NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2542169845|ref|WP_298161730|]
View 

glycosyltransferase [Acidocella sp.]

Protein Classification

glycosyltransferase family 2 protein( domain architecture ID 10009193)

glycosyltransferase family 2 protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
Scw11 COG5309
Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism];
30-538 0e+00

Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism];


:

Pssm-ID: 444107  Cd Length: 512  Bit Score: 577.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845  30 NAKSWAAALGVGAMALGIWGYTNRPVTdIPAYRGEIGGFAFSPFHRGESPQTGDYPSTAEIKSDLTLAARYTHNIRTYTV 109
Cdd:COG5309     4 RLLALLLLLLVALLHFGLWAWLNRPVP-LPALGGKIQGVSYSPYREGQSPLKGDYPSEEQIKEDLKLLAPYTKCIRTYSV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 110 EGDLGQIPALAEGMHLNVTLGGWLDRHPDANAAELKKLVAVANANPD-VKQIMVGNETILRGDLPVNELISDIDTVKAET 188
Cdd:COG5309    83 TEGLEEVPELAAKHGLKVMLGAWLSGDPERNEREIEALIELANEYPDiVKRVIVGNEVLLRGDLTPEELIAYIRRVKAAV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 189 HVPVSTAEPWHVWLKYPQLAAHVDFITVHLLPYWEGVPENIAVQDAMNRLQEVHQAYPDKRIVIGEIGWPSDGIDIGAAR 268
Cdd:COG5309   163 KVPVTYADVWHFWLKHPELADAVDFITIHILPYWEGVPIERALDYAKDRYDEVRAAFPGKPIIIGETGWPSAGRQRGGAV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 269 ASTVNQARFMRDFFNLAQQRHLQYFVMEAFDQPWKTSFEGRAAGYWGMFNLDRQQKWSLTGPVENNPGWIFYALGSVIFS 348
Cdd:COG5309   243 PSEVNQARYLREFLAWANEEGIDYFYFEAFDQPWKRALEGTVGAYWGLFDADRQPKFPLTGPVVENPDWPLLAAAAVLLA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 349 LLATMALLSRRPDVRFAGKLIFAGLVEGFTTILGLLFMNMSETYLSLGAATVWGALAAGQALLLFLLIADSFDLVETIYG 428
Cdd:COG5309   323 LLLLFLLARRRRRLRLLGRLFLAALAQAAATALVWLAYLPADYYLTPLDLLVGGGLLLALLLLLAVLLIEALEFAEVLWA 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 429 RVSKRHYEPMPAPAGAKLPKVSIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWEPVAEHCARLGPKFR 508
Cdd:COG5309   403 RRWRRRFLPLPPAPAERLPFVSIHLACNNEPPLMVIATLASLAALDYPNFEVLVVDNNTKDEVVWKPLEARCARLGPRFR 482
                         490       500       510
                  ....*....|....*....|....*....|
gi 2542169845 509 FFTLGKYKGYKAGALNFGLRETAADAEIIG 538
Cdd:COG5309   483 FFHLPLWPGFKAGALNFGLTATAPAAEVVG 512
Glyco_tranf_GTA_type super family cl11394
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
450-685 1.90e-133

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.


The actual alignment was detected with superfamily member cd06435:

Pssm-ID: 472172 [Multi-domain]  Cd Length: 236  Bit Score: 398.70  E-value: 1.90e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 450 SIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWEPVAEHCARLGPKFRFFTLGKYKGYKAGALNFGLRE 529
Cdd:cd06435     1 SIHVPCYEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEALWKPVEAHCAQLGERFRFFHVEPLPGAKAGALNYALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 530 TAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNERNAIIQHG 609
Cdd:cd06435    81 TAPDAEIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERNAIIQHG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542169845 610 TMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAMRIVRANA 685
Cdd:cd06435   161 TMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKKHW 236
 
Name Accession Description Interval E-value
Scw11 COG5309
Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism];
30-538 0e+00

Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism];


Pssm-ID: 444107  Cd Length: 512  Bit Score: 577.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845  30 NAKSWAAALGVGAMALGIWGYTNRPVTdIPAYRGEIGGFAFSPFHRGESPQTGDYPSTAEIKSDLTLAARYTHNIRTYTV 109
Cdd:COG5309     4 RLLALLLLLLVALLHFGLWAWLNRPVP-LPALGGKIQGVSYSPYREGQSPLKGDYPSEEQIKEDLKLLAPYTKCIRTYSV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 110 EGDLGQIPALAEGMHLNVTLGGWLDRHPDANAAELKKLVAVANANPD-VKQIMVGNETILRGDLPVNELISDIDTVKAET 188
Cdd:COG5309    83 TEGLEEVPELAAKHGLKVMLGAWLSGDPERNEREIEALIELANEYPDiVKRVIVGNEVLLRGDLTPEELIAYIRRVKAAV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 189 HVPVSTAEPWHVWLKYPQLAAHVDFITVHLLPYWEGVPENIAVQDAMNRLQEVHQAYPDKRIVIGEIGWPSDGIDIGAAR 268
Cdd:COG5309   163 KVPVTYADVWHFWLKHPELADAVDFITIHILPYWEGVPIERALDYAKDRYDEVRAAFPGKPIIIGETGWPSAGRQRGGAV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 269 ASTVNQARFMRDFFNLAQQRHLQYFVMEAFDQPWKTSFEGRAAGYWGMFNLDRQQKWSLTGPVENNPGWIFYALGSVIFS 348
Cdd:COG5309   243 PSEVNQARYLREFLAWANEEGIDYFYFEAFDQPWKRALEGTVGAYWGLFDADRQPKFPLTGPVVENPDWPLLAAAAVLLA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 349 LLATMALLSRRPDVRFAGKLIFAGLVEGFTTILGLLFMNMSETYLSLGAATVWGALAAGQALLLFLLIADSFDLVETIYG 428
Cdd:COG5309   323 LLLLFLLARRRRRLRLLGRLFLAALAQAAATALVWLAYLPADYYLTPLDLLVGGGLLLALLLLLAVLLIEALEFAEVLWA 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 429 RVSKRHYEPMPAPAGAKLPKVSIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWEPVAEHCARLGPKFR 508
Cdd:COG5309   403 RRWRRRFLPLPPAPAERLPFVSIHLACNNEPPLMVIATLASLAALDYPNFEVLVVDNNTKDEVVWKPLEARCARLGPRFR 482
                         490       500       510
                  ....*....|....*....|....*....|
gi 2542169845 509 FFTLGKYKGYKAGALNFGLRETAADAEIIG 538
Cdd:COG5309   483 FFHLPLWPGFKAGALNFGLTATAPAAEVVG 512
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
450-685 1.90e-133

