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Conserved domains on  [gi|15218994|ref|NP_175651|]
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UDP-Glycosyltransferase superfamily protein [Arabidopsis thaliana]

Protein Classification

glycosyltransferase( domain architecture ID 13876812)

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

EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  16037492|12691742|10521532
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glyco_trans_4_5 pfam16994
Glycosyl-transferase family 4;
232-402 1.48e-95

Glycosyl-transferase family 4;


:

Pssm-ID: 465332  Cd Length: 172  Bit Score: 291.72  E-value: 1.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   232 WSRRFVLLFHELSMTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKTAMKADLIIAGSA 311
Cdd:pfam16994   1 KSKRVVLISHELSMTGAPLALMELATELRSCGATVVVVVLSKGGGLEQELLRRGIKVLPDKGRLSFRTALKADLVIANTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   312 VCTSWIDQYMNHHPAG-GSQIAWWIMENRREYFDRAKPVLDRVKMLIFLSESQSRQWLTWCEEEHIKLRSQPVIVPLSVN 390
Cdd:pfam16994  81 VCASWIDQYLKEHVAGvLPKVLWWIHENRRHYFDRAKSMLDYVKHLPFLSHSQAEQWLTWTEEELIILMPQTYVVHLSNN 160

                         170
                  ....*....|..
gi 15218994   391 DELAFVAGIPSS 402
Cdd:pfam16994 161 DELYFVAEISVS 172
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 235-664 6.57e-36

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: 138.82  E-value: 6.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 235 RFVLLFHELS--MTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKT------------A 300
Cdd:cd03801   1 KILLLSPELPppVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRArrllrelrpllrL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 301 MKADLIIAGSAVCTSWIDQYMN----------HHPAGGSQIAWWIMENRreYFDRAKPVLDRVKMLIFLSESQSRqwltW 370
Cdd:cd03801  81 RKFDVVHAHGLLAALLAALLALllgaplvvtlHGAEPGRLLLLLAAERR--LLARAEALLRRADAVIAVSEALRD----E 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 371 CEEEHIKLRSQPVIVPLSVNDELafvagipsslntptlspekmrvkrqiLRESVRTELGITDSDMLVMSLSSINPTKGQL 450
Cdd:cd03801 155 LRALGGIPPEKIVVIPNGVDLER--------------------------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVD 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 451 LLLESIALalsergqesqrnhkgiirkekvslsskhrlrgssrqmksvsltldngLRREKQELKVLLgsVGSKSNKVGYV 530
Cdd:cd03801 209 LLLEALAK-----------------------------------------------LLRRGPDVRLVI--VGGDGPLRAEL 239

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 531 KEMlsflsnSGNLSKSVMWTPA--TTRVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMT 608
Cdd:cd03801 240 EEL------ELGLGDRVRFLGFvpDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG 311

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218994 609 GLLHSMGRSgnKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYKRFVDVL 664
Cdd:cd03801 312 GLVVPPDDV--EALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
 
Name Accession Description Interval E-value
Glyco_trans_4_5 pfam16994
Glycosyl-transferase family 4;
232-402 1.48e-95

Glycosyl-transferase family 4;


Pssm-ID: 465332  Cd Length: 172  Bit Score: 291.72  E-value: 1.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   232 WSRRFVLLFHELSMTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKTAMKADLIIAGSA 311
Cdd:pfam16994   1 KSKRVVLISHELSMTGAPLALMELATELRSCGATVVVVVLSKGGGLEQELLRRGIKVLPDKGRLSFRTALKADLVIANTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   312 VCTSWIDQYMNHHPAG-GSQIAWWIMENRREYFDRAKPVLDRVKMLIFLSESQSRQWLTWCEEEHIKLRSQPVIVPLSVN 390
Cdd:pfam16994  81 VCASWIDQYLKEHVAGvLPKVLWWIHENRRHYFDRAKSMLDYVKHLPFLSHSQAEQWLTWTEEELIILMPQTYVVHLSNN 160

