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Conserved domains on  [gi|1275110346|gb|ATS86195|]
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GDP-mannose:cellobiosyl-diphosphopolyprenol alpha-mannosyltransferase [Xanthomonas citri pv. phaseoli var. fuscans]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

glycosyltransferase family 4 (GT4) protein catalyzes the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
SCOP:  3001586

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-367 6.80e-53

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: 179.66  E-value: 6.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHPSIGGMEEVVLNVARQHQATSADtVEVVTLDRVFTDPGAQLAAqdthqglsIRRIGYRGSSRYPLAPSVL 81
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHD-VTVLTPADPGEPPEELEDG--------VIVPLLPSLAALLRARRLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  82 GAIR------SADVVHLHGIDFFYdYLALTKPLHGKPMVVSTHGGFFHTAYASRMKQLWFqtLTRTSAL--AYARVIATS 153
Cdd:cd03801    72 RELRpllrlrKFDVVHAHGLLAAL-LAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL--LARAEALlrRADAVIAVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 154 ENDGDLFAK--VVAPARLRVIENGVDVEKYAGRGATTPG-----RTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLII 226
Cdd:cd03801   149 EALRDELRAlgGIPPEKIVVIPNGVDLERFSPPLRRKLGippdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 227 AGREydlneADLRKAIAER--GLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFV 304
Cdd:cd03801   229 VGGD-----GPLRAELEELelGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275110346 305 RLASESGQGVIVNRDRIEAAADQVQALAlqsdSDFDTRR----SASMAYVSRYDWKHVVGRYVDEYH 367
Cdd:cd03801   304 EVVEDGEGGLVVPPDDVEALADALLRLL----ADPELRArlgrAARERVAERFSWERVAERLLDLYR 366
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-367 6.80e-53

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: 179.66  E-value: 6.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHPSIGGMEEVVLNVARQHQATSADtVEVVTLDRVFTDPGAQLAAqdthqglsIRRIGYRGSSRYPLAPSVL 81
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHD-VTVLTPADPGEPPEELEDG--------VIVPLLPSLAALLRARRLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  82 GAIR------SADVVHLHGIDFFYdYLALTKPLHGKPMVVSTHGGFFHTAYASRMKQLWFqtLTRTSAL--AYARVIATS 153
Cdd:cd03801    72 RELRpllrlrKFDVVHAHGLLAAL-LAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL--LARAEALlrRADAVIAVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 154 ENDGDLFAK--VVAPARLRVIENGVDVEKYAGRGATTPG-----RTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLII 226
Cdd:cd03801   149 EALRDELRAlgGIPPEKIVVIPNGVDLERFSPPLRRKLGippdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 227 AGREydlneADLRKAIAER--GLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFV 304
Cdd:cd03801   229 VGGD-----GPLRAELEELelGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275110346 305 RLASESGQGVIVNRDRIEAAADQVQALAlqsdSDFDTRR----SASMAYVSRYDWKHVVGRYVDEYH 367
Cdd:cd03801   304 EVVEDGEGGLVVPPDDVEALADALLRLL----ADPELRArlgrAARERVAERFSWERVAERLLDLYR 366
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
191-331 1.73e-23

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: 95.42  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 191 RTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGREYDLNEadLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQ 270
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR--LKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275110346 271 FFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQGVIVNRDRIEAAADQVQAL 331
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL 141
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
262-371 2.16e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 77.34  E-value: 2.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 262 LRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQGVIVNRDRIEAAADQVQALaLQSDSDFDT 341
Cdd:COG0438    14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRL-LEDPELRRR 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1275110346 342 RRSASMAYV-SRYDWKHVVGRYVDEYHDTLG 371
Cdd:COG0438    93 LGEAARERAeERFSWEAIAERLLALYEELLA 123
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
171-368 8.01e-16

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


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 78.21  E-value: 8.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 171 VIENGVDVEKY----AGRGATTPGRTMLYFGRWSVNKGLIE----TLELLQA---ALKRDPQWRLIIAGRE----YDLNE 235
Cdd:TIGR04047 163 VVPNGVDAARFspaaDAADAALRRRLGLRGGPYVLAVGGIEprknTIDLLEAfalLRARRPQAQLVIAGGAtlfdYDAYR 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 236 ADLRKAIAERGLQDKVQLSMSP-SQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASEsGQGV 314
Cdd:TIGR04047 243 REFRARAAELGVDPGPVVITGPvPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGR-FDAA 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1275110346 315 IVNRDRIEAAADQVqALALqSDSDFDTRRSASMAYVSRYDWKHVVGRYVDEYHD 368
Cdd:TIGR04047 322 WADPSDPDSIADAL-ALAL-DPARRPALRAAGPELAARYTWDASARAHLEFYRR 373
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
147-371 4.71e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 45.17  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 147 ARVIATSENDGDLFAKVVAPARLRVIENGVDVEKYAGR---------GATTPGRTMLYFGRWSVNKGLIETLELLQAALK 217
Cdd:PRK15484  141 AKIIVPSQFLKKFYEERLPNADISIVPNGFCLETYQSNpqpnlrqqlNISPDETVLLYAGRISPDKGILLLMQAFEKLAT 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 218 RDPQWRLIIAGREYDLNEADlrKAIAERGLQD-----KVQLSMSPSQ--EQLRALMQQAQFFVCLSR-HEGFGIAAVEAM 289
Cdd:PRK15484  221 AHSNLKLVVVGDPTASSKGE--KAAYQKKVLEaakriGDRCIMLGGQppEKMHNYYPLADLVVVPSQvEEAFCMVAVEAM 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 290 SAGLiPILSD----IPPFVrLASESGQGVIVNRDRIEAAADQVQALAlqsDSDFDTRRSASMAYV-SRYDWKHVVGRYVD 364
Cdd:PRK15484  299 AAGK-PVLAStkggITEFV-LEGITGYHLAEPMTSDSIISDINRTLA---DPELTQIAEQAKDFVfSKYSWEGVTQRFEE 373

                  ....*..
gi 1275110346 365 EYHDTLG 371
Cdd:PRK15484  374 QIHNWFD 380
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-367 6.80e-53

