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Conserved domains on  [gi|1246765703|ref|WP_096350468|]
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glycosyltransferase [Variibacter gotjawalensis]

Protein Classification

glycosyltransferase; glycosyltransferase family 4 protein( domain architecture ID 10133552)

bifunctional glycosyltransferase containing N-terminal family 2 and C-terminal family 4 glycosyltransferase domains, catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds| glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
8-367 8.24e-71

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


:

Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 236.49  E-value: 8.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703   8 RLALDMYVLEQGlKTGIHRVCDELFPRIAKSPQFRTTLAFRNG----GESTAWQFSSCAQTTAEQSRLTTKRLRASQ--- 80
Cdd:cd03809     1 KILIDGRSLAQR-LTGIGRYTRELLKALAKNDPDESVLAVPPLpgelLRLLREYPELSLGVIKIKLWRELALLRWLQill 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  81 ------DILLSPFGVAPPSWLEDRSVLhahIVYDLIAIKHPEFFT------HE----AAAEVASIIdsldddteiFAISN 144
Cdd:cd03809    80 pkkdkpDLLHSPHNTAPLLLKGCPQVV---TIHDLIPLRYPEFFPkrfrlyYRlllpISLRRADAI---------ITVSE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 145 FTKQDLLSVRPdLAPQQITVIPLAAGSSFQPNSSDVDRaamRRKYQIPvgLPYVLSVATLEVRKNLEQVVSTFAEFLDEN 224
Cdd:cd03809   148 ATRDDIIKFYG-VPPEKIVVIPLGVDPSFFPPESAAVL---IAKYLLP--EPYFLYVGTLEPRKNHERLLKAFALLKKQG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 225 PhsNLHLVLAGMKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICS 304
Cdd:cd03809   222 G--DLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIAS 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246765703 305 ANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKLFNWDVAAQLVVE 367
Cdd:cd03809   300 NISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
468-667 7.07e-57

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: 193.15  E-value: 7.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 468 SYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRYDREIDYYASAPDTGLYNALNKIIPLARGELIC 547
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 548 VLNSDDWLEPDAAKTAVNRISTKSGANLLLTAARVETLDGPL--AWPPAFVHPGSYFKCANVCHNGIYATRSAYEASGPY 625
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVigRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1246765703 626 DETLKIAADFQWIMDCLEAGVQFVYTNERTINFSLGGVSGNV 667
Cdd:cd06433   161 DESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
8-367 8.24e-71

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 236.49  E-value: 8.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703   8 RLALDMYVLEQGlKTGIHRVCDELFPRIAKSPQFRTTLAFRNG----GESTAWQFSSCAQTTAEQSRLTTKRLRASQ--- 80
Cdd:cd03809     1 KILIDGRSLAQR-LTGIGRYTRELLKALAKNDPDESVLAVPPLpgelLRLLREYPELSLGVIKIKLWRELALLRWLQill 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  81 ------DILLSPFGVAPPSWLEDRSVLhahIVYDLIAIKHPEFFT------HE----AAAEVASIIdsldddteiFAISN 144
Cdd:cd03809    80 pkkdkpDLLHSPHNTAPLLLKGCPQVV---TIHDLIPLRYPEFFPkrfrlyYRlllpISLRRADAI---------ITVSE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 145 FTKQDLLSVRPdLAPQQITVIPLAAGSSFQPNSSDVDRaamRRKYQIPvgLPYVLSVATLEVRKNLEQVVSTFAEFLDEN 224
Cdd:cd03809   148 ATRDDIIKFYG-VPPEKIVVIPLGVDPSFFPPESAAVL---IAKYLLP--EPYFLYVGTLEPRKNHERLLKAFALLKKQG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 225 PhsNLHLVLAGMKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICS 304
Cdd:cd03809   222 G--DLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIAS 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246765703 305 ANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKLFNWDVAAQLVVE 367
Cdd:cd03809   300 NISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
468-667 7.07e-57

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: 193.15  E-value: 7.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 468 SYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRYDREIDYYASAPDTGLYNALNKIIPLARGELIC 547
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 548 VLNSDDWLEPDAAKTAVNRISTKSGANLLLTAARVETLDGPL--AWPPAFVHPGSYFKCANVCHNGIYATRSAYEASGPY 625
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVigRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1246765703 626 DETLKIAADFQWIMDCLEAGVQFVYTNERTINFSLGGVSGNV 667
Cdd:cd06433   161 DESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
196-349 2.59e-33

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 125.46  E-value: 2.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 196 PYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGmkGWKLEKFESALSESR-WRDRIIITGFVDEEDLSALYSD 274
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNP--NLKLVIAG--DGEEEKRLKKLAEKLgLGDNVIFLGFVSDEDLPELLKI 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246765703 275 ALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGD--AGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERG 349
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
464-654 5.88e-24

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.55  E-value: 5.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 464 NPLVSYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRY---DREIDYYASAPDTGLYNALNKIIPL 540
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELaakDPRIRVIRLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 541 ARGELICVLNSDDWLEPDAAKTAVNRIStKSGANLLLTAARVETLDGPL-AWPPAFVHPGSYFKCANVCHNGIYA-TRSA 618
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALE-EGPADLVYGSRLIREGESDLrRLGSRLFNLVRLLTNLPDSTSGFRLfRREV 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1246765703 619 YEASGpYDETLKIAADFQWImdcLEAGVQFVYTNER 654
Cdd:COG0463   160 LEELG-FDEGFLEDTELLRA---LRHGFRIAEVPVR 191
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
268-372 2.76e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.05  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 268 LSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSL 345
Cdd:COG0438    14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIedGETGLLVPPGDPEALAEAILRLLEDPELRRRL 93
                          90       100
                  ....*....|....*....|....*...
gi 1246765703 346 SERGLAR-SKLFNWDVAAQLVVERLAHA 372
Cdd:COG0438    94 GEAARERaEERFSWEAIAERLLALYEEL 121
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
175-368 2.16e-20

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 94.00  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 175 PNSSDVDR---------AAMRRKYQIPVGlPYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGmkGWKL---- 241
Cdd:TIGR04047 165 PNGVDAARfspaadaadAALRRRLGLRGG-PYVLAVGGIEPRKNTIDLLEAFALLRARRP--QAQLVIAG--GATLfdyd 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 242 ---EKFESALSESRWR-DRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGDAG 317
Cdd:TIGR04047 240 ayrREFRARAAELGVDpGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRFD 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246765703 318 LLIV-AEDKRAVRDAFRSIVfDAELRRSLSERGLARSKLFNWDVAAQLVVER 368
Cdd:TIGR04047 320 AAWAdPSDPDSIADALALAL-DPARRPALRAAGPELAARYTWDASARAHLEF 370
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
470-567 6.75e-16

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: 75.89  E-value: 6.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 470 VTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRY---DREIDYYASAPDTGLYNALNKIIPLARGELI 546
Cdd:pfam00535   3 IIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYakkDPRVRVIRLPENRGKAGARNAGLRAATGDYI 82
                          90       100
                  ....*....|....*....|.
gi 1246765703 547 CVLNSDDWLEPDAAKTAVNRI 567
Cdd:pfam00535  83 AFLDADDEVPPDWLEKLVEAL 103
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
196-396 3.38e-09

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 60.11  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 196 PYVLSVATLEVRKNLEQVVstfaEFLDENPHSNLHLVLAGMKGWKLEKFESALsesrwrdRIIITGFVDEEDLSALYSDA 275
Cdd:PLN02871  264 PLIVYVGRLGAEKNLDFLK----RVMERLPGARLAFVGDGPYREELEKMFAGT-------PTVFTGMLQGDELSQAYASG 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 276 LCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV-----GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGL 350
Cdd:PLN02871  333 DVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAR 412
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1246765703 351 ARSKLFNWDVAAQLVVE-------RLAHAHQRHLLRPINLPPRGAWPGSSVRK 396
Cdd:PLN02871  413 EEVEKWDWRAATRKLRNeqysaaiWFWRKKRAQLLGPVQWLPAQLFPAPEVNS 465
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
462-568 1.50e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 44.60  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 462 SSNPLVSYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTD-DTLQ--VIRRYDREIDYYASAPDTGLYNALNKII 538
Cdd:PRK10018    2 KDNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSwEQLQqyVTALNDPRITYIHNDINSGACAVRNQAI 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1246765703 539 PLARGELICVLNSDDWLEPdaaktavNRIS 568
Cdd:PRK10018   82 MLAQGEYITGIDDDDEWTP-------NRLS 104
 
Name Accession Description Interval E-value
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
8-367 8.24e-71

glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. MtfB (mannosyltransferase B) in E. coli has been shown to direct the growth of the O9-specific polysaccharide chain. It transfers two mannoses into the position 3 of the previously synthesized polysaccharide.