                         170
                  ....*....|..
gi 15218994   391 DELAFVAGIPSS 402
Cdd:pfam16994 161 DELYFVAEISVS 172
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 235-664 6.57e-36

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: 138.82  E-value: 6.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 235 RFVLLFHELS--MTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKT------------A 300
Cdd:cd03801   1 KILLLSPELPppVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRArrllrelrpllrL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 301 MKADLIIAGSAVCTSWIDQYMN----------HHPAGGSQIAWWIMENRreYFDRAKPVLDRVKMLIFLSESQSRqwltW 370
Cdd:cd03801  81 RKFDVVHAHGLLAALLAALLALllgaplvvtlHGAEPGRLLLLLAAERR--LLARAEALLRRADAVIAVSEALRD----E 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 371 CEEEHIKLRSQPVIVPLSVNDELafvagipsslntptlspekmrvkrqiLRESVRTELGITDSDMLVMSLSSINPTKGQL 450
Cdd:cd03801 155 LRALGGIPPEKIVVIPNGVDLER--------------------------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVD 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 451 LLLESIALalsergqesqrnhkgiirkekvslsskhrlrgssrqmksvsltldngLRREKQELKVLLgsVGSKSNKVGYV 530
Cdd:cd03801 209 LLLEALAK-----------------------------------------------LLRRGPDVRLVI--VGGDGPLRAEL 239

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 531 KEMlsflsnSGNLSKSVMWTPA--TTRVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMT 608
Cdd:cd03801 240 EEL------ELGLGDRVRFLGFvpDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG 311

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218994 609 GLLHSMGRSgnKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYKRFVDVL 664
Cdd:cd03801 312 GLVVPPDDV--EALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 556-664 1.80e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.43  E-value: 1.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 556 VASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNPDE 635
Cdd:COG0438  14 LEALLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDP--EALAEAILRLLEDPEL 89

                        90       100
                ....*....|....*....|....*....
gi 15218994 636 RLRLGSEGRKMVEKMYMKQHMYKRFVDVL 664
Cdd:COG0438  90 RRRLGEAARERAEERFSWEAIAERLLALY 118
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 477-646 1.77e-18

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: 82.71  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   477 KEKVSLSSkHRLRGssrqMKSVSLTLDN--GLRREKQELKVLLgsVGSKSNKvgyvkEMLSFLSNSGNLSKSVMWTPATT 554
Cdd:pfam00534   1 KKKIILFV-GRLEP----EKGLDLLIKAfaLLKEKNPNLKLVI--AGDGEEE-----KRLKKLAEKLGLGDNVIFLGFVS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   555 R--VASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLhsmGRSGN-KELAHNLLYLLR 631
Cdd:pfam00534  69 DedLPELLKIADVFVLPSRY--EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFL---VKPNNaEALAEAIDKLLE 143

                         170
                  ....*....|....*
gi 15218994   632 NPDERLRLGSEGRKM 646
Cdd:pfam00534 144 DEELRERLGENARKR 158
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 557-649 1.77e-09

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 60.49  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994  557 ASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAGGTKEMV---QHNMTGLLHSmgrSGNKELAHNLL-YLLRN 632
Cdd:PLN02871 326 SQAYASGDVFVMPSES--ETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYT---PGDVDDCVEKLeTLLAD 400

                         90
                 ....*....|....*..
gi 15218994  633 PDERLRLGSEGRKMVEK 649
Cdd:PLN02871 401 PELRERMGAAAREEVEK 417
 
Name Accession Description Interval E-value
Glyco_trans_4_5 pfam16994
Glycosyl-transferase family 4;
232-402 1.48e-95

Glycosyl-transferase family 4;