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 398.70  E-value: 1.90e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 450 SIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWEPVAEHCARLGPKFRFFTLGKYKGYKAGALNFGLRE 529
Cdd:cd06435     1 SIHVPCYEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEALWKPVEAHCAQLGERFRFFHVEPLPGAKAGALNYALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 530 TAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNERNAIIQHG 609
Cdd:cd06435    81 TAPDAEIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERNAIIQHG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542169845 610 TMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAMRIVRANA 685
Cdd:cd06435   161 TMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKKHW 236
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
441-768 4.29e-47

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: 170.31  E-value: 4.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 441 PAGAKLPKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDPAvwEPVAEHCARLGPKFRFFTLGKYKGy 518
Cdd:COG1215    23 RAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYpkEKLEVIVVDDGSTDET--AEIARELAAEYPRVRVIERPENGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 519 KAGALNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFtqspqdyrdndgglfkrmmfweyagffhagmvt 598
Cdd:COG1215    99 KAAALNAGLK--AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGA--------------------------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 599 rnernaiiqHGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAM 678
Cdd:COG1215   144 ---------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 679 RIVRANaDALFNPfnkeltlGQRWHFITGWLPWFGDALGIVFLTMGLAWSVGLVIDPVRFQFPIALFMLPSIGLFFFKIV 758
Cdd:COG1215   215 QLLLKH-RPLLRP-------RRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLL 286
                         330
                  ....*....|
gi 2542169845 759 QILALYKNRV 768
Cdd:COG1215   287 LLAALRGKKV 296
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
450-619 2.56e-25

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: 103.24  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 450 SIHLPICNEPPEMVKlTLDALAAQDYDRFEVLVIDNNTMDPAvWEPVAEHCARlGPKFRFFTLGKYKGyKAGALNFGLRe 529
Cdd:pfam00535   1 SVIIPTYNEEKYLLE-TLESLLNQTYPNFEIIVVDDGSTDGT-VEIAEEYAKK-DPRVRVIRLPENRG-KAGARNAGLR- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 530 tAADAEIIGVIDSDYLVEPDWLRSMVPAFD-NPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNeRNAIIQH 608
Cdd:pfam00535  76 -AATGDYIAFLDADDEVPPDWLEKLVEALEeDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG-LNLPFLI 153
                         170
                  ....*....|.
gi 2542169845 609 GTMTLVRKQAL 619
Cdd:pfam00535 154 GGFALYRREAL 164
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
447-676 4.01e-24

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 101.68  E-value: 4.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPPEMVKlTLDALAAQDYDRFEVLVIDNNTMDPAVwePVAEHCARLGPKFRFFTLGKYK----GYKAGA 522
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGR-VLEAILAQPYPPVEVVVVVNPSDAETL--DVAEEIAARFPDVRLRVIRNARllgpTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 523 LNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRdNDGGLFKRMMFWEYAGFFHAGMVTRNER 602
Cdd:pfam13641  79 LNHGFR--AVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSL-NRSTMLSALGALEFALRHLRMMSLRLAL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542169845 603 NAIIQHGTMTLVRKQALVNENGWAEW-CITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYG 676
Cdd:pfam13641 156 GVLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
451-601 4.48e-17

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: 79.09  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 451 IHLPICNEPPeMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVwePVAEHCARLGPKFRFFTLGKYKGyKAGALNFGLRet 530
Cdd:cd00761     1 VIIPAYNEEP-YLERCLESLLAQTYPNFEVIVVDDGSTDGTL--EILEEYAKKDPRVIRVINEENQG-LAAARNAGLK-- 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542169845 531 AADAEIIGVIDSDYLVEPDWLRSMV-PAFDNPAVGFTQSPQDYrdndggLFKRmMFWEYAGFFHAGMVTRNE 601
Cdd:cd00761    75 AARGEYILFLDADDLLLPDWLERLVaELLADPEADAVGGPGNL------LFRR-ELLEEIGGFDEALLSGEE 139
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
436-748 6.96e-11

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 66.20  E-value: 6.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 436 EPMPAPAGAKL-PKVSIHLPICNEPPEMVKLTLDALAAQDY--DRFEVLVIDNNTMDpavwepvaehcarlgpKFRFFTL 512
Cdd:PRK11498  248 QPVPLPKDMSLwPTVDIFVPTYNEDLNVVKNTIYASLGIDWpkDKLNIWILDDGGRE----------------EFRQFAQ 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 513 GKYKGY---------KAGALNFGLRETaaDAEIIGVIDSDYLVEPDWLR-SMVPAFDNPAVGFTQSPQ------------ 570
Cdd:PRK11498  312 EVGVKYiarpthehaKAGNINNALKYA--KGEFVAIFDCDHVPTRSFLQmTMGWFLKDKKLAMMQTPHhffspdpfernl 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 571 -DYRD--NDGGLFKRMM-----FWEyAGFFHagmvtrnernaiiqhGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFR 642
Cdd:PRK11498  390 gRFRKtpNEGTLFYGLVqdgndMWD-ATFFC---------------GSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHR 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 643 AGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAMRIVRanadaLFNP-FNKELTLGQR-------WHFITGwLPwfgd 714
Cdd:PRK11498  454 RGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFR-----LDNPlTGKGLKLAQRlcyanamLHFLSG-IP---- 523
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2542169845 715 alGIVFLTMGLAWsvgLVIDPVRFQFP---IALFMLP 748
Cdd:PRK11498  524 --RLIFLTAPLAF---LLLHAYIIYAPalmIALFVLP 555
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
434-564 5.09e-10

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 62.85  E-value: 5.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 434 HYEPMPAPAgakLPKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDPAvwEPVAEHCARLGpkFRFFT 511
Cdd:TIGR03965  64 HPRPALLPS---PPSVTVVVPVRNRP-AGLARLLAALLALDYprDRLEVIVVDDGSEDPV--PTRAARGARLP--VRVIR 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2542169845 512 LGKYKGyKAGALNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVG 564
Cdd:TIGR03965 136 HPRRQG-PAAARNAGAR--AARTEFVAFTDSDVVPRPGWLRALLAHFDDPGVA 185
 
Name Accession Description Interval E-value
Scw11 COG5309
Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism];
30-538 0e+00

