NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1210146927|dbj|BAY66028|]
View 

group 1 glycosyl transferase [Calothrix brevissima NIES-22]

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
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

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 ...
 14-354 3.92e-33

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: 128.04  E-value: 3.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  14 GSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLENEGIH-SYCLKFEQDALPNIL--------QWSPDIVHIH----- 79
Cdd:cd03801    15 GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVpLLPSLAALLRARRLLrelrpllrLRKFDVVHAHgllaa 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  80 -----RAGMYDKKVNQIIIDLKKQINPLIL--ETNFFSRVDYKIppGYIDLHLHLTEWCLWKWLQWSSVLGYKPlaSVLP 152
Cdd:cd03801    95 llaalLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALL--RRADAVIAVSEALRDELRALGGIPPEKI--VVIP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 153 NSVITDAFYRSRnedivakKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSIQEKIKKLP 232
Cdd:cd03801   171 NGVDLERFSPPL-------RRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAELEELE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 233 TKIRQKVFVISPVFDDcELRLLYSMMDVMLHASRiGESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHTGIVVNN 312
Cdd:cd03801   244 LGLGDRVRFLGFVPDE-ELPALYAAADVFVLPSR-YEGFGLVVLEAMAAGLPVVATDVGG----LPEVVEDGEGGLVVPP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1210146927 313 QN--AFIEAMIKIAGNYEQAALLGKNGRNQILDKFDNSYICSRL 354
Cdd:cd03801   318 DDveALADALLRLLADPELRARLGRAARERVAERFSWERVAERL 361
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 14-354 3.92e-33

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: 128.04  E-value: 3.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  14 GSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLENEGIH-SYCLKFEQDALPNIL--------QWSPDIVHIH----- 79
Cdd:cd03801    15 GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVpLLPSLAALLRARRLLrelrpllrLRKFDVVHAHgllaa 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  80 -----RAGMYDKKVNQIIIDLKKQINPLIL--ETNFFSRVDYKIppGYIDLHLHLTEWCLWKWLQWSSVLGYKPlaSVLP 152
Cdd:cd03801    95 llaalLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALL--RRADAVIAVSEALRDELRALGGIPPEKI--VVIP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 153 NSVITDAFYRSRnedivakKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSIQEKIKKLP 232
Cdd:cd03801   171 NGVDLERFSPPL-------RRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAELEELE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 233 TKIRQKVFVISPVFDDcELRLLYSMMDVMLHASRiGESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHTGIVVNN 312
Cdd:cd03801   244 LGLGDRVRFLGFVPDE-ELPALYAAADVFVLPSR-YEGFGLVVLEAMAAGLPVVATDVGG----LPEVVEDGEGGLVVPP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1210146927 313 QN--AFIEAMIKIAGNYEQAALLGKNGRNQILDKFDNSYICSRL 354
Cdd:cd03801   318 DDveALADALLRLLADPELRARLGRAARERVAERFSWERVAERL 361
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 180-340 3.39e-17

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: 78.47  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 180 DDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSiQEKIKKLPTK--IRQKVFVISPVfDDCELRLLYSM 257
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEE-EKRLKKLAEKlgLGDNVIFLGFV-SDEDLPELLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 258 MDVMLHASRIgESFGIVLAESLLCETPIITlsspAKDNSQVEVVEHNHTGIVV--NNQNAFIEAMIKIAGNYEQAALLGK 335
Cdd:pfam00534  79 ADVFVLPSRY-EGFGIVLLEAMACGLPVIA----SDVGGPPEVVKDGETGFLVkpNNAEALAEAIDKLLEDEELRERLGE 153


                  ....*
gi 1210146927 336 NGRNQ 340
Cdd:pfam00534 154 NARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 251-362 3.67e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 74.26  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 251 LRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHTGIVVNNQN--AFIEAMIKIAGNYE 328
Cdd:COG0438    14 LEALLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGG----LPEVIEDGETGLLVPPGDpeALAEAILRLLEDPE 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1210146927 329 QAALLGKNGRNQILDKFDNSYICSRL-NILCKLLS 362
Cdd:COG0438    89 LRRRLGEAARERAEERFSWEAIAERLlALYEELLA 123
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
149-345 1.53e-03

