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Conserved domains on  [gi|818370584|gb|KKQ50789|]
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Glycosyl transferase family 2 [Candidatus Woesebacteria bacterium GW2011_GWD1_38_10]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
147-387 1.03e-143

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: 427.83  E-value: 1.03e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 147 PRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLLEEDDTKTINKAYDLNLPSYFRIEVVPNSLPKTKPKACNYGL 226
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPSQPRTKPKACNYAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 227 SKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRLPENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIP 306
Cdd:cd06427   81 AFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLPIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 307 LGGTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDSETLEEANSNIKSWLKQRSRWIKGYMQTYLVHMRN 386
Cdd:cd06427  161 LGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEANNALGNWIRQRSRWIKGYMQTWLVHMRN 240

                 .
gi 818370584 387 P 387
Cdd:cd06427  241 P 241
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
610-970 5.00e-62

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: 215.48  E-value: 5.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 610 NILILNWRDVGHVwkGGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTLYLWVLI---YYVFR 686
Cdd:cd03801    1 KILLLSPELPPPV--GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLlreLRPLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 687 LRKHFDLIVDCENGIPFFSPLYSTLPKILLIHHVHqqifreNLPLPFSWLAMFLESRVMKYVY----RSTKIVTVSESSK 762
Cdd:cd03801   79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLH------GAEPGRLLLLLAAERRLLARAEallrRADAVIAVSEALR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 763 ADIAGLGLSKIEDIEIVTPGINLRNFRKLKKYTF------PTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGR- 835
Cdd:cd03801  153 DELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLgippdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGd 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 836 GQYEEHLnrLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQ 915
Cdd:cd03801  233 GPLRAEL--EELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 818370584 916 TGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW-SRKYSWNVSARLFINILN 970
Cdd:cd03801  311 GGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
147-387 1.03e-143

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: 427.83  E-value: 1.03e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 147 PRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLLEEDDTKTINKAYDLNLPSYFRIEVVPNSLPKTKPKACNYGL 226
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPSQPRTKPKACNYAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 227 SKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRLPENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIP 306
Cdd:cd06427   81 AFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLPIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 307 LGGTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDSETLEEANSNIKSWLKQRSRWIKGYMQTYLVHMRN 386
Cdd:cd06427  161 LGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEANNALGNWIRQRSRWIKGYMQTWLVHMRN 240

                 .
gi 818370584 387 P 387
Cdd:cd06427  241 P 241
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
610-970 5.00e-62

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: 215.48  E-value: 5.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 610 NILILNWRDVGHVwkGGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTLYLWVLI---YYVFR 686
Cdd:cd03801    1 KILLLSPELPPPV--GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLlreLRPLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 687 LRKHFDLIVDCENGIPFFSPLYSTLPKILLIHHVHqqifreNLPLPFSWLAMFLESRVMKYVY----RSTKIVTVSESSK 762
Cdd:cd03801   79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLH------GAEPGRLLLLLAAERRLLARAEallrRADAVIAVSEALR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 763 ADIAGLGLSKIEDIEIVTPGINLRNFRKLKKYTF------PTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGR- 835
Cdd:cd03801  153 DELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLgippdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGd 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 836 GQYEEHLnrLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQ 915
Cdd:cd03801  233 GPLRAEL--EELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 818370584 916 TGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW-SRKYSWNVSARLFINILN 970
Cdd:cd03801  311 GGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLDLYR 366
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
106-457 4.38e-43

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: 159.14  E-value: 4.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 106 LTFIYFADFLFTLLIIARSFANKSEikftndelvelddftLPRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLL 185
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAPAD---------------LPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 186 E--EDDTKTINKAYDLNLPsyfRIEVVPNSLPKTKPKACNYGLSKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRlpENVS 263
Cdd:COG1215   68 DgsTDETAEIARELAAEYP---RVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAD--PGVG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 264 ClqsklnyynqnqniltrlftaeysywfnialtglqtlntiiplGGTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKK 343
Cdd:COG1215  143 A-------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 344 GYRTSVI-DSETLEEANSNIKSWLKQRSRWIKGYMQTYLVHMRnpmeFLIRYKHHALLFQLIIGMRMVFIIINPILWLMT 422
Cdd:COG1215  180 GYRIVYVpDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRP----LLRPRRLLLFLLLLLLPLLLLLLLLALLALLLL 255
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 818370584 423 IAYFSMYPVFGPFIESLYPWYIFYPAVFCLIFANF 457
Cdd:COG1215  256 LLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAA 290
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
801-952 8.01e-42

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: 150.12  E-value: 8.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  801 YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPS 880
Cdd:pfam00534   7 FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPS 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818370584  881 SFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW 952
Cdd:pfam00534  87 RYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
853-971 5.22e-24

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 98.14  E-value: 5.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 853 RFVEFKGYvsENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSM 932
Cdd:COG0438    3 RLVPRKGL--DLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 818370584 933 IALTEMDGFRERISRNAYDWSR-KYSWNVSARLFINILNR 971
Cdd:COG0438   81 LRLLEDPELRRRLGEAARERAEeRFSWEAIAERLLALYEE 120
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
233-426 2.62e-18

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: 83.92  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  233 FVVVYDAEDKPDPLQLKKAYLAFSRlPEnVSCLQSKLnYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIPLGGTSN 312
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PE-VAIIQGPI-LPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  313 HFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDSE-TLEEANSNIKSWLKQRSRWIKGYMQTYLVhmrNPMEFL 391
Cdd:pfam13632  78 FLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSaVYEKSPLTFRDFLRQRRRWAYGCLLILLI---RLLGYL 154
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 818370584  392 IRYKHHALLFQLIIGMRMVFIIINPILWLMTIAYF 426
Cdd:pfam13632 155 GTLLWSGLPLALLLLLLFSISSLALVLLLLALLAG 189
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
797-963 3.42e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 73.21  E-value: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 797 PTYSYLGRLMPYKNIDILikafKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDierfVEFKGYVSENEKREILGRSWFL 876
Cdd:PLN02871 264 PLIVYVGRLGAEKNLDFL----KRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVF 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 877 VQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSV---LDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWS 953
Cdd:PLN02871 336 VMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEV 415
                        170
                 ....*....|
gi 818370584 954 RKYSWNVSAR 963
Cdd:PLN02871 416 EKWDWRAATR 425
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
782-902 7.71e-04

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 43.38  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 782 GINLRNFRKLKKY----TFPTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAG----RGQYEEHLNRLVHKLDIER 853
Cdd:NF038011 288 GIDLPRLAPLRAQrpagIPPVVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVGpeeeDPAYAAECRSLVASLGLQD 367
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818370584 854 FVEFKGYvseNEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIAS 902
Cdd:NF038011 368 KVKFLGF---QKIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTT 413
 
Name Accession Description Interval E-value
CESA_like_2 cd06427
CESA_like_2 is a member of the cellulose synthase superfamily; The cellulose synthase (CESA) ...
147-387 1.03e-143

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: 427.83  E-value: 1.03e-143
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 147 PRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLLEEDDTKTINKAYDLNLPSYFRIEVVPNSLPKTKPKACNYGL 226
Cdd:cd06427    1 PVYTILVPLYKEAEVLPQLIASLSALDYPRSKLDVKLLLEEDDEETIAAARALRLPSIFRVVVVPPSQPRTKPKACNYAL 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 227 SKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRLPENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIP 306
Cdd:cd06427   81 AFARGEYVVIYDAEDAPDPDQLKKAVAAFARLDDKLACVQAPLNYYNARENWLTRMFALEYAAWFDYLLPGLARLGLPIP 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 307 LGGTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDSETLEEANSNIKSWLKQRSRWIKGYMQTYLVHMRN 386
Cdd:cd06427  161 LGGTSNHFRTDVLRELGGWDPFNVTEDADLGLRLARAGYRTGVLNSTTLEEANNALGNWIRQRSRWIKGYMQTWLVHMRN 240

                 .
gi 818370584 387 P 387
Cdd:cd06427  241 P 241
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
610-970 5.00e-62

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: 215.48  E-value: 5.00e-62
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 610 NILILNWRDVGHVwkGGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTLYLWVLI---YYVFR 686
Cdd:cd03801    1 KILLLSPELPPPV--GGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLlreLRPLL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 687 LRKHFDLIVDCENGIPFFSPLYSTLPKILLIHHVHqqifreNLPLPFSWLAMFLESRVMKYVY----RSTKIVTVSESSK 762
Cdd:cd03801   79 RLRKFDVVHAHGLLAALLAALLALLLGAPLVVTLH------GAEPGRLLLLLAAERRLLARAEallrRADAVIAVSEALR 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 763 ADIAGLGLSKIEDIEIVTPGINLRNFRKLKKYTF------PTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGR- 835
Cdd:cd03801  153 DELRALGGIPPEKIVVIPNGVDLERFSPPLRRKLgippdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGd 232
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 836 GQYEEHLnrLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQ 915
Cdd:cd03801  233 GPLRAEL--EELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGE 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 818370584 916 TGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW-SRKYSWNVSARLFINILN 970
Cdd:cd03801  311 GGLVVPPDDVEALADALLRLLADPELRARLGRAARERvAERFSWERVAERLLDLYR 366
BcsA COG1215
Glycosyltransferase, catalytic subunit of cellulose synthase and poly-beta-1, ...
106-457 4.38e-43

