIFwCYRKDFMA 171
Cdd:cd02522   78 FLHADTRLPPDWDAAIIETLRADGAVAGAFRLRFDDpgprlrlLELGANLRSRLFGLP----YG--DQGLF-IRRELFEE 150
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983222625 172 INGFNENMLMaEDADFAKRLKEWGkrnnkKFGTIKNGMITSCRRFDTYGDW-ALLKNPKVILAYLKGNDQKYADKTY 247
Cdd:cd02522  151 LGGFPELPLM-EDVELVRRLRRRG-----RPALLPSPVTTSARRWERNGWLrTTLLNWLLLLLYLLGVSPERLAKRY 221
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
17-192 3.65e-27

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 104.01  E-value: 3.65e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASevyKEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDKN--LSKIRNAGAE 90
Cdd:COG0463    3 LVSVVIPTYNEEEYLEEALESLLAQT---YPDFEIIVVDDGSTDGTAEILRELaakdPRIRVIRLERNrgKGAARNAGLA 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  91 IASGEIIVTIDADTIMTESVLSNVDKYLSSGKY--IGGGVNGKLERMSFGIFFSAMLIIIPLLFKYGAVSVGiFWCYRKD 168
Cdd:COG0463   80 AARGDYIAFLDADDQLDPEKLEELVAALEEGPAdlVYGSRLIREGESDLRRLGSRLFNLVRLLTNLPDSTSG-FRLFRRE 158
                        170       180
                 ....*....|....*....|....
gi 983222625 169 FMAINGFNENMLmaEDADFAKRLK 192
Cdd:COG0463  159 VLEELGFDEGFL--EDTELLRALR 180
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
20-184 2.48e-25

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: 98.45  E-value: 2.48e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAkaSEVYkEQTEVIVVLNRCTDQTEEIAKSY-----NCITLKNDDKNLSKIR--NAGAEIA 92
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLL--ALDY-PKLEVIVVDDGSTDDTLEILEELaalyiRRVLVVRDKENGGKAGalNAGLRHA 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  93 SGEIIVTIDADTIMTESVLSNVDKYLSSGKYIGG---------GVNGKLERMSFGIFFSAMLIIIPLLFKYGAVSV--GI 161
Cdd:cd06423   78 KGDIVVVLDADTILEPDALKRLVVPFFADPKVGAvqgrvrvrnGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVlsGA 157
                        170       180
                 ....*....|....*....|....
gi 983222625 162 FWCYRKD-FMAINGFNENMLmAED 184
Cdd:cd06423  158 FGAFRREaLREVGGWDEDTL-TED 180
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
19-247 3.69e-25

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: 98.74  E-value: 3.69e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   19 SIIIPAHNEEKYIRKCLDSIAkaseVYKEQTEVIVVLNRCTDQTEEIAKSYNCITLKNDdKNLSKIRNAGAEIASGEIIV 98
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADLQ----ALRGDAEVIVVDGGSTDGTVEIARSLGAKVIHSP-KGRARQMNAGAALAKGDILL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   99 TIDADTIMTESVLSNVDKYLSSGKYIGGG----VNGKLERMSFGIFFSAM---LIIIPllfkYGavSVGIFwCYRKDFMA 171
Cdd:TIGR04283  77 FLHADTRLPKDFLEAIRRALAKPGYVAGAfdlrFDGPGLLLRLIEWGVNLrsrLTGIP----YG--DQGLF-VRRSLFEQ 149
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 983222625  172 INGFNENMLMaEDADFAKRLKEWGkrnnkKFGTIKNGMITSCRRFDTYGDWAL-LKNPKVILAYLKGNDQKYADKTY 247
Cdd:TIGR04283 150 IGGFPDIPLM-EDIELSRRLRRLG-----RLAILPAPVVTSARRWEKNGILRTiLLNWRLRLLYRLGVSPEELARLY 220
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
17-198 2.18e-22