Pssm-ID: 465332  Cd Length: 172  Bit Score: 291.72  E-value: 1.48e-95
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   232 WSRRFVLLFHELSMTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKTAMKADLIIAGSA 311
Cdd:pfam16994   1 KSKRVVLISHELSMTGAPLALMELATELRSCGATVVVVVLSKGGGLEQELLRRGIKVLPDKGRLSFRTALKADLVIANTA 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   312 VCTSWIDQYMNHHPAG-GSQIAWWIMENRREYFDRAKPVLDRVKMLIFLSESQSRQWLTWCEEEHIKLRSQPVIVPLSVN 390
Cdd:pfam16994  81 VCASWIDQYLKEHVAGvLPKVLWWIHENRRHYFDRAKSMLDYVKHLPFLSHSQAEQWLTWTEEELIILMPQTYVVHLSNN 160

                         170
                  ....*....|..
gi 15218994   391 DELAFVAGIPSS 402
Cdd:pfam16994 161 DELYFVAEISVS 172
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 235-664 6.57e-36

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: 138.82  E-value: 6.57e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 235 RFVLLFHELS--MTGAPISMMELASELLSCGATVSAVVLSRRGGLMQELSRRRIKVVEDKGELSFKT------------A 300
Cdd:cd03801   1 KILLLSPELPppVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRArrllrelrpllrL 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 301 MKADLIIAGSAVCTSWIDQYMN----------HHPAGGSQIAWWIMENRreYFDRAKPVLDRVKMLIFLSESQSRqwltW 370
Cdd:cd03801  81 RKFDVVHAHGLLAALLAALLALllgaplvvtlHGAEPGRLLLLLAAERR--LLARAEALLRRADAVIAVSEALRD----E 154

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 371 CEEEHIKLRSQPVIVPLSVNDELafvagipsslntptlspekmrvkrqiLRESVRTELGITDSDMLVMSLSSINPTKGQL 450
Cdd:cd03801 155 LRALGGIPPEKIVVIPNGVDLER--------------------------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVD 208

                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 451 LLLESIALalsergqesqrnhkgiirkekvslsskhrlrgssrqmksvsltldngLRREKQELKVLLgsVGSKSNKVGYV 530
Cdd:cd03801 209 LLLEALAK-----------------------------------------------LLRRGPDVRLVI--VGGDGPLRAEL 239

                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 531 KEMlsflsnSGNLSKSVMWTPA--TTRVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMT 608
Cdd:cd03801 240 EEL------ELGLGDRVRFLGFvpDEELPALYAAADVFVLPS--RYEGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEG 311

                       410       420       430       440       450
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 15218994 609 GLLHSMGRSgnKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYKRFVDVL 664
Cdd:cd03801 312 GLVVPPDDV--EALADALLRLLADPELRARLGRAARERVAERFSWERVAERLLDLY 365
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 556-664 1.80e-21

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 90.43  E-value: 1.80e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 556 VASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNPDE 635
Cdd:COG0438  14 LEALLAAADVFVLPS--RSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDP--EALAEAILRLLEDPEL 89

                        90       100
                ....*....|....*....|....*....
gi 15218994 636 RLRLGSEGRKMVEKMYMKQHMYKRFVDVL 664
Cdd:COG0438  90 RRRLGEAARERAEERFSWEAIAERLLALY 118
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 477-646 1.77e-18

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: 82.71  E-value: 1.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   477 KEKVSLSSkHRLRGssrqMKSVSLTLDN--GLRREKQELKVLLgsVGSKSNKvgyvkEMLSFLSNSGNLSKSVMWTPATT 554
Cdd:pfam00534   1 KKKIILFV-GRLEP----EKGLDLLIKAfaLLKEKNPNLKLVI--AGDGEEE-----KRLKKLAEKLGLGDNVIFLGFVS 68

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   555 R--VASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLhsmGRSGN-KELAHNLLYLLR 631
Cdd:pfam00534  69 DedLPELLKIADVFVLPSRY--EGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFL---VKPNNaEALAEAIDKLLE 143

                         170
                  ....*....|....*
gi 15218994   632 NPDERLRLGSEGRKM 646
Cdd:pfam00534 144 DEELRERLGENARKR 158
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 539-659 2.80e-18