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: 159.14  E-value: 4.38e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 106 LTFIYFADFLFTLLIIARSFANKSEikftndelvelddftLPRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLL 185
Cdd:COG1215    3 LLLALLALLYLLLLALARRRRAPAD---------------LPRVSVIIPAYNEEAVIEETLRSLLAQDYPKEKLEVIVVD 67
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 186 E--EDDTKTINKAYDLNLPsyfRIEVVPNSLPKTKPKACNYGLSKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRlpENVS 263
Cdd:COG1215   68 DgsTDETAEIARELAAEYP---RVRVIERPENGGKAAALNAGLKAARGDIVVFLDADTVLDPDWLRRLVAAFAD--PGVG 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 264 ClqsklnyynqnqniltrlftaeysywfnialtglqtlntiiplGGTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKK 343
Cdd:COG1215  143 A-------------------------------------------SGANLAFRREALEEVGGFDEDTLGEDLDLSLRLLRA 179
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 344 GYRTSVI-DSETLEEANSNIKSWLKQRSRWIKGYMQTYLVHMRnpmeFLIRYKHHALLFQLIIGMRMVFIIINPILWLMT 422
Cdd:COG1215  180 GYRIVYVpDAVVYEEAPETLRALFRQRRRWARGGLQLLLKHRP----LLRPRRLLLFLLLLLLPLLLLLLLLALLALLLL 255
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 818370584 423 IAYFSMYPVFGPFIESLYPWYIFYPAVFCLIFANF 457
Cdd:COG1215  256 LLPALLLALLLALRRRRLLLPLLHLLYGLLLLLAA 290
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
801-952 8.01e-42

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: 150.12  E-value: 8.01e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  801 YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPS 880
Cdd:pfam00534   7 FVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIADVFVLPS 86
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 818370584  881 SFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW 952
Cdd:pfam00534  87 RYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKLLEDEELRERLGENARKR 158
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
611-963 6.84e-41

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: 154.44  E-value: 6.84e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 611 ILILNWRDVGHVWKGGAeVYVQEIAERWVKGGYGVTILSGNDG-------NSMYDEKIHGVNIMRRGGFFTLYLWVLIYY 683
Cdd:cd03809    1 KILIDGRSLAQRLTGIG-RYTRELLKALAKNDPDESVLAVPPLpgellrlLREYPELSLGVIKIKLWRELALLRWLQILL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 684 VFRLRKHFDLIVDCENGIPFFSplystLPKILLIHHVHQQIFRENLPLPFSWLAMFLESRVMKyvyRSTKIVTVSESSKA 763
Cdd:cd03809   80 PKKDKPDLLHSPHNTAPLLLKG-----CPQVVTIHDLIPLRYPEFFPKRFRLYYRLLLPISLR---RADAIITVSEATRD 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 764 DIAGLgLSKIEDIEIVTP-GINLRNF-----RKLKKYTFPTYSYL---GRLMPYKNIDILIKAFKEVLQSVPDAKLIIAG 834
Cdd:cd03809  152 DIIKF-YGVPPEKIVVIPlGVDPSFFppesaAVLIAKYLLPEPYFlyvGTLEPRKNHERLLKAFALLKKQGGDLKLVIVG 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 835 RGQYE-EHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRdsVLD 913
Cdd:cd03809  231 GKGWEdEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLP--EVA 308
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|
gi 818370584 914 GQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWSRKYSWNVSAR 963
Cdd:cd03809  309 GDAALYFDPLDPESIADAILRLLEDPSLREELIRKGLERAKKFSWEKTAE 358
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
625-960 2.51e-39

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: 149.70  E-value: 2.51e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILS--GNDGNSMY--DEKIHGVNIMRRGGFFTLYLWVLIYYVFRLRK-----HFDLIV 695
Cdd:cd03820   13 GGAERVAINLANHLAKKGYDVTIISldSAEKPPFYelDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKylknnKPDVVI 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 696 DCENGIPFFSPLYSTLPKILLIHHVHqqifRENLPLPFSWLAMFlesrvmKYVYR-STKIVTVSESSKADIAGLGLSKIE 774
Cdd:cd03820   93 SFRTSLLTFLALIGLKSKLIVWEHNN----YEAYNKGLRRLLLR------RLLYKrADKIVVLTEADKLKKYKQPNSNVV 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 775 DIEIVTPGINLRNFRKLKKYTFPTysyLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERF 854
Cdd:cd03820  163 VIPNPLSFPSEEPSTNLKSKRILA---VGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDR 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 855 VEFKGYVSENEkrEILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASN-TAGLRDSVLDGQTGILVKTKSVKELARSMI 933
Cdd:cd03820  240 VKLLGPTKNIA--EEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALL 317
                        330       340
                 ....*....|....*....|....*..
gi 818370584 934 ALTEMDGFRERISRNAYDWSRKYSWNV 960
Cdd:cd03820  318 RLMEDEELRKKMGKNARKNAERFSIEK 344
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
625-935 2.62e-35

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: 137.87  E-value: 2.62e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMR-RGGFFTLYLWVLIYYVFRLRKH-----FDLIVDCE 698
Cdd:cd03811   12 GGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRlLIRVLKLIKLGLLKAILKLKRIlkrakPDVVISFL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 699 NGIPFFSPLYSTLPKILLIHHvHQqIFRENLPLPFSWLAMFlesrvmKYVYRSTKIVTVSESSKADIAGLGLSKIEDIEI 778
Cdd:cd03811   92 GFATYIVAKLAAARSKVIAWI-HS-SLSKLYYLKKKLLLKL------KLYKKADKIVCVSKGIKEDLIRLGPSPPEKIEV 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 779 VTPGINLRNFRKLKK----YTFPTYSYL---GRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDI 851
Cdd:cd03811  164 IYNPIDIDRIRALAKepilNEPEDGPVIlavGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREELEKLAKELGL 243
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 852 ERFVEFKGYVSeNeKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARS 931
Cdd:cd03811  244 AERVIFLGFQS-N-PYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVPDGDAAALAGI 321

                 ....
gi 818370584 932 MIAL 935
Cdd:cd03811  322 LAAL 325
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
625-951 7.09e-33

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: 131.18  E-value: 7.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNI----MRRGGFFTLYLWVLIYYVFR-LRKHFDLIVDCen 699
Cdd:cd03808   10 GGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKELGVKVidipILRRGINPLKDLKALFKLYKlLKKEKPDIVHC-- 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 700 gipfFSP---LYSTL-------PKIllIHHVHQQIFRENLPLPFSWLAMFLESRVMKYvyrSTKIVTVSESSKADIAGLG 769
Cdd:cd03808   88 ----HTPkpgILGRLaarlagvPKV--IYTVHGLGFVFTEGKLLRLLYLLLEKLALLF---TDKVIFVNEDDRDLAIKKG 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 770 LSKIEDIEIVTP-GINLRNFRKLKKY---TFPTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRL 845
Cdd:cd03808  159 IIKKKKTVLIPGsGVDLDRFQYSPESlpsEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSEIL 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 846 VHKLDIERFVEFKGYVSENekREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSV 925
Cdd:cd03808  239 IEKLGLEGRIEFLGFRSDV--PELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDV 316
                        330       340
                 ....*....|....*....|....*.
gi 818370584 926 KELARSMIALTEMDGFRERISRNAYD 951
Cdd:cd03808  317 EALADAIEKLIEDPELRKEMGEAARK 342
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
801-935 5.98e-32

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 121.46  E-value: 5.98e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  801 YLGRLMP-YKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEhLNRLVHKLDIErfVEFKGYVseNEKREILGRSWFLVQP 879
Cdd:pfam13692   6 FVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEE-LEELAAGLEDR--VIFTGFV--EDLAELLAAADVFVLP 80
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 818370584  880 SSFEGWGMTVTESNAAGTPVIASNTAGLRDsVLDGQTGILVKTKSVKELARSMIAL 935
Cdd:pfam13692  81 SLYEGFGLKLLEAMAAGLPVVATDVGGIPE-LVDGENGLLVPPGDPEALAEAILRL 135
CESA_like cd06423
CESA_like is the cellulose synthase superfamily; The cellulose synthase (CESA) superfamily ...
151-333 2.15e-30

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: 118.48  E-value: 2.15e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 151 ILCPLYKEWEVIEQFVRSIEIIDWPKdkLEVILLLEEDDTKTINKAYDLNLPSYFRIEVVPNSLPKTKPKACNYGLSKTT 230
Cdd:cd06423    1 IIVPAYNEEAVIERTIESLLALDYPK--LEVIVVDDGSTDDTLEILEELAALYIRRVLVVRDKENGGKAGALNAGLRHAK 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 231 GEFVVVYDAEDKPDPLQLKKAYLAFSRLPEnVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIPLGGT 310
Cdd:cd06423   79 GDIVVVLDADTILEPDALKRLVVPFFADPK-VGAVQGRVRVRNGSENLLTRLQAIEYLSIFRLGRRAQSALGGVLVLSGA 157
                        170       180
                 ....*....|....*....|...
gi 818370584 311 SNHFRTPVLKDLQGWDPFNVTED 333
Cdd:cd06423  158 FGAFRREALREVGGWDEDTLTED 180
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
713-957 3.23e-30

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: 123.54  E-value: 3.23e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 713 KILLIH--HVHQQIFRENLPLPFSWLAMFLESRVMKYVYRSTKIVTVSESSKADIAGLGLSKieDIEIVTPGINLRNFRK 790
Cdd:cd03817  108 KIPIVHtyHTMYEDYLHYIPKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVKG--PIEVIPNGIDLDKFEK 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 791 ------LKKYTFPTYS----YLGRLMPYKNIDILIKAFKEVLQSvPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGY 860
Cdd:cd03817  186 plnteeRRKLGLPPDEpillYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGLADKVIFTGF 264
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 861 VSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVkELARSMIALTEMDG 940
Cdd:cd03817  265 VPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLFEPNDE-TLAEKLLHLRENLE 343
                        250
                 ....*....|....*..
gi 818370584 941 FRERISRNAYDWSRKYS 957
Cdd:cd03817  344 LLRKLSKNAEISAREFA 360
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
625-951 1.43e-29