Exo-beta-1,3-glucanase, GH17 family [Carbohydrate transport and metabolism];


Pssm-ID: 444107  Cd Length: 512  Bit Score: 577.36  E-value: 0e+00
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845  30 NAKSWAAALGVGAMALGIWGYTNRPVTdIPAYRGEIGGFAFSPFHRGESPQTGDYPSTAEIKSDLTLAARYTHNIRTYTV 109
Cdd:COG5309     4 RLLALLLLLLVALLHFGLWAWLNRPVP-LPALGGKIQGVSYSPYREGQSPLKGDYPSEEQIKEDLKLLAPYTKCIRTYSV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 110 EGDLGQIPALAEGMHLNVTLGGWLDRHPDANAAELKKLVAVANANPD-VKQIMVGNETILRGDLPVNELISDIDTVKAET 188
Cdd:COG5309    83 TEGLEEVPELAAKHGLKVMLGAWLSGDPERNEREIEALIELANEYPDiVKRVIVGNEVLLRGDLTPEELIAYIRRVKAAV 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 189 HVPVSTAEPWHVWLKYPQLAAHVDFITVHLLPYWEGVPENIAVQDAMNRLQEVHQAYPDKRIVIGEIGWPSDGIDIGAAR 268
Cdd:COG5309   163 KVPVTYADVWHFWLKHPELADAVDFITIHILPYWEGVPIERALDYAKDRYDEVRAAFPGKPIIIGETGWPSAGRQRGGAV 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 269 ASTVNQARFMRDFFNLAQQRHLQYFVMEAFDQPWKTSFEGRAAGYWGMFNLDRQQKWSLTGPVENNPGWIFYALGSVIFS 348
Cdd:COG5309   243 PSEVNQARYLREFLAWANEEGIDYFYFEAFDQPWKRALEGTVGAYWGLFDADRQPKFPLTGPVVENPDWPLLAAAAVLLA 322
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 349 LLATMALLSRRPDVRFAGKLIFAGLVEGFTTILGLLFMNMSETYLSLGAATVWGALAAGQALLLFLLIADSFDLVETIYG 428
Cdd:COG5309   323 LLLLFLLARRRRRLRLLGRLFLAALAQAAATALVWLAYLPADYYLTPLDLLVGGGLLLALLLLLAVLLIEALEFAEVLWA 402
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 429 RVSKRHYEPMPAPAGAKLPKVSIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWEPVAEHCARLGPKFR 508
Cdd:COG5309   403 RRWRRRFLPLPPAPAERLPFVSIHLACNNEPPLMVIATLASLAALDYPNFEVLVVDNNTKDEVVWKPLEARCARLGPRFR 482
                         490       500       510
                  ....*....|....*....|....*....|
gi 2542169845 509 FFTLGKYKGYKAGALNFGLRETAADAEIIG 538
Cdd:COG5309   483 FFHLPLWPGFKAGALNFGLTATAPAAEVVG 512
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
450-685 1.90e-133

NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase. Bradyrhizobium japonicum synthesizes periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans during growth under hypoosmotic conditions. Two genes (ndvB, ndvC) are involved in the beta-(1, 3), beta-(1,6)-glucan synthesis. The ndvC mutant strain resulted in synthesis of altered cyclic beta-glucans composed almost entirely of beta-(1, 3)-glycosyl linkages. The periplasmic cyclic beta-(1,3),beta-(1,6)-D-glucans function for osmoregulation. The ndvC mutation also affects the ability of the bacteria to establish a successful symbiotic interaction with host plant. Thus, the beta-glucans may function as suppressors of a host defense response.


Pssm-ID: 133057 [Multi-domain]  Cd Length: 236  Bit Score: 398.70  E-value: 1.90e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 450 SIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWEPVAEHCARLGPKFRFFTLGKYKGYKAGALNFGLRE 529
Cdd:cd06435     1 SIHVPCYEEPPEMVKETLDSLAALDYPNFEVIVIDNNTKDEALWKPVEAHCAQLGERFRFFHVEPLPGAKAGALNYALER 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 530 TAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNERNAIIQHG 609
Cdd:cd06435    81 TAPDAEIIAVIDADYQVEPDWLKRLVPIFDDPRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERNAIIQHG 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2542169845 610 TMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAMRIVRANA 685
Cdd:cd06435   161 TMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSYGHGLIPDTFEAFKKQRFRWAYGAVQILKKHW 236
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
447-680 3.08e-49

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


Pssm-ID: 133043 [Multi-domain]  Cd Length: 234  Bit Score: 173.91  E-value: 3.08e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPPEMVKLTLDALAAQDY--DRFEVLVIDNNTmDPAVWEPVAEHCARLGpkFRFFTLGKYKGYKAGALN 524
Cdd:cd06421     1 PTVDVFIPTYNEPLEIVRKTLRAALAIDYphDKLRVYVLDDGR-RPELRALAAELGVEYG--YRYLTRPDNRHAKAGNLN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 525 FGLRETaaDAEIIGVIDSDYLVEPDWLRSMVPAF-DNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNER- 602
Cdd:cd06421    78 NALAHT--TGDFVAILDADHVPTPDFLRRTLGYFlDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELFYGVIQPGRDRw 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2542169845 603 NAIIQHGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAMRI 680
Cdd:cd06421   156 GAAFCCGSGAVVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVPEPLAAGLAPETLAAYIKQRLRWARGMLQI 233
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
441-768 4.29e-47

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: 170.31  E-value: 4.29e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 441 PAGAKLPKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDPAvwEPVAEHCARLGPKFRFFTLGKYKGy 518
Cdd:COG1215    23 RAPADLPRVSVIIPAYNEE-AVIEETLRSLLAQDYpkEKLEVIVVDDGSTDET--AEIARELAAEYPRVRVIERPENGG- 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 519 KAGALNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFtqspqdyrdndgglfkrmmfweyagffhagmvt 598
Cdd:COG1215    99 KAAALNAGLK--AARGDIVVFLDADTVLDPDWLRRLVAAFADPGVGA--------------------------------- 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 599 rnernaiiqHGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAM 678
Cdd:COG1215   144 ---------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRAGYRIVYVPDAVVYEEAPETLRALFRQRRRWARGGL 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 679 RIVRANaDALFNPfnkeltlGQRWHFITGWLPWFGDALGIVFLTMGLAWSVGLVIDPVRFQFPIALFMLPSIGLFFFKIV 758
Cdd:COG1215   215 QLLLKH-RPLLRP-------RRLLLFLLLLLLPLLLLLLLLALLALLLLLLPALLLALLLALRRRRLLLPLLHLLYGLLL 286
                         330
                  ....*....|
gi 2542169845 759 QILALYKNRV 768
Cdd:COG1215   287 LLAALRGKKV 296
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
451-633 1.16e-35