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 40.54  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 149 SVLPNSvITDAFYRSRNEDIvaKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPP------- 221
Cdd:PRK15484  164 SIVPNG-FCLETYQSNPQPN--LRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPtasskge 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 222 -PSIQEKIKKLPTKIRQKVFVISPVFDDcELRLLYSMMDVMLHASRIGESFGIVLAESLLCETPIITlsspAKDNSQVEV 300
Cdd:PRK15484  241 kAAYQKKVLEAAKRIGDRCIMLGGQPPE-KMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLA----STKGGITEF 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1210146927 301 VEHNHTGIVVN---NQNAFIEAMIKIAGNYEQAAlLGKNGRNQILDKF 345
Cdd:PRK15484  316 VLEGITGYHLAepmTSDSIISDINRTLADPELTQ-IAEQAKDFVFSKY 362
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 14-354 3.92e-33

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: 128.04  E-value: 3.92e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  14 GSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLENEGIH-SYCLKFEQDALPNIL--------QWSPDIVHIH----- 79
Cdd:cd03801    15 GAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVpLLPSLAALLRARRLLrelrpllrLRKFDVVHAHgllaa 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  80 -----RAGMYDKKVNQIIIDLKKQINPLIL--ETNFFSRVDYKIppGYIDLHLHLTEWCLWKWLQWSSVLGYKPlaSVLP 152
Cdd:cd03801    95 llaalLALLLGAPLVVTLHGAEPGRLLLLLaaERRLLARAEALL--RRADAVIAVSEALRDELRALGGIPPEKI--VVIP 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 153 NSVITDAFYRSRnedivakKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSIQEKIKKLP 232
Cdd:cd03801   171 NGVDLERFSPPL-------RRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAELEELE 243

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 233 TKIRQKVFVISPVFDDcELRLLYSMMDVMLHASRiGESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHTGIVVNN 312
Cdd:cd03801   244 LGLGDRVRFLGFVPDE-ELPALYAAADVFVLPSR-YEGFGLVVLEAMAAGLPVVATDVGG----LPEVVEDGEGGLVVPP 317

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....
gi 1210146927 313 QN--AFIEAMIKIAGNYEQAALLGKNGRNQILDKFDNSYICSRL 354
Cdd:cd03801   318 DDveALADALLRLLADPELRARLGRAARERVAERFSWERVAERL 361
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 11-345 1.44e-18

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: 86.56  E-value: 1.44e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  11 EYRGSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLENeGIHSYCLK-----FEQDALPN------ILQWSPDIVHIH 79
Cdd:cd03795    12 DIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEEN-GIRIHRVKsflnvASTPFSPSyikrfkKLAKEYDIIHYH 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  80 RA----------GMYDKKV-----NQIIID--LKKQINPliLETNFFSRVDYKIP--PGYidlhlhltewclwkwLQWSS 140
Cdd:cd03795    91 FPnpladlllffSGAKKPVvvhwhSDIVKQkkLLKLYKP--LMTRFLRRADRIIAtsPNY---------------VETSP 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 141 VL-GYKPLASVLPnSVITDAFYRSRNEDIVAKKQQIGIPKDDFVFGRVgsyCESKWHPVIINAFKAvaqkvNNISLVLVA 219
Cdd:cd03795   154 TLrEFKNKVRVIP-LGIDKNVYNIPRVDFENIKREKKGKKIFLFIGRL---VYYKGLDYLIEAAQY-----LNYPIVIGG 224

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 220 PPPsIQEKIKKLPTK-IRQKVFVISPVfDDCELRLLYSMMDVMLHASRI-GESFGIVLAESLLCETPIItlsSPAKDNSQ 297
Cdd:cd03795   225 EGP-LKPDLEAQIELnLLDNVKFLGRV-DDEEKVIYLHLCDVFVFPSVLrSEAFGIVLLEAMMCGKPVI---STNIGTGV 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1210146927 298 VEVVEHNHTGIVVNNQN--AFIEAMIKIAGNYEQAALLGKNGRNQILDKF 345
Cdd:cd03795   300 PYVNNNGETGLVVPPKDpdALAEAIDKLLSDEELRESYGENAKKRFEELF 349
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 2-346 1.78e-17