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: 120.92  E-value: 1.43e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSgnDGNSMYDEKIH---GVNIMRRGGFFTLYLWVLIYYVfRLRKHFDLIvDCENGI 701
Cdd:cd03819   11 GGAETYILDLARALAERGHRVLVVT--AGGPLLPRLRQigiGLPGLKVPLLRALLGNVRLARL-IRRERIDLI-HAHSRA 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 702 P-FFSPLYSTLPKILLIHHVHQQIFRENLPLPFSWLAMFlesrvmkyvyRSTKIVTVSESSK-ADIAGLGLSKiEDIEIV 779
Cdd:cd03819   87 PaWLGWLASRLTGVPLVTTVHGSYLATYHPKDFALAVRA----------RGDRVIAVSELVRdHLIEALGVDP-ERIRVI 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 780 TPGINLRNF----------RKLKKYTFPTYSYLGRLMPYKNIDILIKAFkEVLQSVPDAKLIIAGRGQYEEHLNRLVHKL 849
Cdd:cd03819  156 PNGVDTDRFppeaeaeeraQLGLPEGKPVVGYVGRLSPEKGWLLLVDAA-AELKDEPDFRLLVAGDGPERDEIRRLVERL 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 850 DIERFVEFKGYVSEneKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELA 929
Cdd:cd03819  235 GLRDRVTFTGFRED--VPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVPPGDAEALA 312
                        330       340
                 ....*....|....*....|..
gi 818370584 930 RSMIALTEMDGFRERISRNAYD 951
Cdd:cd03819  313 DAIRAAKLLPEAREKLQAAAAL 334
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
625-950 8.08e-29

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: 118.97  E-value: 8.08e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTLYL-------WVLIYYVFRLRKHFDLIVDC 697
Cdd:cd03823   15 GGAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLalkrrgyELFETYNPGLRRLLARLLED 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 698 ENgipffsplystlPKILLIHH---VHQQIFRE----NLPL-----PFSWLAMflesRVMKYVYRSTKIVTVSesskADI 765
Cdd:cd03823   95 FR------------PDVVHTHNlsgLGASLLDAardlGIPVvhtlhDYWLLCP----RQFLFKKGGDAVLAPS----RFT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 766 AGL----GLSKIEdIEIVTPGINLRNfRKLKKYTFPT----YSYLGRLMPYKNIDILIKAFKEVLQsvPDAKLIIAGRGQ 837
Cdd:cd03823  155 ANLheanGLFSAR-ISVIPNAVEPDL-APPPRRRPGTerlrFGYIGRLTEEKGIDLLVEAFKRLPR--EDIELVIAGHGP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 838 yeehLNRLVHkLDIERFVEFKGYVSENEKREILGRSWFLVQPSSF-EGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQT 916
Cdd:cd03823  231 ----LSDERQ-IEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWpEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVN 305
                        330       340       350
                 ....*....|....*....|....*....|....
gi 818370584 917 GILVKTKSVKELARSMIALTEMDGFRERISRNAY 950
Cdd:cd03823  306 GLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAE 339
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
776-964 3.05e-28

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: 118.11  E-value: 3.05e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 776 IEIVTPGINLRNF-----------RKLKKYTFPTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYE----- 839
Cdd:cd03800  189 INVVPPGVDLERFfpvdraearraRLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANLVLVGGPSDDplsmd 268
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 840 -EHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGI 918
Cdd:cd03800  269 rEELAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGL 348
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 818370584 919 LVKTKSVKELARSMIALTEMDGFRERISRNAYDWS-RKYSW-NVSARL 964
Cdd:cd03800  349 LVDPHDPEALAAALRRLLDDPALWQRLSRAGLERArAHYTWeSVADQL 396
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
625-949 6.05e-27

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: 113.57  E-value: 6.05e-27
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIH-GVNIMRRGGFFTLYLWVLiyyvFRLRKHFDLI-VDCENGIP 702
Cdd:cd03807   12 GGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAaGVPVVCLGLSSGKDPGVL----LRLAKLIRKRnPDVVHTWM 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 703 FFSPLYSTLPKIL-----LIHHVHQQIFRENLPLPFSWLAMFLESRVMKYVYrstkivtVSESSKADIAGLGLSKiEDIE 777
Cdd:cd03807   88 YHADLIGGLAAKLaggvkVIWSVRSSNIPQRLTRLVRKLCLLLSKFSPATVA-------NSSAVAEFHQEQGYAK-NKIV 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 778 IVTPGINLRNFRKLKKYTFPTYSYL------------GRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRL 845
Cdd:cd03807  160 VIYNGIDLFKLSPDDASRARARRRLglaedrrvigivGRLHPVKDHSDLLRAAALLVETHPDLRLLLVGRGPERPNLERL 239
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 846 VHKLDIERFVEFKGYVSenEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGqTGILVKTKSV 925
Cdd:cd03807  240 LLELGLEDRVHLLGERS--DVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAELVDDG-TGFLVPAGDP 316
                        330       340
                 ....*....|....*....|....
gi 818370584 926 KELARSMIALTEMDGFRERISRNA 949
Cdd:cd03807  317 QALADAIRALLEDPEKRARLGRAA 340
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
621-962 1.07e-26

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: 113.24  E-value: 1.07e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 621 HVWKGGAEVYVQEIAERWVKGGYGVTILSGNDGNS---------------MYDEKIHGVNIMRRGGFFTLYLWVLIY-YV 684
Cdd:cd03798   10 NANSPGRGIFVRRQVRALSRRGVDVEVLAPAPWGPaaarllrkllgeavpPRDGRRLLPLKPRLRLLAPLRAPSLAKlLK 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 685 FRLRKHFDLIVdcengiPFFspLYSTL------------PKILLIHHVHQQIFRenlplPFSWLAMFlesrvMKYVYRS- 751
Cdd:cd03798   90 RRRRGPPDLIH------AHF--AYPAGfaaallarlygvPYVVTEHGSDINVFP-----PRSLLRKL-----LRWALRRa 151
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 752 TKIVTVSESSKADIAGLGLSKiEDIEIVTPGINLRNFRKL-----KKYTFPTYSYLGRLMPYKNIDILIKAFKEVLQSVP 826
Cdd:cd03798  152 ARVIAVSKALAEELVALGVPR-DRVDVIPNGVDPARFQPEdrglgLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARP 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 827 DAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAG 906
Cdd:cd03798  231 DVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGG 310
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 818370584 907 LRDSVLDGQTGILVKTKSVKELARSMI-ALTEMDGFRERISRNAYdWSRKYSWNVSA 962
Cdd:cd03798  311 IPEVVGDPETGLLVPPGDADALAAALRrALAEPYLRELGEAARAR-VAERFSWVKAA 366
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
624-949 5.29e-25

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: 107.75  E-value: 5.29e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 624 KGGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTL----YLWVLIYYVFRLRKHFDLI-VDCE 698
Cdd:cd03795   13 IGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKSFLNVastpFSPSYIKRFKKLAKEYDIIhYHFP 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 699 NGIPFFSPLYSTLPKILLIHHvHQQIFRENLPLPF--SWLAMFLEsrvmkyvyRSTKIVTVS----ESS--------KAD 764
Cdd:cd03795   93 NPLADLLLFFSGAKKPVVVHW-HSDIVKQKKLLKLykPLMTRFLR--------RADRIIATSpnyvETSptlrefknKVR 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 765 IAGLGLSKIEdieiVTPGINLRNFRKLKKYTFPTYSYLGRLMPYKNIDILIKAFKEVlqsvpDAKLIIAGRGQYEEHLNR 844
Cdd:cd03795  164 VIPLGIDKNV----YNIPRVDFENIKREKKGKKIFLFIGRLVYYKGLDYLIEAAQYL-----NYPIVIGGEGPLKPDLEA 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 845 LVHKLDIERfVEFKGYVSENEKREILGRSWFLVQPSSF--EGWGMTVTESNAAGTPVIASNTA-GLRDSVLDGQTGILVK 921
Cdd:cd03795  235 QIELNLLDN-VKFLGRVDDEEKVIYLHLCDVFVFPSVLrsEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVP 313
                        330       340
                 ....*....|....*....|....*...
gi 818370584 922 TKSVKELARSMIALTEMDGFRERISRNA 949
Cdd:cd03795  314 PKDPDALAEAIDKLLSDEELRESYGENA 341
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
853-971 5.22e-24

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 98.14  E-value: 5.22e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 853 RFVEFKGYvsENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSM 932
Cdd:COG0438    3 RLVPRKGL--DLLLEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAI 80
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 818370584 933 IALTEMDGFRERISRNAYDWSR-KYSWNVSARLFINILNR 971
Cdd:COG0438   81 LRLLEDPELRRRLGEAARERAEeRFSWEAIAERLLALYEE 120
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
610-966 8.72e-24

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: 104.73  E-value: 8.72e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 610 NILILNwrDVGHVWKGGAEVYVQEIAERWVKGGYGVTILSGN---------DGNSMYDEKI----------HGVNIMRRG 670
Cdd:cd03794    1 KILLIS--QYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSpnyplgrifAGATETKDGIrvirvklgpiKKNGLIRRL 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 671 -GFFTLYLWVLIYYVFRLRKhFDLIVdCENGIPFFSPLYSTL------PKILLIHHVHQQIFRENLPLPfSWLAMFLESR 743
Cdd:cd03794   79 lNYLSFALAALLKLLVREER-PDVII-AYSPPITLGLAALLLkklrgaPFILDVRDLWPESLIALGVLK-KGSLLKLLKK 155
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 744 VMKYVYR-STKIVTVSESSKADIAGLGLSKiEDIEIVTPGINLRNFRKLKKYTFPTYS---------YLGRLMPYKNIDI 813
Cdd:cd03794  156 LERKLYRlADAIIVLSPGLKEYLLRKGVPK-EKIIVIPNWADLEEFKPPPKDELRKKLglddkfvvvYAGNIGKAQGLET 234
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 814 LIKAFKEvLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERfVEFKGYVSENEKREILGRS--WFLVQPSSFEGWGMT--- 888
Cdd:cd03794  235 LLEAAER-LKRRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAAdvGLVPLKDNPANRGSSpsk 312
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818370584 889 VTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW-SRKYSWNVSARLFI 966
Cdd:cd03794  313 LFEYMAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENGRELaEEKFSREKLADRLL 391
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
801-957 1.31e-22