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: 133.51  E-value: 1.16e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 451 IHLPICNEPpEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVWepVAEHCARLGPKFRFFTLGKYKGYKAGALNFGLRet 530
Cdd:cd06423     1 IIVPAYNEE-AVIERTIESLLALDYPKLEVIVVDDGSTDDTLE--ILEELAALYIRRVLVVRDKENGGKAGALNAGLR-- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 531 AADAEIIGVIDSDYLVEPDWLRSM-VPAFDNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNERNAIIQ-H 608
Cdd:cd06423    76 HAKGDIVVVLDADTILEPDALKRLvVPFFADPKVGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVlS 155
                         170       180
                  ....*....|....*....|....*
gi 2542169845 609 GTMTLVRKQALVNENGWAEWCITED 633
Cdd:cd06423   156 GAFGAFRREALREVGGWDEDTLTED 180
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
447-676 1.17e-33

Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit substitute of the cellulose synthase complex; Cellulose synthase (CESA) catalyzes the polymerization reaction of cellulose using UDP-glucose as the substrate. Cellulose is an aggregate of unbranched polymers of beta-1,4-linked glucose residues, which is an abundant polysaccharide produced by plants and in varying degrees by several other organisms including algae, bacteria, fungi, and even some animals. Genomes from higher plants harbor multiple CESA genes. There are ten in Arabidopsis. At least three different CESA proteins are required to form a functional complex. In Arabidopsis, CESA1, 3 and 6 and CESA4, 7 and 8, are required for cellulose biosynthesis during primary and secondary cell wall formation. CESA2 is very closely related to CESA6 and is viewed as a prime substitute for CESA6. They functionally compensate each other. The cesa2 and cesa6 double mutant plants were significantly smaller, while the single mutant plants were almost normal.


Pssm-ID: 133059 [Multi-domain]  Cd Length: 232  Bit Score: 129.35  E-value: 1.17e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTmDPAVWEPVAEHC--ARLGPKFRFFTLGKYKGYKAGA 522
Cdd:cd06437     1 PMVTVQLPVFNEK-YVVERLIEAACALDYpkDRLEIQVLDDST-DETVRLAREIVEeyAAQGVNIKHVRRADRTGYKAGA 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 523 LNFGLREtaADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNER 602
Cdd:cd06437    79 LAEGMKV--AKGEYVAIFDADFVPPPDFLQKTPPYFADPKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSST 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542169845 603 NAIIQ-HGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYG 676
Cdd:cd06437   157 GLFFNfNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLDDVVVPAELPASMSAYRSQQHRWSKG 231
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
450-619 2.56e-25

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: 103.24  E-value: 2.56e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 450 SIHLPICNEPPEMVKlTLDALAAQDYDRFEVLVIDNNTMDPAvWEPVAEHCARlGPKFRFFTLGKYKGyKAGALNFGLRe 529
Cdd:pfam00535   1 SVIIPTYNEEKYLLE-TLESLLNQTYPNFEIIVVDDGSTDGT-VEIAEEYAKK-DPRVRVIRLPENRG-KAGARNAGLR- 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 530 tAADAEIIGVIDSDYLVEPDWLRSMVPAFD-NPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNeRNAIIQH 608
Cdd:pfam00535  76 -AATGDYIAFLDADDEVPPDWLEKLVEALEeDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLG-LNLPFLI 153
                         170
                  ....*....|.
gi 2542169845 609 GTMTLVRKQAL 619
Cdd:pfam00535 154 GGFALYRREAL 164
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
447-676 4.01e-24

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


Pssm-ID: 433372 [Multi-domain]  Cd Length: 230  Bit Score: 101.68  E-value: 4.01e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPPEMVKlTLDALAAQDYDRFEVLVIDNNTMDPAVwePVAEHCARLGPKFRFFTLGKYK----GYKAGA 522
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGR-VLEAILAQPYPPVEVVVVVNPSDAETL--DVAEEIAARFPDVRLRVIRNARllgpTGKSRG 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 523 LNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRdNDGGLFKRMMFWEYAGFFHAGMVTRNER 602
Cdd:pfam13641  79 LNHGFR--AVKSDLVVLHDDDSVLHPGTLKKYVQYFDSPKVGAVGTPVFSL-NRSTMLSALGALEFALRHLRMMSLRLAL 155
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542169845 603 NAIIQHGTMTLVRKQALVNENGWAEW-CITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYG 676
Cdd:pfam13641 156 GVLPLSGAGSAIRREVLKELGLFDPFfLLGDDKSLGRRLRRHGWRVAYAPDAAVRTVFPTYLAASIKQRARWVYG 230
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
447-657 1.86e-18

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 84.75  E-value: 1.86e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPpEMVKLTLDALAAQDYDRFEVLVIDNNTMDpAVWEpVAEHCARLGPKFRFFTLGKYKGyKAGALNFG 526
Cdd:COG0463     2 PLVSVVIPTYNEE-EYLEEALESLLAQTYPDFEIIVVDDGSTD-GTAE-ILRELAAKDPRIRVIRLERNRG-KGAARNAG 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 527 LRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSpQDYRDNDGGLFKRMMFWEYAgffhagmVTRNERNAII 606
Cdd:COG0463    78 LA--AARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVYG-SRLIREGESDLRRLGSRLFN-------LVRLLTNLPD 147
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2542169845 607 QHGTMTLVRKQaLVNENGWAEWCItEDSQLgLRLFRAGYEAVYSKKSFGKG 657
Cdd:COG0463   148 STSGFRLFRRE-VLEELGFDEGFL-EDTEL-LRALRHGFRIAEVPVRYRAG 195
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
451-601 4.48e-17

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: 79.09  E-value: 4.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 451 IHLPICNEPPeMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVwePVAEHCARLGPKFRFFTLGKYKGyKAGALNFGLRet 530
Cdd:cd00761     1 VIIPAYNEEP-YLERCLESLLAQTYPNFEVIVVDDGSTDGTL--EILEEYAKKDPRVIRVINEENQG-LAAARNAGLK-- 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2542169845 531 AADAEIIGVIDSDYLVEPDWLRSMV-PAFDNPAVGFTQSPQDYrdndggLFKRmMFWEYAGFFHAGMVTRNE 601
Cdd:cd00761    75 AARGEYILFLDADDLLLPDWLERLVaELLADPEADAVGGPGNL------LFRR-ELLEEIGGFDEALLSGEE 139
WcaE COG1216
Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];
447-555 4.28e-16

