NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1376905710|ref|XP_002963408|]
View 

uncharacterized protein LOC9643618 [Selaginella moellendorffii]

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 ...
 109-509 9.40e-54

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: 185.82  E-value: 9.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 109 RIALFVKKWPVGgvPGGLERHALTLHRNLAARGHEIHVYTSAAAGSDnpeellddqqdHGERGLLHVHFSRPNAGGGFDY 188
Cdd:cd03801     1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTPADPGEP-----------PEELEDGVIVPLLPSLAALLRA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 189 HRAWDQFlaDNSTHPGGFDIVHSESVALPHW---KAQLLGSNLAASWHGIGYEiihsdlvqdlvrkpgeprsaDLQRSLG 265
Cdd:cd03801    68 RRLLREL--RPLLRLRKFDVVHAHGLLAALLaalLALLLGAPLVVTLHGAEPG--------------------RLLLLLA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 266 ERLTRVADEIKFFPSYRHHVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPsldagsAFRRKYGVPVNAsLVFGAA 345
Cdd:cd03801   126 AERRLLARAEALLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSP------PLRRKLGIPPDR-PVLLFV 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 346 GRLVRDKGHPLLFEAFSRIAARHPGVFLLVAG-HGPWGDRYRE----LAPNAKTLGPMDPAHLADFYNALDVFVNPTlRS 420
Cdd:cd03801   199 GRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEElelgLGDRVRFLGFVPDEELPALYAAADVFVLPS-RY 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 421 QGLDHTLLEAMQCGKPLLATHFSSITWSVVVSSDFGHTFSPNVDSLEQAMEAVIAQgRDTMRRKGELCRDYASLMFTATK 500
Cdd:cd03801   278 EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLAD-PELRARLGRAARERVAERFSWER 356


                  ....*....
gi 1376905710 501 MGAAYERLF 509
Cdd:cd03801   357 VAERLLDLY 365
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 109-509 9.40e-54

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: 185.82  E-value: 9.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 109 RIALFVKKWPVGgvPGGLERHALTLHRNLAARGHEIHVYTSAAAGSDnpeellddqqdHGERGLLHVHFSRPNAGGGFDY 188
Cdd:cd03801     1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTPADPGEP-----------PEELEDGVIVPLLPSLAALLRA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 189 HRAWDQFlaDNSTHPGGFDIVHSESVALPHW---KAQLLGSNLAASWHGIGYEiihsdlvqdlvrkpgeprsaDLQRSLG 265
Cdd:cd03801    68 RRLLREL--RPLLRLRKFDVVHAHGLLAALLaalLALLLGAPLVVTLHGAEPG--------------------RLLLLLA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 266 ERLTRVADEIKFFPSYRHHVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPsldagsAFRRKYGVPVNAsLVFGAA 345
Cdd:cd03801   126 AERRLLARAEALLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSP------PLRRKLGIPPDR-PVLLFV 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 346 GRLVRDKGHPLLFEAFSRIAARHPGVFLLVAG-HGPWGDRYRE----LAPNAKTLGPMDPAHLADFYNALDVFVNPTlRS 420
Cdd:cd03801   199 GRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEElelgLGDRVRFLGFVPDEELPALYAAADVFVLPS-RY 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 421 QGLDHTLLEAMQCGKPLLATHFSSITWSVVVSSDFGHTFSPNVDSLEQAMEAVIAQgRDTMRRKGELCRDYASLMFTATK 500
Cdd:cd03801   278 EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLAD-PELRARLGRAARERVAERFSWER 356


                  ....*....
gi 1376905710 501 MGAAYERLF 509
Cdd:cd03801   357 VAERLLDLY 365
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 341-474 5.46e-18

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 81.17  E-value: 5.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 341 VFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRYRELA------PNAKTLGPMDPAHLADFYNALDVFV 414
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAeklglgDNVIFLGFVSDEDLPELLKIADVFV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376905710 415 NPtLRSQGLDHTLLEAMQCGKPLLATHFSSItwSVVVSSDFGHTF--SPNVDSLEQAMEAVI 474
Cdd:pfam00534  84 LP-SRYEGFGIVLLEAMACGLPVIASDVGGP--PEVVKDGETGFLvkPNNAEALAEAIDKLL 142
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 406-509 2.77e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 63.86  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 406 FYNALDVFVNPTlRSQGLDHTLLEAMQCGKPLLATHFSSITWsVVVSSDFGHTFSP-NVDSLEQAMEAVIAQgRDTMRRK 484
Cdd:COG0438    17 LLAAADVFVLPS-RSEGFGLVLLEAMAAGLPVIATDVGGLPE-VIEDGETGLLVPPgDPEALAEAILRLLED-PELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1376905710 485 GELCRDYASLMFTATKMGAAYERLF 509
Cdd:COG0438    94 GEAARERAEERFSWEAIAERLLALY 118
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
295-475 5.04e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 55.18  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 295 LQTIYE--IPLRNVHTILNGVDESRFrpSLDAGSAFRRKYGVPVNASLVFgAAGRLVRDKGHPLLFEAFSRIAARHPGVF 372
Cdd:PRK15484  150 LKKFYEerLPNADISIVPNGFCLETY--QSNPQPNLRQQLNISPDETVLL-YAGRISPDKGILLLMQAFEKLATAHSNLK 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 373 LLVAG------HGPWGDRYRELAPNAKTLGP-------MDPAHLADFYNALDVFVNPTLRSQGLDHTLLEAMQCGKPLLA 439
Cdd:PRK15484  227 LVVVGdptassKGEKAAYQKKVLEAAKRIGDrcimlggQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLA 306

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1376905710 440 THFSSITWSVVVSSDFGHTFSP-NVDSLEQAMEAVIA 475
Cdd:PRK15484  307 STKGGITEFVLEGITGYHLAEPmTSDSIISDINRTLA 343
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 109-509 9.40e-54

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: 185.82  E-value: 9.40e-54
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 109 RIALFVKKWPVGgvPGGLERHALTLHRNLAARGHEIHVYTSAAAGSDnpeellddqqdHGERGLLHVHFSRPNAGGGFDY 188
Cdd:cd03801     1 KILLLSPELPPP--VGGAERHVRELARALAARGHDVTVLTPADPGEP-----------PEELEDGVIVPLLPSLAALLRA 67

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 189 HRAWDQFlaDNSTHPGGFDIVHSESVALPHW---KAQLLGSNLAASWHGIGYEiihsdlvqdlvrkpgeprsaDLQRSLG 265
Cdd:cd03801    68 RRLLREL--RPLLRLRKFDVVHAHGLLAALLaalLALLLGAPLVVTLHGAEPG--------------------RLLLLLA 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 266 ERLTRVADEIKFFPSYRHHVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPsldagsAFRRKYGVPVNAsLVFGAA 345
Cdd:cd03801   126 AERRLLARAEALLRRADAVIAVSEALRDELRALGGIPPEKIVVIPNGVDLERFSP------PLRRKLGIPPDR-PVLLFV 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 346 GRLVRDKGHPLLFEAFSRIAARHPGVFLLVAG-HGPWGDRYRE----LAPNAKTLGPMDPAHLADFYNALDVFVNPTlRS 420
Cdd:cd03801   199 GRLSPRKGVDLLLEALAKLLRRGPDVRLVIVGgDGPLRAELEElelgLGDRVRFLGFVPDEELPALYAAADVFVLPS-RY 277