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: 179.66  E-value: 6.80e-53
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHPSIGGMEEVVLNVARQHQATSADtVEVVTLDRVFTDPGAQLAAqdthqglsIRRIGYRGSSRYPLAPSVL 81
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHD-VTVLTPADPGEPPEELEDG--------VIVPLLPSLAALLRARRLL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  82 GAIR------SADVVHLHGIDFFYdYLALTKPLHGKPMVVSTHGGFFHTAYASRMKQLWFqtLTRTSAL--AYARVIATS 153
Cdd:cd03801    72 RELRpllrlrKFDVVHAHGLLAAL-LAALLALLLGAPLVVTLHGAEPGRLLLLLAAERRL--LARAEALlrRADAVIAVS 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 154 ENDGDLFAK--VVAPARLRVIENGVDVEKYAGRGATTPG-----RTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLII 226
Cdd:cd03801   149 EALRDELRAlgGIPPEKIVVIPNGVDLERFSPPLRRKLGippdrPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVI 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 227 AGREydlneADLRKAIAER--GLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFV 304
Cdd:cd03801   229 VGGD-----GPLRAELEELelGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATDVGGLP 303
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1275110346 305 RLASESGQGVIVNRDRIEAAADQVQALAlqsdSDFDTRR----SASMAYVSRYDWKHVVGRYVDEYH 367
Cdd:cd03801   304 EVVEDGEGGLVVPPDDVEALADALLRLL----ADPELRArlgrAARERVAERFSWERVAERLLDLYR 366
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
2-364 2.91e-37

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: 138.27  E-value: 2.91e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHPSIGGMEEVVLNVARQHQATSADtVEVVTLDRVF-TDPGAQLAAQDTHQgLSIRRIGYRGSS--RYPLAP 78
Cdd:cd03821     1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHE-VTIVSTGDGYeSLVVEENGRYIPPQ-DGFASIPLLRQGagRTDFSP 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  79 S----VLGAIRSADVVHLHGI-DFFYDYLALTKPLHGKPMVVSTHGGFFHTAYA-SRMKQLWFQTLTRTSALAYAR-VIA 151
Cdd:cd03821    79 GlpnwLRRNLREYDVVHIHGVwTYTSLAACKLARRRGIPYVVSPHGMLDPWALQqKHWKKRIALHLIERRNLNNAAlVHF 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 152 TSENDGDLFAKVVAPARLRVIENGVDVEKYAGRGATTP-------GRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRL 224
Cdd:cd03821   159 TSEQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRRkhngledRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHL 238
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 225 IIAGrEYDLNEADLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFV 304
Cdd:cd03821   239 VIAG-PDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVITDKCGLS 317
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275110346 305 RLASEsGQGVIVnRDRIEAAADQVQAlALQSDSDFDTRR---SASMAYVSRYDWKHVVGRYVD 364
Cdd:cd03821   318 ELVEA-GCGVVV-DPNVSSLAEALAE-ALRDPADRKRLGemaRRARQVEENFSWEAVAGQLGE 377
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
3-369 3.78e-29

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: 116.33  E-value: 3.78e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   3 VVHVVRQFHPSI-GGMEEVVLNVARQHQATSADtVEVVTLDRVFTDPGAQLAA-QDTHQGLSIRRIGYRGSSR-YPLAPS 79
Cdd:cd03798     1 VLILTNIYPNANsPGRGIFVRRQVRALSRRGVD-VEVLAPAPWGPAAARLLRKlLGEAVPPRDGRRLLPLKPRlRLLAPL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  80 VLGAI---------RSADVVHLHGiDFFYDYLALT-KPLHGKPMVVSTHGgffhTAYASRMKQLWFQTLTRtSALAYA-R 148
Cdd:cd03798    80 RAPSLakllkrrrrGPPDLIHAHF-AYPAGFAAALlARLYGVPYVVTEHG----SDINVFPPRSLLRKLLR-WALRRAaR 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 149 VIATSENDGDLFAKVVAPA-RLRVIENGVDVEKYAGRGAT----TPGRTMLYFGRWSVNKGLIETLELLQAALKRDPQWR 223
Cdd:cd03798   154 VIAVSKALAEELVALGVPRdRVDVIPNGVDPARFQPEDRGlglpLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVV 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 224 LIIAGReyDLNEADLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLiPILS----D 299
Cdd:cd03798   234 LLIVGD--GPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGL-PVVAtdvgG 310
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 300 IPPFVRlasESGQGVIVNRDRIEAAADQVqALALQSDSDFDTRRSASMAYVSRYDWKHVVGRYVDEYHDT 369
Cdd:cd03798   311 IPEVVG---DPETGLLVPPGDADALAAAL-RRALAEPYLRELGEAARARVAERFSWVKAADRIAAAYRDV 376
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
14-364 7.89e-26

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: 106.55  E-value: 7.89e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  14 IGGMEEVVLNVArQHQATSADTVEVVTLDRVFTDPGAQLAAQDTHQGLSIRRigYRGSSRYPLAPSVLGAIR------SA 87
Cdd:cd03820    12 AGGAERVAINLA-NHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRK--YSHFKLLLKYFKKVRRLRkylknnKP 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  88 DVVhlhgIDF-FYDYLALTKPLHGKPMVVSthggfFHTAYASRMKQLWFQTLTRTSALAYARVIATSENDGDLFaKVVAP 166
Cdd:cd03820    89 DVV----ISFrTSLLTFLALIGLKSKLIVW-----EHNNYEAYNKGLRRLLLRRLLYKRADKIVVLTEADKLKK-YKQPN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 167 ARLRVIENGVDVEKyagRGATTP--GRTMLYFGRWSVNKG---LIETLELLQaalKRDPQWRLIIAGreyDLNEAD-LRK 240
Cdd:cd03820   159 SNVVVIPNPLSFPS---EEPSTNlkSKRILAVGRLTYQKGfdlLIEAWALIA---KKHPDWKLRIYG---DGPEREeLEK 229
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 241 AIAERGLQDKVQLSmsPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQ-GVIVNRD 319
Cdd:cd03820   230 LIDKLGLEDRVKLL--GPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIISFDCPTGPSEIIEDGEnGLLVPNG 307
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*...
gi 1275110346 320 RIEAAADQVQALAlqsdSDFDTRRS---ASMAYVSRYDWKHVVGRYVD 364
Cdd:cd03820   308 DVDALAEALLRLM----EDEELRKKmgkNARKNAERFSIEKIIKQWEE 351
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
2-348 1.05e-25