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 91.21  E-value: 2.18e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASEVykeQTEVIVVLNRCTDQTEEIAKSYNC--ITLKNDDKNL--SKIRNAGAEIA 92
Cdd:COG1216    4 KVSVVIPTYNRPELLRRCLESLLAQTYP---PFEVIVVDNGSTDGTAELLAALAFprVRVIRNPENLgfAAARNLGLRAA 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  93 SGEIIVTIDADTIMTEsvlsnvdkylssgkyigggvnGKLERMsfgIFFSAMLIiipllfkygavsvgifwcyRKD-FMA 171
Cdd:COG1216   81 GGDYLLFLDDDTVVEP---------------------DWLERL---LAAACLLI-------------------RREvFEE 117
                        170       180
                 ....*....|....*....|....*...
gi 983222625 172 INGFNENMLM-AEDADFAKRLKEWGKRN 198
Cdd:COG1216  118 VGGFDERFFLyGEDVDLCLRLRKAGYRI 145
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
20-197 9.09e-21

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: 85.64  E-value: 9.09e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASEvykEQTEVIVVLNRCTDQTEEIAKSY------NCITLKNDDKNLSKIRNAGAEIAS 93
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTY---PNFEVIVVDDGSTDGTLEILEEYakkdprVIRVINEENQGLAAARNAGLKAAR 77
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  94 GEIIVTIDADTIMTESVLSNVDKYLSSGKyigggvngklermsfgiffsamliiipllfKYGAVSVGIFWCYRKD-FMAI 172
Cdd:cd00761   78 GEYILFLDADDLLLPDWLERLVAELLADP------------------------------EADAVGGPGNLLFRRElLEEI 127
                        170       180
                 ....*....|....*....|....*
gi 983222625 173 NGFNENMLMAEDADFAKRLKEWGKR 197
Cdd:cd00761  128 GGFDEALLSGEEDDDFLLRLLRGGK 152
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
20-196 1.63e-19

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: 84.26  E-value: 1.63e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASevY-KEQTEVIVVLNRCTDQTEEIA------KSYNCITLKNDDKNLSKIRNA---GA 89
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALD--YpKEKFEVILVDDHSTDGTVQILefaaakPNFQLKILNNSRVSISGKKNAlttAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  90 EIASGEIIVTIDADTIMTESVLSNVDKYLSSGKY--IGGGVNGKLERMSFGIF------FSAMLIIIPLLFKYGAVSVGI 161
Cdd:cd04192   79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIglVAGPVIYFKGKSLLAKFqrldwlSLLGLIAGSFGLGKPFMCNGA 158
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 983222625 162 FWCYRKD-FMAINGFNENMLMA-EDADF--AKRLKEWGK 196
Cdd:cd04192  159 NMAYRKEaFFEVGGFEGNDHIAsGDDELllAKVASKYPK 197
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
19-168 4.32e-19

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: 81.29  E-value: 4.32e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   19 SIIIPAHNEEKYIRKCLDSIAKAsevYKEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDKNLSKI--RNAGAEIA 92
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQ---TYPNFEIIVVDDGSTDGTVEIAEEYakkdPRVRVIRLPENRGKAgaRNAGLRAA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   93 SGEIIVTIDADTIMTESVLSNV-------DKYLSSGKYIGGGVNGKLERMSFGIFFSAMLIIIPLLFKYGAVSVGIFWC- 164
Cdd:pfam00535  78 TGDYIAFLDADDEVPPDWLEKLvealeedGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIGGFa 157

                  ....*
gi 983222625  165 -YRKD 168
Cdd:pfam00535 158 lYRRE 162
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
17-132 2.79e-18

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: 81.09  E-value: 2.79e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAkASEVYKEQTEVIVVLNRCTDQTEEIAKSY--NCITLKNDDKNLSKIR--NAGAEIA 92
Cdd:cd06439   30 TVTIIIPAYNEEAVIEAKLENLL-ALDYPRDRLEIIVVSDGSTDGTAEIAREYadKGVKLLRFPERRGKAAalNRALALA 108
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 983222625  93 SGEIIVTIDADTIMTESVLSNVDKYLSSGKYigGGVNGKL 132
Cdd:cd06439  109 TGEIVVFTDANALLDPDALRLLVRHFADPSV--GAVSGEL 146
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
20-198 2.48e-16