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


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 83.52  E-value: 1.78e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927   2 KYLTILDNLEYRGSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLENEGIHSYCLKFEQDALP--------NILQWSP 73
Cdd:cd03807     1 KVAHVITGLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLGLSSGKDPgvllrlakLIRKRNP 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  74 DIVHIHragMYDKKVNQIIIDLKKQINPLIletnfFSRVDYKIPPgyiDLHLHLTEWCLWKWLqWSSVL----------- 142
Cdd:cd03807    81 DVVHTW---MYHADLIGGLAAKLAGGVKVI-----WSVRSSNIPQ---RLTRLVRKLCLLLSK-FSPATvanssavaefh 148

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 143 ---GYKPLAS-VLPNSVITDAFYRSRNEDIvAKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLV 218
Cdd:cd03807   149 qeqGYAKNKIvVIYNGIDLFKLSPDDASRA-RARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLLLV 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 219 APPPS---IQEKIKKLptKIRQKVFVISPVFDdceLRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIITLSSPakDN 295
Cdd:cd03807   228 GRGPErpnLERLLLEL--GLEDRVHLLGERSD---VPALLPAMDIFVLSSRT-EGFPNALLEAMACGLPVVATDVG--GA 299

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1210146927 296 SqvEVVEhNHTGIVV--NNQNAFIEAMIKIAGNYEQAALLGKNGRNQILDKFD 346
Cdd:cd03807   300 A--ELVD-DGTGFLVpaGDPQALADAIRALLEDPEKRARLGRAARERIANEFS 349
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 180-340 3.39e-17

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: 78.47  E-value: 3.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 180 DDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSiQEKIKKLPTK--IRQKVFVISPVfDDCELRLLYSM 257
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEE-EKRLKKLAEKlgLGDNVIFLGFV-SDEDLPELLKI 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 258 MDVMLHASRIgESFGIVLAESLLCETPIITlsspAKDNSQVEVVEHNHTGIVV--NNQNAFIEAMIKIAGNYEQAALLGK 335
Cdd:pfam00534  79 ADVFVLPSRY-EGFGIVLLEAMACGLPVIA----SDVGGPPEVVKDGETGFLVkpNNAEALAEAIDKLLEDEELRERLGE 153


                  ....*
gi 1210146927 336 NGRNQ 340
Cdd:pfam00534 154 NARKR 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 251-362 3.67e-16

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 74.26  E-value: 3.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 251 LRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHTGIVVNNQN--AFIEAMIKIAGNYE 328
Cdd:COG0438    14 LEALLAAADVFVLPSRS-EGFGLVLLEAMAAGLPVIATDVGG----LPEVIEDGETGLLVPPGDpeALAEAILRLLEDPE 88

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1210146927 329 QAALLGKNGRNQILDKFDNSYICSRL-NILCKLLS 362
Cdd:COG0438    89 LRRRLGEAARERAEERFSWEAIAERLlALYEELLA 123
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 19-339 9.03e-16

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: 78.47  E-value: 9.03e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  19 AQNYSIGMKNLGHEVKVLT---------INGLGNRADFLENEGIHSYCLKF-EQDALPNILQ-WSPDIVHIH------RA 81
Cdd:cd03817    20 VRNLARALEKRGHEVYVITpsdpgaedeEEVVRYRSFSIPIRKYHRQHIPFpFKKAVIDRIKeLGPDIIHTHtpfslgKL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  82 GMYDKKVNQI----------------IIDLKKQINPLI--LETNFFSRVDYKIPPgyidlhlhlTEWCLWKWLQwssvLG 143
Cdd:cd03817   100 GLRIARKLKIpivhtyhtmyedylhyIPKGKLLVKAVVrkLVRRFYNHTDAVIAP---------SEKIKDTLRE----YG 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 144 YKPLASVLPNSVITDAFYRsrnEDIVAKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKvNNISLVLVAPPP- 222
Cdd:cd03817   167 VKGPIEVIPNGIDLDKFEK---PLNTEERRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPe 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 223 --SIQEKIKKLptKIRQKVFVISPVFDDcELRLLYSMMDVMLHASrIGESFGIVLAESLLCETPIITLSSPAKDnsqvEV 300
Cdd:cd03817   243 reELKELAREL--GLADKVIFTGFVPRE-ELPEYYKAADLFVFAS-TTETQGLVYLEAMAAGLPVVAAKDPAAS----EL 314