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: 86.88  E-value: 2.80e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 539 NSGNLSKSVMWTPATTRVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSg 618
Cdd:cd03808 240 EKLGLEGRIEFLGFRSDVPELLAESDVFVLPS--YREGLPRSLLEAMAAGRPVITTDVPGCRELVIDGVNGFLVPPGDV- 316

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 15218994 619 nKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYKR 659
Cdd:cd03808 317 -EALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNK 356
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 549-663 4.95e-18

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: 86.23  E-value: 4.95e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 549 WTPATTRVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSGnkELAHNLLY 628
Cdd:cd03825 250 YIDDDEQLVDIYSAADLFVHPS--LADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQ--ALAEAIEW 325

                        90       100       110
                ....*....|....*....|....*....|....*
gi 15218994 629 LLRNPDERLRLGSEGRKMVEKMYMKQHMYKRFVDV 663
Cdd:cd03825 326 LLANPKERESLGERARALAENHFDQRVQAQRYLEL 360
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
506-632 4.32e-16

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 75.24  E-value: 4.32e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   506 LRREKQELKVLLgsVGSKSNKvgYVKEMLSflsnsgNLSKSVMWTPATTRVASLYSAADVYVTNSqgVGETFGRVTIEAM 585
Cdd:pfam13692  27 LRKRDNDVRLVI--VGDGPEE--ELEELAA------GLEDRVIFTGFVEDLAELLAAADVFVLPS--LYEGFGLKLLEAM 94

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 15218994   586 AYGLAVVGTDAGGTKEMVqHNMTGLLHSMGRSgnKELAHNLLYLLRN 632
Cdd:pfam13692  95 AAGLPVVATDVGGIPELV-DGENGLLVPPGDP--EALAEAILRLLED 138
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 531-662 1.70e-15

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


Pssm-ID: 340847 [Multi-domain]  Cd Length: 351  Bit Score: 78.43  E-value: 1.70e-15
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 531 KEMLSFLSNSGNLSKSVMWTPATTRVASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDA-GGTKEMVQHNMTG 609
Cdd:cd03820 224 REELEKLIDKLGLEDRVKLLGPTKNIAEEYANSSIFVLSSRY--EGFPMVLLEAMAYGLPIISFDCpTGPSEIIEDGENG 301

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....
gi 15218994 610 LLHsmgRSGNK-ELAHNLLYLLRNPDERLRLGSEGRKMVEKmYMKQHMYKRFVD 662
Cdd:cd03820 302 LLV---PNGDVdALAEALLRLMEDEELRKKMGKNARKNAER-FSIEKIIKQWEE 351
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 556-650 2.26e-14

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: 75.02  E-value: 2.26e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 556 VASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNPDE 635
Cdd:cd03814 261 LARAYASADVFVFPS--RTETFGLVVLEAMASGLPVVAADAGGPRDIVRPGGTGALVEPGDA--AAFAAALRALLEDPEL 336

                        90
                ....*....|....*
gi 15218994 636 RLRLGSEGRKMVEKM 650
Cdd:cd03814 337 RRRMAARARAEAERY 351
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 554-651 1.24e-12

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: 69.69  E-value: 1.24e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 554 TRVASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNP 633
Cdd:cd04962 261 DDVEELLSIADLFLLPSEK--ESFGLAALEAMACGVPVVSSNAGGIPEVVKHGETGFLSDVGDV--DAMAKSALSILEDD 336

                        90
                ....*....|....*...
gi 15218994 634 DERLRLGSEGRKMVEKMY 651
Cdd:cd04962 337 ELYNRMGRAARKRAAERF 354
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 556-663 5.19e-12

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: 68.18  E-value: 5.19e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 556 VASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNPDE 635
Cdd:cd03798 270 VPAYYRACDVFVLPS--RHEGFGLVLLEAMACGLPVVATDVGGIPEVVGDPETGLLVPPGDA--DALAAALRRALAEPYL 345