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: 74.13  E-value: 2.48e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASEVYkeqTEVIVVLNRCTDQTEEIAKSY--NCITLKNdDKNL--SKIRNAGAEIASGE 95
Cdd:cd04186    1 IIIVNYNSLEYLKACLDSLLAQTYPD---FEVIVVDNASTDGSVELLRELfpEVRLIRN-GENLgfGAGNNQGIREAKGD 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  96 IIVTIDADTIMTESVLSNVDKYLSSGKyigggvngklermsfgiffsamliiipllfKYGAVS---VGIFWCYRKD-FMA 171
Cdd:cd04186   77 YVLLLNPDTVVEPGALLELLDAAEQDP------------------------------DVGIVGpkvSGAFLLVRREvFEE 126
                        170       180
                 ....*....|....*....|....*...
gi 983222625 172 INGFNENMLMA-EDADFAKRLKEWGKRN 198
Cdd:cd04186  127 VGGFDEDFFLYyEDVDLCLRARLAGYRV 154
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
20-103 3.36e-14

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: 68.75  E-value: 3.36e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASEvYKEQTEVIVVLNRCTDQTEEIAKSyncitLKNDDKNLSKIRN-----------AG 88
Cdd:cd04179    1 VVIPAYNEEENIPELVERLLAVLE-EGYDYEIIVVDDGSTDGTAEIARE-----LAARVPRVRVIRLsrnfgkgaavrAG 74
                         90
                 ....*....|....*
gi 983222625  89 AEIASGEIIVTIDAD 103
Cdd:cd04179   75 FKAARGDIVVTMDAD 89
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
17-129 3.46e-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: 66.93  E-value: 3.46e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASEvykeqtEVIVVLNRCTDQTEEIAKSYNCITLKNDDKNLSKIRNAGAEIASGEI 96
Cdd:cd02511    1 TLSVVIITKNEERNIERCLESVKWAVD------EIIVVDSGSTDRTVEIAKEYGAKVYQRWWDGFGAQRNFALELATNDW 74
                         90       100       110
                 ....*....|....*....|....*....|...
gi 983222625  97 IVTIDADTIMTESVLSNVDKYLSSGKYIGGGVN 129
Cdd:cd02511   75 VLSLDADERLTPELADEILALLATDDYDGYYVP 107
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
20-121 2.02e-11

EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is predicted to participate in the methanolan synthesis. Methanolan is an exopolysaccharide (EPS), composed of glucose, mannose and galactose. A 21 genes cluster was predicted to participate in the methanolan synthesis. Gene disruption analysis revealed that EpsO is one of the glycosyltransferase enzymes involved in the synthesis of repeating sugar units onto the lipid carrier.


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 61.08  E-value: 2.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIaKASEVYKEQTEVIVVLNRCTDQTEEIAKSYNCITLKNDDKNLskiRNAGAEIASG----- 94
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSL-KAQDYPRELYRIFVVADNCTDDTAQVARAAGATVLERHDPER---RGKGYALDFGfrhll 76
                         90       100       110
                 ....*....|....*....|....*....|...
gi 983222625  95 ------EIIVTIDADTIMTESVLSNVDKYLSSG 121
Cdd:cd06438   77 nladdpDAVVVFDADNLVDPNALEELNARFAAG 109
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
20-103 4.76e-10

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: 57.10  E-value: 4.76e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASEVYKEQTEVIVVLNRCTDQTEEIAKSyncitLKNDDKNLSKIRN-----------AG 88
Cdd:cd04187    1 IVVPVYNEEENLPELYERLKAVLESLGYDYEIIFVDDGSTDRTLEILRE-----LAARDPRVKVIRLsrnfgqqaallAG 75
                         90
                 ....*....|....*
gi 983222625  89 AEIASGEIIVTIDAD 103
Cdd:cd04187   76 LDHARGDAVITMDAD 90
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
20-103 1.82e-09