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: 100.07  E-value: 1.31e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 801 YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYvsENEKREILGRSWFLVQPS 880
Cdd:cd04949  165 TISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY--HSNLDQEYQDAYLSLLTS 242
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818370584 881 SFEGWGMTVTESNAAGTPVIASNTA-GLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWSRKYS 957
Cdd:cd04949  243 QMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIEKNNIDALADKIIELLNDPEKLQQFSEESYKIAEKYS 320
CESA_CaSu_A2 cd06437
Cellulose synthase catalytic subunit A2 (CESA2) is a catalytic subunit or a catalytic subunit ...
147-375 3.74e-22

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: 96.23  E-value: 3.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 147 PRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEvILLLEE--DDTKTINKAYDLNLPSY-FRIE-VVPNSLPKTKPKAC 222
Cdd:cd06437    1 PMVTVQLPVFNEKYVVERLIEAACALDYPKDRLE-IQVLDDstDETVRLAREIVEEYAAQgVNIKhVRRADRTGYKAGAL 79
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 223 NYGLSKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRlpENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLN 302
Cdd:cd06437   80 AEGMKVAKGEYVAIFDADFVPPPDFLQKTPPYFAD--PKLGFVQTRWGHINANYSLLTRVQAMSLDYHFTIEQVARSSTG 157
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 818370584 303 TIIPLGGTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVI-DSETLEEANSNIKSWLKQRSRWIKG 375
Cdd:cd06437  158 LFFNFNGTAGVWRKECIEDAGGWNHDTLTEDLDLSYRAQLKGWKFVYLdDVVVPAELPASMSAYRSQQHRWSKG 231
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
801-920 3.37e-21

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: 93.62  E-value: 3.37e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 801 YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREILGR-SWFLVQP 879
Cdd:cd01635  115 SVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIGGLVDDEVLELLLAaADVFVLP 194
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 818370584 880 SSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILV 920
Cdd:cd01635  195 SRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
801-967 1.45e-20

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: 94.74  E-value: 1.45e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 801 YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRG-QYEEHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQP 879
Cdd:cd03821  209 FLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDdGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLP 288
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 880 SSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGqTGILVKTkSVKELARSMIALTEMDGFRERIS---RNAYDWSRKY 956
Cdd:cd03821  289 SYSENFGNVVAEALACGLPVVITDKCGLSELVEAG-CGVVVDP-NVSSLAEALAEALRDPADRKRLGemaRRARQVEENF 366
                        170
                 ....*....|.
gi 818370584 957 SWNVSARLFIN 967
Cdd:cd03821  367 SWEAVAGQLGE 377
CESA_CelA_like cd06421
CESA_CelA_like are involved in the elongation of the glucan chain of cellulose; Family of ...
147-379 2.94e-20

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: 90.71  E-value: 2.94e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 147 PRYTILCPLYKE-WEVIEQFVRSIEIIDWPKDKLEVILLleeDDTKTINKAydlNLPSYFRIEVVPNSLPKTKP---KA- 221
Cdd:cd06421    1 PTVDVFIPTYNEpLEIVRKTLRAALAIDYPHDKLRVYVL---DDGRRPELR---ALAAELGVEYGYRYLTRPDNrhaKAg 74
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 222 -CNYGLSKTTGEFVVVYDAEDKPDPLQLKkAYLAFSRLPENVSCLQSKLNYYNQNQNILTRLFTAEYSYWF-NIALTGLQ 299
Cdd:cd06421   75 nLNNALAHTTGDFVAILDADHVPTPDFLR-RTLGYFLDDPKVALVQTPQFFYNPDPFDWLADGAPNEQELFyGVIQPGRD 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 300 TLNTIIPLGgtSNH-FRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDsETLE--EANSNIKSWLKQRSRWIKGY 376
Cdd:cd06421  154 RWGAAFCCG--SGAvVRREALDEIGGFPTDSVTEDLATSLRLHAKGWRSVYVP-EPLAagLAPETLAAYIKQRLRWARGM 230

                 ...
gi 818370584 377 MQT 379
Cdd:cd06421  231 LQI 233
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
799-954 1.84e-19

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: 91.19  E-value: 1.84e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 799 YSYLGRLMPYKNIDILIKAFKEVlqsvpDAKLIIAGRGqyeEHLNRLVHKLDieRFVEFKGYVSENEKREILGRSWFLVQ 878
Cdd:cd03804  202 YLTASRLVPYKRIDLAVEAFNEL-----PKRLVVIGDG---PDLDRLRAMAS--PNVEFLGYQPDEVLKELLSKARAFVF 271
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 818370584 879 PSSfEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGF--RERISRNAYDWSR 954
Cdd:cd03804  272 AAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQTVESLKAAVEEFEQNFDRfkPQAIRANAERFSR 348
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
750-955 2.19e-18

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: 88.18  E-value: 2.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 750 RSTKIVTVSESSKADIAGLgLSKIEDIEIVTPGINLRNFRKLkkytfPTYSYLGRLM---------------PYKNIDIL 814
Cdd:cd04962  141 KSDRVTAVSSSLRQETYEL-FDVDKDIEVIHNFIDEDVFKRK-----PAGALKRRLLappdekvvihvsnfrPVKRIDDV 214
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 815 IKAFKEVLQSVPdAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGyvSENEKREILGRSWFLVQPSSFEGWGMTVTESNA 894
Cdd:cd04962  215 VRVFARVRRKIP-AKLLLVGDGPERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPSEKESFGLAALEAMA 291
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818370584 895 AGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWSRK 955
Cdd:cd04962  292 CGVPVVSSNAGGIPEVVKHGETGFLSDVGDVDAMAKSALSILEDDELYNRMGRAARKRAAE 352
Glyco_trans_2_3 pfam13632
Glycosyl transferase family group 2; Members of this family of prokaryotic proteins include ...
233-426 2.62e-18

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: 83.92  E-value: 2.62e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  233 FVVVYDAEDKPDPLQLKKAYLAFSRlPEnVSCLQSKLnYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIPLGGTSN 312
Cdd:pfam13632   1 WILLLDADTVLPPDCLLGIANEMAS-PE-VAIIQGPI-LPMNVGNYLEELAALFFADDHGKSIPVRMALGRVLPFVGSGA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  313 HFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDSE-TLEEANSNIKSWLKQRSRWIKGYMQTYLVhmrNPMEFL 391
Cdd:pfam13632  78 FLRRSALQEVGGWDDGSVSEDFDFGLRLQRAGYRVRFAPYSaVYEKSPLTFRDFLRQRRRWAYGCLLILLI---RLLGYL 154
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 818370584  392 IRYKHHALLFQLIIGMRMVFIIINPILWLMTIAYF 426
Cdd:pfam13632 155 GTLLWSGLPLALLLLLLFSISSLALVLLLLALLAG 189
CESA_NdvC_like cd06435
NdvC_like proteins in this family are putative bacterial beta-(1,6)-glucosyltransferase; ...
150-383 2.70e-18

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: 85.14  E-value: 2.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 150 TILCPLYKEW-EVIEQFVRSIEIIDWPKdkLEVILL---LEEDDTKTINKAYDLNLPSYFR-IEVVPnsLPKTKPKACNY 224
Cdd:cd06435    1 SIHVPCYEEPpEMVKETLDSLAALDYPN--FEVIVIdnnTKDEALWKPVEAHCAQLGERFRfFHVEP--LPGAKAGALNY 76
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 225 GLSKTTG--EFVVVYDAEDKPDPLQLKKAYLAFSRlpENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLN 302
Cdd:cd06435   77 ALERTAPdaEIIAVIDADYQVEPDWLKRLVPIFDD--PRVGFVQAPQDYRDGEESLFKRMCYAEYKGFFDIGMVSRNERN 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 303 TIIPLGgTSNHFRTPVLKDLQGWDPFNVTEDCDLGTRLFKKGYRTSVIDSE----TLEEANSNIKswlKQRSRWIKGYMQ 378
Cdd:cd06435  155 AIIQHG-TMCLIRRSALDDVGGWDEWCITEDSELGLRMHEAGYIGVYVAQSyghgLIPDTFEAFK---KQRFRWAYGAVQ 230

                 ....*
gi 818370584 379 TYLVH 383
Cdd:cd06435  231 ILKKH 235
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
737-949 4.64e-18

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: 87.12  E-value: 4.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 737 AMFLESRVMKYVY---------RSTKIVTVSESSKADIAGLGLSKiEDIEIVTPGINLRNFR-KLKKYTFPTYSYLGRLM 806
Cdd:cd05844  121 AWLAASPGWPSQFqrhrralqrPAALFVAVSGFIRDRLLARGLPA-ERIHVHYIGIDPAKFApRDPAERAPTILFVGRLV 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 807 PYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIerfVEFKGYVSENEKREILGRSWFLVQPS------ 880
Cdd:cd05844  200 EKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALGR---VRFLGALPHAEVQDWMRRAEIFCLPSvtaasg 276
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818370584 881 SFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNA 949
Cdd:cd05844  277 DSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAA 345
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
735-956 9.38e-17

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: 84.31  E-value: 9.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 735 WLAMFleSRVMKYVYR-STKIVTVSESSKADIAGLGlSKIEDIEIVTPGINLRNF----RKLKKYTFPTYSYLGRLMPYK 809
Cdd:cd03813  230 WIRFF--ERLGKLAYQqADKIISLYEGNRRRQIRLG-ADPDKTRVIPNGIDIQRFaparEERPEKEPPVVGLVGRVVPIK 306
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 810 NIDILIKAFKEVLQSVPDAKLIIAG----RGQYEEHLNRLVHKLDIERFVEFKGYVSeneKREILGRSWFLVQPSSFEGW 885
Cdd:cd03813  307 DVKTFIRAFKLVRRAMPDAEGWLIGpedeDPEYAQECKRLVASLGLENKVKFLGFQN---IKEYYPKLGLLVLTSISEGQ 383
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818370584 886 GMTVTESNAAGTPVIASNTAGLRDSVLD-----GQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWSRKY 956
Cdd:cd03813  384 PLVILEAMASGVPVVATDVGSCRELIYGaddalGQAGLVVPPADPEALAEALIKLLRDPELRQAFGEAGRKRVEKY 459
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
625-939 1.31e-16

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: 82.34  E-value: 1.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSGndGNSMYDEKIHGV--------NIMRRGGFFTLYLWVLiyyVFRLRKHFDLIvd 696
Cdd:cd03802   18 GGTELVVSALTEGLVRRGHEVTLFAP--GDSHTSAPLVAVipralrldPIPQESKLAELLEALE---VQLRASDFDVI-- 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 697 cENGIPFFSPLYSTLPKILLIHHVHQQIFRENLPLpfswlamflesrvmKYVYRSTKIVTVSESSKADiaglgLSKIEDI 776
Cdd:cd03802   91 -HNHSYDWLPPFAPLIGTPFVTTLHGPSIPPSLAI--------------YAAEPPVNYVSISDAQRAA-----TPPIDYL 150
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 777 EIVTPGINLRNFR---KLKKYtfptYSYLGRLMPYKNIDILIKAFKEVlqsvpDAKLIIAGRGQYEEHLNRLVHKLDIER 853
Cdd:cd03802  151 TVVHNGLDPADYRfqpDPEDY----LAFLGRIAPEKGLEDAIRVARRA-----GLPLKIAGKVRDEDYFYYLQEPLPGPR 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 854 fVEFKGYVSENEKREILGRSWFLVQPSSF-EGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVktKSVKELARSM 932
Cdd:cd03802  222 -IEFIGEVGHDEKQELLGGARALLFPINWdEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFLV--DSVEEMAEAI 298

                 ....*..
gi 818370584 933 IALTEMD 939
Cdd:cd03802  299 ANIDRID 305
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
710-970 6.79e-16

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: 80.51  E-value: 6.79e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 710 TLPKILLIHHVHQqiFRENLPLPFSWLAMFLEsrvmkyvyRSTKIVTVSESSKADIAGLGLSKIEDIEIVTPGINLRNFR 789
Cdd:cd03822  104 RIPVITTLHTVLD--LSDPGKQALKVLFRIAT--------LSERVVVMAPISRFLLVRIKLIPAVNIEVIPHGVPEVPQD 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 790 K---LKKYTFPT----YSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAG-------RGQYEEHLNRLVHKLDIERFV 855
Cdd:cd03822  174 PttaLKRLLLPEgkkvILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGelhpslaRYEGERYRKAAIEELGLQDHV 253
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 856 EF-KGYVSENEKREILGRSWFLVQPSSFEGWGM--TVTESNAAGTPVIASNTAGLRDSVLDGQtGILVKTKSVKELARSM 932
Cdd:cd03822  254 DFhNNFLPEEEVPRYISAADVVVLPYLNTEQSSsgTLSYAIACGKPVISTPLRHAEELLADGR-GVLVPFDDPSAIAEAI 332
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 818370584 933 IALTEMDGFRERISRNAYDWSRKYSWNVSARLFINILN 970
Cdd:cd03822  333 LRLLEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
Glyco_tranf_2_3 pfam13641
Glycosyltransferase like family 2; Members of this family of prokaryotic proteins include ...
147-375 1.33e-15

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: 77.03  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  147 PRYTILCPLYKEWEVIEQFVRSIEIIDWPKDklEVILLLEEDDTKTINKAYDLNLP-SYFRIEVVPNSL---PKTKPKAC 222
Cdd:pfam13641   2 PDVSVVVPAFNEDSVLGRVLEAILAQPYPPV--EVVVVVNPSDAETLDVAEEIAARfPDVRLRVIRNARllgPTGKSRGL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  223 NYGLSKTTGEFVVVYDAEDKPDPLQLKKaYLAFSRLPeNVSCLQSKLNYYNQNqNILTRLFTAEYSYWFNIALTGLQTLN 302
Cdd:pfam13641  80 NHGFRAVKSDLVVLHDDDSVLHPGTLKK-YVQYFDSP-KVGAVGTPVFSLNRS-TMLSALGALEFALRHLRMMSLRLALG 156
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818370584  303 tIIPLGGTSNHFRTPVLKDLQGWDP-FNVTEDCDLGTRLFKKGYRT-SVIDSETLEEANSNIKSWLKQRSRWIKG 375
Cdd:pfam13641 157 -VLPLSGAGSAIRREVLKELGLFDPfFLLGDDKSLGRRLRRHGWRVaYAPDAAVRTVFPTYLAASIKQRARWVYG 230
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
726-958 2.84e-15

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: 78.49  E-value: 2.84e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 726 RENLPLPFSWLAMflesRVMKYVYR-STKIVTVSESSKADIAGLGlskIEDIEIVTPGINLRNF----------RKLKKY 794
Cdd:cd03814  124 SYYTLGPLSWLAW----AYLRWFHNpFDTTLVPSPSIARELEGHG---FERVRLWPRGVDTELFhpsrrdaalrRRLGPP 196
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 795 TFPTYSYLGRLMPYKNIDILIKAFKEVLQSVPdAKLIIAGRGQYEEHLNRlvhkldieRF--VEFKGYVSENEKREILGR 872
Cdd:cd03814  197 GRPLLLYVGRLAPEKNLEALLDADLPLAASPP-VRLVVVGDGPARAELEA--------RGpdVIFTGFLTGEELARAYAS 267
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 873 SWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDW 952
Cdd:cd03814  268 ADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARARAE 347

                 ....*.
gi 818370584 953 SRKYSW 958
Cdd:cd03814  348 AERYSW 353
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
635-952 4.96e-15

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: 78.40  E-value: 4.96e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 635 AERWV--------KGGYGVTILSgndgnSMYDE------------KIHGV-NIMRR---GGFFTLY-----LWVLIYYVF 685
Cdd:cd03805   15 AERLVvdaalalqSRGHEVTIYT-----SHHDPshcfeetkdgtlPVRVRgDWLPRsifGRFHALCaylrmLYLALYLLL 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 686 RLRKHFDL-IVDC-ENGIPFFsPLYSTlPKILLIHHVHQQ-----------IFRenlpLPFSWLamflESRVMKYvyrST 752
Cdd:cd03805   90 FSGEKYDVfIVDQvSACVPLL-KLFRP-SKILFYCHFPDQllaqrksllkrLYR----KPFDWL----EEFTTGM---AD 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 753 KIV--------TVSESSKadiaglGLSKIEDiEIVTPGINLRNFRKLKKYTFP--------TYSYLG--RLMPYKNIDIL 814
Cdd:cd03805  157 QIVvnsnftagVFKKTFP------SLAKNPP-EVLYPCVDTDSFDSTSEDPDPgdliaksnKKFFLSinRFERKKNIALA 229
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 815 IKAFKEVLQ---SVPDAKLIIAGrG---------QYEEHLNRLVHKL-DIERFVEFKGYVSENEKREILGRSWFLVQPSS 881
Cdd:cd03805  230 IEAFAKLKQklpEFENVRLVIAG-GydprvaenvEYLEELQRLAEELlNVEDQVLFLRSISDSQKEQLLSSALALLYTPS 308
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 818370584 882 FEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKtKSVKELARSMIALTEMDGFRERISRNAYDW 952
Cdd:cd03805  309 NEHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFLCE-PTPEAFAEAMLKLANDPDLADRMGAAGRKR 378
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
774-972 4.49e-14

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 74.79  E-value: 4.49e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 774 EDIEIVTPGINLRNFRkLKKYTFPTYSYL-----GRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHK 848
Cdd:cd03799  148 KKIIVHRSGIDCNKFR-FKPRYLPLDGKIriltvGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQE 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 849 LDIERFVEFKGYVSENEKREILGRSWFLVQPS------SFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVKT 922
Cdd:cd03799  227 LNIGDCVKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPE 306
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 818370584 923 KSVKELARSMIALTEMDGFRERISRNAydwsRKYswnVSARLFINILNRE 972
Cdd:cd03799  307 RDAEAIAEKLTYLIEHPAIWPEMGKAG----RAR---VEEEYDINKLNDE 349
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
625-785 1.45e-13

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 69.48  E-value: 1.45e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTLYLWVLIYYVFRLRKH-----FDLI-VDCE 698
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLlrrerPDVVhAHSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  699 NGIPFFSPLYSTLPKILLIHHVHQQIFRENLPLPFSWLAMFLESRVMKYVY-RSTKIVTVSESSKADIA-GLGLSKiEDI 776
Cdd:pfam13439  81 FPLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRRLLRRLERRLLrRADRVIAVSEAVADELRrLYGVPP-EKI 159

                  ....*....
gi 818370584  777 EIVTPGINL 785
Cdd:pfam13439 160 RVIPNGVDL 168
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
797-963 3.42e-13

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 73.21  E-value: 3.42e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 797 PTYSYLGRLMPYKNIDILikafKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDierfVEFKGYVSENEKREILGRSWFL 876
Cdd:PLN02871 264 PLIVYVGRLGAEKNLDFL----KRVMERLPGARLAFVGDGPYREELEKMFAGTP----TVFTGMLQGDELSQAYASGDVF 335
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 877 VQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSV---LDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWS 953
Cdd:PLN02871 336 VMPSESETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYTPGDVDDCVEKLETLLADPELRERMGAAAREEV 415
                        170
                 ....*....|
gi 818370584 954 RKYSWNVSAR 963
Cdd:PLN02871 416 EKWDWRAATR 425
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
746-968 3.45e-13

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: 72.36  E-value: 3.45e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 746 KYVYRSTKIVTVSESS-KADIA-GLGLSKIEDIEIVTPGINLRNFRKL------KKYTFPTYSYLGrLM-------PYKN 810
Cdd:cd03825  131 REALAKKRLTIVAPSRwLADMVrRSPLLKGLPVVVIPNGIDTEIFAPVdkakarKRLGIPQDKKVI-LFgaesvtkPRKG 209
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 811 IDILIKAFKEvLQSVPDAKLIIAGRGqyeeHLNRLVHKLDIERFvefkGYVSENEK-REILGRSWFLVQPSSFEGWGMTV 889
Cdd:cd03825  210 FDELIEALKL-LATKDDLLLVVFGKN----DPQIVILPFDIISL----GYIDDDEQlVDIYSAADLFVHPSLADNLPNTL 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 890 TESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDGFRERISRNAYD-WSRKYSWNVSARLFINI 968
Cdd:cd03825  281 LEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERARAlAENHFDQRVQAQRYLEL 360
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
803-948 4.72e-13

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: 71.71  E-value: 4.72e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 803 GRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEkrEILGRSWFLVQPSSF 882
Cdd:cd04951  195 GRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLVDRVILLGQISNIS--EYYNAADLFVLSSEW 272
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 818370584 883 EGWGMTVTESNAAGTPVIASNTAGLRDSVldGQTGILVKTKSVKELARSMIALTEMDGFRERISRN 948
Cdd:cd04951  273 EGFGLVVAEAMACERPVVATDAGGVAEVV--GDHNYVVPVSDPQLLAEKIKEIFDMSDEERDILGN 336
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
804-920 1.38e-11

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: 67.35  E-value: 1.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 804 RLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHkldiERFVEFKG-----YVSENEKRE-----ILGRS 873
Cdd:cd03792  205 RFDPSKDPLGVIDAYKLFKRRAEEPQLVICGHGAVDDPEGSVVY----EEVMEYAGddhdiHVLRLPPSDqeinaLQRAA 280
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 818370584 874 WFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILV 920
Cdd:cd03792  281 TVVLQLSTREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLV 327
Glycos_transf_2 pfam00535
Glycosyl transferase family 2; Diverse family, transferring sugar from UDP-glucose, ...
150-306 1.81e-11

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: 63.57  E-value: 1.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  150 TILCPLYKEWEVIEQFVRSIeiIDWPKDKLEVILLL--EEDDTKTINKAYdlnLPSYFRIEVVPNSLPKTKPKACNYGLS 227
Cdd:pfam00535   1 SVIIPTYNEEKYLLETLESL--LNQTYPNFEIIVVDdgSTDGTVEIAEEY---AKKDPRVRVIRLPENRGKAGARNAGLR 75
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 818370584  228 KTTGEFVVVYDAEDKPDPLQLKKAYLAFSRLPENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIP 306
Cdd:pfam00535  76 AATGDYIAFLDADDEVPPDWLEKLVEALEEDGADVVVGSRYVIFGETGEYRRASRITLSRLPFFLGLRLLGLNLPFLIG 154
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
625-782 3.17e-11

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 62.42  E-value: 3.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIHGVNIMRRGGFFTLYLWVLIYYVFRLRKH-----FDLIVDCEN 699
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELVGDGVRVHRLPVPPRPSPLADLAALRRLRRLlraerPDVVHAHSP 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  700 GIPFFSPLYSTLPKILLIHHVHQQIFRENLPLPfSWLAMFLESRVMKyvyRSTKIVTVSESSKADIAGLGLSKiEDIEIV 779
Cdd:pfam13579  81 TAGLAARLARRRRGVPLVVTVHGLALDYGSGWK-RRLARALERRLLR---RADAVVVVSEAEAELLRALGVPA-ARVVVV 155

                  ...
gi 818370584  780 TPG 782
Cdd:pfam13579 156 PNG 158
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
625-904 3.20e-11

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: 66.16  E-value: 3.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 625 GGAEVYVQEIAERWVKGGYGVTILSGNDGNSMYDEKIH--GVNIMR---RGGFFTLYLWVLIYYvfRLRKHFDLIvdcEN 699
Cdd:cd03812   12 GGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEELEelGGKIFYippKKKNIIKYFIKLLKL--IKKEKYDIV---HV 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 700 GIPFFSPLYSTLPKIL----LIHHVH-----QQIFRENLPLPFSWLAMFLesrvmkyvyrSTKIVTVSEssKADIAGLGL 770
Cdd:cd03812   87 HGSSSNGIILLLAAKAgvpvRIAHSHntkdsSIKLRKIRKNVLKKLIERL----------STKYLACSE--DAGEWLFGE 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 771 SKIEDIEIVTPGINLRNF-------RKLKKYTFPT----YSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYE 839
Cdd:cd03812  155 VENGKFKVIPNGIDIEKYkfnkekrRKRRKLLILEdklvLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELK 234
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 818370584 840 EHLNRLVHKLDIERFVEFKGYVSENEkrEILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIASNT 904
Cdd:cd03812  235 EKIKEKVKELGLEDKVIFLGFRNDVS--EILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDT 297
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
700-949 4.52e-11

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 66.09  E-value: 4.52e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 700 GIPFFSPLYSTLPKILLIHHVH-------------QQIFRENLPL------PFSWLAMF---LESRVMKYVYRSTKIVTV 757
Cdd:cd03806  116 GYPFTYPLVRLLGGCPVVAYVHyptistdmlnkvrSREASYNNDStiarssVLSIAKLLyyrLFAFLYGLAGSFADVVMV 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 758 SES-SKADIAGLgLSKIEDIEIVTPGINLRNFRKLKKYTF---PTYSYLGRLMPYKNIDILIKAFKEVLQSVPD-----A 828
Cdd:cd03806  196 NSTwTYNHIRQL-WKRNIKPSIVYPPCDTEELTKLPIDEKtreNQILSIAQFRPEKNHPLQLRAFAELLKRLPEsirsnP 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 829 KLIIAG--RGQ----YEEHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIAS 902
Cdd:cd03806  275 KLVLIGscRNEedkeRVEALKLLAKELILEDSVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAH 354
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 818370584 903 NTAG-LRDSVL---DGQTGILVKTKsvKELARSMIALTEMDgFRERISRNA 949
Cdd:cd03806  355 ASAGpLLDIVVpwdGGPTGFLASTP--EEYAEAIEKILTLS-EEERLQRRE 402
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
797-949 2.62e-10

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: 63.54  E-value: 2.62e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 797 PTYSYLGRLM-PYKNIDILIKAFKEVLQSVPDAKLIIAGR------------GQYEEHLNRLVhKLDIERfVEFKGYVSE 863
Cdd:cd03818  214 PVITYVARNLePYRGFHVFMRALPRIQARRPDARVVVVGGdgvsygspppdgGSWKQKMLAEL-GVDLER-VHFVGKVPY 291
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 864 NEKREILGRS---WFLVQPSSFEgWGMTvtESNAAGTPVIASNTAGLRDSVLDGQTGILVKTKSVKELARSMIALTEMDG 940
Cdd:cd03818  292 DQYVRLLQLSdahVYLTYPFVLS-WSLL--EAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDPDALAAAVLELLEDPD 368

                 ....*....
gi 818370584 941 FRERISRNA 949
Cdd:cd03818  369 RAAALRRAA 377
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
797-968 3.04e-09

Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 family of glycosyltransferases. Glycogen synthase (EC:2.4.1.21) catalyzes the formation and elongation of the alpha-1,4-glucose backbone using ADP-glucose, the second and key step of glycogen biosynthesis. This family includes starch synthases of plants, such as DULL1 in Zea mays and glycogen synthases of various organisms.


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 60.65  E-value: 3.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 797 PTYSYLGRLMPYKNIDILIKAFKEVLQSvpDAKLIIAGRG--QYEEHLNRLvhkldIERFVE-FKGYVSENEK--REILG 871
Cdd:cd03791  295 PLFGFVGRLTEQKGVDLILDALPELLEE--GGQLVVLGSGdpEYEQAFREL-----AERYPGkVAVVIGFDEAlaHRIYA 367
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 872 RSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDG------QTGILVKTKSVKELARSM---IALTEMDGFR 942
Cdd:cd03791  368 GADFFLMPSRFEPCGLVQMYAMRYGTLPIVRRTGGLADTVFDYdpetgeGTGFVFEDYDAEALLAALrraLALYRNPELW 447
                        170       180
                 ....*....|....*....|....*.
gi 818370584 943 ERISRNAYdwSRKYSWNVSARLFINI 968
Cdd:cd03791  448 RKLQKNAM--KQDFSWDKSAKEYLEL 471
PLN02949 PLN02949
transferase, transferring glycosyl groups
733-957 4.49e-09

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 60.14  E-value: 4.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 733 FSWLAM--FLESRVMKYVY----RSTKIVTVSES-SKADIagLGLSKIED-IEIVTPGINLRNFRKLKKYTFPTYSYL-- 802
Cdd:PLN02949 196 SFWLSTckILYYRAFAWMYglvgRCAHLAMVNSSwTKSHI--EALWRIPErIKRVYPPCDTSGLQALPLERSEDPPYIis 273
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 803 -GRLMPYKNIDILIKAFKEVLQS----VPDAKLIIAG--RGQYEEH----LNRLVHKLDIERFVEFKGYVSENEKREILG 871
Cdd:PLN02949 274 vAQFRPEKAHALQLEAFALALEKldadVPRPKLQFVGscRNKEDEErlqkLKDRAKELGLDGDVEFHKNVSYRDLVRLLG 353
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 872 RSWFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLR-DSVLD---GQTGILVKTksVKELARSMIALTEM-DGFRERIS 946
Cdd:PLN02949 354 GAVAGLHSMIDEHFGISVVEYMAAGAVPIAHNSAGPKmDIVLDedgQQTGFLATT--VEEYADAILEVLRMrETERLEIA 431
                        250
                 ....*....|.
gi 818370584 947 RNAYDWSRKYS 957
Cdd:PLN02949 432 AAARKRANRFS 442
CESA_like_1 cd06439
CESA_like_1 is a member of the cellulose synthase (CESA) superfamily; This is a subfamily of ...
146-379 6.39e-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: 57.98  E-value: 6.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 146 LPRYTILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLLE--EDDTKTINKAYDLNlpsyfRIEVVPNSLPKTKPKACN 223
Cdd:cd06439   28 LPTVTIIIPAYNEEAVIEAKLENLLALDYPRDRLEIIVVSDgsTDGTAEIAREYADK-----GVKLLRFPERRGKAAALN 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 224 YGLSKTTGEFVVVYDAED--KPDPLQLKKAYLAfsrlPENVSCLQSKLNYYNQnqnilTRLFTAEYSYW-FNIALTGLQT 300
Cdd:cd06439  103 RALALATGEIVVFTDANAllDPDALRLLVRHFA----DPSVGAVSGELVIVDG-----GGSGSGEGLYWkYENWLKRAES 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 301 -LNTIIPLGGTSNHFRTpvlKDLQGWDPFNVTEDCDLGTRLFKKGYRTsVIDSE--TLEEANSNIKSWLKQRSRWIKGYM 377
Cdd:cd06439  174 rLGSTVGANGAIYAIRR---ELFRPLPADTINDDFVLPLRIARQGYRV-VYEPDavAYEEVAEDGSEEFRRRVRIAAGNL 249

                 ..
gi 818370584 378 QT 379
Cdd:cd06439  250 QA 251
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
803-968 9.86e-09

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 58.95  E-value: 9.86e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 803 GRLMPYKNIDILIKAFKEVLQSvpDAKLIIAGRG--QYEEHLNRLVHKLDiERFVEFKGYvSENEKREILGRSWFLVQPS 880
Cdd:COG0297  302 SRLTEQKGLDLLLEALDELLEE--DVQLVVLGSGdpEYEEAFRELAARYP-GRVAVYIGY-DEALAHRIYAGADFFLMPS 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 881 SFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQ------TGILVKTKSVKELARSM---IALtemdgFR-----ERIS 946
Cdd:COG0297  378 RFEPCGLNQMYALRYGTVPIVRRTGGLADTVIDYNeatgegTGFVFDEYTAEALLAAIrraLAL-----YRdpeawRKLQ 452
                        170       180
                 ....*....|....*....|..
gi 818370584 947 RNAYdwSRKYSWNVSARLFINI 968
Cdd:COG0297  453 RNAM--KQDFSWEKSAKEYLEL 472
GT_2_like_e cd04192
Subfamily of Glycosyltransferase Family GT2 of unknown function; GT-2 includes diverse ...
151-375 9.91e-09

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: 56.91  E-value: 9.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 151 ILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLLE--EDDTKTINKAYdlNLPSYFRIEVVPNSLPKTKPK--ACNYGL 226
Cdd:cd04192    1 VVIAARNEAENLPRLLQSLSALDYPKEKFEVILVDDhsTDGTVQILEFA--AAKPNFQLKILNNSRVSISGKknALTTAI 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 227 SKTTGEFVVVYDAEDKPDPLQLKKAYLAFSrlpENVSCLQSKLNYYNQNQNILTRLFTAEysyWFNIALTGLQTLNTIIP 306
Cdd:cd04192   79 KAAKGDWIVTTDADCVVPSNWLLTFVAFIQ---KEQIGLVAGPVIYFKGKSLLAKFQRLD---WLSLLGLIAGSFGLGKP 152
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818370584 307 LGGTSNHF--RTPVLKDLQGWD--PFNVTEDCDLGTRLFKKGYRTSVI----DSETLEEANSNIKSWLKQRSRWIKG 375
Cdd:cd04192  153 FMCNGANMayRKEAFFEVGGFEgnDHIASGDDELLLAKVASKYPKVAYlknpEALVTTQPVTSWKELLNQRKRWASK 229
WcaA COG0463
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
147-367 1.58e-08

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


Pssm-ID: 440231 [Multi-domain]  Cd Length: 208  Bit Score: 55.86  E-value: 1.58e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 147 PRYTILCPLYKEWEVIEQFVRSIEIIDWPKdkLEVILLleeDD-----TKTINKAYDLNLPsyfRIEVVPNSLPKTKPKA 221
Cdd:COG0463    2 PLVSVVIPTYNEEEYLEEALESLLAQTYPD--FEIIVV---DDgstdgTAEILRELAAKDP---RIRVIRLERNRGKGAA 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 222 CNYGLSKTTGEFVVVYDAEDKPDPLQLKKAYLAFSRLPENVSClqskLNYYNQNQNILTRLFTAEYSYWFNIaltglqtL 301
Cdd:COG0463   74 RNAGLAAARGDYIAFLDADDQLDPEKLEELVAALEEGPADLVY----GSRLIREGESDLRRLGSRLFNLVRL-------L 142
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 818370584 302 NTIIPLGGTSNHFRTPVLKDLqGWDPfNVTEDCDLgTRLFKKGYRTSVIDSETLEEANS-NIKSWLK 367
Cdd:COG0463  143 TNLPDSTSGFRLFRREVLEEL-GFDE-GFLEDTEL-LRALRHGFRIAEVPVRYRAGESKlNLRDLLR 206
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
775-958 1.94e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 57.49  E-value: 1.94e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 775 DIEIVTPGINL----RNFRKLKKYTFPTYS------YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAG---------R 835
Cdd:PRK15484 162 DISIVPNGFCLetyqSNPQPNLRQQLNISPdetvllYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGdptasskgeK 241
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 836 GQYEEHLNRLVHKLDIErfVEFKGYVSENEKREILGRSWFLVQPSSF-EGWGMTVTESNAAGTPVIASNTAGLRDSVLDG 914
Cdd:PRK15484 242 AAYQKKVLEAAKRIGDR--CIMLGGQPPEKMHNYYPLADLVVVPSQVeEAFCMVAVEAMAAGKPVLASTKGGITEFVLEG 319
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 818370584 915 QTGILVKTKSVKELARSMIALTEMDGFRERISRNAYDWS-RKYSW 958
Cdd:PRK15484 320 ITGYHLAEPMTSDSIISDINRTLADPELTQIAEQAKDFVfSKYSW 364
PHA01633 PHA01633
putative glycosyl transferase group 1
744-929 4.97e-07

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 53.06  E-value: 4.97e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 744 VMKYVYRSTKIVTVSESSKADIAGLGLSKieDIEiVTPGINLRNFRKLKKYT----------FP---TYSYLGRLMPYKN 810
Cdd:PHA01633  86 VNKYLLQDVKFIPNSKFSAENLQEVGLQV--DLP-VFHGINFKIVENAEKLVpqlkqkldkdFPdtiKFGIVSGLTKRKN 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 811 IDILIKAFKEVLQSVPDakliIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREIL---GRSWFLVQPSSFEGWGM 887
Cdd:PHA01633 163 MDLMLQVFNELNTKYPD----IAKKIHFFVISHKQFTQLEVPANVHFVAEFGHNSREYIFafyGAMDFTIVPSGTEGFGM 238
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 818370584 888 TVTESNAAGTPVIASNTAGLrDSVLDGQTGILVKTKSVKELA 929
Cdd:PHA01633 239 PVLESMAMGTPVIHQLMPPL-DEFTSWQWNLLIKSSKVEEYY 279
Glyco_tranf_GTA_type cd00761
Glycosyltransferase family A (GT-A) includes diverse families of glycosyl transferases with a ...
151-264 5.74e-06

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: 47.50  E-value: 5.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 151 ILCPLYKEWEVIEQFVRSIEIIDWPKdkLEVILL--LEEDDTKTINKAYDLNlpsYFRIEVVPNSLPKTKPKACNYGLSK 228
Cdd:cd00761    1 VIIPAYNEEPYLERCLESLLAQTYPN--FEVIVVddGSTDGTLEILEEYAKK---DPRVIRVINEENQGLAAARNAGLKA 75
                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 818370584 229 TTGEFVVVYDAEDKPDPLQLKKAYLAFSRLPENVSC 264
Cdd:cd00761   76 ARGEYILFLDADDLLLPDWLERLVAELLADPEADAV 111
EpsO_like cd06438
EpsO protein participates in the methanolan synthesis; The Methylobacillus sp EpsO protein is ...
151-333 6.12e-06

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: 47.60  E-value: 6.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 151 ILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILLLEE--DDTKTINKAY--------DLNLpsyfrievvpnslpKTKPK 220
Cdd:cd06438    1 ILIPAHNEEAVIGNTVRSLKAQDYPRELYRIFVVADNctDDTAQVARAAgatvlerhDPER--------------RGKGY 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 221 ACNYGLSK-----TTGEFVVVYDAEDKPDPLQLKKayLAFsRLPENVSCLQSKLNYYNQNQNILTRLFTAEYSYwFNIAL 295
Cdd:cd06438   67 ALDFGFRHllnlaDDPDAVVVFDADNLVDPNALEE--LNA-RFAAGARVVQAYYNSKNPDDSWITRLYAFAFLV-FNRLR 142
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 818370584 296 T-GLQTLNTIIPLGGTSNHFRTPVLKDLqGWDPFNVTED 333
Cdd:cd06438  143 PlGRSNLGLSCQLGGTGMCFPWAVLRQA-PWAAHSLTED 180
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
691-955 6.76e-06

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 50.03  E-value: 6.76e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 691 FDLIVDCENGIPFFSPLYSTLPKILLIHHVHQQI--------FRENLPLPFSWLAMflesrvMKYVYRSTKIVTVSESSk 762
Cdd:PRK15179 401 PSVVHIWQDGSIFACALAALLAGVPRIVLSVRTMppvdrpdrYRVEYDIIYSELLK------MRGVALSSNSQFAAHRY- 473
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 763 ADIAGLGLSKIE-------DIEIV-TPGINLR--NFRKLKKYTFPTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLII 832
Cdd:PRK15179 474 ADWLGVDERRIPvvynglaPLKSVqDDACTAMmaQFDARTSDARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIM 553
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 833 AGRGQYEEHLNRLVHKLDIERFVEFKG-------YVSENEKREILGRswflvqpssFEGWGMTVTESNAAGTPVIASNTA 905
Cdd:PRK15179 554 VGGGPLLESVREFAQRLGMGERILFTGlsrrvgyWLTQFNAFLLLSR---------FEGLPNVLIEAQFSGVPVVTTLAG 624
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 818370584 906 GLRDSVLDGQTGILVKTKSVK--ELARSMIALTEMDGFRERISRNAYDWSRK 955
Cdd:PRK15179 625 GAGEAVQEGVTGLTLPADTVTapDVAEALARIHDMCAADPGIARKAADWASA 676
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
874-956 7.15e-06

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 45.29  E-value: 7.15e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584  874 WFLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTGILVktKSVKELARSMIALTEMDGFRERISRNAYDWS 953
Cdd:pfam13524   1 IVLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY--RDPEELAEKIRYLLEHPEERRAIAAAGRERV 78

                  ...
gi 818370584  954 RKY 956
Cdd:pfam13524  79 LAE 81
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
805-967 1.88e-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: 48.23  E-value: 1.88e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 805 LMPYKNIDILIKAFKEVLQSVPDAKL--IIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREilgrsWFL------ 876
Cdd:cd04946  233 IVPVKRIDLIIETLNSLCVAHPSICIswTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQ-----LYKendvdv 307
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 877 -VQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQTG-ILVKTKSVKELARSMIALTEMDGFRERISRNAYD-WS 953
Cdd:cd04946  308 fVNVSESEGIPVSIMEAISFGIPVIATNVGGTREIVENETNGlLLDKDPTPNEIVSSIMKFYLDGGDYKTMKISAREcWE 387
                        170
                 ....*....|....
gi 818370584 954 RKYSWNVSARLFIN 967
Cdd:cd04946  388 ERFNAEVNYSKFAN 401
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
801-906 4.84e-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: 46.85  E-value: 4.84e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 801 YLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSENEKREILGRSWFLVQPS 880
Cdd:cd03796  198 VISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTS 277
                         90       100
                 ....*....|....*....|....*.
gi 818370584 881 SFEGWGMTVTESNAAGTPVIASNTAG 906
Cdd:cd03796  278 LTEAFCIAIVEAASCGLLVVSTRVGG 303
Succinoglycan_BP_ExoA cd02525
ExoA is involved in the biosynthesis of succinoglycan; Succinoglycan Biosynthesis Protein ExoA ...
150-383 5.05e-05

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: 46.07  E-value: 5.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 150 TILCPLYKEWEVIEQFVRSIEIIDWPKDKLEVILL--LEEDDTKTINKAYdlnLPSYFRIEVVPNsLPKTKPKACNYGLS 227
Cdd:cd02525    3 SIIIPVRNEEKYIEELLESLLNQSYPKDLIEIIVVdgGSTDGTREIVQEY---AAKDPRIRLIDN-PKRIQSAGLNIGIR 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 228 KTTGEFVVVYDAEDKPDplqlkKAYLAfsrlpENVSCLQsKLNYYNQNQNILTRLFTAeysYWFNIALtglqTLNTIIPL 307
Cdd:cd02525   79 NSRGDIIIRVDAHAVYP-----KDYIL-----ELVEALK-RTGADNVGGPMETIGESK---FQKAIAV----AQSSPLGS 140
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 308 GG--------------TSNH--FRTPVLKDLQGWDP-FNVTEDCDLGTRLFKKGYRTSVIDSETLE-EANSNIKSWLKQR 369
Cdd:cd02525  141 GGsayrggavkigyvdTVHHgaYRREVFEKVGGFDEsLVRNEDAELNYRLRKAGYKIWLSPDIRVYyYPRSTLKKLARQY 220
                        250
                 ....*....|....
gi 818370584 370 SRWIKGYMQTYLVH 383
Cdd:cd02525  221 FRYGKWRARTLRKH 234
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
801-933 6.08e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 46.24  E-value: 6.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 801 YLGRLMPY--KNIDILIKAfkeVLQSVPDAKLIIAGRGQYEEHLNRLVHKLDIERFVEFKGYVSE--NEKREILGRSWFL 876
Cdd:PRK09922 185 YVGRLKFEgqKNVKELFDG---LSQTTGEWQLHIIGDGSDFEKCKAYSRELGIEQRIIWHGWQSQpwEVVQQKIKNVSAL 261
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 818370584 877 VQPSSFEGWGMTVTESNAAGTPVIASN-TAGLRDSVLDGQTGILVKTKSVKELARSMI 933
Cdd:PRK09922 262 LLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPGLNGELYTPGNIDEFVGKLN 319
glgA PRK00654
glycogen synthase GlgA;
797-963 5.70e-04

glycogen synthase GlgA;


Pssm-ID: 234809 [Multi-domain]  Cd Length: 466  Bit Score: 43.57  E-value: 5.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 797 PTYSYLGRLMPYKNIDILIKAFKEVLQSvpDAKLIIAGRG--QYEEHLNRLVHKLDiERFVEFKGYvSENEKREILGRSW 874
Cdd:PRK00654 283 PLFAMVSRLTEQKGLDLVLEALPELLEQ--GGQLVLLGTGdpELEEAFRALAARYP-GKVGVQIGY-DEALAHRIYAGAD 358
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 875 FLVQPSSFEGWGMTVTESNAAGTPVIASNTAGLRDSVLDGQ------TGILVKTKSVKELARSMI-ALtemDGFRE---- 943
Cdd:PRK00654 359 MFLMPSRFEPCGLTQLYALRYGTLPIVRRTGGLADTVIDYNpedgeaTGFVFDDFNAEDLLRALRrAL---ELYRQpplw 435
                        170       180
                 ....*....|....*....|.
gi 818370584 944 -RISRNAYdwSRKYSWNVSAR 963
Cdd:PRK00654 436 rALQRQAM--AQDFSWDKSAE 454
PelF NF038011
GT4 family glycosyltransferase PelF; Proteins of this family are components of the ...
782-902 7.71e-04

GT4 family glycosyltransferase PelF; Proteins of this family are components of the exopolysaccharide Pel transporter. It has been reported that PelF is a soluble glycosyltransferase that uses UDP-glucose as the substrate for the synthesis of exopolysaccharide Pel, whereas PelG is a Wzx-like and PST family exopolysaccharide transporter.


Pssm-ID: 411604 [Multi-domain]  Cd Length: 489  Bit Score: 43.38  E-value: 7.71e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 782 GINLRNFRKLKKY----TFPTYSYLGRLMPYKNIDILIKAFKEVLQSVPDAKLIIAG----RGQYEEHLNRLVHKLDIER 853
Cdd:NF038011 288 GIDLPRLAPLRAQrpagIPPVVGLIGRVVPIKDIKTFIRAMRTVVRAMPEAEGWIVGpeeeDPAYAAECRSLVASLGLQD 367
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 818370584 854 FVEFKGYvseNEKREILGRSWFLVQPSSFEGWGMTVTESNAAGTPVIAS 902
Cdd:NF038011 368 KVKFLGF---QKIDDLLPQVGLMVLSSISEALPLVVLEAFAAGVPVVTT 413
GT2_HAS cd06434
Hyaluronan synthases catalyze polymerization of hyaluronan; Hyaluronan synthases (HASs) are ...
150-376 2.06e-03

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: 41.09  E-value: 2.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 150 TILCPLYKEweVIEQFVRSIE-IIDwpKDKLEVILLLEEDDTKTINKAYDLNLPSYFRIEVVPNSlpkTKPKACNYGLSK 228
Cdd:cd06434    3 TVIIPVYDE--DPDVFRECLRsILR--QKPLEIIVVTDGDDEPYLSILSQTVKYGGIFVITVPHP---GKRRALAEGIRH 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 229 TTGEFVVVYDAEDKPDPLQLKKAYLAFSRlpENVSCLQSKLNYYNQNQNILTRLFTAEYSYWFNIALTGLQTLNTIIPLG 308
Cdd:cd06434   76 VTTDIVVLLDSDTVWPPNALPEMLKPFED--PKVGGVGTNQRILRPRDSKWSFLAAEYLERRNEEIRAAMSYDGGVPCLS 153
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 818370584 309 GTSNHFRTPVLKD-----------LQGWdPFNVTEDCDLGTRLFKKGYRTSV-IDSETLEEANSNIKSWLKQRSRWIKGY 376
Cdd:cd06434  154 GRTAAYRTEILKDflfleeftnetFMGR-RLNAGDDRFLTRYVLSHGYKTVYqYTSEAYTETPENYKKFLKQQLRWSRSN 232
 
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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