Pssm-ID: 340838 [Multi-domain]  Cd Length: 362  Bit Score: 236.49  E-value: 8.24e-71
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703   8 RLALDMYVLEQGlKTGIHRVCDELFPRIAKSPQFRTTLAFRNG----GESTAWQFSSCAQTTAEQSRLTTKRLRASQ--- 80
Cdd:cd03809     1 KILIDGRSLAQR-LTGIGRYTRELLKALAKNDPDESVLAVPPLpgelLRLLREYPELSLGVIKIKLWRELALLRWLQill 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  81 ------DILLSPFGVAPPSWLEDRSVLhahIVYDLIAIKHPEFFT------HE----AAAEVASIIdsldddteiFAISN 144
Cdd:cd03809    80 pkkdkpDLLHSPHNTAPLLLKGCPQVV---TIHDLIPLRYPEFFPkrfrlyYRlllpISLRRADAI---------ITVSE 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 145 FTKQDLLSVRPdLAPQQITVIPLAAGSSFQPNSSDVDRaamRRKYQIPvgLPYVLSVATLEVRKNLEQVVSTFAEFLDEN 224
Cdd:cd03809   148 ATRDDIIKFYG-VPPEKIVVIPLGVDPSFFPPESAAVL---IAKYLLP--EPYFLYVGTLEPRKNHERLLKAFALLKKQG 221
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 225 PhsNLHLVLAGMKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICS 304
Cdd:cd03809   222 G--DLKLVIVGGKGWEDEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIAS 299
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1246765703 305 ANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKLFNWDVAAQLVVE 367
Cdd:cd03809   300 NISVLPEVAGDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAEKTLE 362
GT_2_WfgS_like cd06433
WfgS and WfeV are involved in O-antigen biosynthesis; Escherichia coli WfgS and Shigella ...
468-667 7.07e-57

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: 193.15  E-value: 7.07e-57
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 468 SYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRYDREIDYYASAPDTGLYNALNKIIPLARGELIC 547
Cdd:cd06433     1 SIITPTYNQAETLEETIDSVLSQTYPNIEYIVIDGGSTDGTVDIIKKYEDKITYWISEPDKGIYDAMNKGIALATGDIIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 548 VLNSDDWLEPDAAKTAVNRISTKSGANLLLTAARVETLDGPL--AWPPAFVHPGSYFKCANVCHNGIYATRSAYEASGPY 625
Cdd:cd06433    81 FLNSDDTLLPGALLAVVAAFAEHPEVDVVYGDVLLVDENGRVigRRRPPPFLDKFLLYGMPICHQATFFRRSLFEKYGGF 160
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1246765703 626 DETLKIAADFQWIMDCLEAGVQFVYTNERTINFSLGGVSGNV 667
Cdd:cd06433   161 DESYRIAADYDLLLRLLLAGKIFKYLPEVLAAFRLGGVSSTS 202
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
81-367 7.29e-40

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 151.15  E-value: 7.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  81 DILLSPFGVAPPSWLEDRSVLHAHIVYDLIAIKHPEFFTHEAAAE--VASIIDSLDDDTEIFAISNFTKQDLLSVRPDlA 158
Cdd:cd03801    84 DVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLLLLAAERrlLARAEALLRRADAVIAVSEALRDELRALGGI-P 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 159 PQQITVIPlaagssfqpNSSDVDRAAM--RRKYQIPVGLPYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGM 236
Cdd:cd03801   163 PEKIVVIP---------NGVDLERFSPplRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGP--DVRLVIVGG 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 237 KGWKLEKFESALSESRwrDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV--G 314
Cdd:cd03801   232 DGPLRAELEELELGLG--DRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVedG 309
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1246765703 315 DAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR-SKLFNWDVAAQLVVE 367
Cdd:cd03801   310 EGGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLD 363
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
196-349 2.59e-33

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 125.46  E-value: 2.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 196 PYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGmkGWKLEKFESALSESR-WRDRIIITGFVDEEDLSALYSD 274
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNP--NLKLVIAG--DGEEEKRLKKLAEKLgLGDNVIFLGFVSDEDLPELLKI 78
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246765703 275 ALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGD--AGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERG 349
Cdd:pfam00534  79 ADVFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDgeTGFLVKPNNAEALAEAIDKLLEDEELRERLGENA 155
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
156-365 1.33e-25

sucrose-phosphate synthase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. The sucrose-phosphate synthases in this family may be unique to plants and photosynthetic bacteria. This enzyme catalyzes the synthesis of sucrose 6-phosphate from fructose 6-phosphate and uridine 5'-diphosphate-glucose, a key regulatory step of sucrose metabolism. The activity of this enzyme is regulated by phosphorylation and moderated by the concentration of various metabolites and light.


Pssm-ID: 340830 [Multi-domain]  Cd Length: 398  Bit Score: 110.02  E-value: 1.33e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 156 DLAPQQITVIPLAAG-SSFQPNSsdvDRAAMRRKYQIPVGLPYVLSVATLEVRKNLEQVVSTFAEFLDENPHSNLHLVlA 234
Cdd:cd03800   183 GADPSRINVVPPGVDlERFFPVD---RAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLV-G 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 235 GMKGWKLEKFESALSESRWR----DRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLP 310
Cdd:cd03800   259 GPSDDPLSMDREELAELAEElgliDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQ 338
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246765703 311 EVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSK-LFNWD-VAAQLV 365
Cdd:cd03800   339 DIVrdGRTGLLVDPHDPEALAAALRRLLDDPALWQRLSRAGLERARaHYTWEsVADQLL 397
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
137-363 7.82e-25

Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Bme6 in Brucella melitensis has been shown to be involved in the biosynthesis of a polysaccharide.


Pssm-ID: 340848 [Multi-domain]  Cd Length: 377  Bit Score: 107.07  E-value: 7.82e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 137 TEIFAISNFTKQDLLSVRPDLAPQQITVIPLAAGSS-FQPNSSDvdraamRRKYQIPVGLPYVLSVATLEVRKNLEQVVS 215
Cdd:cd03821   151 NNAALVHFTSEQEADELRRFGLEPPIAVIPNGVDIPeFDPGLRD------RRKHNGLEDRRIILFLGRIHPKKGLDLLIR 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 216 TFAEFLDEnpHSNLHLVLAGMKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAM 295
Cdd:cd03821   225 AARKLAEQ--GRDWHLVIAGPDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEAL 302
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246765703 296 SCGTPVICSANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLA---RSKLFNWDVAAQ 363
Cdd:cd03821   303 ACGLPVVITDKCGLSELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRarqVEENFSWEAVAG 373
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
464-654 5.88e-24

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 100.55  E-value: 5.88e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 464 NPLVSYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRY---DREIDYYASAPDTGLYNALNKIIPL 540
Cdd:COG0463     1 MPLVSVVIPTYNEEEYLEEALESLLAQTYPDFEIIVVDDGSTDGTAEILRELaakDPRIRVIRLERNRGKGAARNAGLAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 541 ARGELICVLNSDDWLEPDAAKTAVNRIStKSGANLLLTAARVETLDGPL-AWPPAFVHPGSYFKCANVCHNGIYA-TRSA 618
Cdd:COG0463    81 ARGDYIAFLDADDQLDPEKLEELVAALE-EGPADLVYGSRLIREGESDLrRLGSRLFNLVRLLTNLPDSTSGFRLfRREV 159
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1246765703 619 YEASGpYDETLKIAADFQWImdcLEAGVQFVYTNER 654
Cdd:COG0463   160 LEELG-FDEGFLEDTELLRA---LRHGFRIAEVPVR 191
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
139-375 2.87e-23