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: 56.04  E-value: 1.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASEVYKEQT-EVIVVLNRCTDQTEEIAKSY--------NCITLkndDKNLSK---IRnA 87
Cdd:cd04188    1 VVIPAYNEEKRLPPTLEEAVEYLEERPSFSyEIIVVDDGSKDGTAEVARKLarknpaliRVLTL---PKNRGKggaVR-A 76
                         90
                 ....*....|....*.
gi 983222625  88 GAEIASGEIIVTIDAD 103
Cdd:cd04188   77 GMLAARGDYILFADAD 92
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
20-191 3.71e-09

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: 54.51  E-value: 3.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSiakasevYKEQT----EVIVVLNRCTDQTEEIAKSYNC---ITLKN----DDKN-LSKIRNA 87
Cdd:cd06420    1 LIITTYNRPEALELVLKS-------VLNQSilpfEVIIADDGSTEETKELIEEFKSqfpIPIKHvwqeDEGFrKAKIRNK 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  88 GAEIASGEIIVTIDADTIMTESVLSNVDKYLSSGKYIGGG-VN---GKLERMSFGIFFSamliiipllfkygavsvgifw 163
Cdd:cd06420   74 AIAAAKGDYLIFIDGDCIPHPDFIADHIELAEPGVFLSGSrVLlneKLTERGIRGCNMS--------------------- 132
                        170       180       190
                 ....*....|....*....|....*....|
gi 983222625 164 CYRKDFMAINGFNENMLMA--EDADFAKRL 191
Cdd:cd06420  133 FWKKDLLAVNGFDEEFTGWggEDSELVARL 162
PRK10073 PRK10073
putative glycosyl transferase; Provisional
17-106 2.51e-08

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 53.51  E-value: 2.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHNEEKYIRKCLDSIAKASEvykEQTEVIVVLNRCTDQTEEIAKSY-----NCITLKNDDKNLSKIRNAGAEI 91
Cdd:PRK10073   7 KLSIIIPLYNAGKDFRAFMESLIAQTW---TALEIIIVNDGSTDNSVEIAKHYaenypHVRLLHQANAGVSVARNTGLAV 83
                         90
                 ....*....|....*
gi 983222625  92 ASGEIIVTIDADTIM 106
Cdd:PRK10073  84 ATGKYVAFPDADDVV 98
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
15-103 5.04e-07

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 49.77  E-value: 5.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  15 DVKFSIIIPAHNEEKYIRKCLDSIAKASEVYKEQT-----EVIVVLNRCTDQTEEIAKSY--NCITLKNDDKNLSKIRNA 87
Cdd:PTZ00260  69 DVDLSIVIPAYNEEDRLPKMLKETIKYLESRSRKDpkfkyEIIIVNDGSKDKTLKVAKDFwrQNINPNIDIRLLSLLRNK 148
                         90       100
                 ....*....|....*....|....
gi 983222625  88 GAEIA--------SGEIIVTIDAD 103
Cdd:PTZ00260 149 GKGGAvrigmlasRGKYILMVDAD 172
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
20-103 7.49e-06