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 421 QGLDHTLLEAMQCGKPLLATHFSSITWSVVVSSDFGHTFSPNVDSLEQAMEAVIAQgRDTMRRKGELCRDYASLMFTATK 500
Cdd:cd03801   278 EGFGLVVLEAMAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLAD-PELRARLGRAARERVAERFSWER 356


                  ....*....
gi 1376905710 501 MGAAYERLF 509
Cdd:cd03801   357 VAERLLDLY 365
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 124-440 2.07e-31

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: 125.18  E-value: 2.07e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 124 GGLERHALTLHRNLAARGHEIHVytsaAAGSDNPEELLDDQQDHGERGLLHVHFSRPNAGGGFDYHRAW------DQFLA 197
Cdd:cd03798    14 PGRGIFVRRQVRALSRRGVDVEV----LAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPlrapslAKLLK 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 198 DnsTHPGGFDIVHsesvalPHWkaqLLGSNLAASWHGIGYEI-----IHSDLVQDLVRKPGepRSADLQRSLgERLTRVa 272
Cdd:cd03798    90 R--RRRGPPDLIH------AHF---AYPAGFAAALLARLYGVpyvvtEHGSDINVFPPRSL--LRKLLRWAL-RRAARV- 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 273 deikffpsyrhhVATSDYVGDVLQTiYEIPLRNVHTILNGVDESRFRPSLDAGsafrrkyGVPVNAsLVFGAAGRLVRDK 352
Cdd:cd03798   155 ------------IAVSKALAEELVA-LGVPRDRVDVIPNGVDPARFQPEDRGL-------GLPLDA-FVILFVGRLIPRK 213

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 353 GHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRYR------ELAPNAKTLGPMDPAHLADFYNALDVFVNPTlRSQGLDHT 426
Cdd:cd03798   214 GIDLLLEAFARLAKARPDVVLLIVGDGPLREALRalaedlGLGDRVTFTGRLPHEQVPAYYRACDVFVLPS-RHEGFGLV 292

                         330
                  ....*....|....
gi 1376905710 427 LLEAMQCGKPLLAT 440
Cdd:cd03798   293 LLEAMACGLPVVAT 306
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 123-509 3.08e-30

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: 121.27  E-value: 3.08e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 123 PGGLERHALTLHRNLAARGHEIHVYTSAAAGSDNpEELLDDQqdhgerglLHVHFsrPNAGGGFD---YHRAWDQFLADN 199
Cdd:cd03807    11 VGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLG-EELLAAG--------VPVVC--LGLSSGKDpgvLLRLAKLIRKRN 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 200 SthpggfDIVHSEsvaLPHwkAQLLGSnLAASWHGIGyEIIHSdlvqdlVRKPGEPrsadlqrslgERLTRVADEIKFFP 279
Cdd:cd03807    80 P------DVVHTW---MYH--ADLIGG-LAAKLAGGV-KVIWS------VRSSNIP----------QRLTRLVRKLCLLL 130

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 280 SY--RHHVATSDYVGDVLQTIYeIPLRNVHTILNGVDESRFRPSLDAGSAFRRKYGVPVNAsLVFGAAGRLVRDKGHPLL 357
Cdd:cd03807   131 SKfsPATVANSSAVAEFHQEQG-YAKNKIVVIYNGIDLFKLSPDDASRARARRRLGLAEDR-RVIGIVGRLHPVKDHSDL 208

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 358 FEAFSRIAARHPGVFLLVAGHGPwgdRYRELAPNAKTLGPMDPAHLA-------DFYNALDVFVNPTlRSQGLDHTLLEA 430
Cdd:cd03807   209 LRAAALLVETHPDLRLLLVGRGP---ERPNLERLLLELGLEDRVHLLgersdvpALLPAMDIFVLSS-RTEGFPNALLEA 284

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1376905710 431 MQCGKPLLATHFSSITWSVVVSSDFGHTFSpNVDSLEQAMEAVIAQgRDTMRRKGELCRDYASLMFTATKMGAAYERLF 509
Cdd:cd03807   285 MACGLPVVATDVGGAAELVDDGTGFLVPAG-DPQALADAIRALLED-PEKRARLGRAARERIANEFSIDAMVRRYETLY 361
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 124-440 1.28e-27

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: 113.61  E-value: 1.28e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 124 GGLERHALTLHRNLAARGHEIHVYTSAAAGSDNPEELLDDQqdhgeRGLLHVHFSRPNAGGGFDYHRAWDQFLADNSthp 203
Cdd:cd03811    12 GGAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVK-----LIRLLIRVLKLIKLGLLKAILKLKRILKRAK--- 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 204 ggFDIVHSESVALPHWkaqllgSNLAASWHGIGYEIIHSDLVQDLVRKPgeprsadlqrslgerltRVADEIKFFPSYRH 283
Cdd:cd03811    84 --PDVVISFLGFATYI------VAKLAAARSKVIAWIHSSLSKLYYLKK-----------------KLLLKLKLYKKADK 138

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 284 HVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPSLDAGSAFRRKygvpvnASLVFGAAGRLVRDKGHPLLFEAFSR 363
Cdd:cd03811   139 IVCVSKGIKEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPILNEPE------DGPVILAVGRLDPQKGHDLLIEAFAK 212

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 364 IAARHPGVFLLVAGHGPWGDRYRELA------PNAKTLGPMDPAhlADFYNALDVFVNPTlRSQGLDHTLLEAMQCGKPL 437
Cdd:cd03811   213 LRKKYPDVKLVILGDGPLREELEKLAkelglaERVIFLGFQSNP--YPYLKKADLFVLSS-RYEGFPNVLLEAMALGTPV 289


                  ...
gi 1376905710 438 LAT 440
Cdd:cd03811   290 VST 292
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 118-440 8.66e-25

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: 106.17  E-value: 8.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 118 PVGGVPGGLERHALTLHRNLAARGHEIHVYTSAAAGSDNPEELLDDqqdhGERgLLHVHFsrpnagGGFDY------HRA 191
Cdd:cd03800    15 PGGADTGGQNVYVLELARALAELGYQVDIFTRRISPADPEVVEIAP----GAR-VIRVPA------GPPEYlpkeelWPY 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 192 WDQFLADNSTH----PGGFDIVHSEsvalpHWKAQLLGSnLAASWHGIGY-EIIHS-DLVQDLVRKPGEPRSADLQRSLG 265
Cdd:cd03800    84 LEEFADGLLRFiareGGRYDLIHSH-----YWDSGLVGA-LLARRLGVPLvHTFHSlGRVKYRHLGAQDTYHPSLRITAE 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 266 ERLTRVADEIkffpsyrhhVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPSLDAGsAFRRKYGVPVNASLVFgAA 345
Cdd:cd03800   158 EQILEAADRV---------IASTPQEADELISLYGADPSRINVVPPGVDLERFFPVDRAE-ARRARLLLPPDKPVVL-AL 226