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: 106.29  E-value: 1.05e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFhpSIGGMEEVVLNVArQHQATSADTVEVVTLDRVFTDPgAQLAAQDTHQGLSIRRIGYRGSSRYPLAPSVL 81
Cdd:cd03811     1 KILFVIPSL--SGGGAERVLLNLA-NALDKRGYDVTLVLLRDEGDLD-KQLNGDVKLIRLLIRVLKLIKLGLLKAILKLK 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  82 GAIRSA--DVVHLHGidFFYDYLALTKPLHGKPmVVSTHGGFFHTAYASRMKQLWFQTLTRtsalAYARVIATSENDGDL 159
Cdd:cd03811    77 RILKRAkpDVVISFL--GFATYIVAKLAAARSK-VIAWIHSSLSKLYYLKKKLLLKLKLYK----KADKIVCVSKGIKED 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 160 FAKV--VAPARLRVIENGVDVE------KYAGRGATTPGRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGrEY 231
Cdd:cd03811   150 LIRLgpSPPEKIEVIYNPIDIDriralaKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILG-DG 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 232 DLnEADLRKAIAERGLQDKVQLSmsPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESG 311
Cdd:cd03811   229 PL-REELEKLAKELGLAERVIFL--GFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGE 305
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1275110346 312 QGVIVNRDRIEAAADQVQALaLQSDSDFDTRRSASMA 348
Cdd:cd03811   306 NGLLVPDGDAAALAGILAAL-LQKKLDAALRERLAKA 341
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
191-331 1.73e-23

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: 95.42  E-value: 1.73e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 191 RTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGREYDLNEadLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQ 270
Cdd:pfam00534   3 KIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKR--LKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275110346 271 FFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQGVIVNRDRIEAAADQVQAL 331
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL 141
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
92-356 5.36e-23

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: 98.59  E-value: 5.36e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  92 LHGIDFFYdYLALTKPLH--GKPMVV----STHggFFHTAYASRMKQLWFQTLTRTSaLAYARVIAT-SENDGDLFAK-- 162
Cdd:cd03809    82 KDKPDLLH-SPHNTAPLLlkGCPQVVtihdLIP--LRYPEFFPKRFRLYYRLLLPIS-LRRADAIITvSEATRDDIIKfy 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 163 VVAPARLRVIENGVD-------VEKYAGRGATTPGRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGREYDLNE 235
Cdd:cd03809   158 GVPPEKIVVIPLGVDpsffppeSAAVLIAKYLLPEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDE 237
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 236 aDLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESgqGVI 315
Cdd:cd03809   238 -ELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDA--ALY 314
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1275110346 316 VNRDRIEAAADQVQALALQSDSdFDTRRSASMAYVSRYDWK 356
Cdd:cd03809   315 FDPLDPESIADAILRLLEDPSL-REELIRKGLERAKKFSWE 354
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
10-346 3.34e-21

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: 93.19  E-value: 3.34e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  10 FHPSIGGMEEVVLNVARqHQATSADTVEVVTLDrvftDPGAQLAAQDthqGLSIRRIGYRGSSRYPLAPSV--LGAIRSA 87
Cdd:cd03819     6 PALEIGGAETYILDLAR-ALAERGHRVLVVTAG----GPLLPRLRQI---GIGLPGLKVPLLRALLGNVRLarLIRRERI 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  88 DVVHLHGidFFYDYLA-LTKPLHGKPMVVSTHGgffHTAYASRMKQLWFQTLTRTsalayARVIATSENDGDLFAKV--V 164
Cdd:cd03819    78 DLIHAHS--RAPAWLGwLASRLTGVPLVTTVHG---SYLATYHPKDFALAVRARG-----DRVIAVSELVRDHLIEAlgV 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 165 APARLRVIENGVDVEKYAGRGATTPGRTM---------LYFGRWSVNKGLIETLELLqAALKRDPQWRLIIAGREydLNE 235
Cdd:cd03819   148 DPERIRVIPNGVDTDRFPPEAEAEERAQLglpegkpvvGYVGRLSPEKGWLLLVDAA-AELKDEPDFRLLVAGDG--PER 224
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 236 ADLRKAIAERGLQDKVQLSMSPsqEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQGVI 315
Cdd:cd03819   225 DEIRRLVERLGLRDRVTFTGFR--EDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGRTGLL 302
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1275110346 316 VNRDRIEAAADQVQALALQSDSDFDTRRSAS 346
Cdd:cd03819   303 VPPGDAEALADAIRAAKLLPEAREKLQAAAA 333
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
88-362 3.45e-20

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: 90.73  E-value: 3.45e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  88 DVVHLHGID-FFYDYLAlTKPLHGKPMVVSTHG-GFFHTAyaSRMKQLWFQTLTRTSALAYARVIATSENDGDLF--AKV 163
Cdd:cd03808    83 DIVHCHTPKpGILGRLA-ARLAGVPKVIYTVHGlGFVFTE--GKLLRLLYLLLEKLALLFTDKVIFVNEDDRDLAikKGI 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 164 VAPARLRVIE-NGVDVEKYAGRGATTPGR--TMLYFGRWSVNKGLietLELLQAA--LK-RDPQWRLIIAGrEYDLNEAD 237
Cdd:cd03808   160 IKKKKTVLIPgSGVDLDRFQYSPESLPSEkvVFLFVARLLKDKGI---DELIEAAkiLKkKGPNVRFLLVG-DGELENPS 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 238 LrKAIAERGLQDKVQLsmsPSQEQ-LRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPfVRLASESGQ-GVI 315
Cdd:cd03808   236 E-ILIEKLGLEGRIEF---LGFRSdVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVPG-CRELVIDGVnGFL 310
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1275110346 316 VNRDRIEAAADQVQALALQSDSDFDTRRSASMAYVSRYDWKHVVGRY 362
Cdd:cd03808   311 VPPGDVEALADAIEKLIEDPELRKEMGEAARKRVEEKFDEEKVVNKL 357
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
2-367 7.70e-20

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: 89.68  E-value: 7.70e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVrqFHPSIGGMEEVVLNVARqHQATSADTVEVVTLdrvfTDPGAqLAAQDTHQGLSIRRIGyRGSSRYPLAPSVL 81
Cdd:cd03807     1 KVAHVI--TGLNVGGAETMLLRLLE-HMDKSRFEHVVISL----TGDGV-LGEELLAAGVPVVCLG-LSSGKDPGVLLRL 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  82 GAI---RSADVVHLHGIDFFYdYLALTKPLHGKPMVVSTHGGFFHTAYASRMKQLWFQTLTRTSALayarVIATSENDGD 158
Cdd:cd03807    72 AKLirkRNPDVVHTWMYHADL-IGGLAAKLAGGVKVIWSVRSSNIPQRLTRLVRKLCLLLSKFSPA----TVANSSAVAE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 159 LFAKV-VAPARLRVIENGVDVEKYA-GRGATTPGRTMLYFGRWSVNKGLIETLE-------LLQAA---LKRDPQWRLII 226
Cdd:cd03807   147 FHQEQgYAKNKIVVIYNGIDLFKLSpDDASRARARRRLGLAEDRRVIGIVGRLHpvkdhsdLLRAAallVETHPDLRLLL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 227 AGREydLNEADLRKAIAERGLQDKVQLSmsPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRL 306
Cdd:cd03807   227 VGRG--PERPNLERLLLELGLEDRVHLL--GERSDVPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATDVGGAAEL 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275110346 307 ASEsGQGVIVNRDRIEAAADQVQALALQSDsDFDTRRSASMAYV-SRYDWKHVVGRYVDEYH 367
Cdd:cd03807   303 VDD-GTGFLVPAGDPQALADAIRALLEDPE-KRARLGRAARERIaNEFSIDAMVRRYETLYY 362
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
3-316 1.07e-17