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1210146927 301 VEHNHTGIVVNNQNAFI-EAMIKIAGNYEQAALLGKNGRN 339
Cdd:cd03817   315 VEDGENGFLFEPNDETLaEKLLHLRENLELLRKLSKNAEI 354
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 171-354 1.58e-15

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


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 77.64  E-value: 1.58e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 171 KKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPS---IQEKIKKLptKIRQKVFVISPVFD 247
Cdd:cd03808   179 QYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELenpSEILIEKL--GLEGRIEFLGFRSD 256

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 248 dceLRLLYSMMDVMLHASRiGESFGIVLAESLLCETPIITLSSPAKDnsqvEVVEHNHTGIVVNNQN--AFIEAMIKIAG 325
Cdd:cd03808   257 ---VPELLAESDVFVLPSY-REGLPRSLLEAMAAGRPVITTDVPGCR----ELVIDGVNGFLVPPGDveALADAIEKLIE 328

                         170       180
                  ....*....|....*....|....*....
gi 1210146927 326 NYEQAALLGKNGRNQILDKFDNSYICSRL 354
Cdd:cd03808   329 DPELRKEMGEAARKRVEEKFDEEKVVNKL 357
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
182-326 4.08e-15

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 71.77  E-value: 4.08e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 182 FVFGRVGSYCE-SKWHPVIINAFKAVAQKVNNISLVLV--APPPSIQEKIKKLPtkirQKVFVISPVFDdceLRLLYSMM 258
Cdd:pfam13692   2 PVILFVGRLHPnVKGVDYLLEAVPLLRKRDNDVRLVIVgdGPEEELEELAAGLE----DRVIFTGFVED---LAELLAAA 74

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 259 DVMLHASRiGESFGIVLAESLLCETPIITLSSPAkdnsQVEVVeHNHTGIVVNNQN--AFIEAMIKIAGN 326
Cdd:pfam13692  75 DVFVLPSL-YEGFGLKLLEAMAAGLPVVATDVGG----IPELV-DGENGLLVPPGDpeALAEAILRLLED 138
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 2-321 5.07e-15

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: 75.86  E-value: 5.07e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927   2 KYLTILDNLEYRGSQRVAQNYSIGMKNLGHEVKVLTINGlGNRADFLENEGIHSYCLKFEQDAL-------------PNI 68
Cdd:cd03811     1 KILFVIPSLSGGGAERVLLNLANALDKRGYDVTLVLLRD-EGDLDKQLNGDVKLIRLLIRVLKLiklgllkailklkRIL 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  69 LQWSPDIVHIHRagmyDKKVNQIIIDLKKQINPLILETNFFSRVDYKIPPGY--------IDLHLHLTEWCLwKWLQwSS 140
Cdd:cd03811    80 KRAKPDVVISFL----GFATYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLlklklykkADKIVCVSKGIK-EDLI-RL 153

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 141 VLGYKPLASVLPNSVITDAFyrsrneDIVAKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAP 220
Cdd:cd03811   154 GPSPPEKIEVIYNPIDIDRI------RALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGD 227

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 221 PP---SIQEKIKKLptKIRQKVFV---ISPVFDdcelrlLYSMMDVMLHASRIgESFGIVLAESLLCETPIItlSSPAKD 294
Cdd:cd03811   228 GPlreELEKLAKEL--GLAERVIFlgfQSNPYP------YLKKADLFVLSSRY-EGFPNVLLEAMALGTPVV--STDCPG 296

                         330       340
                  ....*....|....*....|....*..
gi 1210146927 295 NSqvEVVEHNHTGIVVNNQNAFIEAMI 321
Cdd:cd03811   297 PR--EILDDGENGLLVPDGDAAALAGI 321
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 11-346 1.53e-14