Glycosyltransferase, GT2 family [Carbohydrate transport and metabolism];


Pssm-ID: 440829 [Multi-domain]  Cd Length: 202  Bit Score: 77.73  E-value: 4.28e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNePPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVwEPVAEHcarLGPKFRFFTLGKYKGYkAGALNFG 526
Cdd:COG1216     3 PKVSVVIPTYN-RPELLRRCLESLLAQTYPPFEVIVVDNGSTDGTA-ELLAAL---AFPRVRVIRNPENLGF-AAARNLG 76
                          90       100
                  ....*....|....*....|....*....
gi 2542169845 527 LRetAADAEIIGVIDSDYLVEPDWLRSMV 555
Cdd:COG1216    77 LR--AAGGDYLLFLDDDTVVEPDWLERLL 103
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
536-729 1.28e-15

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


Pssm-ID: 433365 [Multi-domain]  Cd Length: 192  Bit Score: 76.22  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 536 IIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRdNDGGLFKRMMFWEYA-GFFHAGMVTRNERNAIIQHGTMTLV 614
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMASPEVAIIQGPILPM-NVGNYLEELAALFFAdDHGKSIPVRMALGRVLPFVGSGAFL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 615 RKQALVNENGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAmrivranadalfNPFNK 694
Cdd:pfam13632  80 RRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSAVYEKSPLTFRDFLRQRRRWAYGC------------LLILL 147
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2542169845 695 ELTLGQRWHFITGWLPWfGDALGIVFLTMGLAWSV 729
Cdd:pfam13632 148 IRLLGYLGTLLWSGLPL-ALLLLLLFSISSLALVL 181
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
447-678 7.39e-15

CESA_like_2 is a member of 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: 133049 [Multi-domain]  Cd Length: 241  Bit Score: 74.98  E-value: 7.39e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVI----DNNTMDpavwepvAEHCARLGPKFRFFTL--GKYKGy 518
Cdd:cd06427     1 PVYTILVPLYKEA-EVLPQLIASLSALDYprSKLDVKLLleedDEETIA-------AARALRLPSIFRVVVVppSQPRT- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 519 KAGALNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAF--DNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHA-- 594
Cdd:cd06427    72 KPKACNYALA--FARGEYVVIYDAEDAPDPDQLKKAVAAFarLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYll 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 595 -GMVTRNErnAIIQHGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFRAGYEAvyskksfgkGVM--------PDDYTA 665
Cdd:cd06427   150 pGLARLGL--PIPLGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRT---------GVLnsttleeaNNALGN 218
                         250
                  ....*....|...
gi 2542169845 666 FRKQRFRWAYGAM 678
Cdd:cd06427   219 WIRQRSRWIKGYM 231
GT_2_like_c cd04186
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
459-649 4.26e-13

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


Pssm-ID: 133029 [Multi-domain]  Cd Length: 166  Bit Score: 67.97  E-value: 4.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 459 PPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVwepvaEHCARLGPKFRFFTLGKYKGYkAGALNFGLREtaADAEIIG 538
Cdd:cd04186     8 SLEYLKACLDSLLAQTYPDFEVIVVDNASTDGSV-----ELLRELFPEVRLIRNGENLGF-GAGNNQGIRE--AKGDYVL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 539 VIDSDYLVEPDWLRSMVPAFDnpavgftQSPQdyrdndgglfkrmmfweyagffhAGMVTrnernAIIQhGTMTLVRKQA 618
Cdd:cd04186    80 LLNPDTVVEPGALLELLDAAE-------QDPD-----------------------VGIVG-----PKVS-GAFLLVRREV 123
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2542169845 619 LVNENGWAE----WCitEDSQLGLRLFRAGYEAVY 649
Cdd:cd04186   124 FEEVGGFDEdfflYY--EDVDLCLRARLAGYRVLY 156
bcsA PRK11498
cellulose synthase catalytic subunit; Provisional
436-748 6.96e-11

cellulose synthase catalytic subunit; Provisional


Pssm-ID: 236918 [Multi-domain]  Cd Length: 852  Bit Score: 66.20  E-value: 6.96e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 436 EPMPAPAGAKL-PKVSIHLPICNEPPEMVKLTLDALAAQDY--DRFEVLVIDNNTMDpavwepvaehcarlgpKFRFFTL 512
Cdd:PRK11498  248 QPVPLPKDMSLwPTVDIFVPTYNEDLNVVKNTIYASLGIDWpkDKLNIWILDDGGRE----------------EFRQFAQ 311
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 513 GKYKGY---------KAGALNFGLRETaaDAEIIGVIDSDYLVEPDWLR-SMVPAFDNPAVGFTQSPQ------------ 570
Cdd:PRK11498  312 EVGVKYiarpthehaKAGNINNALKYA--KGEFVAIFDCDHVPTRSFLQmTMGWFLKDKKLAMMQTPHhffspdpfernl 389
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 571 -DYRD--NDGGLFKRMM-----FWEyAGFFHagmvtrnernaiiqhGTMTLVRKQALVNENGWAEWCITEDSQLGLRLFR 642
Cdd:PRK11498  390 gRFRKtpNEGTLFYGLVqdgndMWD-ATFFC---------------GSCAVIRRKPLDEIGGIAVETVTEDAHTSLRLHR 453
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 643 AGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYGAMRIVRanadaLFNP-FNKELTLGQR-------WHFITGwLPwfgd 714
Cdd:PRK11498  454 RGYTSAYMRIPQAAGLATESLSAHIGQRIRWARGMVQIFR-----LDNPlTGKGLKLAQRlcyanamLHFLSG-IP---- 523
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 2542169845 715 alGIVFLTMGLAWsvgLVIDPVRFQFP---IALFMLP 748
Cdd:PRK11498  524 --RLIFLTAPLAF---LLLHAYIIYAPalmIALFVLP 555
Glucosylceramide_synthase cd02520
Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid ...
447-674 1.47e-10

Glucosylceramide synthase catalyzes the first glycosylation step of glycosphingolipid synthesis; UDP-glucose:N-acylsphingosine D-glucosyltransferase (glucosylceramide synthase or ceramide glucosyltransferase) catalyzes the first glycosylation step of glycosphingolipid synthesis. Its product, glucosylceramide, serves as the core of more than 300 glycosphingolipids (GSL). GSLs are a group of membrane components that have the lipid portion embedded in the outer plasma membrane leaflet and the sugar chains extended to the outer environment. Several lines of evidence suggest the importance of GSLs in various cellular processes such as differentiation, adhesion, proliferation, and cell-cell recognition. In pathogenic fungus Cryptococcus neoformans, glucosylceramide serves as an antigen that elicits an antibody response in patients and it is essential for fungal growth in host extracellular environment.