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 102.46  E-value: 2.87e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 139 IFAISNFTKQDLLSVRPDlaPQQITVIPLAAGSS-FQPNSSDVDRAAmrrkyqipvGLPYVLSVATLEVRKNLEQVVSTF 217
Cdd:cd03798   154 VIAVSKALAEELVALGVP--RDRVDVIPNGVDPArFQPEDRGLGLPL---------DAFVILFVGRLIPRKGIDLLLEAF 222
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 218 AEFLDENPHsnLHLVLAGmKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSC 297
Cdd:cd03798   223 ARLAKARPD--VVLLIVG-DGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMAC 299
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 298 GTPVICSANSSLPEVVGD--AGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKLFNWDVAAQlvveRLAHAHQR 375
Cdd:cd03798   300 GLPVVATDVGGIPEVVGDpeTGLLVPPGDADALAAALRRALAEPYLRELGEAARARVAERFSWVKAAD----RIAAAYRD 375
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
162-369 3.48e-23

UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. UDP-glucose-diacylglycerol glucosyltransferase (EC 2.4.1.337, UGDG; also known as 1,2-diacylglycerol 3-glucosyltransferase) catalyzes the transfer of glucose from UDP-glucose to 1,2-diacylglycerol forming 3-D-glucosyl-1,2-diacylglycerol.


Pssm-ID: 340844 [Multi-domain]  Cd Length: 372  Bit Score: 102.36  E-value: 3.48e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 162 ITVIPlaAG---SSFQPnssdVDRAAMRRKYQIPVGLPYVLSVATLEVRKNLEQVVSTFAEFLDENphsNLHLVLAGmKG 238
Cdd:cd03817   171 IEVIP--NGidlDKFEK----PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP---NIKLVIVG-DG 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 239 WKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDA 316
Cdd:cd03817   241 PEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVedGEN 320
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1246765703 317 GLLIvAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKLFNWDVAAQLVVERL 369
Cdd:cd03817   321 GFLF-EPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLYEEV 372
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
196-335 2.10e-21

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 90.65  E-value: 2.10e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 196 PYVLSVATL-EVRKNLEQVVSTFAEFLDENphSNLHLVLAGmkGWKLEKFESALSESRwrDRIIITGFVDeeDLSALYSD 274
Cdd:pfam13692   2 PVILFVGRLhPNVKGVDYLLEAVPLLRKRD--NDVRLVIVG--DGPEEELEELAAGLE--DRVIFTGFVE--DLAELLAA 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1246765703 275 ALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV-GDAGLLIVAEDKRAVRDAFRSI 335
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVdGENGLLVPPGDPEALAEAILRL 135
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
268-372 2.76e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.05  E-value: 2.76e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 268 LSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSL 345
Cdd:COG0438    14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIedGETGLLVPPGDPEALAEAILRLLEDPELRRRL 93
                          90       100
                  ....*....|....*....|....*...
gi 1246765703 346 SERGLAR-SKLFNWDVAAQLVVERLAHA 372
Cdd:COG0438    94 GEAARERaEERFSWEAIAERLLALYEEL 121
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
470-582 5.35e-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: 90.26  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 470 VTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRY---DREIDYYASAPDTGLYNALNKIIPLARGELI 546
Cdd:cd00761     2 IIPAYNEEPYLERCLESLLAQTYPNFEVIVVDDGSTDGTLEILEEYakkDPRVIRVINEENQGLAAARNAGLKAARGEYI 81
                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1246765703 547 CVLNSDDWLEPDAAKTAVNRISTKSGANLLLTAARV 582
Cdd:cd00761    82 LFLDADDLLLPDWLERLVAELLADPEADAVGGPGNL 117
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
175-368 2.16e-20

glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from Actinobacteria to Proteobacteria to Cyanobacteria features a radical SAM protein, an N-acetyltransferase, an oxidoreductase, and two additional proteins whose functional classes are unclear. The metabolic role of the cluster is probably biosynthetic. This glycosyltransferase, named from member MSMEG_0565 from Mycobacterium smegmatis, occurs in most but not all instances of the cluster. [Unknown function, Enzymes of unknown specificity]


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 94.00  E-value: 2.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 175 PNSSDVDR---------AAMRRKYQIPVGlPYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGmkGWKL---- 241
Cdd:TIGR04047 165 PNGVDAARfspaadaadAALRRRLGLRGG-PYVLAVGGIEPRKNTIDLLEAFALLRARRP--QAQLVIAG--GATLfdyd 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 242 ---EKFESALSESRWR-DRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGDAG 317
Cdd:TIGR04047 240 ayrREFRARAAELGVDpGPVVITGPVPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGRFD 319
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246765703 318 LLIV-AEDKRAVRDAFRSIVfDAELRRSLSERGLARSKLFNWDVAAQLVVER 368
Cdd:TIGR04047 320 AAWAdPSDPDSIADALALAL-DPARRPALRAAGPELAARYTWDASARAHLEF 370
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
183-370 5.50e-19

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases and includes a sequence annotated as alpha-D-mannose-alpha(1-6)phosphatidyl myo-inositol monomannoside transferase from Bacillus halodurans. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340842 [Multi-domain]  Cd Length: 365  Bit Score: 89.66  E-value: 5.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 183 AAMRRKYQIPvGLPYVLSVATLEVRKNLEQVVSTFAEFLDENPHsnlHLVLAGmKGWKLEKFESALSEsrwrdrIIITGF 262
Cdd:cd03814   187 AALRRRLGPP-GRPLLLYVGRLAPEKNLEALLDADLPLAASPPV---RLVVVG-DGPARAELEARGPD------VIFTGF 255
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 263 VDEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGD--AGLLIVAEDKRAVRDAFRSIVFDAE 340
Cdd:cd03814   256 LTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPggTGALVEPGDAAAFAAALRALLEDPE 335
                         170       180       190
                  ....*....|....*....|....*....|
gi 1246765703 341 LRRSLSERGLARSKLFNWDVAAQLVVERLA 370
Cdd:cd03814   336 LRRRMAARARAEAERYSWEAFLDNLLDYYA 365
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
463-701 5.85e-19

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 85.81  E-value: 5.85e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 463 SNPLVSYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRYDR-EIDYYASAPDTGLYNALNKIIPLA 541
Cdd:COG1216     1 MRPKVSVVIPTYNRPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTAELLAALAFpRVRVIRNPENLGFAAARNLGLRAA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 542 RGELICVLNSDDWLEPDAAKTAVNRistksgANLLLtaarvetldgplawppafvhpgsyfkcanvchngiyaTRSAYEA 621
Cdd:COG1216    81 GGDYLLFLDDDTVVEPDWLERLLAA------ACLLI-------------------------------------RREVFEE 117
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 622 SGPYDETLKIAA-DFQWIMDCLEAGVQFVYTNERTINFSLGGVSGNVRAHRAEC--MQILARRFGTLSEAEIKTLSDIFF 698
Cdd:COG1216   118 VGGFDERFFLYGeDVDLCLRLRKAGYRIVYVPDAVVYHLGGASSGPLLRAYYLGrnRLLFLRKHGPRPLLRLALLRGLRL 197

                  ...
gi 1246765703 699 VFR 701
Cdd:COG1216   198 RLR 200
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
141-349 1.27e-18

Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 family of glycosyltransferases. WavL in Vibrio cholerae has been shown to be involved in the biosynthesis of the lipopolysaccharide core.