                        90       100       110
                ....*....|....*....|....*....|..
gi 15218994 636 RlRLGSEGRKMVEKMY----MKQHMYKRFVDV 663
Cdd:cd03798 346 R-ELGEAARARVAERFswvkAADRIAAAYRDV 376
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 555-651 1.18e-11

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: 66.88  E-value: 1.18e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 555 RVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLL---HSMgrsgnKELAHNLLYLLR 631
Cdd:cd03800 295 DLPELYRAADVFVVPS--LYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLvdpHDP-----EALAAALRRLLD 367

                        90       100
                ....*....|....*....|
gi 15218994 632 NPDERLRLGSEGRKMVEKMY 651
Cdd:cd03800 368 DPALWQRLSRAGLERARAHY 387
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 531-642 4.39e-11

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: 65.07  E-value: 4.39e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 531 KEMLSFLSNSGNLSKSVMWTPATTRVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGL 610
Cdd:cd03811 231 REELEKLAKELGLAERVIFLGFQSNPYPYLKKADLFVLSS--RYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGL 308

                        90       100       110
                ....*....|....*....|....*....|..
gi 15218994 611 LHsmgRSGNKELAHNLLYLLRNPDERLRLGSE 642
Cdd:cd03811 309 LV---PDGDAAALAGILAALLQKKLDAALRER 337
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 555-653 6.87e-11

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: 64.61  E-value: 6.87e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 555 RVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHsmgRSGNKELAHNLLYLLRNPD 634
Cdd:cd03817 269 ELPEYYKAADLFVFAS--TTETQGLVYLEAMAAGLPVVAAKDPAASELVEDGENGFLF---EPNDETLAEKLLHLRENLE 343

                        90       100
                ....*....|....*....|....*...
gi 15218994 635 ERLRLGSEGR---------KMVEKMYMK 653
Cdd:cd03817 344 LLRKLSKNAEisarefafaKSVEKLYEE 371
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 556-656 1.20e-10

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: 63.45  E-value: 1.20e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 556 VASLYSAADVYVTNSQGVGETFGRVTIEAMAYGLAVVGTD-AGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNPD 634
Cdd:cd03795 255 KVIYLHLCDVFVFPSVLRSEAFGIVLLEAMMCGKPVISTNiGTGVPYVNNNGETGLVVPPKDP--DALAEAIDKLLSDEE 332

                        90       100
                ....*....|....*....|..
gi 15218994 635 ERLRLGSEGRKMVEKMYMKQHM 656
Cdd:cd03795 333 LRESYGENAKKRFEELFTAEKM 354
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 555-651 1.27e-10

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: 63.53  E-value: 1.27e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 555 RVASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSmgRSGNKELAHNLLYLLRNPD 634
Cdd:cd03819 248 DVPAALAASDVVVLPS--LHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLLVP--PGDAEALADAIRAAKLLPE 323

                        90
                ....*....|....*..
gi 15218994 635 ERLRLgsEGRKMVEKMY 651
Cdd:cd03819 324 AREKL--QAAAALTEAV 338
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 506-660 1.91e-10

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: 63.51  E-value: 1.91e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 506 LRREKQELKVLLgsVGSKSNKVGYVKEMLSfLSNSGNLSKSVMWTpATTRVASLYSAADVYVTNSqgVGETFGRVTIEAM 585
Cdd:cd03813 318 VRRAMPDAEGWL--IGPEDEDPEYAQECKR-LVASLGLENKVKFL-GFQNIKEYYPKLGLLVLTS--ISEGQPLVILEAM 391

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 586 AYGLAVVGTDAGGTKEMVQhnmtGLLHSMGRSG-------NKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYK 658
Cdd:cd03813 392 ASGVPVVATDVGSCRELIY----GADDALGQAGlvvppadPEALAEALIKLLRDPELRQAFGEAGRKRVEKYYTLEGMID 467