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: 45.60  E-value: 7.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  20 IIIPAHNEEKYIRKCLDSIAKASEvyKEQTEVIVVLNRCTDQTEEIAKSYNCItlknDDKNLSKIRN----------AGA 89
Cdd:cd06442    1 IIIPTYNERENIPELIERLDAALK--GIDYEIIVVDDNSPDGTAEIVRELAKE----YPRVRLIVRPgkrglgsayiEGF 74
                         90
                 ....*....|....
gi 983222625  90 EIASGEIIVTIDAD 103
Cdd:cd06442   75 KAARGDVIVVMDAD 88
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
12-168 7.90e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 45.84  E-value: 7.90e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  12 SQKDVKFSIIIPAHNEEKYIRKCLDSIAKASEVYKEqTEVIVVLNRCTDQTEEIAKSYncITLKNDDKNLSKIRN----- 86
Cdd:PLN02726   5 GEGAMKYSIIVPTYNERLNIALIVYLIFKALQDVKD-FEIIVVDDGSPDGTQDVVKQL--QKVYGEDRILLRPRPgklgl 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  87 -----AGAEIASGEIIVTIDADtimtesvLSNVDKYLSS---------------GKYI-GGGVNG-----KLerMSFGIF 140
Cdd:PLN02726  82 gtayiHGLKHASGDFVVIMDAD-------LSHHPKYLPSfikkqretgadivtgTRYVkGGGVHGwdlrrKL--TSRGAN 152
                        170       180       190
                 ....*....|....*....|....*....|
gi 983222625 141 FSAMLIIIPllfkygAVS--VGIFWCYRKD 168
Cdd:PLN02726 153 VLAQTLLWP------GVSdlTGSFRLYKRS 176
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
17-197 1.03e-05

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: 44.89  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  17 KFSIIIPAHN-EEKYIRKCLDSIakasevyKEQT----EVIVVLNRCTD-QTEEIAKSYN------CITLKNDDKNLSKI 84
Cdd:cd04184    2 LISIVMPVYNtPEKYLREAIESV-------RAQTypnwELCIADDASTDpEVKRVLKKYAaqdpriKVVFREENGGISAA 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  85 RNAGAEIASGEIIVTIDADTIMTESVLSNVDKYLSSGK----------YIggGVNGKLERMSFGIFFSamliiIPLLFKY 154
Cdd:cd04184   75 TNSALELATGEFVALLDHDDELAPHALYEVVKALNEHPdadliysdedKI--DEGGKRSEPFFKPDWS-----PDLLLSQ 147
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 983222625 155 GAvsVGIFWCYRKDFMA-INGFNENMLMAEDADFAKRLKEWGKR 197
Cdd:cd04184  148 NY--IGHLLVYRRSLVRqVGGFREGFEGAQDYDLVLRVSEHTDR 189
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
19-103 1.62e-05

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: 44.46  E-value: 1.62e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  19 SIIIPAHNEEKYIRKCLDSIAkasevykEQT----EVIVVLNRCTDQTEEIAKSYNCITLK---NDDKNLSKIRNAGAEI 91
Cdd:cd06433    1 SIITPTYNQAETLEETIDSVL-------SQTypniEYIVIDGGSTDGTVDIIKKYEDKITYwisEPDKGIYDAMNKGIAL 73
                         90
                 ....*....|..
gi 983222625  92 ASGEIIVTIDAD 103
Cdd:cd06433   74 ATGDIIGFLNSD 85
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
18-105 1.70e-05

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 44.67  E-value: 1.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   18 FSIIIPAHNEEKYIRKCLDSIAKASEVykeQTEVIVVLNRCTDQT----EEIAKSYN-----CITLKNDDKNLSKIR--N 86
Cdd:pfam13641   4 VSVVVPAFNEDSVLGRVLEAILAQPYP---PVEVVVVVNPSDAETldvaEEIAARFPdvrlrVIRNARLLGPTGKSRglN 80
                          90
                  ....*....|....*....
gi 983222625   87 AGAEIASGEIIVTIDADTI 105
Cdd:pfam13641  81 HGFRAVKSDLVVLHDDDSV 99
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
19-105 2.86e-05

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: 43.77  E-value: 2.86e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  19 SIIIPAHNEEKYIRKCLDSIAkasevykEQT----EVIVVLNRCTDQTEEIAKSY-----NCITLKNDDKNLSKIRN--A 87
Cdd:cd04196    1 AVLMATYNGEKYLREQLDSIL-------AQTykndELIISDDGSTDGTVEIIKEYidkdpFIIILIRNGKNLGVARNfeS 73
                         90
                 ....*....|....*...
gi 983222625  88 GAEIASGEIIVTIDADTI 105
Cdd:cd04196   74 LLQAADGDYVFFCDQDDI 91
PRK13915 PRK13915
putative glucosyl-3-phosphoglycerate synthase; Provisional
19-105 1.73e-04

putative glucosyl-3-phosphoglycerate synthase; Provisional


Pssm-ID: 237556 [Multi-domain]  Cd Length: 306  Bit Score: 41.83  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  19 SIIIPAHNEEKYIRKCLDSIaKASEVYKEQTEVIVVLNRCTDQTEEIAKSYNCITLKNDD------------KNLSKirn 86
Cdd:PRK13915  34 SVVLPALNEEETVGKVVDSI-RPLLMEPLVDELIVIDSGSTDATAERAAAAGARVVSREEilpelpprpgkgEALWR--- 109
                         90
                 ....*....|....*....
gi 983222625  87 aGAEIASGEIIVTIDADTI 105
Cdd:PRK13915 110 -SLAATTGDIVVFVDADLI 127
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
19-191 2.83e-04

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: 41.11  E-value: 2.83e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   19 SIIIPAHNEEK--YIRKCLDSIAKaseVYKEQTEVIVVLNRCTDQTEEIAKSY----NCITLKNDDK---NLSKIRNAGA 89
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTF---QYDPEFELIIINDGSTDKTLEEVSSIkdhnLQVYYPNAPDttySLAASRNRGT 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625   90 EIASGEIIVTIDADTIMTESVLSNVDKYLSSGK--------------YIGGGVNGKLERMSF----GIFFSAMLIIIPLL 151
Cdd:pfam10111  78 SHAIGEYISFIDGDCLWSPDKFEKQLKIATSLAlqeniqaavvlpvtDLNDESSNFLRRGGDltasGDVLRDLLVFYSPL 157
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 983222625  152 FKYGAVSVGIFWCYRKDFMAINGFNENMLM--AEDADFAKRL 191
Cdd:pfam10111 158 AIFFAPNSSNALINRQAFIEVGGFDESFRGhgAEDFDIFLRL 199
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
19-181 3.35e-04

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: 40.70  E-value: 3.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  19 SIIIPAHNE-EKYIRKCLDSIAKasevyKEQTEVIVVLNRCTDQTEEI---AKSYNCITLKnDDKNLSKiRNA---GAEI 91
Cdd:cd06434    3 TVIIPVYDEdPDVFRECLRSILR-----QKPLEIIVVTDGDDEPYLSIlsqTVKYGGIFVI-TVPHPGK-RRAlaeGIRH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 983222625  92 ASGEIIVTIDADTIMTESVLSNVDKYLSSGKYIGGGVNGKLER--MSFGIFFSAMLIIIPLLFKYGAVSV-GIFWC---- 164
Cdd:cd06434   76 VTTDIVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQRILRprDSKWSFLAAEYLERRNEEIRAAMSYdGGVPClsgr 155
                        170       180
                 ....*....|....*....|....
gi 983222625 165 ---YR----KDFMAINGFNENMLM 181
Cdd:cd06434  156 taaYRteilKDFLFLEEFTNETFM 179
Glyco_transf_7C pfam02709
N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of ...
160-195 2.84e-03

N-terminal domain of galactosyltransferase; This is the N-terminal domain of a family of galactosyltransferases from a wide range of Metazoa with three related galactosyltransferases activities, all three of which are possessed by one sequence in some cases. EC:2.4.1.90, N-acetyllactosamine synthase; EC:2.4.1.38, Beta-N-acetylglucosaminyl-glycopeptide beta-1,4- galactosyltransferase; and EC:2.4.1.22 Lactose synthase. Note that N-acetyllactosamine synthase is a component of Lactose synthase along with alpha-lactalbumin, in the absence of alpha-lactalbumin EC:2.4.1.90 is the catalyzed reaction.


Pssm-ID: 460659 [Multi-domain]  Cd Length: 78  Bit Score: 35.67  E-value: 2.84e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 983222625  160 GIFWCYRKDFMAINGFNeNMLM---AEDADFAKRLKEWG 195
Cdd:pfam02709  22 GVLALSREDFERINGFS-NGFWgwgGEDDDLYNRLLLAG 59
 
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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