Pssm-ID: 340846 [Multi-domain]  Cd Length: 345  Bit Score: 88.18  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 141 AISNFTKqDLLSVRPDLAPQQITVIPLAAG-SSFQPNSSDVDRAAMRrkyqIPVGLPYVLSVATLEVRKNLEQVVsTFAE 219
Cdd:cd03819   132 AVSELVR-DHLIEALGVDPERIRVIPNGVDtDRFPPEAEAEERAQLG----LPEGKPVVGYVGRLSPEKGWLLLV-DAAA 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 220 FLDENPHsnLHLVLAGmKGWKLEKFESALSESRWRDRIIITGFVdeEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGT 299
Cdd:cd03819   206 ELKDEPD--FRLLVAG-DGPERDEIRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGT 280
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246765703 300 PVICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERG 349
Cdd:cd03819   281 PVVATDVGGAREIVvhGRTGLLVPPGDAEALADAIRAAKLLPEAREKLQAAA 332
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
139-347 5.43e-18

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 86.26  E-value: 5.43e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 139 IFAISNFTKQDLLSVRPDLaPQQITVIPlaagssfqpNSSDVDRAAMRRK---YQIPVGLPYVLSVATLEVRKNLEQVVS 215
Cdd:cd03811   139 IVCVSKGIKEDLIRLGPSP-PEKIEVIY---------NPIDIDRIRALAKepiLNEPEDGPVILAVGRLDPQKGHDLLIE 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 216 TFAEFLDENPhsNLHLVLAG---MKGwKLEKFESALSESrwrDRIIITGFVDeeDLSALYSDALCFIYMSLYEGFGLPPL 292
Cdd:cd03811   209 AFAKLRKKYP--DVKLVILGdgpLRE-ELEKLAKELGLA---ERVIFLGFQS--NPYPYLKKADLFVLSSRYEGFPNVLL 280
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 293 EAMSCGTPVICSANSSLPEVV--GDAGLLIV---AEDKRAVRDAFRSIVFDAELRRSLSE 347
Cdd:cd03811   281 EAMALGTPVVSTDCPGPREILddGENGLLVPdgdAAALAGILAALLQKKLDAALRERLAK 340
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
141-377 2.62e-17

Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbnK in Shigella dysenteriae has been shown to be involved in the type 7 O-antigen biosynthesis.


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 84.29  E-value: 2.62e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 141 AISNFTKQDLLSVrpDLAPQQITVIPLAaGSSFQPNSSDVDRAAMRRKYQIPVGLPYVLSVATLEVRKNLEQVVSTFAEF 220
Cdd:cd03807   139 ANSSAVAEFHQEQ--GYAKNKIVVIYNG-IDLFKLSPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALL 215
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 221 LDEnpHSNLHLVLAGmKGWKLEKFESALSESRWRDRIIITGFVDeeDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTP 300
Cdd:cd03807   216 VET--HPDLRLLLVG-RGPERPNLERLLLELGLEDRVHLLGERS--DVPALLPAMDIFVLSSRTEGFPNALLEAMACGLP 290
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246765703 301 VICSANSSLPEVVGD-AGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARsklfnwdVAAQLVVERLAHAHQRHL 377
Cdd:cd03807   291 VVATDVGGAAELVDDgTGFLVPAGDPQALADAIRALLEDPEKRARLGRAARER-------IANEFSIDAMVRRYETLY 361
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
453-653 4.27e-17

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: 82.87  E-value: 4.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 453 RLVQPLAKLSSNPLVSYVTIVRNNAATLSRAIESVRSQTYP--LVEHVILDGASTDDTLQVIRRY---DREIDYYASAPD 527
Cdd:COG1215    17 ALARRRRAPADLPRVSVIIPAYNEEAVIEETLRSLLAQDYPkeKLEVIVVDDGSTDETAEIARELaaeYPRVRVIERPEN 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 528 TGLYNALNKIIPLARGELICVLNSDDWLEPDAAKTAVnristksganllltaarvetldgplawpPAFVHPgsyfKCANV 607
Cdd:COG1215    97 GGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLV----------------------------AAFADP----GVGAS 144
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1246765703 608 CHNGIYaTRSAYEASGPYDETLkIAADFQWIMDCLEAGVQFVYTNE 653
Cdd:COG1215   145 GANLAF-RREALEEVGGFDEDT-LGEDLDLSLRLLRAGYRIVYVPD 188
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
199-320 5.50e-16

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 78.21  E-value: 5.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 199 LSVATLEVRKNLEQVVSTFAEFLDEnpHSNLHLVLAGMKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCF 278
Cdd:cd01635   114 VSVGRLVPEKGIDLLLEALALLKAR--LPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAAADVF 191
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1246765703 279 IYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDAGLLI 320
Cdd:cd01635   192 VLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVvdGENGLLV 235
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
470-567 6.75e-16

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: 75.89  E-value: 6.75e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 470 VTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRY---DREIDYYASAPDTGLYNALNKIIPLARGELI 546
Cdd:pfam00535   3 IIPTYNEEKYLLETLESLLNQTYPNFEIIVVDDGSTDGTVEIAEEYakkDPRVRVIRLPENRGKAGARNAGLRAATGDYI 82
                          90       100
                  ....*....|....*....|.
gi 1246765703 547 CVLNSDDWLEPDAAKTAVNRI 567
Cdd:pfam00535  83 AFLDADDEVPPDWLEKLVEAL 103
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
139-352 3.03e-15

capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. CapM in Staphylococcus aureus is required for the synthesis of type 1 capsular polysaccharides.


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 78.02  E-value: 3.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 139 IFAISNFTKQDLLSVRPdLAPQQITVIPlaaGSSFqpnssDVDRAAmRRKYQIPVGLPYVLSVATLEVRKNLEQVVStFA 218
Cdd:cd03808   143 VIFVNEDDRDLAIKKGI-IKKKKTVLIP---GSGV-----DLDRFQ-YSPESLPSEKVVFLFVARLLKDKGIDELIE-AA 211
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 219 EFLDEnPHSNLHLVLAGmKGWKLEKFESALSESRWRDRIIITGFVDeeDLSALYSDALCFIYMSLYEGFGLPPLEAMSCG 298
Cdd:cd03808   212 KILKK-KGPNVRFLLVG-DGELENPSEILIEKLGLEGRIEFLGFRS--DVPELLAESDVFVLPSYREGLPRSLLEAMAAG 287
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1246765703 299 TPVICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR 352
Cdd:cd03808   288 RPVITTDVPGCRELVidGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAARKR 343
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
197-363 3.30e-15

amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmSD in Erwinia amylovora has been shown to be involved in the biosynthesis of amylovoran, the acidic exopolysaccharide acting as a virulence factor. This enzyme may be responsible for the formation of galactose alpha-1,6 linkages in amylovoran.


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 77.66  E-value: 3.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 197 YVLSVATLEVRKNLEQVVSTFAEFLDENPHSNLHLVLAGMKGWKLEKFESALsesRWRDRIIITGFVdeEDLSALYSDAL 276
Cdd:cd03820   183 RILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKL---GLEDRVKLLGPT--KNIAEEYANSS 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 277 CFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLP-EVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARS 353
Cdd:cd03820   258 IFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPsEIIedGENGLLVPNGDVDALAEALLRLMEDEELRKKMGKNARKNA 337
                         170
                  ....*....|
gi 1246765703 354 KLFNWDVAAQ 363
Cdd:cd03820   338 ERFSIEKIIK 347
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
149-367 2.10e-14

putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Escherichia coli WcaC has been predicted to function in colanic acid biosynthesis. WcfI in Bacteroides fragilis has been shown to be involved in the capsular polysaccharide biosynthesis.


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 75.45  E-value: 2.10e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 149 DLLSVRPDLAPQQITVIPLAAGSS-FQPnssdVDRAAMRRKYQIPVGLPYVL--SVATLEVRKNleqvvstFAEFLDE-- 223
Cdd:cd03825   150 DMVRRSPLLKGLPVVVIPNGIDTEiFAP----VDKAKARKRLGIPQDKKVILfgAESVTKPRKG-------FDELIEAlk 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 224 --NPHSNLHLVLAGMKGWKLEKFESalsesrwrdRIIITGFV-DEEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTP 300
Cdd:cd03825   219 llATKDDLLLVVFGKNDPQIVILPF---------DIISLGYIdDDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGTP 289
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 301 VICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKL-FNWDVAAQLVVE 367
Cdd:cd03825   290 VVAFDTGGSPEIVqhGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARALAENhFDQRVQAQRYLE 359
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
163-356 4.03e-14

Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP-linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria and eukaryotes.


Pssm-ID: 340826 [Multi-domain]  Cd Length: 355  Bit Score: 74.62  E-value: 4.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 163 TVIPLAAGSSfQPNSSDVDRAAMRRKYqipVGLPYVLSVATLEVRKNLEQVvstfaefLDENPHSNLHLVLAGmkGWKLE 242
Cdd:cd03795   163 RVIPLGIDKN-VYNIPRVDFENIKREK---KGKKIFLFIGRLVYYKGLDYL-------IEAAQYLNYPIVIGG--EGPLK 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 243 KFESALSESRWRDRIIITGFVDEEDLSALY--SDALCFIYMSLYEGFGLPPLEAMSCGTPVI-CSANSSLPEVV--GDAG 317
Cdd:cd03795   230 PDLEAQIELNLLDNVKFLGRVDDEEKVIYLhlCDVFVFPSVLRSEAFGIVLLEAMMCGKPVIsTNIGTGVPYVNnnGETG 309
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1246765703 318 LLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR-SKLF 356
Cdd:cd03795   310 LVVPPKDPDALAEAIDKLLSDEELRESYGENAKKRfEELF 349
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
132-375 6.05e-14

N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340859 [Multi-domain]  Cd Length: 370  Bit Score: 74.31  E-value: 6.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 132 SLDDDTEIFAISNFTKQD---LLSVRPDlapqqITVIPlaagssfqpNSSDVDR------AAMRRKYQIPVGLPYVLSVA 202
Cdd:cd04962   138 SINKSDRVTAVSSSLRQEtyeLFDVDKD-----IEVIH---------NFIDEDVfkrkpaGALKRRLLAPPDEKVVIHVS 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 203 TLEVRKNLEQVVSTFAEFLDENPHSnlhLVLAGmKGWKLEKFESALSESRWRDRIIITGfvDEEDLSALYSDALCFIYMS 282
Cdd:cd04962   204 NFRPVKRIDDVVRVFARVRRKIPAK---LLLVG-DGPERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPS 277
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 283 LYEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARS-KLFNwd 359
Cdd:cd04962   278 EKESFGLAALEAMACGVPVVSSNAGGIPEVVkhGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAaERFD-- 355
                         250
                  ....*....|....*.
gi 1246765703 360 vaAQLVVERLAHAHQR 375
Cdd:cd04962   356 --PERIVPQYEAYYRR 369
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
185-315 1.21e-12

capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. capH in Staphylococcus aureus has been shown to be required for the biosynthesis of the type 1 capsular polysaccharide (CP1).


Pssm-ID: 340840 [Multi-domain]  Cd Length: 357  Bit Score: 70.01  E-value: 1.21e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 185 MRRKYQIPVGLPYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGmKGWKLEKFESALSESRWRDRIIITGFVd 264
Cdd:cd03812   181 KRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNP--NVKLVLVG-EGELKEKIKEKVKELGLEDKVIFLGFR- 256
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1246765703 265 eEDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGD 315
Cdd:cd03812   257 -NDVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITN 306
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
465-632 1.43e-12

Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene encodes a predicted protein of 1,276 amino acids, which is required for O-antigen biosynthesis in Myxococcus xanthus. It is a subfamily of Glycosyltransferase Family GT2, which includes diverse families of glycosyl transferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds.


Pssm-ID: 133027 [Multi-domain]  Cd Length: 202  Bit Score: 67.23  E-value: 1.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 465 PLVSYVTIVRN-NAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQ-VIRRY---DREIDYYASAPDTGLYNALNKIIP 539
Cdd:cd04184     1 PLISIVMPVYNtPEKYLREAIESVRAQTYPNWELCIADDASTDPEVKrVLKKYaaqDPRIKVVFREENGGISAATNSALE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 540 LARGELICVLNSDDWLEPDAAKTAVNRISTKSGANLLLTAARVETLDGPLAWPpafvhpgsYFKCA---------N-VCH 609
Cdd:cd04184    81 LATGEFVALLDHDDELAPHALYEVVKALNEHPDADLIYSDEDKIDEGGKRSEP--------FFKPDwspdlllsqNyIGH 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1246765703 610 NGIYAT---------RSAYEASGPYDETLKIA 632
Cdd:cd04184   153 LLVYRRslvrqvggfREGFEGAQDYDLVLRVS 184
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
139-352 2.05e-11

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 66.46  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 139 IFAISNFTKQDLLSVRPDLAPQQITVI-PLAAGSSFQPNSSDVDRaamrRKYQIPVGLPYVLSVATLEVRKNLEQVVSTF 217
Cdd:cd03805   158 IVVNSNFTAGVFKKTFPSLAKNPPEVLyPCVDTDSFDSTSEDPDP----GDLIAKSNKKFFLSINRFERKKNIALAIEAF 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 218 AEFLDENPH-SNLHLVLAGmkGwklekFESALSESR---------------WRDRII-ITGFVDEEDLSaLYSDALCFIY 280
Cdd:cd03805   234 AKLKQKLPEfENVRLVIAG--G-----YDPRVAENVeyleelqrlaeellnVEDQVLfLRSISDSQKEQ-LLSSALALLY 305
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1246765703 281 MSLYEGFGLPPLEAMSCGTPVIcSANSSLP-EVVGDA--GLLIvaeDKRAVR--DAFRSIVFDAELRRSLSERGLAR 352
Cdd:cd03805   306 TPSNEHFGIVPLEAMYAGKPVI-ACNSGGPlETVVEGvtGFLC---EPTPEAfaEAMLKLANDPDLADRMGAAGRKR 378
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
182-357 2.67e-11

LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after WbdM in Escherichia coli. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 65.93  E-value: 2.67e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 182 RAAMRRKYQIPVGLPYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGmKGWKLEKFESALSESRWRDRIIITG 261
Cdd:cd04951   175 RLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKN--DFKLLIAG-DGPLRNELERLICNLNLVDRVILLG 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 262 FVDeeDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIV-FDAE 340
Cdd:cd04951   252 QIS--NISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGDHNYVVPVSDPQLLAEKIKEIFdMSDE 329
                         170
                  ....*....|....*..
gi 1246765703 341 LRRSLSERGLARSKLFN 357
Cdd:cd04951   330 ERDILGNKNEYIAKNFS 346
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
474-564 3.98e-11

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: 62.63  E-value: 3.98e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 474 RNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRydreidYYASAPDTGLY----------NALNKIIPLARG 543
Cdd:cd06423     6 YNEEAVIERTIESLLALDYPKLEVIVVDDGSTDDTLEILEE------LAALYIRRVLVvrdkenggkaGALNAGLRHAKG 79
                          90       100
                  ....*....|....*....|.
gi 1246765703 544 ELICVLNSDDWLEPDAAKTAV 564
Cdd:cd06423    80 DIVVVLDADTILEPDALKRLV 100
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
470-567 4.63e-11

Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse families of glycosyltransferases with a common GT-A type structural fold, which has two tightly associated beta/alpha/beta domains that tend to form a continuous central sheet of at least eight beta-strands. These are enzymes that catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. Glycosyltransferases have been classified into more than 90 distinct sequence based families.


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 61.81  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 470 VTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRYDREIDYYASAPDTGLYNALNKIIPLARGELICVL 549
Cdd:cd04186     2 IIVNYNSLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSVELLRELFPEVRLIRNGENLGFGAGNNQGIREAKGDYVLLL 81
                          90
                  ....*....|....*...
gi 1246765703 550 NSDDWLEPDAAKTAVNRI 567
Cdd:cd04186    82 NPDTVVEPGALLELLDAA 99
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
227-330 1.05e-10

UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. aviGT4 in Streptomyces viridochromogenes has been shown to be involved in biosynthesis of oligosaccharide antibiotic avilamycin A. Inactivation of aviGT4 resulted in a mutant that accumulated a novel avilamycin derivative lacking the terminal eurekanate residue.


Pssm-ID: 340832 [Multi-domain]  Cd Length: 333  Bit Score: 63.85  E-value: 1.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 227 SNLHLVLAGmKGWKLEKFESaLSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLY-EGFGLPPLEAMSCGTPVICSA 305
Cdd:cd03802   194 AGLPLKIAG-KVRDEDYFYY-LQEPLPGPRIEFIGEVGHDEKQELLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYR 271
                          90       100
                  ....*....|....*....|....*....
gi 1246765703 306 NSSLPEVVGDA--GLLI--VAEDKRAVRD 330
Cdd:cd03802   272 RGGLPEVIQHGetGFLVdsVEEMAEAIAN 300
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
139-352 4.46e-10

glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpE7 in Sinorhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucans (exopolysaccharide II).


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 61.96  E-value: 4.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 139 IFAISNFTKQdlLSVRPDLAPQQITVIPlaagssfqpNSSDVDRAAM--RRKYQIPVGLPYVlsvATLEVRKNLEQVVst 216
Cdd:cd03823   147 VLAPSRFTAN--LHEANGLFSARISVIP---------NAVEPDLAPPprRRPGTERLRFGYI---GRLTEEKGIDLLV-- 210
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 217 faEFLDENPHSNLHLVLAGmkGWKLEKFESALSEsrwrDRIIITGFVDEEDLSALYSDALCFIYMSL-YEGFGLPPLEAM 295
Cdd:cd03823   211 --EAFKRLPREDIELVIAG--HGPLSDERQIEGG----RRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAI 282
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1246765703 296 SCGTPVICSANSSLPEVVGDA--GLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR 352
Cdd:cd03823   283 AAGLPVIASDLGGIAELIQPGvnGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAEPP 341
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
196-396 3.38e-09

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 60.11  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 196 PYVLSVATLEVRKNLEQVVstfaEFLDENPHSNLHLVLAGMKGWKLEKFESALsesrwrdRIIITGFVDEEDLSALYSDA 275
Cdd:PLN02871  264 PLIVYVGRLGAEKNLDFLK----RVMERLPGARLAFVGDGPYREELEKMFAGT-------PTVFTGMLQGDELSQAYASG 332
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 276 LCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV-----GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGL 350
Cdd:PLN02871  333 DVFVMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdqeGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAR 412
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1246765703 351 ARSKLFNWDVAAQLVVE-------RLAHAHQRHLLRPINLPPRGAWPGSSVRK 396
Cdd:PLN02871  413 EEVEKWDWRAATRKLRNeqysaaiWFWRKKRAQLLGPVQWLPAQLFPAPEVNS 465
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
218-363 8.26e-09

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 58.51  E-value: 8.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 218 AEFLDENPHSNLHLVLAGMKGWKLEKFESALSesrwRDRIIITGFVDEEDLSALYSDA-LCFIYMS--LYEGFGLP--PL 292
Cdd:cd03794   239 AERLKRRPDIRFLFVGDGDEKERLKELAKARG----LDNVTFLGRVPKEEVPELLSAAdVGLVPLKdnPANRGSSPskLF 314
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1246765703 293 EAMSCGTPVICSAN--SSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKL-FNWDVAAQ 363
Cdd:cd03794   315 EYMAAGKPILASDDggSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELAEEkFSREKLAD 388
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
466-634 2.06e-08

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: 55.70  E-value: 2.06e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 466 LVSYVTIVRNNAATLSRAIESVRSQTYP--LVEHVILDGASTDDTLQVIRRY---DREIDYYaSAPDTGLYNALNKIIPL 540
Cdd:cd02525     1 FVSIIIPVRNEEKYIEELLESLLNQSYPkdLIEIIVVDGGSTDGTREIVQEYaakDPRIRLI-DNPKRIQSAGLNIGIRN 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 541 ARGELICVLN-----SDDWLEPDAAKtavnriSTKSGANLLLTAARVETlDGPLAWPPAFV--HP----GSYFKCANV-- 607
Cdd:cd02525    80 SRGDIIIRVDahavyPKDYILELVEA------LKRTGADNVGGPMETIG-ESKFQKAIAVAqsSPlgsgGSAYRGGAVki 152
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1246765703 608 -----CHNGIYaTRSAYEASGPYDETLKIAAD 634
Cdd:cd02525   153 gyvdtVHHGAY-RREVFEKVGGFDESLVRNED 183
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
112-357 9.31e-08

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 54.61  E-value: 9.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 112 IKHPeFFTHEAAAEVASIIDSL----DDDTEIFAISNFTKQDLLSV-------------RPDLA---PQQITVIPLAAGS 171
Cdd:cd04949    67 TGQV-ILNTKGPAKKGAVLHNEhvknNDDPEHSLIKNFYKYVFENLnkydaiivsteqqKQDLSerfNKYPPIFTIPVGY 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 172 SfQPNSSDVDRAAmRRKYQIpvglpyvLSVATLEVRKNLEQVVSTFAEFLDENPHSNLHLVLAGMKGWKLEKFESALses 251
Cdd:cd04949   146 V-DQLDTAESNHE-RKSNKI-------ITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEEL--- 213
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 252 RWRDRIIITGFVDeeDLSALYSDALCFIYMSLYEGFGLPPLEAMSCGTPVIC-SANSSLPEVV--GDAGLLIVAEDKRAV 328
Cdd:cd04949   214 HLEDNVFLKGYHS--NLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSyDVKYGPSELIedGENGYLIEKNNIDAL 291
                         250       260
                  ....*....|....*....|....*....
gi 1246765703 329 RDAFRSIVFDAELRRSLSERGLARSKLFN 357
Cdd:cd04949   292 ADKIIELLNDPEKLQQFSEESYKIAEKYS 320
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
196-351 9.33e-08

glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to glycosyltransferase family 4 (GT4). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340860 [Multi-domain]  Cd Length: 365  Bit Score: 54.77  E-value: 9.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 196 PYVLSVATLEVRKNLEQVVSTFAEFLDENPHSNLHLVLAGMKGWKLEKFESALsesrwrDRIIITGFVDEEDLSALYSDA 275
Cdd:cd05844   190 PTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAAL------GRVRFLGALPHAEVQDWMRRA 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 276 LCFIYMSLY------EGFGLPPLEAMSCGTPVICSANSSLPEVVGD--AGLLIVAEDKRAVRDAFRSIVFDAELRRSLSE 347
Cdd:cd05844   264 EIFCLPSVTaasgdsEGLGIVLLEAAACGVPVVSSRHGGIPEAILDgeTGFLVPEGDVDALADALQALLADRALADRMGG 343

                  ....
gi 1246765703 348 RGLA 351
Cdd:cd05844   344 AARA 347
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
197-303 3.33e-07

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 53.06  E-value: 3.33e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 197 YVLSVATLEVRKNLEQVVSTFAEfldenphSNLHLVLAGmKGWKLEKFESALSESrwrdrIIITGFVDEEDLSALYSDAL 276
Cdd:cd03804   201 YYLTASRLVPYKRIDLAVEAFNE-------LPKRLVVIG-DGPDLDRLRAMASPN-----VEFLGYQPDEVLKELLSKAR 267
                          90       100
                  ....*....|....*....|....*..
gi 1246765703 277 CFIYMSlYEGFGLPPLEAMSCGTPVIC 303
Cdd:cd03804   268 AFVFAA-EEDFGIVPVEAQACGTPVIA 293
Beta4Glucosyltransferase cd02511
UDP-glucose LOS-beta-1,4 glucosyltransferase is required for biosynthesis of ...
467-561 5.42e-07

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: 51.52  E-value: 5.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 467 VSYVTIVRNNAATLSRAIESVRsqtyPLV-EHVILDGASTDDTLQVIRRY-----DREIDYYASapdtglynALNKIIPL 540
Cdd:cd02511     2 LSVVIITKNEERNIERCLESVK----WAVdEIIVVDSGSTDRTVEIAKEYgakvyQRWWDGFGA--------QRNFALEL 69
                          90       100
                  ....*....|....*....|.
gi 1246765703 541 ARGELICVLNSDDWLEPDAAK 561
Cdd:cd02511    70 ATNDWVLSLDADERLTPELAD 90
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
161-364 6.43e-07

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 52.39  E-value: 6.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 161 QITVIPlaAGSsfqPNSSDVDRAAMRRKYQiPVGLPYVLSVATLEVRKNLEQVVSTFAEFLDENPhsNLHLVLAGMKGWK 240
Cdd:cd03822   159 NIEVIP--HGV---PEVPQDPTTALKRLLL-PEGKKVILTFGFIGPGKGLEILLEALPELKAEFP--DVRLVIAGELHPS 230
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 241 LEKFESALSESRWRDR-------IIITGFVDEEDLSALYS--DALCFIYMSLYEGFGLPPLEAMSCGTPVICS-ANSSLP 310
Cdd:cd03822   231 LARYEGERYRKAAIEElglqdhvDFHNNFLPEEEVPRYISaaDVVVLPYLNTEQSSSGTLSYAIACGKPVISTpLRHAEE 310
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1246765703 311 EVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKLFNWDVAAQL 364
Cdd:cd03822   311 LLADGRGVLVPFDDPSAIAEAILRLLEDDERRQAIAERAYAYARAMTWESIADR 364
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
198-360 7.14e-07

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 52.03  E-value: 7.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 198 VLSVATLEVRKNLEQVVSTFAEFLDENP--HSNLHLVLAGmKGWKLEKFESALSESRWRDRIIITGfvDEEDLSALYSDA 275
Cdd:TIGR03088 197 VGTVGRLQAVKDQPTLVRAFALLVRQLPegAERLRLVIVG-DGPARGACEQMVRAAGLAHLVWLPG--ERDDVPALMQAL 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 276 LCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR- 352
Cdd:TIGR03088 274 DLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVqhGVTGALVPPGDAVALARALQPYVSDPAARRAHGAAGRARa 353

                  ....*...
gi 1246765703 353 SKLFNWDV 360
Cdd:TIGR03088 354 EQQFSINA 361
GT_2_like_d cd04196
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
475-582 2.33e-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: 133039 [Multi-domain]  Cd Length: 214  Bit Score: 49.17  E-value: 2.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 475 NNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRY---DREIDYYASA-PDTGLYNALNKIIPLARGELICVLN 550
Cdd:cd04196     8 NGEKYLREQLDSILAQTYKNDELIISDDGSTDGTVEIIKEYidkDPFIIILIRNgKNLGVARNFESLLQAADGDYVFFCD 87
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1246765703 551 SDD-WLePDAAKTAVNRISTKSGANLLLTAARV 582
Cdd:cd04196    88 QDDiWL-PDKLERLLKAFLKDDKPLLVYSDLEL 119
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
473-560 4.09e-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: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 48.82  E-value: 4.09e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 473 VRNNAATLSRAIESVRSQTYP--LVEHVILDGASTDDTLQVIRRYdREIDYY-------ASAPDTGLYNALNKIIPLARG 543
Cdd:cd04192     5 ARNEAENLPRLLQSLSALDYPkeKFEVILVDDHSTDGTVQILEFA-AAKPNFqlkilnnSRVSISGKKNALTTAIKAAKG 83
                          90       100
                  ....*....|....*....|...
gi 1246765703 544 ELI------CVLNSDDWLEPDAA 560
Cdd:cd04192    84 DWIvttdadCVVPSNWLLTFVAF 106
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
136-349 5.74e-06

trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly catalyzes trehalose synthesis and degradation from alpha-glucose-1-phosphate (alpha-Glc-1-P) and glucose. The catalyzing activity includes the phosphorolysis of trehalose, which produce alpha-Glc-1-P and glucose, and the subsequent synthesis of trehalose. This family is most closely related to the GT4 family of glycosyltransferases.


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 49.24  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 136 DTEIFAISNFtkqdllsVRPDLAPQQItVIPlAAGSSFQPNSSDVDRAAMRRKYQIPVGL----PYVLSVATLEVRKNLE 211
Cdd:cd03792   143 DLFVFHPPEF-------VPPQVPPPKF-YIP-PSIDPLSGKNKDLSPADIRYYLEKPFVIdperPYILQVARFDPSKDPL 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 212 QVVSTFAEFLDEnpHSNLHLVLAGM------KGWKLekFESALSESRWRDRIIIT--GFVDEEdLSALYSDALCFIYMSL 283
Cdd:cd03792   214 GVIDAYKLFKRR--AEEPQLVICGHgavddpEGSVV--YEEVMEYAGDDHDIHVLrlPPSDQE-INALQRAATVVLQLST 288
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246765703 284 YEGFGLPPLEAMSCGTPVICSANSSLPEVV--GDAGLLIVAEDKRAVRdaFRSIVFDAELRRSLSERG 349
Cdd:cd03792   289 REGFGLTVSEALWKGKPVIATPAGGIPLQVidGETGFLVNSVEGAAVR--ILRLLTDPELRRKMGLAA 354
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
254-359 1.21e-05

glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family of glycosyltransferases. Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in bacteria, while some of them are also found in Archaea and eukaryotes.


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 48.49  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 254 RDRIIITGFVDEEDlsALYSDALcFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGD-------AGLLIVAEDKR 326
Cdd:cd03813   353 ENKVKFLGFQNIKE--YYPKLGL-LVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGaddalgqAGLVVPPADPE 429
                          90       100       110
                  ....*....|....*....|....*....|....
gi 1246765703 327 AVRDAFRSIVFDAELRRSLSERGLAR-SKLFNWD 359
Cdd:cd03813   430 ALAEALIKLLRDPELRQAFGEAGRKRvEKYYTLE 463
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
451-564 1.44e-05

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: 47.19  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 451 GRRLVQPLAKLSSNPLVSYVTIVRNNAATLSRAIESVRSQTYP--LVEHVILDGASTDDTLQVIRRY-DREIDYYASAPD 527
Cdd:cd06439    15 LRPKPPSLPDPAYLPTVTIIIPAYNEEAVIEAKLENLLALDYPrdRLEIIVVSDGSTDGTAEIAREYaDKGVKLLRFPER 94
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1246765703 528 TGLYNALNKIIPLARGELICVLNSDDWLEPDAAKTAV 564
Cdd:cd06439    95 RGKAAALNRALALATGEIVVFTDANALLDPDALRLLV 131
sucrsPsyn_pln TIGR02468
sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this ...
278-517 4.05e-05

sucrose phosphate synthase/possible sucrose phosphate phosphatase, plant; Members of this family are sucrose-phosphate synthases of plants. This enzyme is known to exist in multigene families in several species of both monocots and dicots. The N-terminal domain is the glucosyltransferase domain. Members of this family also have a variable linker region and a C-terminal domain that resembles sucrose phosphate phosphatase (SPP) (EC 3.1.3.24) (see TIGR01485), the next and final enzyme of sucrose biosynthesis. The SPP-like domain likely serves a binding and not a catalytic function, as the reported SPP is always encoded by a distinct protein.


Pssm-ID: 274147 [Multi-domain]  Cd Length: 1050  Bit Score: 47.47  E-value: 4.05e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  278 FIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEV--VGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLARSKL 355
Cdd:TIGR02468  575 FINPAFIEPFGLTLIEAAAHGLPMVATKNGGPVDIhrVLDNGLLVDPHDQQAIADALLKLVADKQLWAECRQNGLKNIHL 654
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  356 FNWDVAAQLVVERLAHAHQRHllrPINLPPRGAWPGSSVRKTRSVSGANIANLDVRVngsigpSFSVGASRPHGERNwpm 435
Cdd:TIGR02468  655 FSWPEHCKTYLSRIASCRPRH---PQWQRDTDDGEEASEDESPGDSLRDIQDISLNL------SVDGDKESNNGSSN--- 722
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703  436 wsdrlQSDEGLLAEGGRRLVQPLAKLSSNPLVSYVTIVRNNAATLSRAIesvRSQTYPLVehVILDGASTDDTLQVIRRY 515
Cdd:TIGR02468  723 -----VEGSGPPADRVAKIENAVRSWSKSPKGSSAKAQQGSGAGKYPAL---RRRKRLFV--IAVDCYDDKDLLQIIKNI 792

                   ..
gi 1246765703  516 DR 517
Cdd:TIGR02468  793 FE 794
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
219-352 4.12e-05

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 46.46  E-value: 4.12e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 219 EFLDE--NPHSNLHLVLAGmKGWklekfesalSESRWRDRIIITGFVDEEDLSALYSDA---LCFIYMSLyEGFGLPP-- 291
Cdd:COG4641   152 ARLEEllLAPAGLRLKIYG-PGW---------PKLALPANVRRGGHLPGEEHPAAYASSkitLNVNRMAA-SPDSPTRrt 220
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1246765703 292 LEAMSCGTPVICSANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR 352
Cdd:COG4641   221 FEAAACGAFLLSDPWEGLEELFEPGEEVLVFRDGEELAEKLRYLLADPEERRAIAEAGRRR 281
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
132-312 4.34e-05

phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Phosphatidylinositol glycan-class A (PIG-A), an X-linked gene in humans, is necessary for the synthesis of N-acetylglucosaminyl-phosphatidylinositol, a very early intermediate in glycosyl phosphatidylinositol (GPI)-anchor biosynthesis. The GPI-anchor is an important cellular structure that facilitates the attachment of many proteins to cell surfaces. Somatic mutations in PIG-A have been associated with Paroxysmal Nocturnal Hemoglobinuria (PNH), an acquired hematological disorder.


Pssm-ID: 340827 [Multi-domain]  Cd Length: 398  Bit Score: 46.46  E-value: 4.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 132 SLDDDTEIFAISNFTKQDLlSVRPDLAPQQITVIPLAAGSS-FQPNSSDVDRAAMRrkyqipvglpyVLSVATLEVRKNL 210
Cdd:cd03796   141 SLADIDHVICVSHTSKENT-VLRASLDPRIVSVIPNAVDSSdFTPDPSKPDPNKIT-----------IVVISRLVYRKGI 208
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 211 EQVVSTFAEFLdeNPHSNLHLVLAGmKGWKLEKFESALSESRWRDRIIITGFVDEEDLSALYSDALCFIYMSLYEGFGLP 290
Cdd:cd03796   209 DLLVGIIPRIC--KKHPNVRFIIGG-DGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIA 285
                         170       180
                  ....*....|....*....|..
gi 1246765703 291 PLEAMSCGTPVICSANSSLPEV 312
Cdd:cd03796   286 IVEAASCGLLVVSTRVGGIPEV 307
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
285-352 7.17e-05

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 42.21  E-value: 7.17e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1246765703 285 EGFGLPPLEAMSCGTPVICSANSSLPEVVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSERGLAR 352
Cdd:pfam13524  10 DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYRDPEELAEKIRYLLEHPEERRAIAAAGRER 77
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
197-321 7.84e-05

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 45.91  E-value: 7.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 197 YVLSVATLEVRKNLEQVVSTFAEFLDENPHSNL---HLVLAGMKGwKLEKFESALSESRwrdRIIITGFVDEEDLSALY- 272
Cdd:cd04946   226 RLVSCSSIVPVKRIDLIIETLNSLCVAHPSICIswtHIGGGPLKE-RLEKLAENKLENV---KVNFTGEVSNKEVKQLYk 301
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1246765703 273 -SDALCFIYMSLYEGFGLPPLEAMSCGTPVICSANSSLPEVVGDA--GLLIV 321
Cdd:cd04946   302 eNDVDVFVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENEtnGLLLD 353
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
475-522 1.23e-04

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: 43.78  E-value: 1.23e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1246765703 475 NNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRR--YDREIDYY 522
Cdd:cd04185     7 NRLDLLKECLDALLAQTRPPDHIIVIDNASTDGTAEWLTSlgDLDNIVYL 56
PRK10018 PRK10018
colanic acid biosynthesis glycosyltransferase WcaA;
462-568 1.50e-04

colanic acid biosynthesis glycosyltransferase WcaA;


Pssm-ID: 182197 [Multi-domain]  Cd Length: 279  Bit Score: 44.60  E-value: 1.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 462 SSNPLVSYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTD-DTLQ--VIRRYDREIDYYASAPDTGLYNALNKII 538
Cdd:PRK10018    2 KDNPLISIYMPTWNRQQLAIRAIKSVLRQDYSNWEMIIVDDCSTSwEQLQqyVTALNDPRITYIHNDINSGACAVRNQAI 81
                          90       100       110
                  ....*....|....*....|....*....|
gi 1246765703 539 PLARGELICVLNSDDWLEPdaaktavNRIS 568
Cdd:PRK10018   82 MLAQGEYITGIDDDDEWTP-------NRLS 104
PHA01633 PHA01633
putative glycosyl transferase group 1
201-311 3.79e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 43.43  E-value: 3.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 201 VATLEVRKNLEQVVSTFAEFLDE--NPHSNLHLVLAGMKGWKleKFESA-----LSESRWRDRIIITGFVDEEDlsalys 273
Cdd:PHA01633  154 VSGLTKRKNMDLMLQVFNELNTKypDIAKKIHFFVISHKQFT--QLEVPanvhfVAEFGHNSREYIFAFYGAMD------ 225
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1246765703 274 dalcFIYM-SLYEGFGLPPLEAMSCGTPVICSANSSLPE 311
Cdd:PHA01633  226 ----FTIVpSGTEGFGMPVLESMAMGTPVIHQLMPPLDE 260
GT28_Beta-DGS-like cd17507
beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol ...
159-347 4.61e-04

beta-diglucosyldiacylglycerol synthase and similar proteins; beta-diglucosyldiacylglycerol synthase (processive diacylglycerol beta-glucosyltransferase EC 2.4.1.315) is involved in the biosynthesis of both the bilayer- and non-bilayer-forming membrane glucolipids. This family of glycosyltransferases also contains plant major galactolipid synthase (chloroplastic monogalactosyldiacylglycerol synthase 1 EC 2.4.1.46). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340861 [Multi-domain]  Cd Length: 364  Bit Score: 43.08  E-value: 4.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 159 PQQITV--IPLAagSSFQpnsSDVDRAAMRRKYQIPVGLPYVLSVATLEVRKNLEQVVSTfaefLDENPHSNLHLVLAGm 236
Cdd:cd17507   164 PSQIKVtgIPVR--PSFA---EVRDKDEARNELNLSPDKPTVLLMGGGGGMGPVKETVEA----LLDSLRAGQVLVVCG- 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 237 kgwKLEKFESALSESRW-RDRIIITGFVDE-EDLSALySDALcfiymsLYEGFGLPPLEAMSCGTPVICSA--------N 306
Cdd:cd17507   234 ---KNKKLYEKLSGLEEdYINVRVLGYVDDmNELMAA-SDLV------ITKPGGLTISEALARGLPVIIYDpipgqeeeN 303
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1246765703 307 SSLpevVGDAGLLIVAEDKRAVRDAFRSIVFDAELRRSLSE 347
Cdd:cd17507   304 ADF---LENNGAGIIARDPEELLEIVARLIDPPSLLRMMSE 341
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
254-370 5.61e-04

Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ExpC in Rhizobium meliloti has been shown to be involved in the biosynthesis of galactoglucan (exopolysaccharide II).


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 43.12  E-value: 5.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 254 RDRIIITGFVDEEDLSALY--SDALCFIYMSLYEGFGLppLEAMSCGTPVICSANSSLPEVV--GDAGLLIVAEDKRAVR 329
Cdd:cd03818   280 LERVHFVGKVPYDQYVRLLqlSDAHVYLTYPFVLSWSL--LEAMACGCPVIGSDTAPVREVIrdGRNGLLVDFFDPDALA 357
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|.
gi 1246765703 330 DAFRSIVFDAELRRSLseRGLARSKLFNWDVAAQLVVERLA 370
Cdd:cd03818   358 AAVLELLEDPDRAAAL--RRAARRTVERSDSLDVCLARYLA 396
PRK10073 PRK10073
putative glycosyl transferase; Provisional
462-586 1.67e-03

putative glycosyl transferase; Provisional


Pssm-ID: 182223 [Multi-domain]  Cd Length: 328  Bit Score: 41.18  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1246765703 462 SSNPLVSYVTIVRNNAATLSRAIESVRSQTYPLVEHVILDGASTDDTLQVIRRYDREIDYYA--SAPDTGLYNALNKIIP 539
Cdd:PRK10073    3 NSTPKLSIIIPLYNAGKDFRAFMESLIAQTWTALEIIIVNDGSTDNSVEIAKHYAENYPHVRllHQANAGVSVARNTGLA 82
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1246765703 540 LARGELICVLNSDDWLEPDAAKTavnristksganlLLTAARVETLD 586
Cdd:PRK10073   83 VATGKYVAFPDADDVVYPTMYET-------------LMTMALEDDLD 116
 
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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