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Conserved domains on  [gi|1762588614|gb|KAB3934823|]
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glycosyltransferase [Bacteroides uniformis]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10157685)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
10-212 4.55e-84

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: 249.38  E-value: 4.55e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIVSEPDKGLYDAMNKGIRLATGDYLC 89
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  90 FLNAGDSFHeDDTLQQMVRSISGNELPDVLYGETELVDKEGHFIRMRRlaaPEVLTWRSFKQGMLVCHQAFFAKASLVE- 168
Cdd:cd06433    81 FLNSDDTLL-PGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRR---PPPFLDKFLLYGMPICHQATFFRRSLFEk 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1762588614 169 --PYDLQYRFSADFDWCIRVMKKARALHNTHLTLIDYLEEGMTTQN 212
Cdd:cd06433   157 ygGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
10-212 4.55e-84

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: 249.38  E-value: 4.55e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIVSEPDKGLYDAMNKGIRLATGDYLC 89
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  90 FLNAGDSFHeDDTLQQMVRSISGNELPDVLYGETELVDKEGHFIRMRRlaaPEVLTWRSFKQGMLVCHQAFFAKASLVE- 168
Cdd:cd06433    81 FLNSDDTLL-PGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRR---PPPFLDKFLLYGMPICHQATFFRRSLFEk 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1762588614 169 --PYDLQYRFSADFDWCIRVMKKARALHNTHLTLIDYLEEGMTTQN 212
Cdd:cd06433   157 ygGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-189 4.95e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 4.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   6 TPKFSIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIV---SEPDKGLYDAMNKGIRL 82
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRvirLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  83 ATGDYLCFLNAGDSFHEDDtLQQMVRSISGNElPDVLYGETelVDKEGHFIRMRRLAAPEVLTWRSFKQGMLVCHQAFFa 162
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEK-LEELVAALEEGP-ADLVYGSR--LIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLF- 155
                         170       180
                  ....*....|....*....|....*..
gi 1762588614 163 KASLVEPYDLQYRFSADFDWcIRVMKK 189
Cdd:COG0463   156 RREVLEELGFDEGFLEDTEL-LRALRH 181
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-162 4.63e-29

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: 107.48  E-value: 4.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYR---DRITRIVSEPDKGLYDAMNKGIRLATGD 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAkkdPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  87 YLCFLNAgDSFHEDDTLQQMVRSISGNElPDVLYGETELVDKEGHFIRMRRLAA----PEVLTWRSFKQGMLVCHQAFFA 162
Cdd:pfam00535  81 YIAFLDA-DDEVPPDWLEKLVEALEEDG-ADVVVGSRYVIFGETGEYRRASRITlsrlPFFLGLRLLGLNLPFLIGGFAL 158
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
10-191 1.04e-16

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: 76.01  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHvEYILVDGASKDGTLSIIDRYRDRItrIVSEPDKGLydAMNKGIRLATGDYLC 89
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADLQALRGDA-EVIVVDGGSTDGTVEIARSLGAKV--IHSPKGRAR--QMNAGAALAKGDILL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  90 FLNAgDSFHEDDTLQQMVRSISGnelPDVLYGETEL-VDKEGHFIRMRRLAApevlTWRSFK-------QGMLVcHQAFF 161
Cdd:TIGR04283  77 FLHA-DTRLPKDFLEAIRRALAK---PGYVAGAFDLrFDGPGLLLRLIEWGV----NLRSRLtgipygdQGLFV-RRSLF 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 1762588614 162 AKASLVEPYDLQyrfsADFDWCIRVMKKAR 191
Cdd:TIGR04283 148 EQIGGFPDIPLM----EDIELSRRLRRLGR 173
PRK10073 PRK10073
putative glycosyl transferase; Provisional
6-95 1.57e-15

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 74.70  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   6 TPKFSIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRIT--RIVSEPDKGLYDAMNKGIRLA 83
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhvRLLHQANAGVSVARNTGLAVA 84
                          90
                  ....*....|..
gi 1762588614  84 TGDYLCFLNAGD 95
Cdd:PRK10073   85 TGKYVAFPDADD 96
 
Name Accession Description Interval E-value
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
10-212 4.55e-84