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: 74.71  E-value: 1.53e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  11 EYRGSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLEN-------EGIHS------------YCLKFEQDALPNILQw 71
Cdd:cd03821    12 KAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENgryippqDGFASipllrqgagrtdFSPGLPNWLRRNLRE- 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  72 sPDIVHIHraGMYDKKVNQIIIDLKKQINPLIL-------ETNFFSRVDYKIPPGYIDLHLHLTEWCL-----WKWLQWS 139
Cdd:cd03821    91 -YDVVHIH--GVWTYTSLAACKLARRRGIPYVVsphgmldPWALQQKHWKKRIALHLIERRNLNNAALvhftsEQEADEL 167

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 140 SVLGYKPLASVLPNSVITDaFYRSRNEDIvakkQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVA 219
Cdd:cd03821   168 RRFGLEPPIAVIPNGVDIP-EFDPGLRDR----RKHNGLEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAG 242

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 220 PPPSIQEKIKKLPTK--IRQKVFVISPVFDDCELRLLYSMmDVMLHASRiGESFGIVLAESLLCETPIITLSSPAKDnsq 297
Cdd:cd03821   243 PDDGAYPAFLQLQSSlgLGDRVTFTGPLYGEAKWALYASA-DLFVLPSY-SENFGNVVAEALACGLPVVITDKCGLS--- 317

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1210146927 298 vEVVEHNHTGIVVNNQNAFIEAMIKIAGNYEQAALLGKNGRN--QILDKFD 346
Cdd:cd03821   318 -ELVEAGCGVVVDPNVSSLAEALAEALRDPADRKRLGEMARRarQVEENFS 367
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 134-353 8.84e-14

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


Pssm-ID: 340851 [Multi-domain]  Cd Length: 364  Bit Score: 72.36  E-value: 8.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 134 KWL----QWSSVLGYKPlASVLPNSVITDAFYRSRNEDIvakKQQIGIPKDDFVFGRVGSYCESKWHPV--IINAFKAVA 207
Cdd:cd03825   146 RWLadmvRRSPLLKGLP-VVVIPNGIDTEIFAPVDKAKA---RKRLGIPQDKKVILFGAESVTKPRKGFdeLIEALKLLA 221

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 208 QKvNNISLVLVAPPPsiqEKIKKLPTKIRqKVFVISpvfDDCELRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIIt 287
Cdd:cd03825   222 TK-DDLLLVVFGKND---PQIVILPFDII-SLGYID---DDEQLVDIYSAADLFVHPSLA-DNLPNTLLEAMACGTPVV- 291

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1210146927 288 lsspAKDNSQV-EVVEHNHTGIVVNNQ--NAFIEAMIKIAGNYEQAALLGKNGRNQILDKFDNSYICSR 353
Cdd:cd03825   292 ----AFDTGGSpEIVQHGVTGYLVPPGdvQALAEAIEWLLANPKERESLGERARALAENHFDQRVQAQR 356
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 151-346 3.14e-11

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


Pssm-ID: 340857 [Multi-domain]  Cd Length: 360  Bit Score: 64.39  E-value: 3.14e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 151 LPNSVITDAFYRSrNEDIVAKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPP---SIQEK 227
Cdd:cd04951   159 VYNGIDLNKFKKD-INVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPlrnELERL 237

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 228 IKKLptKIRQKVFVISPVFDDCElrlLYSMMDVMLHASRiGESFGIVLAESLLCETPIITLSSpakdNSQVEVVEHNHTG 307
Cdd:cd04951   238 ICNL--NLVDRVILLGQISNISE---YYNAADLFVLSSE-WEGFGLVVAEAMACERPVVATDA----GGVAEVVGDHNYV 307

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1210146927 308 IVVNNQNAFIEAMIKIAGNYEQAALLGKNGRNQILDKFD 346
Cdd:cd04951   308 VPVSDPQLLAEKIKEIFDMSDEERDILGNKNEYIAKNFS 346
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 14-323 1.38e-09

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


Pssm-ID: 340850 [Multi-domain]  Cd Length: 357  Bit Score: 59.26  E-value: 1.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  14 GSQRVAQNYSIGMKNLGHEVKVLTINGLGNRADFLENEGIHSYCLKFEQDALPNILQWSPDIVHiHRAGMYDKkVNQIII 93
Cdd:cd03823    16 GAEISVHDLAEALVAEGHEVAVLTAGVGPPGQATVARSVVRYRRAPDETLPLALKRRGYELFET-YNPGLRRL-LARLLE 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927  94 DLKkqinPLILETNFFSRV---------DYKIP-------PGYIDLHLHL-----------TEWCLWKWLQWssvLGYKP 146
Cdd:cd03823    94 DFR----PDVVHTHNLSGLgaslldaarDLGIPvvhtlhdYWLLCPRQFLfkkggdavlapSRFTANLHEAN---GLFSA 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 147 LASVLPNSVITDafyrsrnediVAKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKvnNISLVLVAPPPSIQE 226
Cdd:cd03823   167 RISVIPNAVEPD----------LAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEAFKRLPRE--DIELVIAGHGPLSDE 234

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 227 KIKKLPTKIRQKvfvisPVFDDCELRLLYSMMDVMLHASRIGESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHT 306
Cdd:cd03823   235 RQIEGGRRIAFL-----GRVPTDDIKDFYEKIDVLVVPSIWPEPFGLVVREAIAAGLPVIASDLGG----IAELIQPGVN 305

                         330
                  ....*....|....*....
gi 1210146927 307 GIVV--NNQNAFIEAMIKI 323
Cdd:cd03823   306 GLLFapGDAEDLAAAMRRL 324
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 148-315 1.87e-09

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: 58.93  E-value: 1.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 148 ASVLPNSVITdAFYRSRNEdivakkqQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSiQEK 227
Cdd:cd03798   175 VDVIPNGVDP-ARFQPEDR-------GLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVVLLIVGDGPL-REA 245

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 228 IKKL--PTKIRQKVFVISPVfDDCELRLLYSMMDVMLHASRiGESFGIVLAESLLCETPIItlsspAKDNSQV-EVVEHN 304
Cdd:cd03798   246 LRALaeDLGLGDRVTFTGRL-PHEQVPAYYRACDVFVLPSR-HEGFGLVLLEAMACGLPVV-----ATDVGGIpEVVGDP 318

                         170
                  ....*....|.
gi 1210146927 305 HTGIVVNNQNA 315
Cdd:cd03798   319 ETGLLVPPGDA 329
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 150-346 3.85e-09

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: 58.13  E-value: 3.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 150 VLPNSVITDAFYRSRNEDIvakKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNiSLVLVAPPP---SIQE 226
Cdd:cd04962   168 VIHNFIDEDVFKRKPAGAL---KRRLLAPPDEKVVIHVSNFRPVKRIDDVVRVFARVRRKIPA-KLLLVGDGPervPAEE 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 227 KIKKLptKIRQKVFVISPvFDDCELrlLYSMMDVMLHASRIgESFGIVLAESLLCETPIITlsspakdnSQV----EVVE 302
Cdd:cd04962   244 LAREL--GVEDRVLFLGK-QDDVEE--LLSIADLFLLPSEK-ESFGLAALEAMACGVPVVS--------SNAggipEVVK 309

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1210146927 303 HNHTGIVVN--NQNAFIEAMIKIAGNYEQAALLGKNGRNQILDKFD 346
Cdd:cd04962   310 HGETGFLSDvgDVDAMAKSALSILEDDELYNRMGRAARKRAAERFD 355
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 138-310 6.53e-09

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: 56.26  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 138 WSSVLGYKPLASVLPNSVITDAFYRSRNEDIVAKKQQI---GIPKDDFVFgrVGSYCESKWHPVIINAFKAVAQKVNNIS 214
Cdd:cd01635    66 AALAALLAARLLGIPIVVTVHGPDSLESTRSELLALARllvSLPLADKVS--VGRLVPEKGIDLLLEALALLKARLPDLV 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 215 LVLV---APPPSIQEKIKKLptKIRQKVFVISPVFDDCELRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIITlssp 291
Cdd:cd01635   144 LVLVgggGEREEEEALAAAL--GLLERVVIIGGLVDDEVLELLLAAADVFVLPSRS-EGFGLVLLEAMAAGKPVIA---- 216

                         170
                  ....*....|....*....
gi 1210146927 292 AKDNSQVEVVEHNHTGIVV 310
Cdd:cd01635   217 TDVGGIPEFVVDGENGLLV 235
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 150-340 2.07e-08

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: 55.82  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 150 VLPNSVITDAFyrsRNEDIVAKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFkAVAQKVNNISLVLVAPPP---SIQE 226
Cdd:cd03819   154 VIPNGVDTDRF---PPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLVDAA-AELKDEPDFRLLVAGDGPerdEIRR 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 227 KIKKLptKIRQKVFVISPVFDdceLRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIITLSSPAkdnsQVEVVEHNHT 306
Cdd:cd03819   230 LVERL--GLRDRVTFTGFRED---VPAALAASDVVVLPSLH-EEFGRVALEAMACGTPVVATDVGG----AREIVVHGRT 299

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1210146927 307 GIVVNNQN--AFIEAMIKIAGNYEQAALLGKNGRNQ 340
Cdd:cd03819   300 GLLVPPGDaeALADAIRAAKLLPEAREKLQAAAALT 335
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 149-287 3.71e-08

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: 55.06  E-value: 3.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 149 SVLPNSVitDAFYRSRNEDIVAKKQQIgiPKDDFVFgRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPPSIQEKI 228
Cdd:cd03809   165 VVIPLGV--DPSFFPPESAAVLIAKYL--LPEPYFL-YVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGGKGWEDEEL 239

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1210146927 229 KKL--PTKIRQKVFVISPVfDDCELRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIIT 287
Cdd:cd03809   240 LDLvkKLGLGGRVRFLGYV-SDEDLPALYRGARAFVFPSLY-EGFGLPVLEAMACGTPVIA 298
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 187-353 1.91e-07

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: 52.62  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 187 VGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPP---SIQEKIKKLptKIRQKVFVISPVFDdceLRLLYSMMDVMLH 263
Cdd:cd03820   187 VGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPereELEKLIDKL--GLEDRVKLLGPTKN---IAEEYANSSIFVL 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 264 ASRIgESFGIVLAESLLCETPIITLSSPAKDNsqvEVVEHNHTGIVVNNQN--AFIEAMIKIAGNYEQAALLGKNGRnQI 341
Cdd:cd03820   262 SSRY-EGFPMVLLEAMAYGLPIISFDCPTGPS---EIIEDGENGLLVPNGDvdALAEALLRLMEDEELRKKMGKNAR-KN 336

                         170
                  ....*....|..
gi 1210146927 342 LDKFDNSYICSR 353
Cdd:cd03820   337 AERFSIEKIIKQ 348
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
 269-354 1.85e-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: 46.81  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 269 ESFGIVLAESLLCETPIITLSS--PakdnsqVEVVEHNHTG-IVVNNQNAFIEAMIKIAGNYEQAALLGKNGRNQILDKF 345
Cdd:cd03805   310 EHFGIVPLEAMYAGKPVIACNSggP------LETVVEGVTGfLCEPTPEAFAEAMLKLANDPDLADRMGAAGRKRVKEKF 383


                  ....*....
gi 1210146927 346 DNSYICSRL 354
Cdd:cd03805   384 SREAFAERL 392
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 260-324 3.42e-05

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: 45.74  E-value: 3.42e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1210146927 260 VMLHASRIGESFGIVLAESLLCETPIITLS--SPAkdnsqvEVVEHNHTGIVVNNQNAFIEAMIKIA 324
Cdd:cd03802   242 ALLFPINWDEPFGLVMIEAMACGTPVIAYRrgGLP------EVIQHGETGFLVDSVEEMAEAIANID 302
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 149-354 4.23e-05

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: 45.41  E-value: 4.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 149 SVLPNSVITDAFYRSRNEDIVAKKqqigIPKDDFVFGRVGSYceSKWH--PVIINAFKAVAQKvNNISLVLVAPPPSIQE 226
Cdd:cd03794   189 IVIPNWADLEEFKPPPKDELRKKL----GLDDKFVVVYAGNI--GKAQglETLLEAAERLKRR-PDIRFLFVGDGDEKER 261

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 227 KIKKLPTKIRQKVFVISPVFDDcELRLLYSMMDVML------HASRIgeSFGIVLAESLLCETPIItLSSPAkdNSQVEV 300
Cdd:cd03794   262 LKELAKARGLDNVTFLGRVPKE-EVPELLSAADVGLvplkdnPANRG--SSPSKLFEYMAAGKPIL-ASDDG--GSDLAV 335