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 346 GRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGhGPWGDRyRELAPNAK--------------TLGPMDPAHLADFYNALD 411
Cdd:cd03800   227 GRLDPRKGIDTLVRAFAQLPELRELANLVLVG-GPSDDP-LSMDREELaelaeelglidrvrFPGRVSRDDLPELYRAAD 304

                         330       340       350
                  ....*....|....*....|....*....|
gi 1376905710 412 VFVNPTL-RSQGLdhTLLEAMQCGKPLLAT 440
Cdd:cd03800   305 VFVVPSLyEPFGL--TAIEAMACGTPVVAT 332
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 109-486 1.21e-23

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: 102.74  E-value: 1.21e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 109 RIALFVKKWP--VGGVpgglERHALTLHRNLAARGHEIHVYTSAAAGSDNPEEllddqqDHGER-------GLLHVHFSR 179
Cdd:cd03817     1 KIAIFTDTYLpqVNGV----ATSVRNLARALEKRGHEVYVITPSDPGAEDEEE------VVRYRsfsipirKYHRQHIPF 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 180 PNAGGGFDYHRAWDqfladnsthpggFDIVHSESvalpHWKAQLLGSNLA--------ASWHGIGYEIIHSdlvqdlVRK 251
Cdd:cd03817    71 PFKKAVIDRIKELG------------PDIIHTHT----PFSLGKLGLRIArklkipivHTYHTMYEDYLHY------IPK 128

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 252 PGEPRSADLQRslgerltrvadEIKFFPSYRHHVAT-SDYVGDVLQtIYEIpLRNVHTILNGVDESRFRPSLDagSAFRR 330
Cdd:cd03817   129 GKLLVKAVVRK-----------LVRRFYNHTDAVIApSEKIKDTLR-EYGV-KGPIEVIPNGIDLDKFEKPLN--TEERR 193

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 331 KYGVPVNA-SLVFgaAGRLVRDKGHPLLFEAFSRIAARhPGVFLLVAGHGPWGDRYRELAPNAK------TLGPMDPAHL 403
Cdd:cd03817   194 KLGLPPDEpILLY--VGRLAKEKNIDFLLRAFAELKKE-PNIKLVIVGDGPEREELKELARELGladkviFTGFVPREEL 270

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 404 ADFYNALDVFVNP-TLRSQGLdhTLLEAMQCGKPLLATHFSSITwSVVVSSDFGHTFSPNVDSLEQAMEAVIAQ--GRDT 480
Cdd:cd03817   271 PEYYKAADLFVFAsTTETQGL--VYLEAMAAGLPVVAAKDPAAS-ELVEDGENGFLFEPNDETLAEKLLHLRENleLLRK 347


                  ....*.
gi 1376905710 481 MRRKGE 486
Cdd:cd03817   348 LSKNAE 353
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 122-440 7.62e-23

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: 99.74  E-value: 7.62e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 122 VPGGLERHALTLHRNLAARGHEIHVYTsaAAGSDNPEELLDDQqdhGERGLLHVHFSRPNAgggfdyhrawdqflADNST 201
Cdd:cd03819     9 EIGGAETYILDLARALAERGHRVLVVT--AGGPLLPRLRQIGI---GLPGLKVPLLRALLG--------------NVRLA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 202 HPGG---FDIVH---SESVALPHWKAQLLGSNLAASWHGigyeiihsdlVQDLVRKPGEPRSAdlQRSLGERltrvadei 275
Cdd:cd03819    70 RLIRrerIDLIHahsRAPAWLGWLASRLTGVPLVTTVHG----------SYLATYHPKDFALA--VRARGDR-------- 129

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 276 kffpsyrhHVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPSLDAgsAFRRKYGVPvNASLVFGAAGRLVRDKGHP 355
Cdd:cd03819   130 --------VIAVSELVRDHLIEALGVDPERIRVIPNGVDTDRFPPEAEA--EERAQLGLP-EGKPVVGYVGRLSPEKGWL 198

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 356 LLFEAFSRIAARhPGVFLLVAGHGPwgdRYRELAPNAKTLGPMDPAHL-------ADFYNALDVFVNPTLRsQGLDHTLL 428
Cdd:cd03819   199 LLVDAAAELKDE-PDFRLLVAGDGP---ERDEIRRLVERLGLRDRVTFtgfredvPAALAASDVVVLPSLH-EEFGRVAL 273

                         330
                  ....*....|..
gi 1376905710 429 EAMQCGKPLLAT 440
Cdd:cd03819   274 EAMACGTPVVAT 285
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 122-506 1.65e-22

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: 98.82  E-value: 1.65e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 122 VPGGLERHALTLHRNLAARGHEIHVytsaaAGSDNpEELLDDQQDHGERgllHVHFSRPNAG--GGFDYH--RAWDQFLA 197
Cdd:cd03808     8 VDGGFQSFRLPLIKALVKKGYEVHV-----IAPDG-DKLSDELKELGVK---VIDIPILRRGinPLKDLKalFKLYKLLK 78

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 198 DNSthpggFDIVHSESValphwKAQLLGSnLAASW----------HGIGYEiihsdlvqdlvrKPGEPRSADLQRSLGER 267
Cdd:cd03808    79 KEK-----PDIVHCHTP-----KPGILGR-LAARLagvpkviytvHGLGFV------------FTEGKLLRLLYLLLEKL 135

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 268 LTRVADEIkFFpsyrhhVATSDYvgDVLQTIYEIPLRNVHTIL-NGVDESRFRPSLDagsafrrkygVPVNASLVFGAAG 346
Cdd:cd03808   136 ALLFTDKV-IF------VNEDDR--DLAIKKGIIKKKKTVLIPgSGVDLDRFQYSPE----------SLPSEKVVFLFVA 196

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 347 RLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRY------RELAPNAKTLGPMDpaHLADFYNALDVFVNPTLRs 420
Cdd:cd03808   197 RLLKDKGIDELIEAAKILKKKGPNVRFLLVGDGELENPSeiliekLGLEGRIEFLGFRS--DVPELLAESDVFVLPSYR- 273

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 421 QGLDHTLLEAMQCGKPLLATHfssI--TWSVVVSSDFGHTFSP-NVDSLEQAMEAVIAQG--RDTMRRKGelcRDYASLM 495
Cdd:cd03808   274 EGLPRSLLEAMAAGRPVITTD---VpgCRELVIDGVNGFLVPPgDVEALADAIEKLIEDPelRKEMGEAA---RKRVEEK 347

                         410
                  ....*....|.
gi 1376905710 496 FTATKMGAAYE 506
Cdd:cd03808   348 FDEEKVVNKLL 358
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 285-509 2.79e-20

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: 92.39  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 285 VATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFRPsLDAGSAfRRKYGVPVNASLV-FGAAGRLVRDKGHPLLFEAfSR 363
Cdd:cd03825   142 VAPSRWLADMVRRSPLLKGLPVVVIPNGIDTEIFAP-VDKAKA-RKRLGIPQDKKVIlFGAESVTKPRKGFDELIEA-LK 218

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 364 IAARHPGVFLLVAGHGPwgdryrelAPNAKTLGPM-------DPAHLADFYNALDVFVNPTlRSQGLDHTLLEAMQCGKP 436
Cdd:cd03825   219 LLATKDDLLLVVFGKND--------PQIVILPFDIislgyidDDEQLVDIYSAADLFVHPS-LADNLPNTLLEAMACGTP 289

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376905710 437 LLATHFSSITwSVVVSSDFGHTFSP-NVDSLEQAMEAVIAQGrDTMRRKGELCRDYASLMFTATKMGAAYERLF 509
Cdd:cd03825   290 VVAFDTGGSP-EIVQHGVTGYLVPPgDVQALAEAIEWLLANP-KERESLGERARALAENHFDQRVQAQRYLELY 361
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 118-485 1.34e-19

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: 90.50  E-value: 1.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 118 PVGGVPGGLERHALTLHRNLAARGHEIHVYtsAAAGSDNPEELLDDQQDHGERGLLHVHFSRpnagggfdyHRAWDQFLA 197
Cdd:cd03809     8 SLAQRLTGIGRYTRELLKALAKNDPDESVL--AVPPLPGELLRLLREYPELSLGVIKIKLWR---------ELALLRWLQ 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 198 DNSTHPGGFDIVHSesvalPHWkaqllgsnlAASWHGIGYEIIHsdLVQDL--VRKPGE-PRSADLQRSLGERLT-RVAD 273
Cdd:cd03809    77 ILLPKKDKPDLLHS-----PHN---------TAPLLLKGCPQVV--TIHDLipLRYPEFfPKRFRLYYRLLLPISlRRAD 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 274 eikffpsyrhHVAT-SDYVGDVLQTIYEIPLRNVHTILNGVDESRFrpSLDAGSAFRRKYGVPVNASLVfgaAGRLVRDK 352
Cdd:cd03809   141 ----------AIITvSEATRDDIIKFYGVPPEKIVVIPLGVDPSFF--PPESAAVLIAKYLLPEPYFLY---VGTLEPRK 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 353 GHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRY-------RELAPNAKTLGPMDPAHLADFYNALDVFVNPTLR-SQGLd 424
Cdd:cd03809   206 NHERLLKAFALLKKQGGDLKLVIVGGKGWEDEElldlvkkLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYeGFGL- 284

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1376905710 425 hTLLEAMQCGKPLLATHFSSItwsVVVSSDFGHTFSP-NVDSLEQAMEAVIAQG--RDTMRRKG 485
Cdd:cd03809   285 -PVLEAMACGTPVIASNISVL---PEVAGDAALYFDPlDPESIADAILRLLEDPslREELIRKG 344
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 341-474 5.46e-18

Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease (Paroxysmal Nocturnal haemoglobinuria). Members of this family transfer activated sugars to a variety of substrates, including glycogen, Fructose-6-phosphate and lipopolysaccharides. Members of this family transfer UDP, ADP, GDP or CMP linked sugars. The eukaryotic glycogen synthases may be distant members of this family.


Pssm-ID: 425737 [Multi-domain]  Cd Length: 158  Bit Score: 81.17  E-value: 5.46e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 341 VFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRYRELA------PNAKTLGPMDPAHLADFYNALDVFV 414
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAeklglgDNVIFLGFVSDEDLPELLKIADVFV 83

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376905710 415 NPtLRSQGLDHTLLEAMQCGKPLLATHFSSItwSVVVSSDFGHTF--SPNVDSLEQAMEAVI 474
Cdd:pfam00534  84 LP-SRYEGFGIVLLEAMACGLPVIASDVGGP--PEVVKDGETGFLvkPNNAEALAEAIDKLL 142
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 285-506 4.66e-17

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: 82.89  E-value: 4.66e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 285 VATSDYVGDVLQTIyEIPLRNVHTILNGVDESRFRPSLDAGSAFRrkygvpvnasLVFgaAGRLVRDKGHPLLFEAFSRI 364
Cdd:cd05844   148 VAVSGFIRDRLLAR-GLPAERIHVHYIGIDPAKFAPRDPAERAPT----------ILF--VGRLVEKKGCDVLIEAFRRL 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 365 AARHPGVFLLVAGHGPWGDRYRELAPNAKT---LGPMDPAHLADFYNALDVFVNPTL-----RSQGLDHTLLEAMQCGKP 436
Cdd:cd05844   215 AARHPTARLVIAGDGPLRPALQALAAALGRvrfLGALPHAEVQDWMRRAEIFCLPSVtaasgDSEGLGIVLLEAAACGVP 294

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1376905710 437 LLATHFSSITwSVVVSSDFGHTFSP-NVDSLEQAMEAVIAQ--GRDTMRRKGelcRDYASLMFTATKMGAAYE 506
Cdd:cd05844   295 VVSSRHGGIP-EAILDGETGFLVPEgDVDALADALQALLADraLADRMGGAA---RAFVCEQFDIRVQTAKLE 363
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
341-440 7.29e-17

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 77.17  E-value: 7.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 341 VFGAAGRLV-RDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWgDRYRELAPNAKT----LGPMDPahLADFYNALDVFVN 415
Cdd:pfam13692   3 VILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPE-EELEELAAGLEDrvifTGFVED--LAELLAAADVFVL 79

                          90       100
                  ....*....|....*....|....*
gi 1376905710 416 PtLRSQGLDHTLLEAMQCGKPLLAT 440
Cdd:pfam13692  80 P-SLYEGFGLKLLEAMAAGLPVVAT 103
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 109-439 2.42e-16

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: 80.36  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 109 RIALFVkkwPVGGVPGGLERHALTLHRNLAARGHEIHVYTSAAAGSDNPEEL--------LDDQQDHGERGLLHVhfsrp 180
Cdd:cd03820     1 KIAIVI---PSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELddnikiknLGDRKYSHFKLLLKY----- 72

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 181 nagggFDYHRAWDQFLADNSthpggFDIVHSESVALPHWKAQL-LGSNLAASWHgIGYEIIHSDLVQDLVRKPGEPRSAD 259
Cdd:cd03820    73 -----FKKVRRLRKYLKNNK-----PDVVISFRTSLLTFLALIgLKSKLIVWEH-NNYEAYNKGLRRLLLRRLLYKRADK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 260 LQRslgerLTRvADEIKFfpsyrhhvatsdyvgdvlqtiYEIPLRNVHTILNGVDESRFRPSLDAGSafrrKYgvpvnas 339
Cdd:cd03820   142 IVV-----LTE-ADKLKK---------------------YKQPNSNVVVIPNPLSFPSEEPSTNLKS----KR------- 183

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 340 lvFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRYRELapnAKTLGPMDPAHL-------ADFYNALDV 412
Cdd:cd03820   184 --ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKL---IDKLGLEDRVKLlgptkniAEEYANSSI 258

                         330       340
                  ....*....|....*....|....*..
gi 1376905710 413 FVNPTlRSQGLDHTLLEAMQCGKPLLA 439
Cdd:cd03820   259 FVLSS-RYEGFPMVLLEAMAYGLPIIS 284
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 109-439 2.83e-16

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: 80.42  E-value: 2.83e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 109 RIALFVKKWP--VGGVPGGLERhaltLHRNLAARGHEIHVYTSAAAgsdnpeellDDQQDHGERGLLHVHFSRPnagGGF 186
Cdd:cd03814     1 RIALVTDTYHpqVNGVVRTLER----LVDHLRRRGHEVRVVAPGPF---------DEAESAEGRVVSVPSFPLP---FYP 64

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 187 DYHRAWDQFLADNS-THPGGFDIVHSESVALPHWKAQLLGSNLAASWHGIgYeiiHSDLVQDLVRKPGEPRSADLQRSLg 265
Cdd:cd03814    65 EYRLALPLPRRVRRlIKEFQPDIIHIATPGPLGLAALRAARRLGLPVVTS-Y---HTDFPEYLSYYTLGPLSWLAWAYL- 139

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 266 ERLTRVADEIkffpsyrhhVATSDYVGDVLQtiyEIPLRNVHTILNGVDESRFRPSLdAGSAFRRKYGVPVNASLVFgaA 345
Cdd:cd03814   140 RWFHNPFDTT---------LVPSPSIARELE---GHGFERVRLWPRGVDTELFHPSR-RDAALRRRLGPPGRPLLLY--V 204

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 346 GRLVRDKGHPLLFEAFSRiAARHPGVFLLVAGHGPWGDRYRELAPNAKTLGPMDPAHLADFYNALDVFVNPTlRSQGLDH 425
Cdd:cd03814   205 GRLAPEKNLEALLDADLP-LAASPPVRLVVVGDGPARAELEARGPDVIFTGFLTGEELARAYASADVFVFPS-RTETFGL 282

                         330
                  ....*....|....
gi 1376905710 426 TLLEAMQCGKPLLA 439
Cdd:cd03814   283 VVLEAMASGLPVVA 296
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
124-314 6.11e-16

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 75.65  E-value: 6.11e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 124 GGLERHALTLHRNLAARGHEIHVYTSaaagsdNPEELLDDQQDHGERGLLHVHFSRPNAGGGFDYHRAWDQFLADNsthp 203
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTP------GGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRE---- 70

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 204 gGFDIVHSesvalPHWKAQLLGSNLAASWHGIGY-EIIHSDLVQDLVRKPGEPRSADLQRSLGERLTRVADeikffpsyr 282
Cdd:pfam13439  71 -RPDVVHA-----HSPFPLGLAALAARLRLGIPLvVTYHGLFPDYKRLGARLSPLRRLLRRLERRLLRRAD--------- 135

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1376905710 283 HHVATSDYVGDVLQTIYEIPLRNVHTILNGVD 314
Cdd:pfam13439 136 RVIAVSEAVADELRRLYGVPPEKIRVIPNGVD 167
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 345-446 7.91e-15

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: 73.98  E-value: 7.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 345 AGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRYRELA-------PNAKTLGPMDPAHLADFYNALDVFVNPT 417
Cdd:cd01635   116 VGRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALAaalglleRVVIIGGLVDDEVLELLLAAADVFVLPS 195

                          90       100
                  ....*....|....*....|....*....
gi 1376905710 418 lRSQGLDHTLLEAMQCGKPLLATHFSSIT 446
Cdd:cd01635   196 -RSEGFGLVLLEAMAAGKPVIATDVGGIP 223
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 137-506 5.11e-14

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: 73.92  E-value: 5.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 137 LAARGHEIHVYTSaaaGSDNPEELLDDQQDHGERGLLHVHFSRPNAGGGFDYHRAWDQF--------LADNSTHPggFDI 208
Cdd:cd03794    27 LVRRGHEVTVLTP---SPNYPLGRIFAGATETKDGIRVIRVKLGPIKKNGLIRRLLNYLsfalaallKLLVREER--PDV 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 209 VHSESV-ALPHWKAQLLGSNLAASWhgiGYEIihSDLVQDLVRKPGePRSADLQRSLGERLTRVAdeikffpsYRHhvat 287
Cdd:cd03794   102 IIAYSPpITLGLAALLLKKLRGAPF---ILDV--RDLWPESLIALG-VLKKGSLLKLLKKLERKL--------YRL---- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 288 SDYVGDVLQTIYE------IPLRNVHTILNGVDESRFRPSLDAGSAFRRkygvPVNASLVFGAAGRLvrdkGHP----LL 357
Cdd:cd03794   164 ADAIIVLSPGLKEyllrkgVPKEKIIVIPNWADLEEFKPPPKDELRKKL----GLDDKFVVVYAGNI----GKAqgleTL 235

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 358 FEAFSRIaARHPGVFLLVAGHGPWGDRYRELA-----PNAKTLGPMDPAHLADFYNALDVFVNPTLRSQGLDHT----LL 428
Cdd:cd03794   236 LEAAERL-KRRPDIRFLFVGDGDEKERLKELAkarglDNVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGSspskLF 314

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 429 EAMQCGKPLLAthfSSITWS--VVVSSDFGHTFSP-NVDSLEQAMEAVIAQgRDTMRRKGELCRDYASLMFTATKMGAAY 505
Cdd:cd03794   315 EYMAAGKPILA---SDDGGSdlAVEINGCGLVVEPgDPEALADAILELLDD-PELRRAMGENGRELAEEKFSREKLADRL 390


                  .
gi 1376905710 506 E 506
Cdd:cd03794   391 L 391
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 308-440 5.41e-14

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: 73.63  E-value: 5.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 308 TILNGVDESRFRPSLDAGSAFRRKYGVPVNASLVFgAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRYRE 387
Cdd:cd04951   158 PVYNGIDLNKFKKDINVRLKIRNKLNLKNDEFVIL-NVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELER 236

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1376905710 388 ------LAPNAKTLGPMDpaHLADFYNALDVFVNPTlRSQGLDHTLLEAMQCGKPLLAT 440
Cdd:cd04951   237 licnlnLVDRVILLGQIS--NISEYYNAADLFVLSS-EWEGFGLVVAEAMACERPVVAT 292
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 124-482 2.17e-13

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: 71.59  E-value: 2.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 124 GGLERHALTLHRNLAARGHEIHVYTSAAAGSdnpeellddQQDHGERGLLHVH----FSRPNAGGGFDYHRA--WDQFLA 197
Cdd:cd03823    15 GGAEISVHDLAEALVAEGHEVAVLTAGVGPP---------GQATVARSVVRYRrapdETLPLALKRRGYELFetYNPGLR 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 198 D---NSTHPGGFDIVHSES---VALPHWK-AQLLGSNLAASWHGIGYEIIHSDLV---QDLVRKPgeprSADLQRSLGER 267
Cdd:cd03823    86 RllaRLLEDFRPDVVHTHNlsgLGASLLDaARDLGIPVVHTLHDYWLLCPRQFLFkkgGDAVLAP----SRFTANLHEAN 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 268 LtrvadeikFFPSyrhhvatsdyvgdvlqtiyeiplrNVHTILNGVdesrfRPSLDagsafRRKYGVPVNASLVFGAAGR 347
Cdd:cd03823   162 G--------LFSA------------------------RISVIPNAV-----EPDLA-----PPPRRRPGTERLRFGYIGR 199

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 348 LVRDKGHPLLFEAFSRIAArhPGVFLLVAGHGPWGDRYR-ELAPNAKTLGPMDPAHLADFYNALDVFVNPTLRSQGLDHT 426
Cdd:cd03823   200 LTEEKGIDLLVEAFKRLPR--EDIELVIAGHGPLSDERQiEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIWPEPFGLV 277

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1376905710 427 LLEAMQCGKPLLATHFSSITWSVVVSSDfGHTFSP-NVDSLEQAMEAVIAQGRDTMR 482
Cdd:cd03823   278 VREAIAAGLPVIASDLGGIAELIQPGVN-GLLFAPgDAEDLAAAMRRLLTDPALLER 333
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 241-501 2.43e-13

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: 71.54  E-value: 2.43e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 241 HSDLV-QDLVRKpgeprsadLQRSLGERLTRVADEIkfFPSYRHHVATSDYVGDVLQTIYEIPLRNVHTILNGVDESRFR 319
Cdd:cd03795   114 HSDIVkQKKLLK--------LYKPLMTRFLRRADRI--IATSPNYVETSPTLREFKNKVRVIPLGIDKNVYNIPRVDFEN 183

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 320 PSLDAgsAFRRkygvpvnaslVFGAAGRLVRDKGHPLLFEAFSRIaaRHPgvfLLVAGHGPWGDRYRELAP-----NAKT 394
Cdd:cd03795   184 IKREK--KGKK----------IFLFIGRLVYYKGLDYLIEAAQYL--NYP---IVIGGEGPLKPDLEAQIElnlldNVKF 246

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 395 LGPMDPAHLADFYNALDVFVNPT-LRSQGLDHTLLEAMQCGKPLLATHFSSITWSVVVSSDFGHTFSP-NVDSLEQAMEA 472
Cdd:cd03795   247 LGRVDDEEKVIYLHLCDVFVFPSvLRSEAFGIVLLEAMMCGKPVISTNIGTGVPYVNNNGETGLVVPPkDPDALAEAIDK 326

                         250       260       270
                  ....*....|....*....|....*....|.
gi 1376905710 473 VIaqgRDTMRRK--GELCRDYASLMFTATKM 501
Cdd:cd03795   327 LL---SDEELREsyGENAKKRFEELFTAEKM 354
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 117-490 1.31e-12

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: 69.32  E-value: 1.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 117 WPVGGVPGGLERHALTLHRNLAARGHEIHVYTSAAAGSDNPEELLDDQQDHGERGLLHVHFSRPNagGGFDYHRAWDQFL 196
Cdd:cd03821     7 PSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDGYESLVVEENGRYIPPQDGFASIPLLRQGA--GRTDFSPGLPNWL 84

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 197 ADNSThpgGFDIVHSESValphWKAQLLGSNLAASWHGIGYEI-IHSDLVQdlvrkpgeprsADLQRSlgerltRVADEI 275
Cdd:cd03821    85 RRNLR---EYDVVHIHGV----WTYTSLAACKLARRRGIPYVVsPHGMLDP-----------WALQQK------HWKKRI 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 276 KFFPSYRHHVATSDYVGDVLQTIYeiplRNVHT---------ILNGVDESRFrpslDAGSAFRRKYGVPVNAS-LVFgaA 345
Cdd:cd03821   141 ALHLIERRNLNNAALVHFTSEQEA----DELRRfgleppiavIPNGVDIPEF----DPGLRDRRKHNGLEDRRiILF--L 210

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 346 GRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPwGDRYRELAPNAKTL--------GPMDPAHLADFYNALDVFVNPT 417
Cdd:cd03821   211 GRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGPDD-GAYPAFLQLQSSLGlgdrvtftGPLYGEAKWALYASADLFVLPS 289

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376905710 418 lRSQGLDHTLLEAMQCGKPLLAThfSSITWSVVVSSDFGHTFSPNVDSLEQAMEAVI--AQGRDTMRRKGELCRD 490
Cdd:cd03821   290 -YSENFGNVVAEALACGLPVVIT--DKCGLSELVEAGCGVVVDPNVSSLAEALAEALrdPADRKRLGEMARRARQ 361
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 406-509 2.77e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 63.86  E-value: 2.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 406 FYNALDVFVNPTlRSQGLDHTLLEAMQCGKPLLATHFSSITWsVVVSSDFGHTFSP-NVDSLEQAMEAVIAQgRDTMRRK 484
Cdd:COG0438    17 LLAAADVFVLPS-RSEGFGLVLLEAMAAGLPVIATDVGGLPE-VIEDGETGLLVPPgDPEALAEAILRLLED-PELRRRL 93

                          90       100
                  ....*....|....*....|....*
gi 1376905710 485 GELCRDYASLMFTATKMGAAYERLF 509
Cdd:COG0438    94 GEAARERAEERFSWEAIAERLLALY 118
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 116-509 4.68e-12

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: 67.31  E-value: 4.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 116 KWPVG-GVPGGLERHALTLHRNLAARGHEIHVYtsAAAGSDN-------PEELLDDQQDHGERGLLHvHFSRPNAgggfd 187
Cdd:cd03802     9 RGPVPpGKYGGTELVVSALTEGLVRRGHEVTLF--APGDSHTsaplvavIPRALRLDPIPQESKLAE-LLEALEV----- 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 188 YHRAWDqfladnsthpggFDIVHSESVALPHWKAQLLGSNLAASWHGigyeiihsdlvqdlvrkpgeprsadlqrslgeR 267
Cdd:cd03802    81 QLRASD------------FDVIHNHSYDWLPPFAPLIGTPFVTTLHG--------------------------------P 116

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 268 LTRVADEIKFFPSYRHHVATSDyvgdvLQTIYEIPLRNVHTILNGVDESRFRPSLDAGSafrrkygvpvnaslVFGAAGR 347
Cdd:cd03802   117 SIPPSLAIYAAEPPVNYVSISD-----AQRAATPPIDYLTVVHNGLDPADYRFQPDPED--------------YLAFLGR 177

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 348 LVRDKGhplLFEAFSriAARHPGVFLLVAGHGPWGDRYRELA-----PNAKTLGPMDPAHLADFYNALDVFVNPTLRSQ- 421
Cdd:cd03802   178 IAPEKG---LEDAIR--VARRAGLPLKIAGKVRDEDYFYYLQeplpgPRIEFIGEVGHDEKQELLGGARALLFPINWDEp 252

                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 422 -GLdhTLLEAMQCGKPLLATHFSSItwSVVVssDFGHT-FSpnVDSLEQAMEAViaqgRDTMRRKGELCRDYASLMFTAT 499
Cdd:cd03802   253 fGL--VMIEAMACGTPVIAYRRGGL--PEVI--QHGETgFL--VDSVEEMAEAI----ANIDRIDRAACRRYAEDRFSAA 320

                         410
                  ....*....|
gi 1376905710 500 KMGAAYERLF 509
Cdd:cd03802   321 RMADRYEALY 330
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 280-438 1.71e-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: 59.61  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 280 SYRHHVATSDYVGDVLQTIYEIplRNVHTILNGVDESRFRPSlDAGSAFRRKYGVPVNAsLVFGAAGRLVRDKGHPLLFE 359
Cdd:cd03812   136 LSTKYLACSEDAGEWLFGEVEN--GKFKVIPNGIDIEKYKFN-KEKRRKRRKLLILEDK-LVLGHVGRFNEQKNHSFLID 211

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 360 AFSRIAARHPGVFLLVAGHGPwgDRY--------RELAPNAKTLGPMDPAHlaDFYNALDVFVNPTLrSQGLDHTLLEAM 431
Cdd:cd03812   212 IFEELKKKNPNVKLVLVGEGE--LKEkikekvkeLGLEDKVIFLGFRNDVS--EILSAMDVFLFPSL-YEGLPLVAVEAQ 286


                  ....*..
gi 1376905710 432 QCGKPLL 438
Cdd:cd03812   287 ASGLPCL 293
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 130-440 6.46e-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: 57.75  E-value: 6.46e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 130 ALTLHRNLAARGHEIHVYTSAAagsdnPEELLDDQqdhgerGLLHVHFSRPNAGGGFD---YHRAWDQFLADNSTHPGgF 206
Cdd:cd04962    18 ATELGLELAERGHEVHFISSAI-----PFRLNLYS------GNIFFHEVEVPNYPLFEyppYTLALASKIVEVAKEHK-L 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 207 DIVHSEsVALPHWKAQLLGSnlaaswhgigyEIIHSDLvqdlvrkpgePRSADLQrslGERLTRVADEIKFFPSYRHHVA 286
Cdd:cd04962    86 DVLHAH-YAIPHASCAYLAR-----------EILGEKI----------PIVTTLH---GTDITLVGYDPSLQPAVRFSIN 140

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 287 TSDYVGDV----LQTIYEI--PLRNVHTILNGVDESRFRPsLDAGSAFRRKYGVPVNASLVFGAAGRLVrdKGHPLLFEA 360
Cdd:cd04962   141 KSDRVTAVssslRQETYELfdVDKDIEVIHNFIDEDVFKR-KPAGALKRRLLAPPDEKVVIHVSNFRPV--KRIDDVVRV 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 361 FSRIAARHPGVFLLVaGHGPWGDRYRELAPN------AKTLGPMDpaHLADFYNALDVFVNPTLR-SQGLdhTLLEAMQC 433
Cdd:cd04962   218 FARVRRKIPAKLLLV-GDGPERVPAEELARElgvedrVLFLGKQD--DVEELLSIADLFLLPSEKeSFGL--AALEAMAC 292


                  ....*..
gi 1376905710 434 GKPLLAT 440
Cdd:cd04962   293 GVPVVSS 299
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
295-475 5.04e-08

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 55.18  E-value: 5.04e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 295 LQTIYE--IPLRNVHTILNGVDESRFrpSLDAGSAFRRKYGVPVNASLVFgAAGRLVRDKGHPLLFEAFSRIAARHPGVF 372
Cdd:PRK15484  150 LKKFYEerLPNADISIVPNGFCLETY--QSNPQPNLRQQLNISPDETVLL-YAGRISPDKGILLLMQAFEKLATAHSNLK 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 373 LLVAG------HGPWGDRYRELAPNAKTLGP-------MDPAHLADFYNALDVFVNPTLRSQGLDHTLLEAMQCGKPLLA 439
Cdd:PRK15484  227 LVVVGdptassKGEKAAYQKKVLEAAKRIGDrcimlggQPPEKMHNYYPLADLVVVPSQVEEAFCMVAVEAMAAGKPVLA 306

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1376905710 440 THFSSITWSVVVSSDFGHTFSP-NVDSLEQAMEAVIA 475
Cdd:PRK15484  307 STKGGITEFVLEGITGYHLAEPmTSDSIISDINRTLA 343
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 300-475 1.22e-07

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: 53.78  E-value: 1.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 300 EIPLRNVHTILNGVDESRFRPSldagsAFRRKygvpvNASLVFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHG 379
Cdd:cd03796   164 SLDPRIVSVIPNAVDSSDFTPD-----PSKPD-----PNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDG 233

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 380 PWGDRYRE------LAPNAKTLGPMDPAHLADFYNALDVFVNPTLrSQGLDHTLLEAMQCGKPLLATHFSSItwSVVVSS 453
Cdd:cd03796   234 PKRIELEEmrekyqLQDRVELLGAVPHEEVRDVLVQGHIFLNTSL-TEAFCIAIVEAASCGLLVVSTRVGGI--PEVLPP 310

                         170       180
                  ....*....|....*....|..
gi 1376905710 454 DFGHTFSPNVDSLEQAMEAVIA 475
Cdd:cd03796   311 DMILLAEPDPEDIVRKLEEAIS 332
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 196-510 1.25e-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: 54.26  E-value: 1.25e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 196 LADNSTHPGGFDIVHSESVALphwkAQLLGSNLAASW--------HGIgY------EIIHSDLVQDLVRKpgepRSADLQ 261
Cdd:cd03813   164 LAIAADDLPEADLYHSVSTGY----AGLLGALARHRRgipfllteHGI-YtrerkiEILQSTWIMGYIKK----LWIRFF 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 262 RSLGERLTRVADEIkfFPSYRHHvatsdyvgdvlqTIYEIPL----RNVHTILNGVDESRFRPSLDagsafRRKYGVPVN 337
Cdd:cd03813   235 ERLGKLAYQQADKI--ISLYEGN------------RRRQIRLgadpDKTRVIPNGIDIQRFAPARE-----ERPEKEPPV 295

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 338 ASLVfgaaGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDRY----RELAPNA------KTLGPMDpahLADFY 407
Cdd:cd03813   296 VGLV----GRVVPIKDVKTFIRAFKLVRRAMPDAEGWLIGPEDEDPEYaqecKRLVASLglenkvKFLGFQN---IKEYY 368

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 408 NALDVFVnPTLRSQGLDHTLLEAMQCGKPLLATHFSSITWSVV-VSSDFGHTFS--PNVDSLEQAmEAVIAQGRDTMRRK 484
Cdd:cd03813   369 PKLGLLV-LTSISEGQPLVILEAMASGVPVVATDVGSCRELIYgADDALGQAGLvvPPADPEALA-EALIKLLRDPELRQ 446

                         330       340
                  ....*....|....*....|....*...
gi 1376905710 485 --GELCRDYASLMFTATKMGAAYERLFL 510
Cdd:cd03813   447 afGEAGRKRVEKYYTLEGMIDSYRKLYL 474
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 301-509 3.54e-07

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 53.11  E-value: 3.54e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 301 IPLRNVHTILNGVDESRFRPSlDAGSA----FRRKYGvpvNASLVFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVA 376
Cdd:PRK15179  479 VDERRIPVVYNGLAPLKSVQD-DACTAmmaqFDARTS---DARFTVGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMV 554

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 377 GHGPWGDRYRELapnAKTLGPMD-------PAHLADFYNALDVFVNPTlRSQGLDHTLLEAMQCGKPLLAThFSSITWSV 449
Cdd:PRK15179  555 GGGPLLESVREF---AQRLGMGErilftglSRRVGYWLTQFNAFLLLS-RFEGLPNVLIEAQFSGVPVVTT-LAGGAGEA 629

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1376905710 450 VVSSDFGHTFSPNV---DSLEQAMEAVIAQGR--DTMRRKGelcRDYASLMFTATKMGAAYERLF 509
Cdd:PRK15179  630 VQEGVTGLTLPADTvtaPDVAEALARIHDMCAadPGIARKA---ADWASARFSLNQMIASTVRCY 691
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 254-509 8.30e-07

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: 51.23  E-value: 8.30e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 254 EPRSADLQRSLGERLTRVADEIKffpsyrhhVATSDYVGDvLQTIYEIPLRNVHTILNGVDESRFRPSldagsaFRRKYG 333
Cdd:cd03822   117 LSDPGKQALKVLFRIATLSERVV--------VMAPISRFL-LVRIKLIPAVNIEVIPHGVPEVPQDPT------TALKRL 181

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 334 VPVNASLVFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGhGP-------WGDRYRELAPNAKTL--------GPM 398
Cdd:cd03822   182 LLPEGKKVILTFGFIGPGKGLEILLEALPELKAEFPDVRLVIAG-ELhpslaryEGERYRKAAIEELGLqdhvdfhnNFL 260

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 399 DPAHLADFYNALDVFVNPTL-RSQGLDHTLLEAMQCGKPllathfssitwsvVVSSDFGHTFSPNVD----SLEQAMEAV 473
Cdd:cd03822   261 PEEEVPRYISAADVVVLPYLnTEQSSSGTLSYAIACGKP-------------VISTPLRHAEELLADgrgvLVPFDDPSA 327

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1376905710 474 IAQG-----RDTMRRKGELCRDYA-SLMFTATKMGAAYERLF 509
Cdd:cd03822   328 IAEAilrllEDDERRQAIAERAYAyARAMTWESIADRYLRLF 369
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 283-439 1.02e-06

mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. WbaZ in Salmonella enterica has been shown to possess mannosyltransferase activity.


Pssm-ID: 340833 [Multi-domain]  Cd Length: 356  Bit Score: 50.75  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 283 HHVATSDYVGDVLQTIYEiplRNVHTILNGVDESRFRPSLDAGSAFRrkygvpvnaslvfgAAGRLVRDKGHPLLFEAFS 362
Cdd:cd03804   160 LFIANSQFVARRIKKFYG---RESTVIYPPVDTDAFAPAADKEDYYL--------------TASRLVPYKRIDLAVEAFN 222

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1376905710 363 RIAARhpgvfLLVAGHGPWGDRYRELA-PNAKTLGPMDPAHLADFYNALDVFVNPTLRSQGLdhTLLEAMQCGKPLLA 439
Cdd:cd03804   223 ELPKR-----LVVIGDGPDLDRLRAMAsPNVEFLGYQPDEVLKELLSKARAFVFAAEEDFGI--VPVEAQACGTPVIA 293
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 305-445 3.76e-05

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: 45.90  E-value: 3.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 305 NVHTIlnGVDESRFRpsldagsaFRRKYgVPVNASLVFGAAGRLVRDKGHPLLFEAFSRIAARHPGVFLLVAGHGPWGDR 384
Cdd:cd03799   151 IVHRS--GIDCNKFR--------FKPRY-LPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQ 219

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1376905710 385 YREL------APNAKTLGPMDPAHLADFYNALDVFVNPTLRSQ-----GLDHTLLEAMQCGKPLLATHFSSI 445
Cdd:cd03799   220 LQQLiqelniGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAAdgdqdGPPNTLKEAMAMGLPVISTEHGGI 291
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
124-312 2.02e-04

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 42.00  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 124 GGLERHALTLHRNLAARGHEIHVYTSAAAGSDNPEEllddqqdhgERGLLHVHFSRPNAGGGFDYHRAWDQFLAdnSTHP 203
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTPGGPPGRPELV---------GDGVRVHRLPVPPRPSPLADLAALRRLRR--LLRA 69

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 204 GGFDIVHSESvalphWKAQLLGsNLAASWHGIGYeIIHsdlVQDLVRKPGEPRSADLQRSLGERLTRVADEIkffpsyrh 283
Cdd:pfam13579  70 ERPDVVHAHS-----PTAGLAA-RLARRRRGVPL-VVT---VHGLALDYGSGWKRRLARALERRLLRRADAV-------- 131

                         170       180
                  ....*....|....*....|....*....
gi 1376905710 284 hVATSDYVGDVLQTIYeIPLRNVHTILNG 312
Cdd:pfam13579 132 -VVVSEAEAELLRALG-VPAARVVVVPNG 158
COG4641 COG4641
Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];
275-441 4.10e-04

Spore maturation protein CgeB [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 443679 [Multi-domain]  Cd Length: 303  Bit Score: 42.61  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 275 IKFFPSYRHHVATSdyvGDVLQTIYEIPLRNVHTILNGVDESRFRPsldAGSAFRRKYGVpvnaslVFGAAGRLVRdkgh 354
Cdd:COG4641    87 RELLPLYDLVFTFD---GDCVEEYRALGARRVFYLPFAADPELHRP---VPPEARFRYDV------AFVGNYYPDR---- 150

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 355 pllFEAFSRIAARHPGVFLLVAGHGpWGDryRELAPNAKTLGPMDPAHLADFYNALDVFVNPTLRSQGLD-HT--LLEAM 431
Cdd:COG4641   151 ---RARLEELLLAPAGLRLKIYGPG-WPK--LALPANVRRGGHLPGEEHPAAYASSKITLNVNRMAASPDsPTrrTFEAA 224

                         170
                  ....*....|
gi 1376905710 432 QCGKPLLATH 441
Cdd:COG4641   225 ACGAFLLSDP 234
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 309-389 5.00e-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: 42.55  E-value: 5.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 309 ILNGVDESRFRPSLDAGS-----------------AFRRKYGVPVNAS-LVFGAAGRLVRDKGHPLLFEAFSRIAARHPG 370
Cdd:cd03791   246 ILNGIDYDEWNPATDKLIpanysandlegkaenkaALQKELGLPVDPDaPLFGFVGRLTEQKGVDLILDALPELLEEGGQ 325

                          90
                  ....*....|....*....
gi 1376905710 371 VFLLVAGHGPWGDRYRELA 389
Cdd:cd03791   326 LVVLGSGDPEYEQAFRELA 344
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
309-389 4.99e-03

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 39.30  E-value: 4.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1376905710 309 ILNGVDESRFRPSLD------------AG-----SAFRRKYGVPVNASL-VFGAAGRLVRDKGHPLLFEAFSRIAARhpG 370
Cdd:COG0297   247 ILNGIDYDVWNPATDpylpanysaddlEGkaankAALQEELGLPVDPDApLIGMVSRLTEQKGLDLLLEALDELLEE--D 324

                          90       100
                  ....*....|....*....|.
gi 1376905710 371 VFLLVAGHGPWG--DRYRELA 389
Cdd:COG0297   325 VQLVVLGSGDPEyeEAFRELA 345
 
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