Pssm-ID: 133012 [Multi-domain]  Cd Length: 196  Bit Score: 61.46  E-value: 1.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPPEMVKlTLDALAAQDYDRFEVLVIDNNTMDPAVwePVAEhcaRLGPKF-----RFFTLGKYKGY--K 519
Cdd:cd02520     1 PGVSILKPLCGVDPNLYE-NLESFFQQDYPKYEILFCVQDEDDPAI--PVVR---KLIAKYpnvdaRLLIGGEKVGInpK 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 520 AGALNFGLREtaADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPqdyrdndgglfkrmmfweyagfFHAGMVTR 599
Cdd:cd02520    75 VNNLIKGYEE--ARYDILVISDSDISVPPDYLRRMVAPLMDPGVGLVTCL----------------------CAFGKSMA 130
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2542169845 600 NERNAIIQHGTMtlvrkQALVNEngwaewcITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWA 674
Cdd:cd02520   131 LRREVLDAIGGF-----EAFADY-------LAEDYFLGKLIWRLGYRVVLSPYVVMQPLGSTSLASFWRRQLRWS 193
GT2_RfbC_Mx_like cd04184
Myxococcus xanthus RfbC like proteins are required for O-antigen biosynthesis; The rfbC gene ...
447-580 1.60e-10

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: 61.45  E-value: 1.60e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 447 PKVSIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVwEPVAEHCARLGPKFRFFTLGKYKGYkAGALNFG 526
Cdd:cd04184     1 PLISIVMPVYNTPEKYLREAIESVRAQTYPNWELCIADDASTDPEV-KRVLKKYAAQDPRIKVVFREENGGI-SAATNSA 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2542169845 527 LRetAADAEIIGVIDSDYLVEPDWLRSMVPAFD-NPAVGFTQSPQDYRDNDGGLF 580
Cdd:cd04184    79 LE--LATGEFVALLDHDDELAPHALYEVVKALNeHPDADLIYSDEDKIDEGGKRS 131
mycofact_glyco TIGR03965
mycofactocin system glycosyltransferase; Members of this protein family are putative ...
434-564 5.09e-10

mycofactocin system glycosyltransferase; Members of this protein family are putative glycosyltransferases, members of pfam00535 (glycosyl transferase family 2). Members appear mostly in the Actinobacteria, where they appear to be part of a system for converting a precursor peptide (TIGR03969) into a novel redox carrier designated mycofactocin. A radical SAM enzyme, TIGR03962, is a proposed to be a key maturase for mycofactocin.


Pssm-ID: 274884 [Multi-domain]  Cd Length: 466  Bit Score: 62.85  E-value: 5.09e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 434 HYEPMPAPAgakLPKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDPAvwEPVAEHCARLGpkFRFFT 511
Cdd:TIGR03965  64 HPRPALLPS---PPSVTVVVPVRNRP-AGLARLLAALLALDYprDRLEVIVVDDGSEDPV--PTRAARGARLP--VRVIR 135
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2542169845 512 LGKYKGyKAGALNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVG 564
Cdd:TIGR03965 136 HPRRQG-PAAARNAGAR--AARTEFVAFTDSDVVPRPGWLRALLAHFDDPGVA 185
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
431-679 1.15e-09

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: 59.90  E-value: 1.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 431 SKRHYEPMPAPAGAKLPKVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDPAVwEPVAEHcarLGPKFR 508
Cdd:cd06439    13 ARLRPKPPSLPDPAYLPTVTIIIPAYNEE-AVIEAKLENLLALDYprDRLEIIVVSDGSTDGTA-EIAREY---ADKGVK 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 509 FFTLGKYKGyKAGALNFGLREtaADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSpqDYRDNDGGLFKRMM--FW 586
Cdd:cd06439    88 LLRFPERRG-KAAALNRALAL--ATGEIVVFTDANALLDPDALRLLVRHFADPSVGAVSG--ELVIVDGGGSGSGEglYW 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 587 EYAGF-------FHAgmvtrnernAIIQHGTMTLVRKQALvneNGWAEWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVM 659
Cdd:cd06439   163 KYENWlkraesrLGS---------TVGANGAIYAIRRELF---RPLPADTINDDFVLPLRIARQGYRVVYEPDAVAYEEV 230
                         250       260
                  ....*....|....*....|
gi 2542169845 660 PDDYTAFRKQRFRWAYGAMR 679
Cdd:cd06439   231 AEDGSEEFRRRVRIAAGNLQ 250
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
448-691 1.37e-09

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: 59.55  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 448 KVSIHLPICNEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDpAVWEPVAEHCARlGPKFRFftLGKYKGYKAGALNF 525
Cdd:cd02525     1 FVSIIIPVRNEE-KYIEELLESLLNQSYpkDLIEIIVVDGGSTD-GTREIVQEYAAK-DPRIRL--IDNPKRIQSAGLNI 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 526 GLREtaADAEIIGVIDSDYLVEPDWLRSMVPAF---DNPAVGftqspqDYRDNDG-GLFKRMMFWEYAGFFHAGmVTRNE 601
Cdd:cd02525    76 GIRN--SRGDIIIRVDAHAVYPKDYILELVEALkrtGADNVG------GPMETIGeSKFQKAIAVAQSSPLGSG-GSAYR 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 602 RNAIIQHGTMTLV----RKQALVNENGWAEWCIT-EDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYTAFRKQRFRWAYG 676
Cdd:cd02525   147 GGAVKIGYVDTVHhgayRREVFEKVGGFDESLVRnEDAELNYRLRKAGYKIWLSPDIRVYYYPRSTLKKLARQYFRYGKW 226
                         250
                  ....*....|....*
gi 2542169845 677 AMRIVRANADALFNP 691
Cdd:cd02525   227 RARTLRKHRKSLSLR 241
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
449-674 1.04e-08