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: 249.38  E-value: 4.55e-84
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIVSEPDKGLYDAMNKGIRLATGDYLC 89
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  90 FLNAGDSFHeDDTLQQMVRSISGNELPDVLYGETELVDKEGHFIRMRRlaaPEVLTWRSFKQGMLVCHQAFFAKASLVE- 168
Cdd:cd06433    81 FLNSDDTLL-PGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVIGRRR---PPPFLDKFLLYGMPICHQATFFRRSLFEk 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1762588614 169 --PYDLQYRFSADFDWCIRVMKKARALHNTHLTLIDYLEEGMTTQN 212
Cdd:cd06433   157 ygGFDESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
6-189 4.95e-33

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 119.04  E-value: 4.95e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   6 TPKFSIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIV---SEPDKGLYDAMNKGIRL 82
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELAAKDPRIRvirLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  83 ATGDYLCFLNAGDSFHEDDtLQQMVRSISGNElPDVLYGETelVDKEGHFIRMRRLAAPEVLTWRSFKQGMLVCHQAFFa 162
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEK-LEELVAALEEGP-ADLVYGSR--LIREGESDLRRLGSRLFNLVRLLTNLPDSTSGFRLF- 155
                         170       180
                  ....*....|....*....|....*..
gi 1762588614 163 KASLVEPYDLQYRFSADFDWcIRVMKK 189
Cdd:COG0463   156 RREVLEELGFDEGFLEDTEL-LRALRH 181
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
10-162 4.63e-29

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: 107.48  E-value: 4.63e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYR---DRITRIVSEPDKGLYDAMNKGIRLATGD 86
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYAkkdPRVRVIRLPENRGKAGARNAGLRAATGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  87 YLCFLNAgDSFHEDDTLQQMVRSISGNElPDVLYGETELVDKEGHFIRMRRLAA----PEVLTWRSFKQGMLVCHQAFFA 162
Cdd:pfam00535  81 YIAFLDA-DDEVPPDWLEKLVEALEEDG-ADVVVGSRYVIFGETGEYRRASRITlsrlPFFLGLRLLGLNLPFLIGGFAL 158
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
11-157 7.84e-28

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: 104.13  E-value: 7.84e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYR---DRITRIVSEPDKGLYDAMNKGIRLATGDY 87
Cdd:cd00761     1 VIIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYAkkdPRVIRVINEENQGLAAARNAGLKAARGEY 80
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1762588614  88 LCFLNAgDSFHEDDTLQQMVRSISGNELPDVLYG------ETELVDKEGHFIRMRRLAAPEVLTWRSFKQGMLVCH 157
Cdd:cd00761    81 ILFLDA-DDLLLPDWLERLVAELLADPEADAVGGpgnllfRRELLEEIGGFDEALLSGEEDDDFLLRLLRGGKVAF 155
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
5-108 9.91e-25

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 96.99  E-value: 9.91e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   5 PTPKFSIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYR-DRITRIVSEPDKGLYDAMNKGIRLA 83
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAfPRVRVIRNPENLGFAAARNLGLRAA 80
                          90       100
                  ....*....|....*....|....*
gi 1762588614  84 TGDYLCFLNAgDSFHEDDTLQQMVR 108
Cdd:COG1216    81 GGDYLLFLDD-DTVVEPDWLERLLA 104
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
4-108 2.62e-22

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: 92.88  E-value: 2.62e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   4 HPTPKFSIITVTYNAEAVLEDTIQSVISQTY--HHVEYILVDGASKDGTLSIIDRYRD---RITRIVSEPDKGLYDAMNK 78
Cdd:COG1215    26 ADLPRVSVIIPAYNEEAVIEETLRSLLAQDYpkEKLEVIVVDDGSTDETAEIARELAAeypRVRVIERPENGGKAAALNA 105
                          90       100       110
                  ....*....|....*....|....*....|
gi 1762588614  79 GIRLATGDYLCFLNAgDSFHEDDTLQQMVR 108
Cdd:COG1215   106 GLKAARGDIVVFLDA-DTVLDPDWLRRLVA 134
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-118 8.22e-20

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: 83.38  E-value: 8.22e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIVSEPDKGLYDAMNKGIRLATGDYLCF 90
Cdd:cd04186     1 IIIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLL 80
                          90       100
                  ....*....|....*....|....*...
gi 1762588614  91 LNAgDSFHEDDTLQQMVRSISGNelPDV 118
Cdd:cd04186    81 LNP-DTVVEPGALLELLDAAEQD--PDV 105
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
7-132 5.73e-18

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: 79.17  E-value: 5.73e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   7 PKFSIITVTYNA-EAVLEDTIQSVISQTYHHVEYILVDGAS-KDGTLSIIDRYR---DRITRIVSEPDKGLYDAMNKGIR 81
Cdd:cd04184     1 PLISIVMPVYNTpEKYLREAIESVRAQTYPNWELCIADDAStDPEVKRVLKKYAaqdPRIKVVFREENGGISAATNSALE 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1762588614  82 LATGDYLCFLNAGDSFHEdDTLQQMVRSISGNELPDVLYGETELVDKEGHF 132
Cdd:cd04184    81 LATGEFVALLDHDDELAP-HALYEVVKALNEHPDADLIYSDEDKIDEGGKR 130
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
8-110 6.34e-18

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: 79.97  E-value: 6.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   8 KFSIITVTYNAEAVLEDTIQSVISQTYHH--VEYILVDGASKDGTLSIIDRYRDR--ITRIVSEPDKGLYDAMNKGIRLA 83
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPKdlIEIIVVDGGSTDGTREIVQEYAAKdpRIRLIDNPKRIQSAGLNIGIRNS 80
                          90       100
                  ....*....|....*....|....*..
gi 1762588614  84 TGDYLCFLNAgDSFHEDDTLQQMVRSI 110
Cdd:cd02525    81 RGDIIIRVDA-HAVYPKDYILELVEAL 106
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
5-169 1.23e-17

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: 79.16  E-value: 1.23e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   5 PTPKFSIITVTYNAEAVLEDTIQSVISQTY--HHVEYILVDGASKDGTLSIIDRYRD-RITRIVSEPDKGLYDAMNKGIR 81
Cdd:cd06439    27 YLPTVTIIIPAYNEEAVIEAKLENLLALDYprDRLEIIVVSDGSTDGTAEIAREYADkGVKLLRFPERRGKAAALNRALA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  82 LATGDYLCFLNAgDSFHEDDTLQQMVR--------SISGNelpDVLYGETELVDKEGHF----IRMRRlaapevltWRSF 149
Cdd:cd06439   107 LATGEIVVFTDA-NALLDPDALRLLVRhfadpsvgAVSGE---LVIVDGGGSGSGEGLYwkyeNWLKR--------AESR 174
                         170       180
                  ....*....|....*....|.
gi 1762588614 150 KQGMLVCHQAFFA-KASLVEP 169
Cdd:cd06439   175 LGSTVGANGAIYAiRRELFRP 195
glyco_like_mftF TIGR04283
transferase 2, rSAM/selenodomain-associated; This enzyme may transfer a nucleotide, or it ...
10-191 1.04e-16

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: 76.01  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHvEYILVDGASKDGTLSIIDRYRDRItrIVSEPDKGLydAMNKGIRLATGDYLC 89
Cdd:TIGR04283   2 SIIIPVLNEAATLPELLADLQALRGDA-EVIVVDGGSTDGTVEIARSLGAKV--IHSPKGRAR--QMNAGAALAKGDILL 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  90 FLNAgDSFHEDDTLQQMVRSISGnelPDVLYGETEL-VDKEGHFIRMRRLAApevlTWRSFK-------QGMLVcHQAFF 161
Cdd:TIGR04283  77 FLHA-DTRLPKDFLEAIRRALAK---PGYVAGAFDLrFDGPGLLLRLIEWGV----NLRSRLtgipygdQGLFV-RRSLF 147
                         170       180       190
                  ....*....|....*....|....*....|
gi 1762588614 162 AKASLVEPYDLQyrfsADFDWCIRVMKKAR 191
Cdd:TIGR04283 148 EQIGGFPDIPLM----EDIELSRRLRRLGR 173
GT_2_like_a cd02522
GT_2_like_a represents a glycosyltransferase family-2 subfamily with unknown function; ...
10-178 3.83e-16