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: 81.30  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   3 VVHVVRQFHPSIGGMEEVVLNVARqhqATSADTVEVVTLDRVFtdpgaqlaaqdthqgLSIRRIGYRGSsryplapsvlg 82
Cdd:cd01635     1 ILLVTGEYPPLRGGLELHVRALAR---ALAALGHEVTVLALLL---------------LALRRILKKLL----------- 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  83 aIRSADVVHLHGIDFFYDYLALTKPLHGKPMVVSTHGGFFHTAYASRMKQLWFQTLTRtsalayarviatsendgdlfak 162
Cdd:cd01635    52 -ELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARLLVSL---------------------- 108
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 163 vvaparlrviengvdvekyagrgattPGRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGReYDLNEADLRKAI 242
Cdd:cd01635   109 --------------------------PLADKVSVGRLVPEKGIDLLLEALALLKARLPDLVLVLVGG-GGEREEEEALAA 161
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1275110346 243 AERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQGVIV 316
Cdd:cd01635   162 ALGLLERVVIIGGLVDDEVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLLV 235
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
262-371 2.16e-17

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 77.34  E-value: 2.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 262 LRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGQGVIVNRDRIEAAADQVQALaLQSDSDFDT 341
Cdd:COG0438    14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEALAEAILRL-LEDPELRRR 92
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1275110346 342 RRSASMAYV-SRYDWKHVVGRYVDEYHDTLG 371
Cdd:COG0438    93 LGEAARERAeERFSWEAIAERLLALYEELLA 123
MSMEG_0565_glyc TIGR04047
glycosyltransferase, MSMEG_0565 family; A conserved gene cluster found sporadically from ...
171-368 8.01e-16

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


Pssm-ID: 274943 [Multi-domain]  Cd Length: 373  Bit Score: 78.21  E-value: 8.01e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 171 VIENGVDVEKY----AGRGATTPGRTMLYFGRWSVNKGLIE----TLELLQA---ALKRDPQWRLIIAGRE----YDLNE 235
Cdd:TIGR04047 163 VVPNGVDAARFspaaDAADAALRRRLGLRGGPYVLAVGGIEprknTIDLLEAfalLRARRPQAQLVIAGGAtlfdYDAYR 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 236 ADLRKAIAERGLQDKVQLSMSP-SQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASEsGQGV 314
Cdd:TIGR04047 243 REFRARAAELGVDPGPVVITGPvPDADLPALYRCADAFAFPSLKEGFGLVVLEALASGIPVVASDIAPFTEYLGR-FDAA 321
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1275110346 315 IVNRDRIEAAADQVqALALqSDSDFDTRRSASMAYVSRYDWKHVVGRYVDEYHD 368
Cdd:TIGR04047 322 WADPSDPDSIADAL-ALAL-DPARRPALRAAGPELAARYTWDASARAHLEFYRR 373
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
190-331 1.53e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 72.93  E-value: 1.53e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 190 GRTMLYFGRWSVN-KGLIETLELLQAALKRDPQWRLIIAGREydlNEADLRKAIaeRGLQDKVQLSmsPSQEQLRALMQQ 268
Cdd:pfam13692   1 RPVILFVGRLHPNvKGVDYLLEAVPLLRKRDNDVRLVIVGDG---PEEELEELA--AGLEDRVIFT--GFVEDLAELLAA 73
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275110346 269 AQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPFVRLASESGqGVIVNRDRIEAAADQVQAL 331
Cdd:pfam13692  74 ADVFVLPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGEN-GLLVPPGDPEALAEAILRL 135
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
15-179 2.97e-14

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 70.25  E-value: 2.97e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  15 GGMEEVVLNVARQHQAtsaDTVEVVtldrVFTDPGAQLAAQDTHQGLSIRRIGYRGSSRYPLAPSVLGAIRSA------D 88
Cdd:pfam13439   1 GGVERYVLELARALAR---RGHEVT----VVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLlrrerpD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  89 VVHLHGIDFFYDYLALTKPLHGKPMVVSTHGGFF---HTAYASRMKQLWFQTLTRTSALAYARVIATSENDGDLFAKV-- 163
Cdd:pfam13439  74 VVHAHSPFPLGLAALAARLRLGIPLVVTYHGLFPdykRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLyg 153
                         170
                  ....*....|....*.
gi 1275110346 164 VAPARLRVIENGVDVE 179
Cdd:pfam13439 154 VPPEKIRVIPNGVDLE 169
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
2-367 1.97e-12

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: 67.70  E-value: 1.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHPSIGGMEEVVLNVARQHQATSADtVEVVTLDrvfTDPGAQLAAQDTHQGLSIR---RIGYRGSsrYPLAP 78
Cdd:cd03814     1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHE-VRVVAPG---PFDEAESAEGRVVSVPSFPlpfYPEYRLA--LPLPR 74
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  79 SVLGAIRSA--DVVHLHGIDFFYDYLALTKPLHGKPMVVSTHGGFFHtaYASRMKQLWFQTLT----RTSALAYARVIAT 152
Cdd:cd03814    75 RVRRLIKEFqpDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPE--YLSYYTLGPLSWLAwaylRWFHNPFDTTLVP 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 153 SENDGDLFAKVvAPARLRVIENGVDVE--------KYAGRGATTPGRTML-YFGRWSVNKGLiETLELLQAALKRDPQWR 223
Cdd:cd03814   153 SPSIARELEGH-GFERVRLWPRGVDTElfhpsrrdAALRRRLGPPGRPLLlYVGRLAPEKNL-EALLDADLPLAASPPVR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 224 LIIAGreydlnEADLRKAIAERGLQdkVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPPF 303
Cdd:cd03814   231 LVVVG------DGPARAELEARGPD--VIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVAADAGGP 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1275110346 304 VRLASESGQGVIVNRDRIEAAADQVQALaLQSDSDFDTRRSASMAYVSRYDWKHVVGRYVDEYH 367
Cdd:cd03814   303 RDIVRPGGTGALVEPGDAAAFAAALRAL-LEDPELRRRMAARARAEAERYSWEAFLDNLLDYYA 365
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
2-332 2.30e-12

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: 67.30  E-value: 2.30e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHPSIGGMEEVVLNVArqhQATSADTVEVVTLdrvftdpgaqLAAQDTHQ------GLSIRRIGYRGS-SRY 74
Cdd:cd03795     1 KVLHVFKFYYPDIGGIEQVIYDLA---EGLKKKGIEVDVL----------CFSKEKETpekeenGIRIHRVKSFLNvAST 67
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  75 PLAPSVLGAIR----SADVVHLHGIDFFYDyLALTKPLHGKPMVVSTHGGFFHTAYASRM-KQLWFQTLTRTsalayARV 149
Cdd:cd03795    68 PFSPSYIKRFKklakEYDIIHYHFPNPLAD-LLLFFSGAKKPVVVHWHSDIVKQKKLLKLyKPLMTRFLRRA-----DRI 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 150 IATSENDGDLfAKVVAPAR--LRVIENGVDVEKY-AGRGATTP-------GRTMLYFGRWSVNKG---LIETLELLQAAl 216
Cdd:cd03795   142 IATSPNYVET-SPTLREFKnkVRVIPLGIDKNVYnIPRVDFENikrekkgKKIFLFIGRLVYYKGldyLIEAAQYLNYP- 219
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 217 krdpqwrLIIAGreyDLNEADLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLS--RHEGFGIAAVEAMSAGLI 294
Cdd:cd03795   220 -------IVIGG---EGPLKPDLEAQIELNLLDNVKFLGRVDDEEKVIYLHLCDVFVFPSvlRSEAFGIVLLEAMMCGKP 289
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 1275110346 295 PILSDIP---PFVRLASESGqgvivnrdrIEAAADQVQALA 332
Cdd:cd03795   290 VISTNIGtgvPYVNNNGETG---------LVVPPKDPDALA 321
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
40-352 2.97e-12

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: 67.09  E-value: 2.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  40 TLDRVFTDPGAQLAAQDTHQGLSIRRIGYRGSSRYPLAPsVLGAIRSADVVHLH-GIDFFYDyLALTKPLhGKPMVVSTH 118
Cdd:cd05844    36 RLAPAPFDGVALRALGGSGPLRWLRQMAQRLLGWSAPRL-GGAAGLAPALVHAHfGRDGVYA-LPLARAL-GVPLVVTFH 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 119 GG--FFHTAYASRMKQLWFQTLTRTSALAY--ARVIATSENDGD-LFAKVVAPARLRVIENGVDVEKYAGRGATTPGRTM 193
Cdd:cd05844   113 GFdiTTSRAWLAASPGWPSQFQRHRRALQRpaALFVAVSGFIRDrLLARGLPAERIHVHYIGIDPAKFAPRDPAERAPTI 192
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 194 LYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGREYDLNEADLRKAIAERglqdkVQLSMSPSQEQLRALMQQAQFFV 273
Cdd:cd05844   193 LFVGRLVEKKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALGR-----VRFLGALPHAEVQDWMRRAEIFC 267
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 274 CLS------RHEGFGIAAVEAMSAGlIPILSDIPPFVRLASESGQ-GVIVNRDRIEAAADQVQALaLQSDSDFDTRRSAS 346
Cdd:cd05844   268 LPSvtaasgDSEGLGIVLLEAAACG-VPVVSSRHGGIPEAILDGEtGFLVPEGDVDALADALQAL-LADRALADRMGGAA 345

                  ....*.
gi 1275110346 347 MAYVSR 352
Cdd:cd05844   346 RAFVCE 351
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
43-299 1.37e-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: 65.38  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  43 RVFT--DPGAQLAAQDthQGLSIRRIGYRGSSRYPLA----PSVLGAIRS--ADVVHLHGiDFFYDYLALTKplhGKPM- 113
Cdd:cd03817    35 YVITpsDPGAEDEEEV--VRYRSFSIPIRKYHRQHIPfpfkKAVIDRIKElgPDIIHTHT-PFSLGKLGLRI---ARKLk 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 114 --VVSThggfFHTA------YASRMKQLWFQTLTRTSALAYAR---VIATSENDGDLFAKVVAPARLRVIENGVDVEKYA 182
Cdd:cd03817   109 ipIVHT----YHTMyedylhYIPKGKLLVKAVVRKLVRRFYNHtdaVIAPSEKIKDTLREYGVKGPIEVIPNGIDLDKFE 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 183 G---------RGATTPGRTMLYFGRWSVNKGLIETLELLqAALKRDPQWRLIIAGREYDlnEADLRKAIAERGLQDKVQL 253
Cdd:cd03817   185 KplnteerrkLGLPPDEPILLYVGRLAKEKNIDFLLRAF-AELKKEPNIKLVIVGDGPE--REELKELARELGLADKVIF 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1275110346 254 SMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLiPILSD 299
Cdd:cd03817   262 TGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGL-PVVAA 306
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
58-363 3.81e-11

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: 63.90  E-value: 3.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  58 HQGLSIRRIGYRGSS-RYPLAPSVLGAIRSADVVHLHGIDFFYDYLALT-KPLHGKPMVVSTHGGFFHTAYASRM--KQL 133
Cdd:cd03794    69 IKKNGLIRRLLNYLSfALAALLKLLVREERPDVIIAYSPPITLGLAALLlKKLRGAPFILDVRDLWPESLIALGVlkKGS 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 134 WFQTLTRTSALAYA---RVIATSENDGDLFA-KVVAPARLRVIENGVDVE------KYAGRGATTPGRTM--LYFGrwsv 201
Cdd:cd03794   149 LLKLLKKLERKLYRladAIIVLSPGLKEYLLrKGVPKEKIIVIPNWADLEefkpppKDELRKKLGLDDKFvvVYAG---- 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 202 NKGLIETLE-LLQAA--LKRDPQWRLIIAG--REYDLneadLRKAIAERGLQDkvqLSMSPSQ--EQLRALMQQAQF-FV 273
Cdd:cd03794   225 NIGKAQGLEtLLEAAerLKRRPDIRFLFVGdgDEKER----LKELAKARGLDN---VTFLGRVpkEEVPELLSAADVgLV 297
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 274 CLSRHEGFGIAA----VEAMSAGLiPIL-SDIPPFVRLASESGQGVIVNRDRIEAAADQVQALALQSdsdfDTRRSASMA 348
Cdd:cd03794   298 PLKDNPANRGSSpsklFEYMAAGK-PILaSDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDP----ELRRAMGEN 372
                         330
                  ....*....|....*....
gi 1275110346 349 ----YVSRYDWKHVVGRYV 363
Cdd:cd03794   373 grelAEEKFSREKLADRLL 391
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
15-298 5.10e-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: 63.41  E-value: 5.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  15 GGMEEVVLNVARqHQATSADTVEVVTldRVFTDpgAQLAAQDTHQGLSIRRI---GYRGSSRYPLAPS-------VLGAI 84
Cdd:cd03800    21 GGQNVYVLELAR-ALAELGYQVDIFT--RRISP--ADPEVVEIAPGARVIRVpagPPEYLPKEELWPYleefadgLLRFI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  85 RSA----DVVHLHGIDFFYDYLALTKPLhGKPMVVSthggfFHTAYASRMKQL----WFQTLTRTSA--LAYA---RVIA 151
Cdd:cd03800    96 AREggryDLIHSHYWDSGLVGALLARRL-GVPLVHT-----FHSLGRVKYRHLgaqdTYHPSLRITAeeQILEaadRVIA 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 152 TSENDG-DLFAKVVA-PARLRVIENGVDVEKY----------AGRGATTPGRTMLYFGRWSVNKGLIETLELLQAALKRD 219
Cdd:cd03800   170 STPQEAdELISLYGAdPSRINVVPPGVDLERFfpvdraearrARLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELR 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 220 PQWRLIIA-GREYDLNEAD--LRKAIAER-GLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLiP 295
Cdd:cd03800   250 ELANLVLVgGPSDDPLSMDreELAELAEElGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAMACGT-P 328