                ..
gi 15218994 659 RF 660
Cdd:cd03813 468 SY 469
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 506-612 2.75e-10

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: 60.88  E-value: 2.75e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 506 LRREKQELKVLLGSVGSKSNKVGYVKEMLSFLSNSGNLSksvmWTPATTRVASLYSAADVYVTNSQGvgETFGRVTIEAM 585
Cdd:cd01635 135 LKARLPDLVLVLVGGGGEREEEEALAAALGLLERVVIIG----GLVDDEVLELLLAAADVFVLPSRS--EGFGLVLLEAM 208

                        90       100
                ....*....|....*....|....*..
gi 15218994 586 AYGLAVVGTDAGGTKEMVQHNMTGLLH 612
Cdd:cd01635 209 AAGKPVIATDVGGIPEFVVDGENGLLV 235
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 575-660 7.59e-10

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: 61.45  E-value: 7.59e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 575 ETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLhsmgRSGN-KELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMK 653
Cdd:cd03805 310 EHFGIVPLEAMYAGKPVIACNSGGPLETVVEGVTGFL----CEPTpEAFAEAMLKLANDPDLADRMGAAGRKRVKEKFSR 385


                ....*..
gi 15218994 654 QHMYKRF 660
Cdd:cd03805 386 EAFAERL 392
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 555-661 8.79e-10

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: 61.20  E-value: 8.79e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 555 RVASLYSAADV-YVTNSQGVgETFGRV---TIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHsmgRSGN-KELAHNLLYL 629
Cdd:cd03794 284 EVPELLSAADVgLVPLKDNP-ANRGSSpskLFEYMAAGKPILASDDGGSDLAVEINGCGLVV---EPGDpEALADAILEL 359

                        90       100       110
                ....*....|....*....|....*....|..
gi 15218994 630 LRNPDERLRLGSEGRKMVEKMYMKQHMYKRFV 661
Cdd:cd03794 360 LDDPELRRAMGENGRELAEEKFSREKLADRLL 391
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 557-649 1.77e-09

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 60.49  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994  557 ASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAGGTKEMV---QHNMTGLLHSmgrSGNKELAHNLL-YLLRN 632
Cdd:PLN02871 326 SQAYASGDVFVMPSES--ETLGFVVLEAMASGVPVVAARAGGIPDIIppdQEGKTGFLYT---PGDVDDCVEKLeTLLAD 400

                         90
                 ....*....|....*..
gi 15218994  633 PDERLRLGSEGRKMVEK 649
Cdd:PLN02871 401 PELRERMGAAAREEVEK 417
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 555-660 3.10e-09

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: 59.26  E-value: 3.10e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 555 RVASLYSAADVYVTNSQGvGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSmgRSGNKELAHNLLYLLRNPD 634
Cdd:cd03823 253 DIKDFYEKIDVLVVPSIW-PEPFGLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFA--PGDAEDLAAAMRRLLTDPA 329

                        90       100
                ....*....|....*....|....*.
gi 15218994 635 ERLRLGSEGRKMVEKMYMKQHMYKRF 660
Cdd:cd03823 330 LLERLRAGAEPPRSTESQAEEYLKLY 355
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 556-662 3.20e-09

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: 59.25  E-value: 3.20e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 556 VASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQhNMTGLLHSMGRSGNkeLAHNLLYLLRNPDE 635
Cdd:cd03807 258 VPALLPAMDIFVLSS--RTEGFPNALLEAMACGLPVVATDVGGAAELVD-DGTGFLVPAGDPQA--LADAIRALLEDPEK 332

                        90       100
                ....*....|....*....|....*..
gi 15218994 636 RLRLGSEGRKMVEKMYMKQHMYKRFVD 662
Cdd:cd03807 333 RARLGRAARERIANEFSIDAMVRRYET 359
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 542-666 1.85e-08

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: 56.68  E-value: 1.85e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 542 NLSKSVMWTPATTRVASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHnmtgllhsmgrsgnke 621
Cdd:cd04951 242 NLVDRVILLGQISNISEYYNAADLFVLSSEW--EGFGLVVAEAMACERPVVATDAGGVAEVVGD---------------- 303

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 15218994 622 laHNLLYLLRNP-------DERLRLGSEGRKMVEKmyMKQHMYKRF-VDVLVK 666
Cdd:cd04951 304 --HNYVVPVSDPqllaekiKEIFDMSDEERDILGN--KNEYIAKNFsINTIVN 352
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 539-651 2.68e-08

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: 56.30  E-value: 2.68e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 539 NSGNLSKSVMWTPaTTRVASLYSAADVY----VTNSQGVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSM 614
Cdd:cd03799 228 NIGDCVKLLGWKP-QEEIIEILDEADIFiapsVTAADGDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPE 306

                        90       100       110
                ....*....|....*....|....*....|....*..
gi 15218994 615 GRSgnKELAHNLLYLLRNPDERLRLGSEGRKMVEKMY 651
Cdd:cd03799 307 RDA--EAIAEKLTYLIEHPAIWPEMGKAGRARVEEEY 341
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 559-647 5.11e-08

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: 55.40  E-value: 5.11e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 559 LYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRsgnkELAHNLLYLLRNPDERLR 638
Cdd:cd03792 276 LQRAATVVLQLS--TREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVE----GAAVRILRLLTDPELRRK 349


                ....*....
gi 15218994 639 LGSEGRKMV 647
Cdd:cd03792 350 MGLAAREHV 358
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
394-664 2.51e-07

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 53.26  E-value: 2.51e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994  394 AFVAGIPSSLNTPTLSPEKMRVKRQilresvrtELGITDSDMLVMSLSSINPTKGQLLLLESIalalsergqesqrnhkg 473
Cdd:PRK15484 161 ADISIVPNGFCLETYQSNPQPNLRQ--------QLNISPDETVLLYAGRISPDKGILLLMQAF----------------- 215

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994  474 iirkekvslsskhrlrgssrqmksvsltldNGLRREKQELK-VLLGS--VGSKSNKVGYVKEMLSFLSNSGnlSKSVMW- 549
Cdd:PRK15484 216 ------------------------------EKLATAHSNLKlVVVGDptASSKGEKAAYQKKVLEAAKRIG--DRCIMLg 263

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994  550 TPATTRVASLYSAADVYVTNSQgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGlLHSMGRSGNKELAHNLLYL 629
Cdd:PRK15484 264 GQPPEKMHNYYPLADLVVVPSQ-VEEAFCMVAVEAMAAGKPVLASTKGGITEFVLEGITG-YHLAEPMTSDSIISDINRT 341

                        250       260       270
                 ....*....|....*....|....*....|....*
gi 15218994  630 LRNPDeRLRLGSEGRKMVEKMYMKQHMYKRFVDVL 664
Cdd:PRK15484 342 LADPE-LTQIAEQAKDFVFSKYSWEGVTQRFEEQI 375
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 549-651 1.15e-06

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: 51.30  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 549 WTPATtRVASLYSAADVY----VTNSQGVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAH 624
Cdd:cd05844 250 ALPHA-EVQDWMRRAEIFclpsVTAASGDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDV--DALAD 326

                        90       100
                ....*....|....*....|....*..
gi 15218994 625 NLLYLLRNPDERLRLGSEGRKMVEKMY 651
Cdd:cd05844 327 ALQALLADRALADRMGGAARAFVCEQF 353
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 542-659 7.96e-06

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: 48.45  E-value: 7.96e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 542 NLSKSVMWTPATTRVASLYSAADVYVTNSQGvgETFGRVTIEAMAYGLAVVGTDAG-GTKEMVQHNMTGLLHSmgrSGNK 620
Cdd:cd04949 214 HLEDNVFLKGYHSNLDQEYQDAYLSLLTSQM--EGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYLIE---KNNI 288