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: 74.53  E-value: 3.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRItrIVSEPDKGLydAMNKGIRLATGDYLC 89
Cdd:cd02522     2 SIIIPTLNEAENLPRLLASLRRLNPLPLEIIVVDGGSTDGTVAIARSAGVVV--ISSPKGRAR--QMNAGAAAARGDWLL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  90 FLNAgDSFHEDDTLQQMVRSISGNelPDVLYGETELVDKEGHfiRMRRLAAPEVLTWRSFK-----QGMLVCHQAF---- 160
Cdd:cd02522    78 FLHA-DTRLPPDWDAAIIETLRAD--GAVAGAFRLRFDDPGP--RLRLLELGANLRSRLFGlpygdQGLFIRRELFeelg 152
                         170
                  ....*....|....*....
gi 1762588614 161 -FAKASLVEPYDLQYRFSA 178
Cdd:cd02522   153 gFPELPLMEDVELVRRLRR 171
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
11-108 5.02e-16

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: 73.42  E-value: 5.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRD----RITRIVSEPDKGLYDAMNKGIRLATGD 86
Cdd:cd06423     1 IIVPAYNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEELAAlyirRVLVVRDKENGGKAGALNAGLRHAKGD 80
                          90       100
                  ....*....|....*....|..
gi 1762588614  87 YLCFLNAgDSFHEDDTLQQMVR 108
Cdd:cd06423    81 IVVVLDA-DTILEPDALKRLVV 101
PRK10073 PRK10073
putative glycosyl transferase; Provisional
6-95 1.57e-15

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 74.70  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   6 TPKFSIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRIT--RIVSEPDKGLYDAMNKGIRLA 83
Cdd:PRK10073    5 TPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPhvRLLHQANAGVSVARNTGLAVA 84
                          90
                  ....*....|..
gi 1762588614  84 TGDYLCFLNAGD 95
Cdd:PRK10073   85 TGKYVAFPDADD 96
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
10-130 8.12e-14

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: 68.04  E-value: 8.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIV----SEPDKGLYDAMNKGIRLATG 85
Cdd:cd04196     1 AVLMATYNGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYIDKDPFIIilirNGKNLGVARNFESLLQAADG 80
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1762588614  86 DYLCFLNAGDSFHEdDTLQQMVRSISGNELPDVLYGETELVDKEG 130
Cdd:cd04196    81 DYVFFCDQDDIWLP-DKLERLLKAFLKDDKPLLVYSDLELVDENG 124
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
11-93 4.88e-11

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: 59.89  E-value: 4.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVIS--QTYHHVEYILVDGASKDGTLSIIDRYRDRITR---IVSEPDKGLYDAMNKGIRLATG 85
Cdd:cd04179     1 VVIPAYNEEENIPELVERLLAvlEEGYDYEIIVVDDGSTDGTAEIARELAARVPRvrvIRLSRNFGKGAAVRAGFKAARG 80

                  ....*...
gi 1762588614  86 DYLCFLNA 93
Cdd:cd04179    81 DIVVTMDA 88
beta3GnTL1_like cd06913
Beta 1, 3-N-acetylglucosaminyltransferase is essential for the formation of ...
11-100 6.63e-09

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: 54.39  E-value: 6.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVISQTYHH-VEYILVDGASKDGTLSIIDRYR-----DRITRIVSEPD----KGLYDAMNKGI 80
Cdd:cd06913     1 IILPVHNGEQWLDECLESVLQQDFEGtLELSVFNDASTDKSAEIIEKWRkkledSGVIVLVGSHNspspKGVGYAKNQAI 80
                          90       100
                  ....*....|....*....|
gi 1762588614  81 RLATGDYLCFLNAGDSFHED 100
Cdd:cd06913    81 AQSSGRYLCFLDSDDVMMPQ 100
pp-GalNAc-T cd02510
pp-GalNAc-T initiates the formation of mucin-type O-linked glycans; UDP-GalNAc: polypeptide ...
10-93 7.41e-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: 49.12  E-value: 7.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYN-AEAVLEDTIQSVISQT--YHHVEYILVDGASKDGTL-----SIIDRYRDRITRIVSEPDKGLYDAMNKGIR 81
Cdd:cd02510     1 SVIIIFHNeALSTLLRTVHSVINRTppELLKEIILVDDFSDKPELkllleEYYKKYLPKVKVLRLKKREGLIRARIAGAR 80
                          90
                  ....*....|..
gi 1762588614  82 LATGDYLCFLNA 93
Cdd:cd02510    81 AATGDVLVFLDS 92
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
11-133 8.91e-07

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: 48.44  E-value: 8.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVISQTY--HHVEYILVDGASKDGTLSIIDRYRD------RITRIVSEPDKGLYDAMNKGIRL 82
Cdd:cd04192     1 VVIAARNEAENLPRLLQSLSALDYpkEKFEVILVDDHSTDGTVQILEFAAAkpnfqlKILNNSRVSISGKKNALTTAIKA 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1762588614  83 ATGDYLCFLNAgDSFHEDDTLQQMVRSISGNELPDVLYGETELvdKEGHFI 133
Cdd:cd04192    81 AKGDWIVTTDA-DCVVPSNWLLTFVAFIQKEQIGLVAGPVIYF--KGKSLL 128
GT2_Chondriotin_Pol_N cd06420
N-terminal domain of Chondroitin polymerase functions as a GalNAc transferase; Chondroitin ...
11-95 9.25e-07

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


Pssm-ID: 133042 [Multi-domain]  Cd Length: 182  Bit Score: 47.57  E-value: 9.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITvTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRIT---RIVSEPDKG--LYDAMNKGIRLATG 85
Cdd:cd06420     2 IIT-TYNRPEALELVLKSVLNQSILPFEVIIADDGSTEETKELIEEFKSQFPipiKHVWQEDEGfrKAKIRNKAIAAAKG 80
                          90
                  ....*....|
gi 1762588614  86 DYLCFLNaGD 95
Cdd:cd06420    81 DYLIFID-GD 89
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
7-108 3.48e-06

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 46.60  E-value: 3.48e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   7 PKFSIITVTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIID----RYRDRITRIVSEPDK----GLYDAMNK 78
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPVEVVVVVNPSDAETLDVAEeiaaRFPDVRLRVIRNARLlgptGKSRGLNH 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1762588614  79 GIRLATGDYLCFLNAgDSFHEDDTLQQMVR 108
Cdd:pfam13641  82 GFRAVKSDLVVLHDD-DSVLHPGTLKKYVQ 110
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
8-93 7.74e-06

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: 45.74  E-value: 7.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   8 KFSIITVTYNAEAVLEDTIQSVIsqtyHHV-EYILVDGASKDGTLSIIDRYRDritRIVSEPDKGLYDAMNKGIRLATGD 86
Cdd:cd02511     1 TLSVVIITKNEERNIERCLESVK----WAVdEIIVVDSGSTDRTVEIAKEYGA---KVYQRWWDGFGAQRNFALELATND 73

                  ....*..
gi 1762588614  87 YLCFLNA 93
Cdd:cd02511    74 WVLSLDA 80
PLN02726 PLN02726
dolichyl-phosphate beta-D-mannosyltransferase
7-98 8.22e-06

dolichyl-phosphate beta-D-mannosyltransferase


Pssm-ID: 215385 [Multi-domain]  Cd Length: 243  Bit Score: 45.46  E-value: 8.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   7 PKFSIITVTYNaEAVLEDTIQSVISQTYHHV---EYILVDGASKDGTLSII----DRYRDRITRIVSEPDK-GLYDAMNK 78
Cdd:PLN02726    9 MKYSIIVPTYN-ERLNIALIVYLIFKALQDVkdfEIIVVDDGSPDGTQDVVkqlqKVYGEDRILLRPRPGKlGLGTAYIH 87
                          90       100
                  ....*....|....*....|
gi 1762588614  79 GIRLATGDYLCFLNAGDSFH 98
Cdd:PLN02726   88 GLKHASGDFVVIMDADLSHH 107
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
14-83 8.43e-06

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: 45.32  E-value: 8.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1762588614  14 VTYNAEAVLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDR--YRDRITRIVSEPDKGLYDAMNKGIRLA 83
Cdd:cd04185     4 VTYNRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSlgDLDNIVYLRLPENLGGAGGFYEGVRRA 75
DPM1_like cd06442
DPM1_like represents putative enzymes similar to eukaryotic DPM1; Proteins similar to ...
11-110 9.06e-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: 45.22  E-value: 9.06e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDTIQSVISQTY-HHVEYILVDGASKDGTLSIIDRYR---DRITRIVSEPDKGLYDAMNKGIRLATGD 86
Cdd:cd06442     1 IIIPTYNERENIPELIERLDAALKgIDYEIIVVDDNSPDGTAEIVRELAkeyPRVRLIVRPGKRGLGSAYIEGFKAARGD 80
                          90       100
                  ....*....|....*....|....
gi 1762588614  87 YLCFLNAgDSFHEDDTLQQMVRSI 110
Cdd:cd06442    81 VIVVMDA-DLSHPPEYIPELLEAQ 103
DPM1_like_bac cd04187
Bacterial DPM1_like enzymes are related to eukaryotic DPM1; A family of bacterial enzymes ...
11-87 1.91e-05