                  ...
gi 1275110346 296 ILS 298
Cdd:cd03800   329 VVA 331
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
2-331 7.30e-11

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: 62.73  E-value: 7.30e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346   2 KVVHVVRQFHP-SIGGMEEVVLNVARqHQATSADTVEVVTLD----RVFTDPGAQ---LAAQDTHQGLSIRRIGYRGSSR 73
Cdd:cd03823     1 KILLVNSLYPPqRVGGAEISVHDLAE-ALVAEGHEVAVLTAGvgppGQATVARSVvryRRAPDETLPLALKRRGYELFET 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  74 Y--PLAPSVLGAIR--SADVVHLHGIDFFyDYLALTKPLH-GKPMVVSthggfFHTAYASRMkqlwFQTLTRtsaLAYAR 148
Cdd:cd03823    80 YnpGLRRLLARLLEdfRPDVVHTHNLSGL-GASLLDAARDlGIPVVHT-----LHDYWLLCP----RQFLFK---KGGDA 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 149 VIATSENDGDLF-AKVVAPARLRVIENGVDVEKYA-GRGATTPGRT-MLYFGRWSVNKGLietlELLQAALKR--DPQWR 223
Cdd:cd03823   147 VLAPSRFTANLHeANGLFSARISVIPNAVEPDLAPpPRRRPGTERLrFGYIGRLTEEKGI----DLLVEAFKRlpREDIE 222
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 224 LIIAGREYDlneadlrKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSR-HEGFGIAAVEAMSAGLIPILSD--- 299
Cdd:cd03823   223 LVIAGHGPL-------SDERQIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAIAAGLPVIASDlgg 295
                         330       340       350
                  ....*....|....*....|....*....|..
gi 1275110346 300 IPPFVRlasESGQGVIVNRDRIEAAADQVQAL 331
Cdd:cd03823   296 IAELIQ---PGVNGLLFAPGDAEDLAAAMRRL 324
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
97-328 2.56e-10

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: 61.16  E-value: 2.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  97 FFYDYLALTKP-----------------LHGKPMVV----STHGGFFHTAYASRMKQLW---FQTLTRTSALayarVIAT 152
Cdd:cd04949    46 FFIEQLNLQKGdifisdrptltgqvilnTKGPAKKGavlhNEHVKNNDDPEHSLIKNFYkyvFENLNKYDAI----IVST 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 153 SENDGDL---FAKVVapaRLRVIENG-VDVEKYAGRGATTPGRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAG 228
Cdd:cd04949   122 EQQKQDLserFNKYP---PIFTIPVGyVDQLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYG 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 229 reYDLNEADLRKAIAERGLQDKVQLSmsPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDI----PPFV 304
Cdd:cd04949   199 --YGEEREKLKKLIEELHLEDNVFLK--GYHSNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVkygpSELI 274
                         250       260
                  ....*....|....*....|....*
gi 1275110346 305 rlasESGQ-GVIVNRDRIEAAADQV 328
Cdd:cd04949   275 ----EDGEnGYLIEKNNIDALADKI 295
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
88-302 1.21e-09

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: 59.23  E-value: 1.21e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  88 DVVHLHG--IDFFYDYLALTKplhGKPMVVST-HGGFFHTAYASRMKQLWFQTLTRTSALAYarvIATSENDGDLFAKVV 164
Cdd:cd03812    82 DIVHVHGssSNGIILLLAAKA---GVPVRIAHsHNTKDSSIKLRKIRKNVLKKLIERLSTKY---LACSEDAGEWLFGEV 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 165 APARLRVIENGVDVEKYAGRGATTPGRTMLYF----------GRWSVNKG---LIETLELLQaalKRDPQWRLIIAGREY 231
Cdd:cd03812   156 ENGKFKVIPNGIDIEKYKFNKEKRRKRRKLLIledklvlghvGRFNEQKNhsfLIDIFEELK---KKNPNVKLVLVGEGE 232
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275110346 232 DLNEadLRKAIAERGLQDKVQL--SMSPSQEqlraLMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDIPP 302
Cdd:cd03812   233 LKEK--IKEKVKELGLEDKVIFlgFRNDVSE----ILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTIT 299
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
15-175 1.45e-09

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 56.26  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  15 GGMEEVVLNVARqhqATSADTVEVvtldRVFTDPGAQLAAQDTHQGLSIRRIGYRGSSRYPLAPSVLGAIRSA------D 88
Cdd:pfam13579   1 GGIGVYVLELAR---ALAALGHEV----RVVTPGGPPGRPELVGDGVRVHRLPVPPRPSPLADLAALRRLRRLlraerpD 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  89 VVHLHGIdFFYDYLALTKPLHGKPMVVSTHGGFFHtaYASRMKQLWFQTLTRTSALAYARVIATSENDGDLF-AKVVAPA 167
Cdd:pfam13579  74 VVHAHSP-TAGLAARLARRRRGVPLVVTVHGLALD--YGSGWKRRLARALERRLLRRADAVVVVSEAEAELLrALGVPAA 150

                  ....*...
gi 1275110346 168 RLRVIENG 175
Cdd:pfam13579 151 RVVVVPNG 158
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
164-375 4.76e-09

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: 57.63  E-value: 4.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 164 VAPARLRVIENGVDVEKYagrgatTP--------GRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGreYDLNE 235
Cdd:cd03796   165 LDPRIVSVIPNAVDSSDF------TPdpskpdpnKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGG--DGPKR 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 236 ADLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLIPILSDI-------PP-FVRLA 307
Cdd:cd03796   237 IELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAFCIAIVEAASCGLLVVSTRVggipevlPPdMILLA 316
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1275110346 308 SESGQGVIvnrDRIEAAADQVQALALQSDSDFDtrRSASMayvsrYDWKHVVGRYVDEYHDTLGIPRV 375
Cdd:cd03796   317 EPDPEDIV---RKLEEAISILRTGKHDPWSFHN--RVKKM-----YSWEDVARRTEKVYDRILSTPNR 374
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
206-368 1.57e-08

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: 55.82  E-value: 1.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 206 IETLELLQAALKRdpqwRLIIAGREYDLNEAdlRKAIAERGLQDKVQlsMSPSQEQLRALMQQAQFFVCLSRHEGFGIAA 285
Cdd:cd04962   215 VRVFARVRRKIPA----KLLLVGDGPERVPA--EELARELGVEDRVL--FLGKQDDVEELLSIADLFLLPSEKESFGLAA 286
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 286 VEAMSAGLIPILSD---IPPFVRlasESGQGVIVNRDRIEAAADqvQALALQSDSDFDTRRSASMA--YVSRYDWKHVVG 360
Cdd:cd04962   287 LEAMACGVPVVSSNaggIPEVVK---HGETGFLSDVGDVDAMAK--SALSILEDDELYNRMGRAARkrAAERFDPERIVP 361

                  ....*...
gi 1275110346 361 RYVDEYHD 368
Cdd:cd04962   362 QYEAYYRR 369
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
48-369 5.72e-08

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: 53.87  E-value: 5.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  48 PGAQLAAQDTHQGL-----SIRRIGYRGSSRYPLApsvlgAIRSADVVHLHGI-DFFYDYLALTKPLHGKPMVVSTH--- 118
Cdd:cd03825    13 GGAARAAYRLHQALlaygiDSTMLVGRKKNLISKP-----EFIEADIIHLHWIhGGYLSLKALFKLLRRKPVVWTLHdmw 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 119 ---GGFFHT-----------------AYASRMKQLWFQTLTRTSAL---AYARVIATSENDGDLF--AKVVAPARLRVIE 173
Cdd:cd03825    88 pftGGCHYPmecegwktgcgncpnlnSYPPAKKDLSRQLFRRKREAlakKRLTIVAPSRWLADMVrrSPLLKGLPVVVIP 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 174 NGVDVEKYAGRGAT-------TPGRTML-YFGRWSV---NKGLIETLELLQAALKRDpQWRLIIAGReYDLNEADLRKAI 242
Cdd:cd03825   168 NGIDTEIFAPVDKAkarkrlgIPQDKKViLFGAESVtkpRKGFDELIEALKLLATKD-DLLLVVFGK-NDPQIVILPFDI 245
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 243 AERGLQDkvqlsmspSQEQLRALMQQAQFFVCLSRHEGFGIAAVEAMSAGLiPILS----DIPPFVRlasESGQGVIVNR 318
Cdd:cd03825   246 ISLGYID--------DDEQLVDIYSAADLFVHPSLADNLPNTLLEAMACGT-PVVAfdtgGSPEIVQ---HGVTGYLVPP 313
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1275110346 319 DRIEAAADQVQALALQSDSDFDTRRSASMAYVSRYDWKHVVGRYVDEYHDT 369
Cdd:cd03825   314 GDVQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQRYLELYKDL 364
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
103-300 1.17e-07

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: 53.49  E-value: 1.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 103 ALTKPLHGKPMVVSTHG------------GFFHTAYasrMKQLWFQTLTRTSALAY---ARVIATSEN-------DGdlf 160
Cdd:cd03813   190 ALARHRRGIPFLLTEHGiytrerkieilqSTWIMGY---IKKLWIRFFERLGKLAYqqaDKIISLYEGnrrrqirLG--- 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 161 AKvvaPARLRVIENGVDVEKYAGRGATTPGRTMLYFGrwSVN--------KGLIETLELLqaaLKRDPQWRLIIAGREYD 232
Cdd:cd03813   264 AD---PDKTRVIPNGIDIQRFAPAREERPEKEPPVVG--LVGrvvpikdvKTFIRAFKLV---RRAMPDAEGWLIGPEDE 335
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1275110346 233 LNE--ADLRKAIAERGLQDKVQ-LSMSPSQEQLRALmqqaQFFVCLSRHEGFGIAAVEAMSAGLIPILSDI 300
Cdd:cd03813   336 DPEyaQECKRLVASLGLENKVKfLGFQNIKEYYPKL----GLLVLTSISEGQPLVILEAMASGVPVVATDV 402
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
87-292 2.89e-07

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: 51.90  E-value: 2.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  87 ADVVHLHgidfFYDYLALTKPLHGKPMVVSTHGGFFHTAYASRmkqlwfqtltrtSALAYARVIATSENDGDLFAKVVAP 166
Cdd:cd03802    87 FDVIHNH----SYDWLPPFAPLIGTPFVTTLHGPSIPPSLAIY------------AAEPPVNYVSISDAQRAATPPIDYL 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 167 ArlrVIENGVDVEKYagRGATTPGRTMLYFGRWSVNKGLIETLELLQAAlkrdpQWRLIIAGREYDLNEADLrkaIAERG 246
Cdd:cd03802   151 T---VVHNGLDPADY--RFQPDPEDYLAFLGRIAPEKGLEDAIRVARRA-----GLPLKIAGKVRDEDYFYY---LQEPL 217
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1275110346 247 LQDKVQLSMSPSQEQLRALMQQAQFFVCLSR-HEGFGIAAVEAMSAG 292
Cdd:cd03802   218 PGPRIEFIGEVGHDEKQELLGGARALLFPINwDEPFGLVMIEAMACG 264
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
209-296 4.90e-06

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: 48.37  E-value: 4.90e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 209 LELLQAALKR-----DPQWRLIIAG--ReydlNEAD------LRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVcl 275
Cdd:cd03806   256 LRAFAELLKRlpesiRSNPKLVLIGscR----NEEDkerveaLKLLAKELILEDSVEFVVDAPYEELKELLSTASIGL-- 329
                          90       100
                  ....*....|....*....|....*
gi 1275110346 276 srH----EGFGIAAVEAMSAGLIPI 296
Cdd:cd03806   330 --HtmwnEHFGIGVVEYMAAGLIPL 352
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
147-371 4.71e-05