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


Pssm-ID: 133056 [Multi-domain]  Cd Length: 235  Bit Score: 56.88  E-value: 1.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 449 VSIHLPICNEPPEMVKLTLDALAAQDYDRFEVLVIDNNtmdpavwEPVAEHCARLGPKFRFFTLGKYKGYKAGALNFGLR 528
Cdd:cd06434     2 VTVIIPVYDEDPDVFRECLRSILRQKPLEIIVVTDGDD-------EPYLSILSQTVKYGGIFVITVPHPGKRRALAEGIR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 529 ETAADaeIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGlfkrmmFWEYAGffhAGMVTR-NE------ 601
Cdd:cd06434    75 HVTTD--IVVLLDSDTVWPPNALPEMLKPFEDPKVGGVGTNQRILRPRDS------KWSFLA---AEYLERrNEeiraam 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 602 ----------------RNAIIQHGTMTLvrkqALVNENGWAEWCIT-EDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYT 664
Cdd:cd06434   144 sydggvpclsgrtaayRTEILKDFLFLE----EFTNETFMGRRLNAgDDRFLTRYVLSHGYKTVYQYTSEAYTETPENYK 219
                         250
                  ....*....|
gi 2542169845 665 AFRKQRFRWA 674
Cdd:cd06434   220 KFLKQQLRWS 229
Glyco_hydro_17 pfam00332
Glycosyl hydrolases family 17;
230-327 1.32e-08

Glycosyl hydrolases family 17;


Pssm-ID: 366033  Cd Length: 309  Bit Score: 57.51  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 230 AVQDAMNRLqevhqAYPDKRIVIGEIGWPSDG---IDIGAARASTVNQARFMRDFFNLAQQRHLQYFVMEAFDQPWKTsf 306
Cdd:pfam00332 214 SVYFAQEKL-----GGTDIEIWVSETGWPSDGhpgATLENAATYVRNLIQHVKEGTPSKPGWGIETYVFAMFDENWKP-- 286
                          90       100
                  ....*....|....*....|.
gi 2542169845 307 EGRAAGYWGMFNLDRQQKWSL 327
Cdd:pfam00332 287 GTSVEKHWGVFQPDKSPKYSL 307
Glyco_transf_21 pfam13506
Glycosyl transferase family 21; This is a family of ceramide beta-glucosyltransferases - EC:2. ...
517-674 1.06e-07

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


Pssm-ID: 433264 [Multi-domain]  Cd Length: 173  Bit Score: 52.67  E-value: 1.06e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 517 GYKAGALNFGLRetAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGglfkrmmFW---EYAGF-F 592
Cdd:pfam13506  16 NPKVNNLLQGLE--AAKYDLLVISDSDIRVPPDYLRDLLAPLADPKVGLVTSPPVGSDPKG-------LAaalEAAFFnT 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 593 HAGMVTRN-ERNAIIQHGTMTLvRKQALVNENGWAEWC--ITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDDYT--AFR 667
Cdd:pfam13506  87 LAGVLQAAlSGIGFAVGMSMAF-RRADLERIGGFEALAdyLAEDYALGKLLRAAGLKVVLSPRPILQTSGPRRTSfrAFM 165

                  ....*..
gi 2542169845 668 KQRFRWA 674
Cdd:pfam13506 166 ARQLRWA 172
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
457-676 3.42e-07

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


Pssm-ID: 133035 [Multi-domain]  Cd Length: 229  Bit Score: 52.29  E-value: 3.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 457 NEPpEMVKLTLDALAAQDY--DRFEVLVIDNNTMDP--AVWEPVAEHcarlgPKFRFFTLGKYKGY---KAGALNFGLRe 529
Cdd:cd04192     7 NEA-ENLPRLLQSLSALDYpkEKFEVILVDDHSTDGtvQILEFAAAK-----PNFQLKILNNSRVSisgKKNALTTAIK- 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 530 tAADAEIIGVIDSDYLVEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGL--FKRMMFWE----YAGFFHAGM-VTRNER 602
Cdd:cd04192    80 -AAKGDWIVTTDADCVVPSNWLLTFVAFIQKEQIGLVAGPVIYFKGKSLLakFQRLDWLSllglIAGSFGLGKpFMCNGA 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2542169845 603 NAIIqhgtmtlvRKQALVNENGWA--EWCITEDSQLGLRLFRAGYEAVYSKKSFGKGVMPDD---YTAFRKQRFRWAYG 676
Cdd:cd04192   159 NMAY--------RKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPKVAYLKNPEALVTTQPvtsWKELLNQRKRWASK 229
Glucan_BSP_MdoH cd04191
Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic ...
449-569 1.88e-05

Glucan_BSP_MdoH catalyzes the elongation of beta-1,2 polyglucose chains of glucan; Periplasmic Glucan Biosynthesis protein MdoH is a glucosyltransferase that catalyzes the elongation of beta-1,2 polyglucose chains of glucan, requiring a beta-glucoside as a primer and UDP-glucose as a substrate. Glucans are composed of 5 to 10 units of glucose forming a highly branched structure, where beta-1,2-linked glucose constitutes a linear backbone to which branches are attached by beta-1,6 linkages. In Escherichia coli, glucans are located in the periplasmic space, functioning as regulator of osmolarity. It is synthesized at a maximum when cells are grown in a medium with low osmolarity. It has been shown to span the cytoplasmic membrane.


Pssm-ID: 133034 [Multi-domain]  Cd Length: 254  Bit Score: 47.27  E-value: 1.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 449 VSIHLPICNEPPEMVKLTLDALAA-----QDYDRFEVLVIdNNTMDPAVWepVAEH------CARLGPKFRFFtlgkYK- 516
Cdd:cd04191     1 TAIVMPVYNEDPARVFAGLRAMYEslaktGLADHFDFFIL-SDTRDPDIW--LAEEaawldlCEELGAQGRIY----YRr 73
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2542169845 517 -----GYKAGALNFGLRETAADAEIIGVIDSDYLVEPDWLRSMVPAFD-NPAVGFTQSP 569
Cdd:cd04191    74 rrentGRKAGNIADFCRRWGSRYDYMVVLDADSLMSGDTIVRLVRRMEaNPRAGIIQTA 132
GlcNAc-1-P_transferase cd06436
N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1, ...
478-633 3.90e-05

N-acetyl-glucosamine transferase is involved in the synthesis of Poly-beta-1,6-N-acetyl-D-glucosamine; N-acetyl-glucosamine transferase is responsible for the synthesis of bacteria Poly-beta-1,6-N-acetyl-D-glucosamine (PGA). Poly-beta-1,6-N-acetyl-D-glucosamine is a homopolymer that serves as an adhesion for the maintenance of biofilm structural stability in diverse eubacteria. N-acetyl-glucosamine transferase is the product of gene pgaC. Genetic analysis indicated that all four genes of the pgaABCD locus were required for the PGA production, pgaC being a glycosyltransferase.