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: 44.01  E-value: 1.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  11 IITVTYNAEAVLEDT---IQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIvsepdKGL--------YDAMNKG 79
Cdd:cd04187     1 IVVPVYNEEENLPELyerLKAVLESLGYDYEIIFVDDGSTDRTLEILRELAARDPRV-----KVIrlsrnfgqQAALLAG 75

                  ....*...
gi 1762588614  80 IRLATGDY 87
Cdd:cd04187    76 LDHARGDA 83
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
16-93 2.66e-05

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


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 43.71  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  16 YNAEAVLEDTIQSVIS-----QTYHHvEYILVDGASKDGTLSIIDRYRDR----ITRIVSEPDKGLYDAMNKGIRLATGD 86
Cdd:cd04188     6 YNEEKRLPPTLEEAVEyleerPSFSY-EIIVVDDGSKDGTAEVARKLARKnpalIRVLTLPKNRGKGGAVRAGMLAARGD 84

                  ....*..
gi 1762588614  87 YLCFLNA 93
Cdd:cd04188    85 YILFADA 91
GT2_AmsE_like cd04195
GT2_AmsE_like is involved in exopolysaccharide amylovora biosynthesis; AmsE is a ...
10-138 2.80e-04

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: 40.76  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAE--AVLEDTIQSVISQTYHHVEYILV-DGASKDGTLSIIDRYRDR--ITRIVSEPDKGLYDAMNKGIRLAT 84
Cdd:cd04195     1 SVLMSVYIKEkpEFLREALESILKQTLPPDEVVLVkDGPVTQSLNEVLEEFKRKlpLKVVPLEKNRGLGKALNEGLKHCT 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1762588614  85 GDyLCFLNAGDSFHEDDTLQQMVRSISGNELPDVLYGETELVDKEGHFIRMRRL 138
Cdd:cd04195    81 YD-WVARMDTDDISLPDRFEKQLDFIEKNPEIDIVGGGVLEFDSDGNDIGKRRL 133
Glyco_tranf_2_2 pfam10111
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
10-168 8.34e-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: 39.95  E-value: 8.34e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  10 SIITVTYNAEA--VLEDTIQSVISQTYHHVEYILVDGASKDGTLSIIDRYRDRITRIV--SEPDK--GLYDAMNKGIRLA 83
Cdd:pfam10111   1 SVVIPVYNGEKthWIQERILNQTFQYDPEFELIIINDGSTDKTLEEVSSIKDHNLQVYypNAPDTtySLAASRNRGTSHA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614  84 TGDYLCFLNaGDSFHEDDTLQQMVRSISG---NELPD--VLYGETELVDKEGHFIRMRrlaapEVLTWRSfkqgmLVCHQ 158
Cdd:pfam10111  81 IGEYISFID-GDCLWSPDKFEKQLKIATSlalQENIQaaVVLPVTDLNDESSNFLRRG-----GDLTASG-----DVLRD 149
                         170
                  ....*....|
gi 1762588614 159 AFFAKASLVE 168
Cdd:pfam10111 150 LLVFYSPLAI 159
PTZ00260 PTZ00260
dolichyl-phosphate beta-glucosyltransferase; Provisional
9-129 6.05e-03

dolichyl-phosphate beta-glucosyltransferase; Provisional


Pssm-ID: 240336 [Multi-domain]  Cd Length: 333  Bit Score: 37.44  E-value: 6.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1762588614   9 FSIITVTYNAEA----VLEDTIQSVIS----QTYHHVEYILVDGASKDGTLSIIDRY-RDRI-----TRIVS-EPDKGLY 73
Cdd:PTZ00260   72 LSIVIPAYNEEDrlpkMLKETIKYLESrsrkDPKFKYEIIIVNDGSKDKTLKVAKDFwRQNInpnidIRLLSlLRNKGKG 151
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1762588614  74 DAMNKGIRLATGDYLCFLNAGDS--FHEDDTLQQMVRSISGNELPDVLYGETELVDKE 129
Cdd:PTZ00260  152 GAVRIGMLASRGKYILMVDADGAtdIDDFDKLEDIMLKIEQNGLGIVFGSRNHLVDSD 209
 
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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