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 45.17  E-value: 4.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 147 ARVIATSENDGDLFAKVVAPARLRVIENGVDVEKYAGR---------GATTPGRTMLYFGRWSVNKGLIETLELLQAALK 217
Cdd:PRK15484  141 AKIIVPSQFLKKFYEERLPNADISIVPNGFCLETYQSNpqpnlrqqlNISPDETVLLYAGRISPDKGILLLMQAFEKLAT 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 218 RDPQWRLIIAGREYDLNEADlrKAIAERGLQD-----KVQLSMSPSQ--EQLRALMQQAQFFVCLSR-HEGFGIAAVEAM 289
Cdd:PRK15484  221 AHSNLKLVVVGDPTASSKGE--KAAYQKKVLEaakriGDRCIMLGGQppEKMHNYYPLADLVVVPSQvEEAFCMVAVEAM 298
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 290 SAGLiPILSD----IPPFVrLASESGQGVIVNRDRIEAAADQVQALAlqsDSDFDTRRSASMAYV-SRYDWKHVVGRYVD 364
Cdd:PRK15484  299 AAGK-PVLAStkggITEFV-LEGITGYHLAEPMTSDSIISDINRTLA---DPELTQIAEQAKDFVfSKYSWEGVTQRFEE 373

                  ....*..
gi 1275110346 365 EYHDTLG 371
Cdd:PRK15484  374 QIHNWFD 380
PLN02949 PLN02949
transferase, transferring glycosyl groups
206-296 6.80e-05

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 44.73  E-value: 6.80e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 206 IETLELLQAALKRD-PQWRLIIAG---REYDLNE-ADLRKAIAERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSRHEG 280
Cdd:PLN02949  287 LEAFALALEKLDADvPRPKLQFVGscrNKEDEERlQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEH 366
                          90
                  ....*....|....*.
gi 1275110346 281 FGIAAVEAMSAGLIPI 296
Cdd:PLN02949  367 FGISVVEYMAAGAVPI 382
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
206-292 7.22e-05

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: 44.50  E-value: 7.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 206 IETLELLQAALKRDPQWRLIIAGrEYD--LNE-----ADLRKAIAE-RGLQDKVQLSMSPSQEQLRALMQQAQFFVCLSR 277
Cdd:cd03805   230 IEAFAKLKQKLPEFENVRLVIAG-GYDprVAEnveylEELQRLAEElLNVEDQVLFLRSISDSQKEQLLSSALALLYTPS 308
                          90
                  ....*....|....*
gi 1275110346 278 HEGFGIAAVEAMSAG 292
Cdd:cd03805   309 NEHFGIVPLEAMYAG 323
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
88-367 6.15e-04

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: 41.60  E-value: 6.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346  88 DVVHL-HGIDFF-YDYL--ALTKPLHGKPMVVSThggfFHTAYASR----MKQLWFQTLTRTSAlayARVIATSENDGDL 159
Cdd:cd03822    77 DVVHIqHEFGIFgGKYGlyALGLLLHLRIPVITT----LHTVLDLSdpgkQALKVLFRIATLSE---RVVVMAPISRFLL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 160 FAKVVAPA-RLRVIENGV------DVEKYAGRGATTPGRTMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGR--- 229
Cdd:cd03822   150 VRIKLIPAvNIEVIPHGVpevpqdPTTALKRLLLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAGElhp 229
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 230 --EYDLNEADLRKAIAERGLQDKVQLSMS--PSQEQLRaLMQQAQFFVCLSRHEGFGIAAVEAMSAGL-IPILSDIPPFV 304
Cdd:cd03822   230 slARYEGERYRKAAIEELGLQDHVDFHNNflPEEEVPR-YISAADVVVLPYLNTEQSSSGTLSYAIACgKPVISTPLRHA 308
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1275110346 305 RLASESGQGVIVNRDRIEAAADQVQALaLQSDSDFDTRRSASMAYVSRYDWKHVVGRYVDEYH 367
Cdd:cd03822   309 EELLADGRGVLVPFDDPSAIAEAILRL-LEDDERRQAIAERAYAYARAMTWESIADRYLRLFN 370
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
197-368 6.91e-04

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: 41.39  E-value: 6.91e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 197 GRWSVNKGLIETLELLQAALKRDPQWRLIIAGrEYDLNEADlrKAIAERGlQDKVQLSMSPSQEQLRALMQQAQFFVCLS 276
Cdd:cd03791   301 GRLTEQKGVDLILDALPELLEEGGQLVVLGSG-DPEYEQAF--RELAERY-PGKVAVVIGFDEALAHRIYAGADFFLMPS 376
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 277 RHEGFGIAAVEAMSAGLIPI------LSDIPPFVRLASESGQGVIVNRDRIEAAADQVQ-ALAL-QSDSDFDTRRSASMA 348
Cdd:cd03791   377 RFEPCGLVQMYAMRYGTLPIvrrtggLADTVFDYDPETGEGTGFVFEDYDAEALLAALRrALALyRNPELWRKLQKNAMK 456
                         170       180
                  ....*....|....*....|
gi 1275110346 349 yvSRYDWKHVVGRYVDEYHD 368
Cdd:cd03791   457 --QDFSWDKSAKEYLELYRS 474
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
216-299 2.58e-03

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: 39.35  E-value: 2.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 216 LKRDPQWRLIIAGreydlnEADLRK----AIAERGLQDKVQLSMSPSQeqLRALMQQAQFFVCLSRHEGFGIAAVEAMSA 291
Cdd:cd04951   214 ILSKNDFKLLIAG------DGPLRNelerLICNLNLVDRVILLGQISN--ISEYYNAADLFVLSSEWEGFGLVVAEAMAC 285

                  ....*...
gi 1275110346 292 GLIPILSD 299
Cdd:cd04951   286 ERPVVATD 293
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
166-304 7.41e-03

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: 38.20  E-value: 7.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1275110346 166 PARLRVIENGVDVEKYAGRGATTPGR---TMLYFGRWSVNKGLIETLELLQAALKRDPQWRLIIAGrEYDLnEADLRKAI 242
Cdd:cd03799   147 EKKIIVHRSGIDCNKFRFKPRYLPLDgkiRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIG-DGDL-KEQLQQLI 224
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1275110346 243 AERGLQDKVQLSMSPSQEQLRALMQQAQFFVCLS------RHEGFGIAAVEAMSAGLiPILSD----IPPFV 304
Cdd:cd03799   225 QELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGL-PVISTehggIPELV 295
 
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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