                        90       100       110       120
                ....*....|....*....|....*....|....*....|
gi 15218994 621 E-LAHNLLYLLRNPDERLRLGSEGRKMVEKmYMKQHMYKR 659
Cdd:cd04949 289 DaLADKIIELLNDPEKLQQFSEESYKIAEK-YSTENVMEK 327
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
 583-651 3.30e-05

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: 46.59  E-value: 3.30e-05
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218994 583 EAMAYGLAVVGTDAGGTKEMVQHNMTGLLHSMGRSgnKELAHNLLYLLRNPDERLRLGSEGRKMVEKMY 651
Cdd:cd03818 319 EAMACGCPVIGSDTAPVREVIRDGRNGLLVDFFDP--DALAAAVLELLEDPDRAAALRRAARRTVERSD 385
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 557-647 4.63e-05

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: 46.21  E-value: 4.63e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 557 ASLYSAADVYVTNSqgVGETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLlhsmGRSGNKELAHNLLYLLRNPDER 636
Cdd:cd03821 276 WALYASADLFVLPS--YSENFGNVVAEALACGLPVVITDKCGLSELVEAGCGVV----VDPNVSSLAEALAEALRDPADR 349

                        90
                ....*....|.
gi 15218994 637 LRLGSEGRKMV 647
Cdd:cd03821 350 KRLGEMARRAR 360
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 575-611 1.32e-04

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: 44.59  E-value: 1.32e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15218994 575 ETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLL 611
Cdd:cd03802 251 EPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFL 287
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 509-661 1.95e-04

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: 44.37  E-value: 1.95e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 509 EKQELKVLlgsVGSKSNKVGYvkEMLSFLSNSGnlsksvmwtpattrVASLY--SAADVYV--TNSQGVgetfgRVTI-E 583
Cdd:cd04946 268 LKERLEKL---AENKLENVKV--NFTGEVSNKE--------------VKQLYkeNDVDVFVnvSESEGI-----PVSImE 323

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 15218994 584 AMAYGLAVVGTDAGGTKEMVQHNMTGLLHSmGRSGNKELAHNLLYLLRNPDERLRLGSEGRKMVEKMYMKQHMYKRFV 661
Cdd:cd04946 324 AISFGIPVIATNVGGTREIVENETNGLLLD-KDPTPNEIVSSIMKFYLDGGDYKTMKISARECWEERFNAEVNYSKFA 400
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 506-645 3.96e-04

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: 43.12  E-value: 3.96e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994 506 LRREKQELKVLLgsVGSKSNKVGYVKEMLsflsNSGNLSKSVMWT--PATTRVASLYSAADVYVTNSqgVGETFGRVTIE 583
Cdd:cd03809 217 LKKQGGDLKLVI--VGGKGWEDEELLDLV----KKLGLGGRVRFLgyVSDEDLPALYRGARAFVFPS--LYEGFGLPVLE 288

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 15218994 584 AMAYGLAVVGTDAGGTKEMVqhnmtgllhsmGRSGN-------KELAHNLLYLLRNPDERLRLGSEGRK 645
Cdd:cd03809 289 AMACGTPVIASNISVLPEVA-----------GDAALyfdpldpESIADAILRLLEDPSLREELIRKGLE 346
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
575-662 1.82e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 37.97  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15218994   575 ETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLLHsmgRSGnKELAHNLLYLLRNPDERLRLGSEGRKMVekmyMKQ 654
Cdd:pfam13524  10 DSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLY---RDP-EELAEKIRYLLEHPEERRAIAAAGRERV----LAE 81


                  ....*...
gi 15218994   655 HMYKRFVD 662
Cdd:pfam13524  82 HTYAHRAE 89
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 575-611 2.06e-03

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: 40.73  E-value: 2.06e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 15218994 575 ETFGRVTIEAMAYGLAVVGTDAGGTKEMVQHNMTGLL 611
Cdd:cd03804 275 EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGIL 311
 
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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