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1210146927 301 VEHNhTGIVVNNQN--AFIEAMIKIAGNYEQAALLGKNGRNQILDKFDNSYICSRL 354
Cdd:cd03794   336 EING-CGLVVEPGDpeALADAILELLDDPELRRAMGENGRELAEEKFSREKLADRL 390
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 176-294 6.24e-05

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: 44.97  E-value: 6.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 176 GIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPPP---SIQEKIKKLptKIRQKVFVISPVFDDCElr 252
Cdd:cd03812   186 LILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGElkeKIKEKVKEL--GLEDKVIFLGFRNDVSE-- 261

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1210146927 253 lLYSMMDVMLHASRIgESFGIVLAESLLCETPIITLSSPAKD 294
Cdd:cd03812   262 -ILSAMDVFLFPSLY-EGLPLVAVEAQASGLPCLLSDTITKE 301
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 137-345 5.81e-04

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: 41.84  E-value: 5.81e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 137 QWSSVLGYKPLASVLPNSVITDAFY-RSRNEDIVAkkqQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISL 215
Cdd:cd03800   178 LISLYGADPSRINVVPPGVDLERFFpVDRAEARRA---RLLLPPDKPVVLALGRLDPRKGIDTLVRAFAQLPELRELANL 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 216 VLVA-PPPSIQEKIKKLPTKIRQ-----KVFVISPVFDDCELRLLYSMMDVMLHASRIgESFGIVLAESLLCETPIITls 289
Cdd:cd03800   255 VLVGgPSDDPLSMDREELAELAEelgliDRVRFPGRVSRDDLPELYRAADVFVVPSLY-EPFGLTAIEAMACGTPVVA-- 331

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1210146927 290 spAKDNSQVEVVEHNHTGIVVN--NQNAFIEAMIKIAGNYEQAALLGKNGRNQILDKF 345
Cdd:cd03800   332 --TAVGGLQDIVRDGRTGLLVDphDPEALAAALRRLLDDPALWQRLSRAGLERARAHY 387
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 193-346 9.76e-04

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


Pssm-ID: 340823 [Multi-domain]  Cd Length: 378  Bit Score: 41.15  E-value: 9.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 193 SKWHPVIINAFKAVAQKVNNISLVLVAPPPS-------IQEKIKKLPtKIRQKVFVISPVFDDCELRLLYSMMDVMLHAS 265
Cdd:cd03792   209 SKDPLGVIDAYKLFKRRAEEPQLVICGHGAVddpegsvVYEEVMEYA-GDDHDIHVLRLPPSDQEINALQRAATVVLQLS 287

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 266 rIGESFGIVLAESLLCETPIITL---SSPakdnSQVEvveHNHTGIVVN-NQNAFIEAMIKIAgNYEQAALLGKNGRNQI 341
Cdd:cd03792   288 -TREGFGLTVSEALWKGKPVIATpagGIP----LQVI---DGETGFLVNsVEGAAVRILRLLT-DPELRRKMGLAAREHV 358


                  ....*
gi 1210146927 342 LDKFD 346
Cdd:cd03792   359 RDNFL 363
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
149-345 1.53e-03

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 40.54  E-value: 1.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 149 SVLPNSvITDAFYRSRNEDIvaKKQQIGIPKDDFVFGRVGSYCESKWHPVIINAFKAVAQKVNNISLVLVAPP------- 221
Cdd:PRK15484  164 SIVPNG-FCLETYQSNPQPN--LRQQLNISPDETVLLYAGRISPDKGILLLMQAFEKLATAHSNLKLVVVGDPtasskge 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1210146927 222 -PSIQEKIKKLPTKIRQKVFVISPVFDDcELRLLYSMMDVMLHASRIGESFGIVLAESLLCETPIITlsspAKDNSQVEV 300
Cdd:PRK15484  241 kAAYQKKVLEAAKRIGDRCIMLGGQPPE-KMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLA----STKGGITEF 315

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1210146927 301 VEHNHTGIVVN---NQNAFIEAMIKIAGNYEQAAlLGKNGRNQILDKF 345
Cdd:PRK15484  316 VLEGITGYHLAepmTSDSIISDINRTLADPELTQ-IAEQAKDFVFSKY 362
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH