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Conserved domains on  [gi|505028577|ref|WP_015215679|]
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MULTISPECIES: glycosyltransferase [Anabaena]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

glycosyltransferase family protein may synthesize oligosaccharides, polysaccharides, and glycoconjugates by transferring the sugar moiety from an activated nucleotide-sugar donor to an acceptor molecule, which may be a growing oligosaccharide, a lipid, or a protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 30-386 6.53e-39

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.


The actual alignment was detected with superfamily member cd03808:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 358  Bit Score: 143.50  E-value: 6.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  30 VWGGSEELLAATAKYLKQQGHEVHVFKlqiSDHP-RILELQAAGVKVIALNSLRLmGIKHFV-FKCIYHLVRLLKFLPlP 107
Cdd:cd03808    8 VDGGFQSFRLPLIKALVKKGYEVHVIA---PDGDkLSDELKELGVKVIDIPILRR-GINPLKdLKALFKLYKLLKKEK-P 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 108 AswyFIHTDPQRTFILQTL-RRIKPSLVVISqgdNFDGLnygdiclelklPYVMLSHKASHHIWpvdalRPMMRKVFQQA 186
Cdd:cd03808   83 D---IVHCHTPKPGILGRLaARLAGVPKVIY---TVHGL-----------GFVFTEGKLLRLLY-----LLLEKLALLFT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 187 KRCFFVSEHNLFLTQMQLGQGLSHAEVV--------RNPYLTsateslpwPEIKDNCFKLACVGRLwLVDKGQDILLEVL 258
Cdd:cd03808  141 DKVIFVNEDDRDLAIKKGIIKKKKTVLIpgsgvdldRFQYSP--------ESLPSEKVVFLFVARL-LKDKGIDELIEAA 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 259 AQEKWKYRNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAI 337
Cdd:cd03808  212 KILKKKGPNVRFLLVGDGELENPSEILIEKLGLeGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVI 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 505028577 338 TTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:cd03808  292 TTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAA 340
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 30-386 6.53e-39

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: 143.50  E-value: 6.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  30 VWGGSEELLAATAKYLKQQGHEVHVFKlqiSDHP-RILELQAAGVKVIALNSLRLmGIKHFV-FKCIYHLVRLLKFLPlP 107
Cdd:cd03808    8 VDGGFQSFRLPLIKALVKKGYEVHVIA---PDGDkLSDELKELGVKVIDIPILRR-GINPLKdLKALFKLYKLLKKEK-P 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 108 AswyFIHTDPQRTFILQTL-RRIKPSLVVISqgdNFDGLnygdiclelklPYVMLSHKASHHIWpvdalRPMMRKVFQQA 186
Cdd:cd03808   83 D---IVHCHTPKPGILGRLaARLAGVPKVIY---TVHGL-----------GFVFTEGKLLRLLY-----LLLEKLALLFT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 187 KRCFFVSEHNLFLTQMQLGQGLSHAEVV--------RNPYLTsateslpwPEIKDNCFKLACVGRLwLVDKGQDILLEVL 258
Cdd:cd03808  141 DKVIFVNEDDRDLAIKKGIIKKKKTVLIpgsgvdldRFQYSP--------ESLPSEKVVFLFVARL-LKDKGIDELIEAA 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 259 AQEKWKYRNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAI 337
Cdd:cd03808  212 KILKKKGPNVRFLLVGDGELENPSEILIEKLGLeGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVI 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 505028577 338 TTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:cd03808  292 TTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAA 340
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 236-372 4.32e-29

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: 111.21  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  236 FKLACVGRLWLVdKGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGLK-NVNFPGFV--ENIESVWQDYHA 312
Cdd:pfam00534   3 KIILFVGRLEPE-KGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVsdEDLPELLKIADV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  313 LILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERA 372
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL 141
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 285-409 2.77e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 85.81  E-value: 2.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 285 MANLLGLKNVNFPgfvenIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAA 364
Cdd:COG0438    1 MGRLVPRKGLDLL-----LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505028577 365 IDEALERAWQRSDEWENMGTQASISIRKQIpkDPERlFADKLLQL 409
Cdd:COG0438   76 LAEAILRLLEDPELRRRLGEAARERAEERF--SWEA-IAERLLAL 117
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 217-371 1.93e-16

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 80.15  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  217 PYLTSATESLPWPEIKDNCFKLACVGRLWLVdKGQDILLEVLA----QEKWKYRNLQVSFFGEGANRDTLIDMANLLGLK 292
Cdd:TIGR03088 176 PSRGDRSPILPPDFFADESVVVGTVGRLQAV-KDQPTLVRAFAllvrQLPEGAERLRLVIVGDGPARGACEQMVRAAGLA 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  293 N-VNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALER 371
Cdd:TIGR03088 255 HlVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQP 334
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 241-371 4.08e-07

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 52.34  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 241 VGRLWLVDKGQDILLEVLAQEKWKYRNLQVSFF--GEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQDYHALILPS 317
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFImvGGGPLLESVREFAQRLGMgERILFTGLSRRVGYWLTQFNAFLLLS 599

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505028577 318 RAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAID--EALER 371
Cdd:PRK15179 600 RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTAPDvaEALAR 655
 
Name Accession Description Interval E-value
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 30-386 6.53e-39

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: 143.50  E-value: 6.53e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  30 VWGGSEELLAATAKYLKQQGHEVHVFKlqiSDHP-RILELQAAGVKVIALNSLRLmGIKHFV-FKCIYHLVRLLKFLPlP 107
Cdd:cd03808    8 VDGGFQSFRLPLIKALVKKGYEVHVIA---PDGDkLSDELKELGVKVIDIPILRR-GINPLKdLKALFKLYKLLKKEK-P 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 108 AswyFIHTDPQRTFILQTL-RRIKPSLVVISqgdNFDGLnygdiclelklPYVMLSHKASHHIWpvdalRPMMRKVFQQA 186
Cdd:cd03808   83 D---IVHCHTPKPGILGRLaARLAGVPKVIY---TVHGL-----------GFVFTEGKLLRLLY-----LLLEKLALLFT 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 187 KRCFFVSEHNLFLTQMQLGQGLSHAEVV--------RNPYLTsateslpwPEIKDNCFKLACVGRLwLVDKGQDILLEVL 258
Cdd:cd03808  141 DKVIFVNEDDRDLAIKKGIIKKKKTVLIpgsgvdldRFQYSP--------ESLPSEKVVFLFVARL-LKDKGIDELIEAA 211

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 259 AQEKWKYRNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAI 337
Cdd:cd03808  212 KILKKKGPNVRFLLVGDGELENPSEILIEKLGLeGRIEFLGFRSDVPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVI 291

                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*....
gi 505028577 338 TTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:cd03808  292 TTDVPGCRELVIDGVNGFLVPPGDVEALADAIEKLIEDPELRKEMGEAA 340
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 22-393 6.77e-36

phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 family of glycosyltransferases and named after PimA in Propionibacterium freudenreichii, which is involved in the biosynthesis of phosphatidyl-myo-inositol mannosides (PIM) which are early precursors in the biosynthesis of lipomannans (LM) and lipoarabinomannans (LAM), and catalyzes the addition of a mannosyl residue from GDP-D-mannose (GDP-Man) to the position 2 of the carrier lipid phosphatidyl-myo-inositol (PI) to generate a phosphatidyl-myo-inositol bearing an alpha-1,2-linked mannose residue (PIM1). Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found mainly in certain bacteria and archaea.


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 135.36  E-value: 6.77e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  22 VFISSCFDVWGGSEELLAATAKYLKQQGHEVHVFKLQISDHPRILELQAAGVKVIALnslrlmgikHFVFKCIYHLVRLL 101
Cdd:cd03801    4 LLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPS---------LAALLRARRLLREL 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 102 KFLplpaswyfihtdpqrtfilqtLRRIKPSLVVISqgDNFDGLNYGDICLELKLPYVMLSHkaSHHIWPVDALRPMMRK 181
Cdd:cd03801   75 RPL---------------------LRLRKFDVVHAH--GLLAALLAALLALLLGAPLVVTLH--GAEPGRLLLLLAAERR 129

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 182 VFQQAKRCFFVSEHNLFLTQMQ-------LGQGLSHAEVVRNPYLTS--ATESLPWPEIKDNCFKLACVGRLWLVdKGQD 252
Cdd:cd03801  130 LLARAEALLRRADAVIAVSEALrdelralGGIPPEKIVVIPNGVDLErfSPPLRRKLGIPPDRPVLLFVGRLSPR-KGVD 208

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 253 ILLEVLAQEKWKYRNLQVSFFG-EGANRDTLIDMANLLGlKNVNFPGFV--ENIESVWQDYHALILPSRAEGLPITLVEA 329
Cdd:cd03801  209 LLLEALAKLLRRGPDVRLVIVGgDGPLRAELEELELGLG-DRVRFLGFVpdEELPALYAAADVFVLPSRYEGFGLVVLEA 287

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505028577 330 MMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQASISIRKQ 393
Cdd:cd03801  288 MAAGLPVVATDVGGLPEVVEDGEGGLVVPPDDVEALADALLRLLADPELRARLGRAARERVAER 351
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
 21-393 3.13e-30

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: 119.65  E-value: 3.13e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  21 FVFISSCFDVWGGSEELLAATAKYLKQQGHEVHVFKLQISDHPRILELqAAGVKVIALNSLRLMGIKhFVFKCIYHLVRL 100
Cdd:cd03820    2 IAIVIPSISNAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYEL-DDNIKIKNLGDRKYSHFK-LLLKYFKKVRRL 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 101 LKFLplpaswyfihtdpqrtfilqtlRRIKPSlVVISqgdNFDGLNYGDICLELKLPYVMLSHkASHHIWPVDALRPMMR 180
Cdd:cd03820   80 RKYL----------------------KNNKPD-VVIS---FRTSLLTFLALIGLKSKLIVWEH-NNYEAYNKGLRRLLLR 132

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 181 KVfqQAKRCFFV---SEHNLFLTQmqlGQGLSHAEVVRNPYltsateSLPWPEIKDNC--FKLACVGRLWlVDKGQDILL 255
Cdd:cd03820  133 RL--LYKRADKIvvlTEADKLKKY---KQPNSNVVVIPNPL------SFPSEEPSTNLksKRILAVGRLT-YQKGFDLLI 200

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 256 EVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGLKN-VNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGR 334
Cdd:cd03820  201 EAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLGLEDrVKLLGPTKNIAEEYANSSIFVLSSRYEGFPMVLLEAMAYGL 280

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 335 IAITTN-VGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGtQASISIRKQ 393
Cdd:cd03820  281 PIISFDcPTGPSEIIEDGENGLLVPNGDVDALAEALLRLMEDEELRKKMG-KNARKNAER 339
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 236-372 4.32e-29

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: 111.21  E-value: 4.32e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  236 FKLACVGRLWLVdKGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGLK-NVNFPGFV--ENIESVWQDYHA 312
Cdd:pfam00534   3 KIILFVGRLEPE-KGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGdNVIFLGFVsdEDLPELLKIADV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  313 LILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERA 372
Cdd:pfam00534  82 FVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNAEALAEAIDKL 141
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
236-371 1.07e-26

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 104.13  E-value: 1.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  236 FKLACVGRLWLVDKGQDILLEVLAQEKWKYRNLQVSFFGEGaNRDTLIDMANLLGlKNVNFPGFVENIESVWQDYHALIL 315
Cdd:pfam13692   2 PVILFVGRLHPNVKGVDYLLEAVPLLRKRDNDVRLVIVGDG-PEEELEELAAGLE-DRVIFTGFVEDLAELLAAADVFVL 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 505028577  316 PSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLeDNITGFIAKGTSFAAIDEALER 371
Cdd:pfam13692  80 PSLYEGFGLKLLEAMAAGLPVVATDVGGIPELV-DGENGLLVPPGDPEALAEAILR 134
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
 49-382 1.22e-26

Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. Staphylococcus aureus CapJ may be involved in capsule polysaccharide biosynthesis. WlbH in Bordetella parapertussis has been shown to be required for the biosynthesis of a trisaccharide that, when attached to the B. pertussis lipopolysaccharide (LPS) core (band B), generates band A LPS.


Pssm-ID: 340828 [Multi-domain]  Cd Length: 376  Bit Score: 110.16  E-value: 1.22e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  49 GHEVHVFKlqisdhpRILELQAAGVKVialnslRLMGIKHFVFKCIYHLVRLLKFLPLPASWYFIHTDPQRTFILQTLR- 127
Cdd:cd03798   15 GRGIFVRR-------QVRALSRRGVDV------EVLAPAPWGPAAARLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRa 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 128 -RIKPSLVVISQGDnFD------GLNYGDICL----ELKLPYVMLSHKASHHIWPVD-ALRPMMRKVFQQAKRCFFVSeh 195
Cdd:cd03798   82 pSLAKLLKRRRRGP-PDlihahfAYPAGFAAAllarLYGVPYVVTEHGSDINVFPPRsLLRKLLRWALRRAARVIAVS-- 158

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 196 nlflTQMQ-----LGQGLSHAEVVRNPYLTS----ATESLPWPEikdNCFKLACVGRLWLVdKGQDILLEVLAQEKWKYR 266
Cdd:cd03798  159 ----KALAeelvaLGVPRDRVDVIPNGVDPArfqpEDRGLGLPL---DAFVILFVGRLIPR-KGIDLLLEAFARLAKARP 230

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 267 NLQVSFFGEGANRDTLIDMANLLGLKN-VNFPGFVENIE-SVWQD-YHALILPSRAEGLPITLVEAMMCGRIAITTNVGG 343
Cdd:cd03798  231 DVVLLIVGDGPLREALRALAEDLGLGDrVTFTGRLPHEQvPAYYRaCDVFVLPSRHEGFGLVLLEAMACGLPVVATDVGG 310

                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 505028577 344 IPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENM 382
Cdd:cd03798  311 IPEVVGDPETGLLVPPGDADALAAALRRALAEPYLRELG 349
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 31-394 1.02e-25

family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most closely related to the GT1 family of glycosyltransferases. WabH in Klebsiella pneumoniae has been shown to transfer a GlcNAc residue from UDP-GlcNAc onto the acceptor GalUA residue in the cellular outer core.


Pssm-ID: 340839 [Multi-domain]  Cd Length: 351  Bit Score: 107.06  E-value: 1.02e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  31 WGGSEELLAATAKYLKQQGHEVHVFklqISDHPRILELQAAGVKVIALNSLRLMGIKHfvfkciyhlVRLLKFLPlpasw 110
Cdd:cd03811   11 GGGAERVLLNLANALDKRGYDVTLV---LLRDEGDLDKQLNGDVKLIRLLIRVLKLIK---------LGLLKAIL----- 73

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 111 yfihtdpqrtFILQTLRRIKPSlVVISQGDNFdgLNYGDICLELKLPYVMLSHKASHHIWPVDALRPMMRKVFQQAKRCF 190
Cdd:cd03811   74 ----------KLKRILKRAKPD-VVISFLGFA--TYIVAKLAAARSKVIAWIHSSLSKLYYLKKKLLLKLKLYKKADKIV 140

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 191 FVSEH--NLFLTQmqLGQGLSHAEVVRNP---YLTSATESLPWPEIKDNCFKLACVGRLWLVdKGQDILLEVLAQEKWKY 265
Cdd:cd03811  141 CVSKGikEDLIRL--GPSPPEKIEVIYNPidiDRIRALAKEPILNEPEDGPVILAVGRLDPQ-KGHDLLIEAFAKLRKKY 217

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 266 RNLQVSFFGEGANRDTLIDMANLLGLKN-VNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGI 344
Cdd:cd03811  218 PDVKLVILGDGPLREELEKLAKELGLAErVIFLGFQSNPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGP 297

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 505028577 345 PEVLEDNITGFIAKGTS---FAAIDEALERAWQRSDEWENMGTQASISIRKQI 394
Cdd:cd03811  298 REILDDGENGLLVPDGDaaaLAGILAALLQKKLDAALRERLAKAQEAVFREYT 350
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
 32-393 6.39e-22

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: 96.23  E-value: 6.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  32 GGSEELLAATAKYLKQQGHEVHVFKLQiSDHPRILELQAAGVKVIALNslrlMGIKHFVFKciyhLVRLLKFLplpaswy 111
Cdd:cd03807   12 GGAETMLLRLLEHMDKSRFEHVVISLT-GDGVLGEELLAAGVPVVCLG----LSSGKDPGV----LLRLAKLI------- 75

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 112 fihtdpqrtfilqtlRRIKPSLVvisQGDNFDGLNYGDIC--LELKLPYVMlshkASHHIWPVDALRPMMRKV------F 183
Cdd:cd03807   76 ---------------RKRNPDVV---HTWMYHADLIGGLAakLAGGVKVIW----SVRSSNIPQRLTRLVRKLclllskF 133

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 184 QQAKRCffVSEHNLFLTQmqlGQGLSHA--EVVRNPY-----------LTSATESLPwpeIKDNCFKLACVGRLWLVdKG 250
Cdd:cd03807  134 SPATVA--NSSAVAEFHQ---EQGYAKNkiVVIYNGIdlfklspddasRARARRRLG---LAEDRRVIGIVGRLHPV-KD 204

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 251 QDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGLKN-VNFPGFVENIESVWQDYHALILPSRAEGLPITLVEA 329
Cdd:cd03807  205 HSDLLRAAALLVETHPDLRLLLVGRGPERPNLERLLLELGLEDrVHLLGERSDVPALLPAMDIFVLSSRTEGFPNALLEA 284

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 505028577 330 MMCGRIAITTNVGGIPEVLEDNiTGFIAKGTSFAAIDEALERAWQRSDEWENMGTQASISIRKQ 393
Cdd:cd03807  285 MACGLPVVATDVGGAAELVDDG-TGFLVPAGDPQALADAIRALLEDPEKRARLGRAARERIANE 347
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 285-409 2.77e-20

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 85.81  E-value: 2.77e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 285 MANLLGLKNVNFPgfvenIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAA 364
Cdd:COG0438    1 MGRLVPRKGLDLL-----LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDPEA 75

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 505028577 365 IDEALERAWQRSDEWENMGTQASISIRKQIpkDPERlFADKLLQL 409
Cdd:COG0438   76 LAEAILRLLEDPELRRRLGEAARERAEERF--SWEA-IAERLLAL 117
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 42-386 7.02e-20

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: 90.86  E-value: 7.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  42 AKYLKQQGHEVHVFkLQISDHPRILELQAA-----GVKVIAlnslrlmgIKHFVFKCIYHLVRLLKFLplpaSWYFihtd 116
Cdd:cd03794   24 AKELVRRGHEVTVL-TPSPNYPLGRIFAGAtetkdGIRVIR--------VKLGPIKKNGLIRRLLNYL----SFAL---- 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 117 pqRTFILQTLRRIKPSLVVISQGDNFDGLNYGDICLELKLPYVMLSHkashHIWP--------------VDALRPMMRKV 182
Cdd:cd03794   87 --AALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVR----DLWPeslialgvlkkgslLKLLKKLERKL 160

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 183 FQQAKRCFFVSEhnLFLTQM-QLGQGLSHAEVVRNPYLTSATESLPWPEIK-----DNCFKLACVGRLWLVDkGQDILLE 256
Cdd:cd03794  161 YRLADAIIVLSP--GLKEYLlRKGVPKEKIIVIPNWADLEEFKPPPKDELRkklglDDKFVVVYAGNIGKAQ-GLETLLE 237

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 257 VLAQEKwKYRNLQVSFFGEGANRDTLIDMANLLGLKNVNFPGFV--ENIESVWQDYHALILPSRAE-----GLPITLVEA 329
Cdd:cd03794  238 AAERLK-RRPDIRFLFVGDGDEKERLKELAKARGLDNVTFLGRVpkEEVPELLSAADVGLVPLKDNpanrgSSPSKLFEY 316

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 505028577 330 MMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:cd03794  317 MAAGKPILASDDGGSDLAVEINGCGLVVEPGDPEALADAILELLDDPELRRAMGENG 373
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 30-387 7.64e-20

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: 90.11  E-value: 7.64e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  30 VWGGSEELLAATAKYLKQQGHEVHVFKLQISDHPRileLQAAGVKVialnslrlMGIKHFVFKCIYHLVRLLKflplpas 109
Cdd:cd03819    9 EIGGAETYILDLARALAERGHRVLVVTAGGPLLPR---LRQIGIGL--------PGLKVPLLRALLGNVRLAR------- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 110 wyfihtdpqrtfilqTLRRIKPSLV-VISQGDNFDGLnygDICLELKLPYVMLSHkaSHHI---WPVDALRPMMRKVFQQ 185
Cdd:cd03819   71 ---------------LIRRERIDLIhAHSRAPAWLGW---LASRLTGVPLVTTVH--GSYLatyHPKDFALAVRARGDRV 130

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 186 AKRCFFVSEHNLFLTqmqlgqGLSHAEVVRNPY--------LTSATESLPWPEIKDNCFKLACVGRLWlVDKGQDILLEV 257
Cdd:cd03819  131 IAVSELVRDHLIEAL------GVDPERIRVIPNgvdtdrfpPEAEAEERAQLGLPEGKPVVGYVGRLS-PEKGWLLLVDA 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 258 LAqeKWKyRNLQVSFF--GEGANRDTLIDMANLLGLKN-VNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGR 334
Cdd:cd03819  204 AA--ELK-DEPDFRLLvaGDGPERDEIRRLVERLGLRDrVTFTGFREDVPAALAASDVVVLPSLHEEFGRVALEAMACGT 280

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505028577 335 IAITTNVGGIPEVLEDNITG-FIAKGTSfAAIDEALERAWQRSDEWENMGTQAS 387
Cdd:cd03819  281 PVVATDVGGAREIVVHGRTGlLVPPGDA-EALADAIRAAKLLPEAREKLQAAAA 333
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
 240-356 2.10e-19

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: 86.69  E-value: 2.10e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 240 CVGRLWlVDKGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDM-ANLLGLKNVNFPGF---VENIESVWQDYHALIL 315
Cdd:cd01635  115 SVGRLV-PEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEALaAALGLLERVVIIGGlvdDEVLELLLAAADVFVL 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 505028577 316 PSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFI 356
Cdd:cd01635  194 PSRSEGFGLVLLEAMAAGKPVIATDVGGIPEFVVDGENGLL 234
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
 23-387 1.40e-18

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: 86.61  E-value: 1.40e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  23 FISSCFDVW--GGSEELLAATAKYLKQQGHEVHVFklqisdhpRILELQAAGVKVIAlnslRLMGIKHFVFKCIYHLvrl 100
Cdd:cd03823    4 LVNSLYPPQrvGGAEISVHDLAEALVAEGHEVAVL--------TAGVGPPGQATVAR----SVVRYRRAPDETLPLA--- 68

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 101 lkfLPLPASWYFIHTDPQRTFILQT-LRRIKPSLVVISqgdNFDGLNYG--DICLELKLPYVMLSHKAshhiWPVDaLRP 177
Cdd:cd03823   69 ---LKRRGYELFETYNPGLRRLLARlLEDFRPDVVHTH---NLSGLGASllDAARDLGIPVVHTLHDY----WLLC-PRQ 137

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 178 MMRKVFQqaKRCFFVSEH--NLFLTQmqlGQGLSHAEVVRNpyltsateSLPWPEIKDNC-------FKLACVGRLwLVD 248
Cdd:cd03823  138 FLFKKGG--DAVLAPSRFtaNLHEAN---GLFSARISVIPN--------AVEPDLAPPPRrrpgterLRFGYIGRL-TEE 203

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 249 KGQDILLEV---LAQEKWKyrnlqVSFFGEGANRDtlidMANLLGLKNVNFPGFV--ENIESVWQDYHALILPSR-AEGL 322
Cdd:cd03823  204 KGIDLLVEAfkrLPREDIE-----LVIAGHGPLSD----ERQIEGGRRIAFLGRVptDDIKDFYEKIDVLVVPSIwPEPF 274

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505028577 323 PITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQAS 387
Cdd:cd03823  275 GLVVREAIAAGLPVIASDLGGIAELIQPGVNGLLFAPGDAEDLAAAMRRLLTDPALLERLRAGAE 339
stp2 TIGR03088
sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match ...
 217-371 1.93e-16

sugar transferase, PEP-CTERM/EpsH1 system associated; Members of this family include a match to the pfam00534 Glycosyl transferases group 1 domain. Nearly all are found in species that encode the PEP-CTERM/exosortase system predicted to act in protein sorting in a number of Gram-negative bacteria. In particular, these transferases are found proximal to a particular variant of exosortase, EpsH1, which appears to travel with a conserved group of genes summarized by Genome Property GenProp0652. The nature of the sugar transferase reaction catalyzed by members of this clade is unknown and may conceivably be variable with respect to substrate by species, but we hypothesize a conserved substrate.


Pssm-ID: 132132 [Multi-domain]  Cd Length: 374  Bit Score: 80.15  E-value: 1.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  217 PYLTSATESLPWPEIKDNCFKLACVGRLWLVdKGQDILLEVLA----QEKWKYRNLQVSFFGEGANRDTLIDMANLLGLK 292
Cdd:TIGR03088 176 PSRGDRSPILPPDFFADESVVVGTVGRLQAV-KDQPTLVRAFAllvrQLPEGAERLRLVIVGDGPARGACEQMVRAAGLA 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  293 N-VNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALER 371
Cdd:TIGR03088 255 HlVWLPGERDDVPALMQALDLFVLPSLAEGISNTILEAMASGLPVIATAVGGNPELVQHGVTGALVPPGDAVALARALQP 334
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
 241-386 1.40e-15

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: 77.70  E-value: 1.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 241 VGRLWLVdKGQDILLEVLaqekwKYRNLQVSFFGEGANRDTLIDMANLLGLKNVNFPGFVENIESVwqDYH----ALILP 316
Cdd:cd03795  197 IGRLVYY-KGLDYLIEAA-----QYLNYPIVIGGEGPLKPDLEAQIELNLLDNVKFLGRVDDEEKV--IYLhlcdVFVFP 268

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 505028577 317 S--RAEGLPITLVEAMMCGRIAITTNVG-GIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:cd03795  269 SvlRSEAFGIVLLEAMMCGKPVISTNIGtGVPYVNNNGETGLVVPPKDPDALAEAIDKLLSDEELRESYGENA 341
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
 226-386 5.76e-15

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: 76.13  E-value: 5.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 226 LPWPEIKdncFKLACVGRLWLVdKGQDILLEVLAQEKWKYRNLQVSFFG----EGANRDT--LIDMANLLGL-KNVNFPG 298
Cdd:cd03800  214 LLLPPDK---PVVLALGRLDPR-KGIDTLVRAFAQLPELRELANLVLVGgpsdDPLSMDReeLAELAEELGLiDRVRFPG 289

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 299 FVENIESV----WQDyhALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQ 374
Cdd:cd03800  290 RVSRDDLPelyrAAD--VFVVPSLYEPFGLTAIEAMACGTPVVATAVGGLQDIVRDGRTGLLVDPHDPEALAAALRRLLD 367

                        170
                 ....*....|..
gi 505028577 375 RSDEWENMGTQA 386
Cdd:cd03800  368 DPALWQRLSRAG 379
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
 42-404 2.00e-14

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: 74.24  E-value: 2.00e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  42 AKYLKQQGHEVHVFKLQISDHPRilelqAAGVKVIALNSLrLMGIKHFvfkciYHLVRLLKFLPL--PASWYF--IHTdp 117
Cdd:cd03817   24 ARALEKRGHEVYVITPSDPGAED-----EEEVVRYRSFSI-PIRKYHR-----QHIPFPFKKAVIdrIKELGPdiIHT-- 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 118 QRTFILQTLrrikpslvvisqgdnfdGLNygdICLELKLPYVMLSH----KASHHIWPVDAL-RPMMRKVFQqaKRCFFV 192
Cdd:cd03817   91 HTPFSLGKL-----------------GLR---IARKLKIPIVHTYHtmyeDYLHYIPKGKLLvKAVVRKLVR--RFYNHT 148

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 193 sEHNLFLTQMQLGQ-----GLSHAEVVRNPYLTSATESLPWPE------IKDNCFKLACVGRL-WlvDKGQDILLEVLAQ 260
Cdd:cd03817  149 -DAVIAPSEKIKDTlreygVKGPIEVIPNGIDLDKFEKPLNTEerrklgLPPDEPILLYVGRLaK--EKNIDFLLRAFAE 225

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 261 EKWKYrNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIE--SVWQDYHALILPSRAEGLPITLVEAMMCGRIAI 337
Cdd:cd03817  226 LKKEP-NIKLVIVGDGPEREELKELARELGLaDKVIFTGFVPREElpEYYKAADLFVFASTTETQGLVYLEAMAAGLPVV 304

                        330       340       350       360       370       380
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 505028577 338 TTNVGGIPEVLEDNITGFIAKGTSFaAIDEALERAWQRSDEWENMGTQASISIRK-QIPKDPERLFAD 404
Cdd:cd03817  305 AAKDPAASELVEDGENGFLFEPNDE-TLAEKLLHLRENLELLRKLSKNAEISAREfAFAKSVEKLYEE 371
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
 240-401 3.05e-14

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: 73.64  E-value: 3.05e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 240 CVGRLwlVD-KGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGlkNVNFPGFVENIESV-WQD-YHALILP 316
Cdd:cd05844  194 FVGRL--VEkKGCDVLIEAFRRLAARHPTARLVIAGDGPLRPALQALAAALG--RVRFLGALPHAEVQdWMRrAEIFCLP 269

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 317 S------RAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQASISI 390
Cdd:cd05844  270 SvtaasgDSEGLGIVLLEAAACGVPVVSSRHGGIPEAILDGETGFLVPEGDVDALADALQALLADRALADRMGGAARAFV 349

                        170
                 ....*....|...
gi 505028577 391 RKQ--IPKDPERL 401
Cdd:cd05844  350 CEQfdIRVQTAKL 362
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
 231-350 3.87e-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: 73.25  E-value: 3.87e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 231 IKDNCFKLACVGRLwlVD-KGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQ 308
Cdd:cd04951  184 LKNDEFVILNVGRL--TEaKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELERLICNLNLvDRVILLGQISNISEYYN 261

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 505028577 309 DYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLED 350
Cdd:cd04951  262 AADLFVLSSEWEGFGLVVAEAMACERPVVATDAGGVAEVVGD 303
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 229-355 6.38e-14

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: 72.71  E-value: 6.38e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 229 PEIKDNCFKLACVGRLwLVDKGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIESVW 307
Cdd:cd03812  185 LLILEDKLVLGHVGRF-NEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLeDKVIFLGFRNDVSEIL 263

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 505028577 308 QDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGF 355
Cdd:cd03812  264 SAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEFL 311
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
 232-383 1.07e-13

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: 71.71  E-value: 1.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 232 KDNCFKLACVGRLwLVDKGQDILLEVLAQEKWKYRNLQVSFFGEG---ANRDTLI------DMANLLGLKNVnfpgfvEN 302
Cdd:cd03799  171 LDGKIRILTVGRL-TEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGdlkEQLQQLIqelnigDCVKLLGWKPQ------EE 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 303 IESVWQDYHALILPS------RAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRS 376
Cdd:cd03799  244 IIEILDEADIFIAPSvtaadgDQDGPPNTLKEAMAMGLPVISTEHGGIPELVEDGVSGFLVPERDAEAIAEKLTYLIEHP 323


                 ....*..
gi 505028577 377 DEWENMG 383
Cdd:cd03799  324 AIWPEMG 330
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
 236-386 1.47e-12

accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases and is named after gtfA in Streptococcus gordonii, where it plays a role in the O-linked glycosylation of GspB, a cell surface glycoprotein involved in platelet binding. In general glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. This group of glycosyltransferases is most closely related to the previously defined glycosyltransferase family 1 (GT1). The members of this family may transfer UDP, ADP, GDP, or CMP linked sugars. The diverse enzymatic activities among members of this family reflect a wide range of biological functions. The protein structure available for this family has the GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility. The members of this family are found in bacteria.


Pssm-ID: 340855 [Multi-domain]  Cd Length: 328  Bit Score: 68.10  E-value: 1.47e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 236 FKLACVGRLWLvDKGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQDYHALI 314
Cdd:cd04949  161 NKIITISRLAP-EKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLeDNVFLKGYHSNLDQEYQDAYLSL 239

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505028577 315 LPSRAEGLPITLVEAMMCGRIAITTNVG-GIPEVLEDNITGF-IAKG---TSFAAIDEALErawqRSDEWENMGTQA 386
Cdd:cd04949  240 LTSQMEGFGLTLMEAIGHGLPVVSYDVKyGPSELIEDGENGYlIEKNnidALADKIIELLN----DPEKLQQFSEES 312
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
 249-386 1.51e-12

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: 68.51  E-value: 1.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 249 KGQDILLEVLAQEKWKyRNLQVSFFGEGANRDTLIDManllglkNVNFPGFVENIESVWQDYHA---LILPSRAEGLPIT 325
Cdd:cd03825  208 KGFDELIEALKLLATK-DDLLLVVFGKNDPQIVILPF-------DIISLGYIDDDEQLVDIYSAadlFVHPSLADNLPNT 279

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505028577 326 LVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:cd03825  280 LLEAMACGTPVVAFDTGGSPEIVQHGVTGYLVPPGDVQALAEAIEWLLANPKERESLGERA 340
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
 249-356 2.76e-11

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: 64.68  E-value: 2.76e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 249 KGQDILLEVLA--QEKWKYRNLQVsffGEGANRDTLIDMANLLGLKN-VNFPGFVENIESVWQDYHALILPSRAEGLPIT 325
Cdd:cd04962  209 KRIDDVVRVFArvRRKIPAKLLLV---GDGPERVPAEELARELGVEDrVLFLGKQDDVEELLSIADLFLLPSEKESFGLA 285

                         90       100       110
                 ....*....|....*....|....*....|.
gi 505028577 326 LVEAMMCGRIAITTNVGGIPEVLEDNITGFI 356
Cdd:cd04962  286 ALEAMACGVPVVSSNAGGIPEVVKHGETGFL 316
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 89-382 2.96e-11

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: 64.31  E-value: 2.96e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  89 FVFKCIYHLVRLLKFLPLPASWYFIHTDPQRTFILqtLRRIKPSLVVISQGDNFDGLNYGDICLELKLPYVMLSHKASHH 168
Cdd:cd03809   37 LAVPPLPGELLRLLREYPELSLGVIKIKLWRELAL--LRWLQILLPKKDKPDLLHSPHNTAPLLLKGCPQVVTIHDLIPL 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 169 IWP-------VDALRPMMRKVFQQAKRCFFVSEH--NLFLTQmqLGQGLSHAEVVRNPYLTSATESLPWPEIKDN----C 235
Cdd:cd03809  115 RYPeffpkrfRLYYRLLLPISLRRADAIITVSEAtrDDIIKF--YGVPPEKIVVIPLGVDPSFFPPESAAVLIAKyllpE 192

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 236 FKLACVGRLWlVDKGQDILLEVLAQEKWKYRNLQVSFFGE-GANRDTLIDMANLLGL-KNVNFPGFV--ENIESVWQDYH 311
Cdd:cd03809  193 PYFLYVGTLE-PRKNHERLLKAFALLKKQGGDLKLVIVGGkGWEDEELLDLVKKLGLgGRVRFLGYVsdEDLPALYRGAR 271

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 505028577 312 ALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNitGFIAKGTSFAAIDEALERAWQRSDEWENM 382
Cdd:cd03809  272 AFVFPSLYEGFGLPVLEAMACGTPVIASNISVLPEVAGDA--ALYFDPLDPESIADAILRLLEDPSLREEL 340
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
 252-356 8.65e-10

amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. AmsK is involved in the biosynthesis of amylovoran, which functions as a virulence factor. It functions as a glycosyl transferase which transfers galactose from UDP-galactose to a lipid-linked amylovoran-subunit precursor. The members of this family are found mainly in bacteria and Archaea.


Pssm-ID: 340854 [Multi-domain]  Cd Length: 401  Bit Score: 60.17  E-value: 8.65e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 252 DILLEVLAQEKWKYRNLQVSF--FGEGANRDTLIDMA-NLLGLKNVNFPGFVENIEsVWQ-----DYHALILPSRAEGLP 323
Cdd:cd04946  240 DLIIETLNSLCVAHPSICISWthIGGGPLKERLEKLAeNKLENVKVNFTGEVSNKE-VKQlykenDVDVFVNVSESEGIP 318

                         90       100       110
                 ....*....|....*....|....*....|...
gi 505028577 324 ITLVEAMMCGRIAITTNVGGIPEVLEDNITGFI 356
Cdd:cd04946  319 VSIMEAISFGIPVIATNVGGTREIVENETNGLL 351
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 286-383 2.03e-09

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: 59.27  E-value: 2.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 286 ANLLGLKNVNFPGFVeNIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNI-----TGFIAKGT 360
Cdd:cd03813  348 ASLGLENKVKFLGFQ-NIKEYYPKLGLLVLTSISEGQPLVILEAMASGVPVVATDVGSCRELIYGADdalgqAGLVVPPA 426

                         90       100
                 ....*....|....*....|...
gi 505028577 361 SFAAIDEALERAWQRSDEWENMG 383
Cdd:cd03813  427 DPEALAEALIKLLRDPELRQAFG 449
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
 249-408 4.40e-08

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: 54.68  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 249 KGQDILLEVLAQEKWKYRNLQVSFFG--EGANRDTLIDMANLLGLKNVNFPGFV--ENIESVWQDYHALILPSRAEGLPI 324
Cdd:cd03821  217 KGLDLLIRAARKLAEQGRDWHLVIAGpdDGAYPAFLQLQSSLGLGDRVTFTGPLygEAKWALYASADLFVLPSYSENFGN 296

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 325 TLVEAMMCGRIAITTNVGGIPEVLEDNItGFIAKgTSFAAIDEALERAWQRSDEWENMGTQASiSIRKQIPKDPERLFAD 404
Cdd:cd03821  297 VVAEALACGLPVVITDKCGLSELVEAGC-GVVVD-PNVSSLAEALAEALRDPADRKRLGEMAR-RARQVEENFSWEAVAG 373


                 ....
gi 505028577 405 KLLQ 408
Cdd:cd03821  374 QLGE 377
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
 249-353 1.89e-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: 53.01  E-value: 1.89e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 249 KGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGLKN-VNFPGFV--ENIESVWQDYHALILPSRAEGLPIT 325
Cdd:cd03796  206 KGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDrVELLGAVphEEVRDVLVQGHIFLNTSLTEAFCIA 285

                         90       100
                 ....*....|....*....|....*...
gi 505028577 326 LVEAMMCGRIAITTNVGGIPEVLEDNIT 353
Cdd:cd03796  286 IVEAASCGLLVVSTRVGGIPEVLPPDMI 313
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
 38-387 3.85e-07

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: 51.91  E-value: 3.85e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  38 LAATAKYLKQQGHEVHVfklqISDHPRIlELQAAGVKVIALNSLRLMGikhfvfkciYHLVRLlkFLPLPAswyfihtdp 117
Cdd:cd03814   20 LERLVDHLRRRGHEVRV----VAPGPFD-EAESAEGRVVSVPSFPLPF---------YPEYRL--ALPLPR--------- 74

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 118 qrtFILQTLRRIKPSLVVISQGDNFdGLNYGDICLELKLPYVMLSH-------KASHHIWPVDALRPMMRKVFQQAKRCF 190
Cdd:cd03814   75 ---RVRRLIKEFQPDIIHIATPGPL-GLAALRAARRLGLPVVTSYHtdfpeylSYYTLGPLSWLAWAYLRWFHNPFDTTL 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 191 FVSEhnlFLTQMQLGQGLSHAEVV-------------RNPYLTSATESLPWPeikdncfKLACVGRLwLVDKGQDILLEv 257
Cdd:cd03814  151 VPSP---SIARELEGHGFERVRLWprgvdtelfhpsrRDAALRRRLGPPGRP-------LLLYVGRL-APEKNLEALLD- 218

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 258 LAQEKWKYRNLQVSFFGEGANRDTLidMANLLglkNVNFPGFVENIEsvWQDYHA----LILPSRAEGLPITLVEAMMCG 333
Cdd:cd03814  219 ADLPLAASPPVRLVVVGDGPARAEL--EARGP---DVIFTGFLTGEE--LARAYAsadvFVFPSRTETFGLVVLEAMASG 291

                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....
gi 505028577 334 RIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDEALERAWQRSDEWENMGTQAS 387
Cdd:cd03814  292 LPVVAADAGGPRDIVRPGGTGALVEPGDAAAFAAALRALLEDPELRRRMAARAR 345
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
 241-371 4.08e-07

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 52.34  E-value: 4.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 241 VGRLWLVDKGQDILLEVLAQEKWKYRNLQVSFF--GEGANRDTLIDMANLLGL-KNVNFPGFVENIESVWQDYHALILPS 317
Cdd:PRK15179 520 VGTVMRVDDNKRPFLWVEAAQRFAASHPKVRFImvGGGPLLESVREFAQRLGMgERILFTGLSRRVGYWLTQFNAFLLLS 599

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 505028577 318 RAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAID--EALER 371
Cdd:PRK15179 600 RFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEGVTGLTLPADTVTAPDvaEALAR 655
PRK15490 PRK15490
Vi polysaccharide biosynthesis glycosyltransferase TviE;
274-381 1.01e-06

Vi polysaccharide biosynthesis glycosyltransferase TviE;


Pssm-ID: 185387 [Multi-domain]  Cd Length: 578  Bit Score: 50.85  E-value: 1.01e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 274 GEGANRDTLIDMANLLG-LKNVNFPGFVENIESVWQDYHALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNI 352
Cdd:PRK15490 436 GDGDLRAEAQKRAEQLGiLERILFVGASRDVGYWLQKMNVFILFSRYEGLPNVLIEAQMVGVPVISTPAGGSAECFIEGV 515

                         90       100
                 ....*....|....*....|....*....
gi 505028577 353 TGFIAKGTSFAAIDEALERAWQRSDEWEN 381
Cdd:PRK15490 516 SGFILDDAQTVNLDQACRYAEKLVNLWRS 544
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
 274-380 1.48e-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: 49.98  E-value: 1.48e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 274 GEGANRDTLIDMANllglKNVNFPGFVEniESVWQDY----HALILPSRaEGLPITLVEAMMCGRIAITTNVGGIPEVLE 349
Cdd:cd03804  232 GDGPDLDRLRAMAS----PNVEFLGYQP--DEVLKELlskaRAFVFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVR 304

                         90       100       110
                 ....*....|....*....|....*....|.
gi 505028577 350 DNITGFIAKGTSFAAIDEALERAWQRSDEWE 380
Cdd:cd03804  305 PGPTGILFGEQTVESLKAAVEEFEQNFDRFK 335
GT4_trehalose_phosphorylase cd03792
trehalose phosphorylase and similar proteins; Trehalose phosphorylase (TP) reversibly ...
 317-393 1.67e-06

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: 49.63  E-value: 1.67e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 505028577 317 SRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAIDeaLERAWQRSDEWENMGTQASISIRKQ 393
Cdd:cd03792  287 STREGFGLTVSEALWKGKPVIATPAGGIPLQVIDGETGFLVNSVEGAAVR--ILRLLTDPELRRKMGLAAREHVRDN 361
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
 238-371 4.12e-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: 45.36  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 238 LACVGRLWlVDKGQDILLEVLAQEKWKyrnLQVsfFGEGANRDTLIDMANLLGLKNVNFPGFVENIE--SVWQDYHALIL 315
Cdd:cd03802  172 LAFLGRIA-PEKGLEDAIRVARRAGLP---LKI--AGKVRDEDYFYYLQEPLPGPRIEFIGEVGHDEkqELLGGARALLF 245

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 505028577 316 PSR---AEGLPItlVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKGTSFAAidEALER 371
Cdd:cd03802  246 PINwdePFGLVM--IEAMACGTPVIAYRRGGLPEVIQHGETGFLVDSVEEMA--EAIAN 300
PRK09922 PRK09922
lipopolysaccharide 1,6-galactosyltransferase;
201-354 6.15e-05

lipopolysaccharide 1,6-galactosyltransferase;


Pssm-ID: 182148 [Multi-domain]  Cd Length: 359  Bit Score: 44.70  E-value: 6.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 201 QMQ-LGQGLSHAEVVRNPyLTSATESLPWPEiKDNCFKLACVGRLwLVDKGQDI--LLEVLAQEKWKYrnlQVSFFGEGA 277
Cdd:PRK09922 147 QMMaRGISAQRISVIYNP-VEIKTIIIPPPE-RDKPAVFLYVGRL-KFEGQKNVkeLFDGLSQTTGEW---QLHIIGDGS 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 278 NRDTLIDMANLLGLK-NVNFPGFVENI-ESVWQDYH---ALILPSRAEGLPITLVEAMMCGRIAITTN-VGGIPEVLEDN 351
Cdd:PRK09922 221 DFEKCKAYSRELGIEqRIIWHGWQSQPwEVVQQKIKnvsALLLTSKFEGFPMTLLEAMSYGIPCISSDcMSGPRDIIKPG 300


                 ...
gi 505028577 352 ITG 354
Cdd:PRK09922 301 LNG 303
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
 240-372 5.89e-04

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 42.01  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 240 CVGRLWlVDKGQDILLEVLAqekwKYRNLQVSFFGEGANRDTLIDManLLGLkNVNFPGFVENiESVWQDYHAL---ILP 316
Cdd:PLN02871 268 YVGRLG-AEKNLDFLKRVME----RLPGARLAFVGDGPYREELEKM--FAGT-PTVFTGMLQG-DELSQAYASGdvfVMP 338

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 317 SRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGfiakGTSF----AAIDEALERA 372
Cdd:PLN02871 339 SESETLGFVVLEAMASGVPVVAARAGGIPDIIPPDQEG----KTGFlytpGDVDDCVEKL 394
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
 230-382 8.41e-04

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


Pssm-ID: 340822 [Multi-domain]  Cd Length: 474  Bit Score: 41.39  E-value: 8.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 230 EIKDNCFKLACVGRLwlVD-KGQDILLEVLaqEKWKYRNLQVSFFGEGanRDTLIDMANLLGLKnvnFPGFVenieSVWQ 308
Cdd:cd03791  289 PVDPDAPLFGFVGRL--TEqKGVDLILDAL--PELLEEGGQLVVLGSG--DPEYEQAFRELAER---YPGKV----AVVI 355

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 309 DYH------------ALILPSRAE--GLpiTLVEAMMCGRIAITTNVGG-----IPEVLEDNI-TGFIAKGTSFAAIDEA 368
Cdd:cd03791  356 GFDealahriyagadFFLMPSRFEpcGL--VQMYAMRYGTLPIVRRTGGladtvFDYDPETGEgTGFVFEDYDAEALLAA 433

                        170
                 ....*....|....*..
gi 505028577 369 LERA---WQRSDEWENM 382
Cdd:cd03791  434 LRRAlalYRNPELWRKL 450
PLN00142 PLN00142
sucrose synthase
 312-355 1.31e-03

sucrose synthase


Pssm-ID: 215073 [Multi-domain]  Cd Length: 815  Bit Score: 41.12  E-value: 1.31e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 505028577 312 ALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGF 355
Cdd:PLN00142 669 AFVQPALYEAFGLTVVEAMTCGLPTFATCQGGPAEIIVDGVSGF 712
PLN02846 PLN02846
digalactosyldiacylglycerol synthase
 249-340 1.78e-03

digalactosyldiacylglycerol synthase


Pssm-ID: 166487 [Multi-domain]  Cd Length: 462  Bit Score: 40.57  E-value: 1.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577 249 KGQDILLEVLAQEKWKYRNLQVSFFGEGANRDTLIDMANLLGLKNVNFPGFvENIESVWQDYHALILPSRAEGLPITLVE 328
Cdd:PLN02846 241 KGYKELLKLLHKHQKELSGLEVDLYGSGEDSDEVKAAAEKLELDVRVYPGR-DHADPLFHDYKVFLNPSTTDVVCTTTAE 319

                         90
                 ....*....|..
gi 505028577 329 AMMCGRIAITTN 340
Cdd:PLN02846 320 ALAMGKIVVCAN 331
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
32-195 3.30e-03

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 38.28  E-value: 3.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577   32 GGSEELLAATAKYLKQQGHEVHVFKLQISDHPRILElqaagvkvialnslrlmgikhfvfkciyHLVRLLKFLPLPASWY 111
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEV----------------------------VRVVRVPRVPLPLPPR 52

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505028577  112 FIHTDPQRTFILQTLRRIKPSlVVISQGDNFDGLNYGDICLELKLPYVMLSH--------KASHHIWPVDALRPMMRKVF 183
Cdd:pfam13439  53 LLRSLAFLRRLRRLLRRERPD-VVHAHSPFPLGLAALAARLRLGIPLVVTYHglfpdykrLGARLSPLRRLLRRLERRLL 131

                         170
                  ....*....|..
gi 505028577  184 QQAKRCFFVSEH 195
Cdd:pfam13439 132 RRADRVIAVSEA 143
Glyco_trans_1_2 pfam13524
Glycosyl transferases group 1;
312-386 4.10e-03

Glycosyl transferases group 1;


Pssm-ID: 433281 [Multi-domain]  Cd Length: 93  Bit Score: 36.43  E-value: 4.10e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 505028577  312 ALILPSRAEGLPITLVEAMMCGRIAITTNVGGIPEVLEDNITGFIAKgtSFAAIDEALERAWQRSDEWENMGTQA 386
Cdd:pfam13524   2 VLNPSRRPDSPNMRVFEAAACGAPLLTDRTPGLEELFEPGEEILLYR--DPEELAEKIRYLLEHPEERRAIAAAG 74
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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