Pssm-ID: 133058 [Multi-domain]  Cd Length: 191  Bit Score: 45.45  E-value: 3.90e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 478 FEVLVIDNNTMDPAVwepVAEHCARLGPKFRFFTLGK---YKGyKAGALNFG-------LRETAADAE--IIGVIDSDYL 545
Cdd:cd06436    26 FLVLVIDDASDDDTA---GIVRLAITDSRVHLLRRHLpnaRTG-KGDALNAAydqirqiLIEEGADPErvIIAVIDADGR 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 546 VEPDWLRSMVPAFDNPAVGFTQSPQDYRDNDGGLFKRMMFWEYAGFFHAGMVTRNERNAIIQHGTMTLVRKQALVNENGW 625
Cdd:cd06436   102 LDPNALEAVAPYFSDPRVAGTQSRVRMYNRHKNLLTILQDLEFFIIIAATQSLRALTGTVGLGGNGQFMRLSALDGLIGE 181
                         170
                  ....*....|
gi 2542169845 626 AEW--CITED 633
Cdd:cd06436   182 EPWsdSLLED 191
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
466-636 1.17e-04

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


Pssm-ID: 133060 [Multi-domain]  Cd Length: 183  Bit Score: 43.74  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 466 TLDALAAQDY--DRFEVLVI-DNNTMDPA---------VWEpvaehcarlgpkfRFFTLGKYKGYkagALNFGLRETAA- 532
Cdd:cd06438    15 TVRSLKAQDYprELYRIFVVaDNCTDDTAqvaraagatVLE-------------RHDPERRGKGY---ALDFGFRHLLNl 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 533 --DAEIIGVIDSDYLVEPDWLRSMVPAFdnpAVGFT--QSPQDYRDNDGGLFKRMM---FWEYAGFFHAGMVTRNERNAI 605
Cdd:cd06438    79 adDPDAVVVFDADNLVDPNALEELNARF---AAGARvvQAYYNSKNPDDSWITRLYafaFLVFNRLRPLGRSNLGLSCQL 155
                         170       180       190
                  ....*....|....*....|....*....|..
gi 2542169845 606 iqHGT-MTLVRkqALVNENGWAEWCITEDSQL 636
Cdd:cd06438   156 --GGTgMCFPW--AVLRQAPWAAHSLTEDLEF 183
DPM_DPG-synthase_like cd04179
DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the ...
460-555 4.95e-04

DPM_DPG-synthase_like is a member of the Glycosyltransferase 2 superfamily; DPM1 is the catalytic subunit of eukaryotic dolichol-phosphate mannose (DPM) synthase. DPM synthase is required for synthesis of the glycosylphosphatidylinositol (GPI) anchor, N-glycan precursor, protein O-mannose, and C-mannose. In higher eukaryotes,the enzyme has three subunits, DPM1, DPM2 and DPM3. DPM is synthesized from dolichol phosphate and GDP-Man on the cytosolic surface of the ER membrane by DPM synthase and then is flipped onto the luminal side and used as a donor substrate. In lower eukaryotes, such as Saccharomyces cerevisiae and Trypanosoma brucei, DPM synthase consists of a single component (Dpm1p and TbDpm1, respectively) that possesses one predicted transmembrane region near the C terminus for anchoring to the ER membrane. In contrast, the Dpm1 homologues of higher eukaryotes, namely fission yeast, fungi, and animals, have no transmembrane region, suggesting the existence of adapter molecules for membrane anchoring. This family also includes bacteria and archaea DPM1_like enzymes. However, the enzyme structure and mechanism of function are not well understood. The UDP-glucose:dolichyl-phosphate glucosyltransferase (DPG_synthase) is a transmembrane-bound enzyme of the endoplasmic reticulum involved in protein N-linked glycosylation. This enzyme catalyzes the transfer of glucose from UDP-glucose to dolichyl phosphate. This protein family belongs to Glycosyltransferase 2 superfamily.


Pssm-ID: 133022 [Multi-domain]  Cd Length: 185  Bit Score: 42.18  E-value: 4.95e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 460 PEMVKLTLDALAAQDydRFEVLVIDNNTMDpAVWEPVAEHCARLgPKFRFFTLGKYKGyKAGALNFGLRetAADAEIIGV 539
Cdd:cd04179    13 PELVERLLAVLEEGY--DYEIIVVDDGSTD-GTAEIARELAARV-PRVRVIRLSRNFG-KGAAVRAGFK--AARGDIVVT 85
                          90
                  ....*....|....*.
gi 2542169845 540 IDSDYLVEPDWLRSMV 555
Cdd:cd04179    86 MDADLQHPPEDIPKLL 101
DPG_synthase cd04188
DPG_synthase is involved in protein N-linked glycosylation; UDP-glucose:dolichyl-phosphate ...
460-543 6.69e-03

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


Pssm-ID: 133031 [Multi-domain]  Cd Length: 211  Bit Score: 39.09  E-value: 6.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 460 PEMVKLTLDALAAQDYDRFEVLVIDNNTMDPAVwEPVAEHCARLGPKFRFFTLGKYKGyKAGALNFGLRetAADAEIIGV 539
Cdd:cd04188    13 PPTLEEAVEYLEERPSFSYEIIVVDDGSKDGTA-EVARKLARKNPALIRVLTLPKNRG-KGGAVRAGML--AARGDYILF 88

                  ....
gi 2542169845 540 IDSD 543
Cdd:cd04188    89 ADAD 92
GT_2_like_b cd04185
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
466-577 7.79e-03

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: 38.77  E-value: 7.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2542169845 466 TLDALAAQDYDRFEVLVIDNNTMDPAvwepvAEHCARLGPKFRF--FTLGKYKGyKAGALNFGLRE-TAADAEIIGVIDS 542
Cdd:cd04185    15 CLDALLAQTRPPDHIIVIDNASTDGT-----AEWLTSLGDLDNIvyLRLPENLG-GAGGFYEGVRRaYELGYDWIWLMDD 88
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2542169845 543 DYLVEPDWLRSMVPAFDNPAVGFTQSPQdyRDNDG 577
Cdd:cd04185    89 DAIPDPDALEKLLAYADKDNPQFLAPLV--LDPDG 121
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH