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Conserved domains on  [gi|1622294796|ref|WP_136262550|]
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glycosyltransferase family 4 protein [Streptococcus pyogenes]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133603)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
2-376 1.11e-129

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: 379.32  E-value: 1.11e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIA 81
Cdd:cd03817     1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  82 KHYNLDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTQYEDYVSYIANGKIIRPSMVKPLLRGYLKDLDGVICPSRIVLN 161
Cdd:cd03817    81 KELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 162 LLEGYEVTIPKRVIPTGIPLEKYIRDDITAEevtnlKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENaKIKL 241
Cdd:cd03817   161 TLREYGVKGPIEVIPNGIDLDKFEKPLNTEE-----RRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP-NIKL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 242 IIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDV 321
Cdd:cd03817   235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASEL 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 322 VTDKMFGTLYYAETDLTDAIIDAILKTPVMDKRLLAKKRYEISAQHFGKSIYTFY 376
Cdd:cd03817   315 VEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLY 369
 
Name Accession Description Interval E-value
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
2-376 1.11e-129

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: 379.32  E-value: 1.11e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIA 81
Cdd:cd03817     1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  82 KHYNLDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTQYEDYVSYIANGKIIRPSMVKPLLRGYLKDLDGVICPSRIVLN 161
Cdd:cd03817    81 KELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 162 LLEGYEVTIPKRVIPTGIPLEKYIRDDITAEevtnlKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENaKIKL 241
Cdd:cd03817   161 TLREYGVKGPIEVIPNGIDLDKFEKPLNTEE-----RRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP-NIKL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 242 IIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDV 321
Cdd:cd03817   235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASEL 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 322 VTDKMFGTLYYAETDLTDAIIDAILKTPVMDKRLLAKKRYEISAQHFGKSIYTFY 376
Cdd:cd03817   315 VEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLY 369
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
16-182 1.18e-32

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 121.49  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  16 GVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIAKHYNLDIIHTQTEF 95
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  96 SLGLLGKMIGKALRIPVVHTYHTQYEDYVSYIANGKIIRPsMVKPLLRGYLKDLDGVICPSRIVLNLLEGYEVTIPKR-- 173
Cdd:pfam13439  82 PLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRR-LLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKir 160

                  ....*....
gi 1622294796 174 VIPTGIPLE 182
Cdd:pfam13439 161 VIPNGVDLE 169
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
2-363 9.18e-22

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 97.09  E-value: 9.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTD-TYFPQVSGVATSIRTLKEELEKEGHEVYIFTTtDRDV-KRFEDPTIIRLPSVPF-----VSFT---DRRVvy 71
Cdd:PLN02871   60 RIALFVEpSPFSYVSGYKNRFQNFIRYLREMGDEVLVVTT-DEGVpQEFHGAKVIGSWSFPCpfyqkVPLSlalSPRI-- 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  72 rglissYKIAKHYNLDIIHTQtefSLGLL---GKMIGKALRIPVVHTYHTQYEDYV-SYIANGkiirpsMVKP---LLRG 144
Cdd:PLN02871  137 ------ISEVARFKPDLIHAS---SPGIMvfgALFYAKLLCVPLVMSYHTHVPVYIpRYTFSW------LVKPmwdIIRF 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 145 YLKDLDGVICPSRIVLNLLEGYEVTIPKR--VIPTGIPLEKY---IRDDITAEEVTNlkaelGIAGDETMLlSLSRISYE 219
Cdd:PLN02871  202 LHRAADLTLVTSPALGKELEAAGVTAANRirVWNKGVDSESFhprFRSEEMRARLSG-----GEPEKPLIV-YVGRLGAE 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 220 KNIQAIINqmpaILAENAKIKLIIVGDGPYLQDL-KHLAmqlevDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGL 298
Cdd:PLN02871  276 KNLDFLKR----VMERLPGARLAFVGDGPYREELeKMFA-----GTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGF 346
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622294796 299 TYIESLASGTPIIAHGNPYLDDVVTDKMFG--TLYYAETDLTDAI--IDAILKTPVMDKRLLAKKRYEI 363
Cdd:PLN02871  347 VVLEAMASGVPVVAARAGGIPDIIPPDQEGktGFLYTPGDVDDCVekLETLLADPELRERMGAAAREEV 415
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
277-368 1.14e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 64.63  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 277 VALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMFGTLYYAET--DLTDAIIDaILKTPVMDKR 354
Cdd:COG0438    14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDpeALAEAILR-LLEDPELRRR 92
                          90
                  ....*....|....
gi 1622294796 355 lLAKKRYEISAQHF 368
Cdd:COG0438    93 -LGEAARERAEERF 105
 
Name Accession Description Interval E-value
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
2-376 1.11e-129

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: 379.32  E-value: 1.11e-129
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIA 81
Cdd:cd03817     1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITPSDPGAEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVIDRI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  82 KHYNLDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTQYEDYVSYIANGKIIRPSMVKPLLRGYLKDLDGVICPSRIVLN 161
Cdd:cd03817    81 KELGPDIIHTHTPFSLGKLGLRIARKLKIPIVHTYHTMYEDYLHYIPKGKLLVKAVVRKLVRRFYNHTDAVIAPSEKIKD 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 162 LLEGYEVTIPKRVIPTGIPLEKYIRDDITAEevtnlKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENaKIKL 241
Cdd:cd03817   161 TLREYGVKGPIEVIPNGIDLDKFEKPLNTEE-----RRKLGLPPDEPILLYVGRLAKEKNIDFLLRAFAELKKEP-NIKL 234
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 242 IIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDV 321
Cdd:cd03817   235 VIVGDGPEREELKELARELGLADKVIFTGFVPREELPEYYKAADLFVFASTTETQGLVYLEAMAAGLPVVAAKDPAASEL 314
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 322 VTDKMFGTLYYAETDLTDAIIDAILKTPVMDKRLLAKKRYEISAQHFGKSIYTFY 376
Cdd:cd03817   315 VEDGENGFLFEPNDETLAEKLLHLRENLELLRKLSKNAEISAREFAFAKSVEKLY 369
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
2-347 1.27e-51

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: 178.12  E-value: 1.27e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVsftDRRVVYRGLISSYKIA 81
Cdd:cd03801     1 KILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSL---AALLRARRLLRELRPL 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  82 KHY-NLDIIHTQTEFSLgLLGKMIGKALRIPVVHTYHTQYEDYVSYIANGKiirpsmvKPLLRGYLKDL---DGVICPSR 157
Cdd:cd03801    78 LRLrKFDVVHAHGLLAA-LLAALLALLLGAPLVVTLHGAEPGRLLLLLAAE-------RRLLARAEALLrraDAVIAVSE 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 158 IVLNLLEGYEVTIPKR--VIPTGIPLEKYIRDditaeevtnLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAE 235
Cdd:cd03801   150 ALRDELRALGGIPPEKivVIPNGVDLERFSPP---------LRRKLGIPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRR 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 236 NAKIKLIIVG-DGPYLQDLKhlAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHG 314
Cdd:cd03801   221 GPDVRLVIVGgDGPLRAELE--ELELGLGDRVRFLGFVPDEELPALYAAADVFVLPSRYEGFGLVVLEAMAAGLPVVATD 298
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1622294796 315 NPYLDDVVTDKmfGTLYYAETDLTDAIIDAILK 347
Cdd:cd03801   299 VGGLPEVVEDG--EGGLVVPPDDVEALADALLR 329
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
2-312 5.68e-50

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: 173.63  E-value: 5.68e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIA 81
Cdd:cd03814     1 RIALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVAPGPFDEAESAEGRVVSVPSFPLPFYPEYRLALPLPRRVRRLI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  82 KHYNLDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTQYEDYVSYIAngkiirPSMVKPLLRGYLKDL----DGVICPSR 157
Cdd:cd03814    81 KEFQPDIIHIATPGPLGLAALRAARRLGLPVVTSYHTDFPEYLSYYT------LGPLSWLAWAYLRWFhnpfDTTLVPSP 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 158 IVLNLLEGYEVTiPKRVIPTGIPLEKY---IRDDItaeevtnLKAELGiAGDETMLLSLSRISYEKNIQAIINQMPAiLA 234
Cdd:cd03814   155 SIARELEGHGFE-RVRLWPRGVDTELFhpsRRDAA-------LRRRLG-PPGRPLLLYVGRLAPEKNLEALLDADLP-LA 224
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622294796 235 ENAKIKLIIVGDGPYLQDLKHlamqleVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIA 312
Cdd:cd03814   225 ASPPVRLVVVGDGPARAELEA------RGPDVIFTGFLTGEELARAYASADVFVFPSRTETFGLVVLEAMASGLPVVA 296
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
9-378 1.38e-35

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: 134.40  E-value: 1.38e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   9 TYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEdPTIIRLPSVpFVSFTdrrVVYRGLISSYKIAKHYNLDI 88
Cdd:cd03819     5 TPALEIGGAETYILDLARALAERGHRVLVVTAGGPLLPRLR-QIGIGLPGL-KVPLL---RALLGNVRLARLIRRERIDL 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  89 IHTQTeFSLGLLGKMIGKALRIPVVHTYHtqyedyVSYIANgKIIRPSMVKPLLRGylkdlDGVICPSRIVLNLLEGYEV 168
Cdd:cd03819    80 IHAHS-RAPAWLGWLASRLTGVPLVTTVH------GSYLAT-YHPKDFALAVRARG-----DRVIAVSELVRDHLIEALG 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 169 TIPKR--VIPTGIPLEKYirddiTAEEVTNLKAELGIAGDETMLLSLSRISYEKNIQAIInQMPAILAENAKIKLIIVGD 246
Cdd:cd03819   147 VDPERirVIPNGVDTDRF-----PPEAEAEERAQLGLPEGKPVVGYVGRLSPEKGWLLLV-DAAAELKDEPDFRLLVAGD 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 247 GPYLQDLKHLAMQLEVDKHVTFTGMvsHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKM 326
Cdd:cd03819   221 GPERDEIRRLVERLGLRDRVTFTGF--REDVPAALAASDVVVLPSLHEEFGRVALEAMACGTPVVATDVGGAREIVVHGR 298
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622294796 327 FGTLYYAETD--LTDAIIDAILKTPvmdkrlLAKKRYEISAQhfGKSIYTFYLD 378
Cdd:cd03819   299 TGLLVPPGDAeaLADAIRAAKLLPE------AREKLQAAAAL--TEAVRELLLR 344
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
16-182 1.18e-32

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 121.49  E-value: 1.18e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  16 GVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIAKHYNLDIIHTQTEF 95
Cdd:pfam13439   2 GVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVRVVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVHAHSPF 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  96 SLGLLGKMIGKALRIPVVHTYHTQYEDYVSYIANGKIIRPsMVKPLLRGYLKDLDGVICPSRIVLNLLEGYEVTIPKR-- 173
Cdd:pfam13439  82 PLGLAALAARLRLGIPLVVTYHGLFPDYKRLGARLSPLRR-LLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKir 160

                  ....*....
gi 1622294796 174 VIPTGIPLE 182
Cdd:pfam13439 161 VIPNGVDLE 169
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
16-365 2.43e-31

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: 122.85  E-value: 2.43e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  16 GVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYK-IAKHYNLDIIHTQTE 94
Cdd:cd03811    13 GAERVLLNLANALDKRGYDVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIKLGLLKAILKLKrILKRAKPDVVISFLG 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  95 FSLGLLGKMigKALRIPVVHTYHTQYEDYVSYiangkiirPSMVKPLLRGYLKdLDGVICPSRIVLNLLEGYEVTIPKR- 173
Cdd:cd03811    93 FATYIVAKL--AAARSKVIAWIHSSLSKLYYL--------KKKLLLKLKLYKK-ADKIVCVSKGIKEDLIRLGPSPPEKi 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 174 -VIPTGIplekyirdDITAEEVTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQD 252
Cdd:cd03811   162 eVIYNPI--------DIDRIRALAKEPILNEPEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPLREE 233
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 253 LKHLAMQLEVDKHVTFTGMVShdKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMFGTLYY 332
Cdd:cd03811   234 LEKLAKELGLAERVIFLGFQS--NPYPYLKKADLFVLSSRYEGFPNVLLEAMALGTPVVSTDCPGPREILDDGENGLLVP 311
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1622294796 333 AETDLTDAIIDAILKTPVMDKRLLAKKRYEISA 365
Cdd:cd03811   312 DGDAAALAGILAALLQKKLDAALRERLAKAQEA 344
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
9-379 9.47e-30

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: 119.02  E-value: 9.47e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   9 TYFPQVS--GVATSIRTLKEELEKEGHEVYIFTTTD-------RDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISS-- 77
Cdd:cd03798     6 NIYPNANspGRGIFVRRQVRALSRRGVDVEVLAPAPwgpaaarLLRKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPSla 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  78 --YKIAKHYNLDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTqyedyvSYIanGKIIRPSMVKPLLRGYLKDLDGVICP 155
Cdd:cd03798    86 klLKRRRRGPPDLIHAHFAYPAGFAAALLARLYGVPYVVTEHG------SDI--NVFPPRSLLRKLLRWALRRAARVIAV 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 156 SRIVLNLLEGYEVtIPKR--VIPTGIPLEKYirdditaeevTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAIL 233
Cdd:cd03798   158 SKALAEELVALGV-PRDRvdVIPNGVDPARF----------QPEDRGLGLPLDAFVILFVGRLIPRKGIDLLLEAFARLA 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 234 AENAKIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAH 313
Cdd:cd03798   227 KARPDVVLLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYYRACDVFVLPSRHEGFGLVLLEAMACGLPVVAT 306
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622294796 314 GNPYLDDVVTDKMFGTLyYAETD---LTDAIIDAILKTPVMDKRLLAKKRY--EISAQHFGKSIYTFYLDT 379
Cdd:cd03798   307 DVGGIPEVVGDPETGLL-VPPGDadaLAAALRRALAEPYLRELGEAARARVaeRFSWVKAADRIAAAYRDV 376
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
206-367 8.65e-26

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: 102.35  E-value: 8.65e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 206 DETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACD 285
Cdd:pfam00534   1 KKKIILFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELLKIAD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 286 FFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMFGTLYYAETDltDAIIDAILKtpVMDKRLLAKKRYEISA 365
Cdd:pfam00534  81 VFVLPSRYEGFGIVLLEAMACGLPVIASDVGGPPEVVKDGETGFLVKPNNA--EALAEAIDK--LLEDEELRERLGENAR 156

                  ..
gi 1622294796 366 QH 367
Cdd:pfam00534 157 KR 158
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
21-316 3.54e-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: 106.56  E-value: 3.54e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  21 IRTLKEELEKEGHEVYIFT--TTDRDVKRFEDPT---IIRLPSVPFVsFTDRRVVYR-------GLISSYKiAKHYNLDI 88
Cdd:cd03800    27 VLELARALAELGYQVDIFTrrISPADPEVVEIAPgarVIRVPAGPPE-YLPKEELWPyleefadGLLRFIA-REGGRYDL 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  89 IHTQteFSL-GLLGKMIGKALRIPVVHTYHT-------------QYEDYVSYIANGKIIRPSmvkpllrgylkdlDGVI- 153
Cdd:cd03800   105 IHSH--YWDsGLVGALLARRLGVPLVHTFHSlgrvkyrhlgaqdTYHPSLRITAEEQILEAA-------------DRVIa 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 154 -CPSRIV--LNLLEGYEVTIpkRVIPTGIPLEKYIRDDitaeEVTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMP 230
Cdd:cd03800   170 sTPQEADelISLYGADPSRI--NVVPPGVDLERFFPVD----RAEARRARLLLPPDKPVVLALGRLDPRKGIDTLVRAFA 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 231 AILAENAKIKLIIVG---DGPYLQD---LKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESL 304
Cdd:cd03800   244 QLPELRELANLVLVGgpsDDPLSMDreeLAELAEELGLIDRVRFPGRVSRDDLPELYRAADVFVVPSLYEPFGLTAIEAM 323
                         330
                  ....*....|....
gi 1622294796 305 ASGTPIIA--HGNP 316
Cdd:cd03800   324 ACGTPVVAtaVGGL 337
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
2-347 3.24e-24

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: 103.58  E-value: 3.24e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFT---------TTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYR 72
Cdd:cd03794     1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTpspnyplgrIFAGATETKDGIRVIRVKLGPIKKNGLIRRLLN 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  73 GLISSYKIAKHYNL-----DIIHTQTE-FSLGLLGKMIGKALRIPVVHTYHTQYEDyvSYIANGKIIRPSMVKPLLRGY- 145
Cdd:cd03794    81 YLSFALAALLKLLVreerpDVIIAYSPpITLGLAALLLKKLRGAPFILDVRDLWPE--SLIALGVLKKGSLLKLLKKLEr 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 146 --LKDLDGVICPSRIVLNLLEGYEVTIPK-RVIPTGIPLEKYIRDDItaeevtNLKAELGIAGDETMLLSLSRISYEKNI 222
Cdd:cd03794   159 klYRLADAIIVLSPGLKEYLLRKGVPKEKiIVIPNWADLEEFKPPPK------DELRKKLGLDDKFVVVYAGNIGKAQGL 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 223 QAIINQMpAILAENAKIKLIIVGDGPYLQDLKHLAMQLEVDKhVTFTGMVSHDKVALYYKACDF-FISASTSETQGLTY- 300
Cdd:cd03794   233 ETLLEAA-ERLKRRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAADVgLVPLKDNPANRGSSp 310
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622294796 301 ---IESLASGTPIIAHGNPYLDDVVTDKMFGtlYYAETDLTDAIIDAILK 347
Cdd:cd03794   311 sklFEYMAAGKPILASDDGGSDLAVEINGCG--LVVEPGDPEALADAILE 358
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
2-374 5.08e-23

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: 99.66  E-value: 5.08e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVP-FVSFTDRRVVYRGLISSYKI 80
Cdd:cd03795     1 KVLHVFKFYYPDIGGIEQVIYDLAEGLKKKGIEVDVLCFSKEKETPEKEENGIRIHRVKsFLNVASTPFSPSYIKRFKKL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  81 AKHYnlDIIHTQTEFSLGLLGKMIGKALRiPVVHTYHtqyedyvSYIANGKIIRPsMVKPLLRGYLKDLDGVICPSRIVL 160
Cdd:cd03795    81 AKEY--DIIHYHFPNPLADLLLFFSGAKK-PVVVHWH-------SDIVKQKKLLK-LYKPLMTRFLRRADRIIATSPNYV 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 161 N---LLEGYEVtiPKRVIPTGIPLEKYIRDDITAEEVTNLKAELGIagdetmLLSLSRISYEKNIQAIINQMPAIlaena 237
Cdd:cd03795   150 EtspTLREFKN--KVRVIPLGIDKNVYNIPRVDFENIKREKKGKKI------FLFIGRLVYYKGLDYLIEAAQYL----- 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 238 KIKLIIVGDGPYLQDLKHLAMQLEVDKhVTFTGMVSHDKVALYYKACDFFI--SASTSETQGLTYIESLASGTPIIA--- 312
Cdd:cd03795   217 NYPIVIGGEGPLKPDLEAQIELNLLDN-VKFLGRVDDEEKVIYLHLCDVFVfpSVLRSEAFGIVLLEAMMCGKPVIStni 295
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622294796 313 -HGNPYlddVVTDKMFGTLYYAET--DLTDAiIDAILKTPVMDKRL--LAKKRYEisaQHFGKSIYT 374
Cdd:cd03795   296 gTGVPY---VNNNGETGLVVPPKDpdALAEA-IDKLLSDEELRESYgeNAKKRFE---ELFTAEKMK 355
PLN02871 PLN02871
UDP-sulfoquinovose:DAG sulfoquinovosyltransferase
2-363 9.18e-22

UDP-sulfoquinovose:DAG sulfoquinovosyltransferase


Pssm-ID: 215469 [Multi-domain]  Cd Length: 465  Bit Score: 97.09  E-value: 9.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTD-TYFPQVSGVATSIRTLKEELEKEGHEVYIFTTtDRDV-KRFEDPTIIRLPSVPF-----VSFT---DRRVvy 71
Cdd:PLN02871   60 RIALFVEpSPFSYVSGYKNRFQNFIRYLREMGDEVLVVTT-DEGVpQEFHGAKVIGSWSFPCpfyqkVPLSlalSPRI-- 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  72 rglissYKIAKHYNLDIIHTQtefSLGLL---GKMIGKALRIPVVHTYHTQYEDYV-SYIANGkiirpsMVKP---LLRG 144
Cdd:PLN02871  137 ------ISEVARFKPDLIHAS---SPGIMvfgALFYAKLLCVPLVMSYHTHVPVYIpRYTFSW------LVKPmwdIIRF 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 145 YLKDLDGVICPSRIVLNLLEGYEVTIPKR--VIPTGIPLEKY---IRDDITAEEVTNlkaelGIAGDETMLlSLSRISYE 219
Cdd:PLN02871  202 LHRAADLTLVTSPALGKELEAAGVTAANRirVWNKGVDSESFhprFRSEEMRARLSG-----GEPEKPLIV-YVGRLGAE 275
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 220 KNIQAIINqmpaILAENAKIKLIIVGDGPYLQDL-KHLAmqlevDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGL 298
Cdd:PLN02871  276 KNLDFLKR----VMERLPGARLAFVGDGPYREELeKMFA-----GTPTVFTGMLQGDELSQAYASGDVFVMPSESETLGF 346
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622294796 299 TYIESLASGTPIIAHGNPYLDDVVTDKMFG--TLYYAETDLTDAI--IDAILKTPVMDKRLLAKKRYEI 363
Cdd:PLN02871  347 VVLEAMASGVPVVAARAGGIPDIIPPDQEGktGFLYTPGDVDDCVekLETLLADPELRERMGAAAREEV 415
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
13-364 3.28e-21

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: 94.28  E-value: 3.28e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  13 QVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEDptIIRLPSVPFVSFTDRRVVYRGLISSYKIAKHYNLDIIHTQ 92
Cdd:cd03812    10 NVGGIETFLMNLYRKLDKSKIEFDFLATSDDKGEYDEE--LEELGGKIFYIPPKKKNIIKYFIKLLKLIKKEKYDIVHVH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  93 TEFSLGLLGKMIGKA-LRIPVVHTYHTQYEDyvsyIANGKIIRPSMVKPLLRGYlkdlDGVICPSRIVLNLLEGYEVTIP 171
Cdd:cd03812    88 GSSSNGIILLLAAKAgVPVRIAHSHNTKDSS----IKLRKIRKNVLKKLIERLS----TKYLACSEDAGEWLFGEVENGK 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 172 KRVIPTGIPLEKYIRDDitaeEVTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQ 251
Cdd:cd03812   160 FKVIPNGIDIEKYKFNK----EKRRKRRKLLILEDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGEGELKE 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 252 DLKHLAMQLEVDKHVTFTGMVShdKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMF---- 327
Cdd:cd03812   236 KIKEKVKELGLEDKVIFLGFRN--DVSEILSAMDVFLFPSLYEGLPLVAVEAQASGLPCLLSDTITKECDITNNVEflpl 313
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1622294796 328 --GTLYYAETDLTDAIIDAILKTPVMDKRLLAKKRYEIS 364
Cdd:cd03812   314 neTPSTWAEKILKLIKRKRRINKEINKEKKELGYDDESL 352
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
2-312 4.50e-21

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: 93.93  E-value: 4.50e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIR-TLKEELEKEGHEVYIFTTTDRD--VKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISSY 78
Cdd:cd03823     1 KILLVNSLYPPQRVGGAEISVhDLAEALVAEGHEVAVLTAGVGPpgQATVARSVVRYRRAPDETLPLALKRRGYELFETY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  79 --KIAKHYNL-------DIIHTQ--TEFSLGLLgKMIgKALRIPVVHTYHtqyeDYvsyiaNGKIIRPSMVKpllrgylK 147
Cdd:cd03823    81 npGLRRLLARlledfrpDVVHTHnlSGLGASLL-DAA-RDLGIPVVHTLH----DY-----WLLCPRQFLFK-------K 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 148 DLDGVICPSRIVLNLLE--GYEvTIPKRVIPTGIPLEKYiRDDITAEEVTNLKaeLGIAGdetmllslsRISYEKNIQAI 225
Cdd:cd03823   143 GGDAVLAPSRFTANLHEanGLF-SARISVIPNAVEPDLA-PPPRRRPGTERLR--FGYIG---------RLTEEKGIDLL 209
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 226 INQMPAILAENakIKLIIVGDGPyLQDLKhlamQLEVDKHVTFTGMVSHDKVALYYKACDFFISAST-SETQGLTYIESL 304
Cdd:cd03823   210 VEAFKRLPRED--IELVIAGHGP-LSDER----QIEGGRRIAFLGRVPTDDIKDFYEKIDVLVVPSIwPEPFGLVVREAI 282

                  ....*...
gi 1622294796 305 ASGTPIIA 312
Cdd:cd03823   283 AAGLPVIA 290
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
210-347 1.25e-20

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 87.57  E-value: 1.25e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 210 LLSLSRIS-YEKNIQAIINQMPAILAENAKIKLIIVGDGPyLQDLKHLAmqLEVDKHVTFTGMVshDKVALYYKACDFFI 288
Cdd:pfam13692   4 ILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGP-EEELEELA--AGLEDRVIFTGFV--EDLAELLAAADVFV 78
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622294796 289 SASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKmfgTLYYAETDLTDAIIDAILK 347
Cdd:pfam13692  79 LPSLYEGFGLKLLEAMAAGLPVVATDVGGIPELVDGE---NGLLVPPGDPEALAEAILR 134
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
14-376 1.46e-20

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


Pssm-ID: 340836 [Multi-domain]  Cd Length: 362  Bit Score: 92.77  E-value: 1.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  14 VSGVATSIRTLKEELEKEGHEVYIFTTTDRDVkRFEDptiIRLPSVPFV-----SFTDRRVVYRgLIssyKIAKHYNLDI 88
Cdd:cd03807    11 VGGAETMLLRLLEHMDKSRFEHVVISLTGDGV-LGEE---LLAAGVPVVclglsSGKDPGVLLR-LA---KLIRKRNPDV 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  89 IHTQ---TEFSLGLLGKMIGKalrIPVVHTYHTQYEDYVSyiaNGKIIRpsmVKPLLRGYLKDldgVICPSRIVLNLLEg 165
Cdd:cd03807    83 VHTWmyhADLIGGLAAKLAGG---VKVIWSVRSSNIPQRL---TRLVRK---LCLLLSKFSPA---TVANSSAVAEFHQ- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 166 yEVTIPK---RVIPTGIPLEKYirdDITAEEVTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLI 242
Cdd:cd03807   150 -EQGYAKnkiVVIYNGIDLFKL---SPDDASRARARRRLGLAEDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLL 225
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 243 IVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHdkVALYYKACDFFISASTSETQGLTYIESLASGTPIIAH---GNPYLd 319
Cdd:cd03807   226 LVGRGPERPNLERLLLELGLEDRVHLLGERSD--VPALLPAMDIFVLSSRTEGFPNALLEAMACGLPVVATdvgGAAEL- 302
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622294796 320 dvvTDKMFGTLYYAET--DLTDAIIDAIL---KTPVMDKRLLAKKRYEISAQHFGKSIYTFY 376
Cdd:cd03807   303 ---VDDGTGFLVPAGDpqALADAIRALLEdpeKRARLGRAARERIANEFSIDAMVRRYETLY 361
GT4_BshA-like cd04962
N-acetyl-alpha-D-glucosaminyl L-malate synthase BshA and similar proteins; This family is most ...
1-312 2.74e-19

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: 88.95  E-value: 2.74e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   1 MRIGLftdTYFPQVSG---VATSirtLKEELEKEGHEVYiFTTTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLISS 77
Cdd:cd04962     1 MKIGI---VCYPSYGGsgvVATE---LGLELAERGHEVH-FISSAIPFRLNLYSGNIFFHEVEVPNYPLFEYPPYTLALA 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  78 YKIA---KHYNLDIIHTQTEF---SLGLL-GKMIGKalRIPVVHTYHTQYEDYVSYiangkiiRPSMvKPLLRGYLKDLD 150
Cdd:cd04962    74 SKIVevaKEHKLDVLHAHYAIphaSCAYLaREILGE--KIPIVTTLHGTDITLVGY-------DPSL-QPAVRFSINKSD 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 151 GVICPSRIVLN-LLEGYEVTIPKRVIPTGIPLEKYIRDDITAeevtnLKAELGIAGDETMLLSLSRISYEKNIQAIInQM 229
Cdd:cd04962   144 RVTAVSSSLRQeTYELFDVDKDIEVIHNFIDEDVFKRKPAGA-----LKRRLLAPPDEKVVIHVSNFRPVKRIDDVV-RV 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 230 PAILAENAKIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGmvSHDKVALYYKACDFFISASTSETQGLTYIESLASGTP 309
Cdd:cd04962   218 FARVRRKIPAKLLLVGDGPERVPAEELARELGVEDRVLFLG--KQDDVEELLSIADLFLLPSEKESFGLAALEAMACGVP 295

                  ...
gi 1622294796 310 IIA 312
Cdd:cd04962   296 VVS 298
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
2-355 8.55e-19

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: 87.42  E-value: 8.55e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTD----RDVKRFEDPTIIRL--PSVPFVSFTDRRVVYRGLI 75
Cdd:cd03821     1 KILHVTPSISPKAGGPVKVVLRLAAALAALGHEVTIVSTGDgyesLVVEENGRYIPPQDgfASIPLLRQGAGRTDFSPGL 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  76 SSYKIAKHYNLDIIHTQTEFSLGLL-GKMIGKALRIPVVHTYHTqyeDYVSYIANGKIIRPSMVKPL-LRGYLKDLDGVI 153
Cdd:cd03821    81 PNWLRRNLREYDVVHIHGVWTYTSLaACKLARRRGIPYVVSPHG---MLDPWALQQKHWKKRIALHLiERRNLNNAALVH 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 154 CPSRIVLNLLEGYEVTIPKRVIPTGIPLEKYIRDDITAEEVtnlkaelGIAGDETMLLSLSRISYEKNIQAIINQMPAIL 233
Cdd:cd03821   158 FTSEQEADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRRKH-------NGLEDRRIILFLGRIHPKKGLDLLIRAARKLA 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 234 AENAKIKLIIVG-DGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIA 312
Cdd:cd03821   231 EQGRDWHLVIAGpDDGAYPAFLQLQSSLGLGDRVTFTGPLYGEAKWALYASADLFVLPSYSENFGNVVAEALACGLPVVI 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|...
gi 1622294796 313 HGNPYLDDVVTDKMFGTLYYAETDLTDAIIdAILKTPVMDKRL 355
Cdd:cd03821   311 TDKCGLSELVEAGCGVVVDPNVSSLAEALA-EALRDPADRKRL 352
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
3-324 2.77e-18

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: 83.61  E-value: 2.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   3 IGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFEdptiirlpsvpfvsftdrrvvyrglissyKIAK 82
Cdd:cd01635     1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLALRRIL-----------------------------KKLL 51
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  83 HYNLDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTqyeDYVSYIANGKIIRPSMVKPLLRGYLKdldgvicpsrivlnl 162
Cdd:cd01635    52 ELKPDVVHAHSPHAAALAALLAARLLGIPIVVTVHG---PDSLESTRSELLALARLLVSLPLADK--------------- 113
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 163 legyevtipkrviptgiplekyirdditaeevtnlkaelgiagdetmlLSLSRISYEKNIQAIINQMPAILAENAKIKLI 242
Cdd:cd01635   114 ------------------------------------------------VSVGRLVPEKGIDLLLEALALLKARLPDLVLV 145
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 243 IVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHD-KVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDV 321
Cdd:cd01635   146 LVGGGGEREEEEALAAALGLLERVVIIGGLVDDeVLELLLAAADVFVLPSRSEGFGLVLLEAMAAGKPVIATDVGGIPEF 225

                  ...
gi 1622294796 322 VTD 324
Cdd:cd01635   226 VVD 228
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
15-312 7.42e-17

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: 81.64  E-value: 7.42e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  15 SGVATSIRTLKEELEK-EGHEVYIFTttdrdvkrFEDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIAKHYNLDIIHTQT 93
Cdd:cd03809    14 TGIGRYTRELLKALAKnDPDESVLAV--------PPLPGELLRLLREYPELSLGVIKIKLWRELALLRWLQILLPKKDKP 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  94 EFSLGLLGKMIGKALRIPVVHTYHT-QYEDYVSYIANGKIIRPSMVKPLLrgyLKDLDGVICPSRIVLN-LLEGYEVTIP 171
Cdd:cd03809    86 DLLHSPHNTAPLLLKGCPQVVTIHDlIPLRYPEFFPKRFRLYYRLLLPIS---LRRADAIITVSEATRDdIIKFYGVPPE 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 172 K-RVIPTGIPLEKYIRDdiTAEEVTNLKAElgiagDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVG-DGPY 249
Cdd:cd03809   163 KiVVIPLGVDPSFFPPE--SAAVLIAKYLL-----PEPYFLYVGTLEPRKNHERLLKAFALLKKQGGDLKLVIVGgKGWE 235
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622294796 250 LQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIA 312
Cdd:cd03809   236 DEELLDLVKKLGLGGRVRFLGYVSDEDLPALYRGARAFVFPSLYEGFGLPVLEAMACGTPVIA 298
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
13-372 7.40e-16

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: 78.41  E-value: 7.40e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  13 QVSGVATSIRTLKEELEKEGHEVYIFTTTDRDVKRFED-----PTIIRLPSVPFVSFTDrrvvYRGLISSYKIAKHYNLD 87
Cdd:cd03808     8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSDELKelgvkVIDIPILRRGINPLKD----LKALFKLYKLLKKEKPD 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  88 IIHTQTEFSlGLLG----KMIGKALRIPVVHTYHTQYedyvsyiANGKIIRpSMVKPLLRGYLKDLDGVICPSR------ 157
Cdd:cd03808    84 IVHCHTPKP-GILGrlaaRLAGVPKVIYTVHGLGFVF-------TEGKLLR-LLYLLLEKLALLFTDKVIFVNEddrdla 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 158 IVLNLLEGYEVTIpkrVIPTGIPLEKYIRDDITAEEvtnlkaelgiagDETMLLSLSRISYEKNIQAIINQMpAILAENA 237
Cdd:cd03808   155 IKKGIIKKKKTVL---IPGSGVDLDRFQYSPESLPS------------EKVVFLFVARLLKDKGIDELIEAA-KILKKKG 218
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 238 -KIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHdkVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNP 316
Cdd:cd03808   219 pNVRFLLVGDGELENPSEILIEKLGLEGRIEFLGFRSD--VPELLAESDVFVLPSYREGLPRSLLEAMAAGRPVITTDVP 296
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622294796 317 YLDDVVTDKMFGTLY--YAETDLTDAIIdAILKTPvmDKRL-LAKKRYEISAQHFGKSI 372
Cdd:cd03808   297 GCRELVIDGVNGFLVppGDVEALADAIE-KLIEDP--ELRKeMGEAARKRVEEKFDEEK 352
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
175-312 3.80e-15

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: 76.33  E-value: 3.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 175 IPTGIPLEKYIRDDitaEEVTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDLK 254
Cdd:cd04951   159 VYNGIDLNKFKKDI---NVRLKIRNKLNLKNDEFVILNVGRLTEAKDYPNLLLAISELILSKNDFKLLIAGDGPLRNELE 235
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622294796 255 HLAMQLEVDKHVTFTGmvSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIA 312
Cdd:cd04951   236 RLICNLNLVDRVILLG--QISNISEYYNAADLFVLSSEWEGFGLVVAEAMACERPVVA 291
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
2-307 3.88e-14

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: 73.81  E-value: 3.88e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTDTYFPQVSGVATSIRTLKEELEKEGHEVYIFTttdrdvKRFEDPTIIR----------LPSVPFVsftdRRVVY 71
Cdd:cd03796     1 RICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVIT------HAYGNRVGVRyltnglkvyyLPFKVFY----NQSTL 70
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  72 RGLISSYKIAKHY----NLDIIHTQTEFS-LGLLGKMIGKALRIPVVHTYHTQYE--DYVSYIANgkiirpsmvkPLLRG 144
Cdd:cd03796    71 PTLFSTFPLLRNIlireRIQIVHGHQAFSsLAHEALFHARTLGLKTVFTDHSLFGfaDASSILTN----------KLLRF 140
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 145 YLKDLDGVICPSRIvlnlleGYEVTI------PKR--VIPTGIPLEKYIRDDITAEEvtnlkaelgiagDETMLLSLSRI 216
Cdd:cd03796   141 SLADIDHVICVSHT------SKENTVlrasldPRIvsVIPNAVDSSDFTPDPSKPDP------------NKITIVVISRL 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 217 SYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQ 296
Cdd:cd03796   203 VYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEEMREKYQLQDRVELLGAVPHEEVRDVLVQGHIFLNTSLTEAF 282
                         330
                  ....*....|.
gi 1622294796 297 GLTYIESLASG 307
Cdd:cd03796   283 CIAIVEAASCG 293
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
15-178 1.59e-13

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 68.20  E-value: 1.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  15 SGVATSIRTLKEELEKEGHEVYIFT---TTDRDVKRFEDPTIIRLPSVPFVSFTDRRVVYRGLissYKIAKHYNLDIIHT 91
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVVTpggPPGRPELVGDGVRVHRLPVPPRPSPLADLAALRRL---RRLLRAERPDVVHA 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  92 QTeFSLGLLGKMIGKALRIPVVHTYHTQYEDYvsyianGKIIRPSMVKPLLRGYLKDLDGVICPSRIVLNLLEGYEVTIP 171
Cdd:pfam13579  78 HS-PTAGLAARLARRRRGVPLVVTVHGLALDY------GSGWKRRLARALERRLLRRADAVVVVSEAEAELLRALGVPAA 150

                  ....*...
gi 1622294796 172 K-RVIPTG 178
Cdd:pfam13579 151 RvVVVPNG 158
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
277-368 1.14e-12

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 64.63  E-value: 1.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 277 VALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMFGTLYYAET--DLTDAIIDaILKTPVMDKR 354
Cdd:COG0438    14 LEALLAAADVFVLPSRSEGFGLVLLEAMAAGLPVIATDVGGLPEVIEDGETGLLVPPGDpeALAEAILR-LLEDPELRRR 92
                          90
                  ....*....|....
gi 1622294796 355 lLAKKRYEISAQHF 368
Cdd:COG0438    93 -LGEAARERAEERF 105
PRK15484 PRK15484
lipopolysaccharide N-acetylglucosaminyltransferase;
152-366 2.22e-12

lipopolysaccharide N-acetylglucosaminyltransferase;


Pssm-ID: 185381 [Multi-domain]  Cd Length: 380  Bit Score: 68.28  E-value: 2.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 152 VICPSRIVLNLLEGYEVTIPKRVIPTGIPLEKYIRDDitaeeVTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPA 231
Cdd:PRK15484  143 IIVPSQFLKKFYEERLPNADISIVPNGFCLETYQSNP-----QPNLRQQLNISPDETVLLYAGRISPDKGILLLMQAFEK 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 232 ILAENAKIKLIIVGD---------GPYLQDLKHLAMQLEVDKHVtfTGMVSHDKVALYYKACDFFISAST-SETQGLTYI 301
Cdd:PRK15484  218 LATAHSNLKLVVVGDptasskgekAAYQKKVLEAAKRIGDRCIM--LGGQPPEKMHNYYPLADLVVVPSQvEEAFCMVAV 295
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 302 ESLASGTPIIAHGNPYLDDVVTDKMFGtLYYAETDLTDAIIDAILKTpvmdkrLLAKKRYEISAQ 366
Cdd:PRK15484  296 EAMAAGKPVLASTKGGITEFVLEGITG-YHLAEPMTSDSIISDINRT------LADPELTQIAEQ 353
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
23-312 4.08e-12

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: 67.26  E-value: 4.08e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  23 TLKEELEKEGHEVYIFTTTDRDVKRF----EDPTIIRLPSVPFVSFTDRRVVYRGLISSYKIAKHYNLDIIHTqteFSLG 98
Cdd:cd03820    21 NLANHLAKKGYDVTIISLDSAEKPPFyeldDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVVIS---FRTS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  99 LLGKMIGKALRIPVVHTYHTqyedyvSYIANGKIIRPSMVKpllRGYLKDLDGVICPSRIVLnlLEGYEVTIPK-RVIPT 177
Cdd:cd03820    98 LLTFLALIGLKSKLIVWEHN------NYEAYNKGLRRLLLR---RLLYKRADKIVVLTEADK--LKKYKQPNSNvVVIPN 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 178 GIPLEKYirdditaEEVTNLKAELgiagdetmLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDLKHLA 257
Cdd:cd03820   167 PLSFPSE-------EPSTNLKSKR--------ILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLI 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 258 MQLEVDKHVTFTGMVSHdkVALYYKACDFFISASTSETQGLTYIESLASGTPIIA 312
Cdd:cd03820   232 DKLGLEDRVKLLGPTKN--IAEEYANSSIFVLSSRYEGFPMVLLEAMAYGLPIIS 284
GT4_GtfA-like cd04949
accessory Sec system glycosyltransferase GtfA and similar proteins; This family is most ...
195-373 1.41e-11

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: 65.40  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 195 TNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGMvsH 274
Cdd:cd04949   148 QLDTAESNHERKSNKIITISRLAPEKQLDHLIEAVAKAVKKVPEITLDIYGYGEEREKLKKLIEELHLEDNVFLKGY--H 225
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 275 DKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPY-LDDVVTDKMFGTL--YYAETDLTDAIIDAILKTPVM 351
Cdd:cd04949   226 SNLDQEYQDAYLSLLTSQMEGFGLTLMEAIGHGLPVVSYDVKYgPSELIEDGENGYLieKNNIDALADKIIELLNDPEKL 305
                         170       180
                  ....*....|....*....|..
gi 1622294796 352 DKrlLAKKRYEISAQHFGKSIY 373
Cdd:cd04949   306 QQ--FSEESYKIAEKYSTENVM 325
GT4-like cd03813
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
86-312 4.61e-10

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


Pssm-ID: 340841 [Multi-domain]  Cd Length: 474  Bit Score: 61.20  E-value: 4.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  86 LDIIHTQTEFSLGLLGKMIGKALRIPVVHTYHTQY--EDYVsyiangKIIRPSMVKPLLRGYLKDLDGVICP-----SRI 158
Cdd:cd03813   174 ADLYHSVSTGYAGLLGALARHRRGIPFLLTEHGIYtrERKI------EILQSTWIMGYIKKLWIRFFERLGKlayqqADK 247
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 159 VLNLLEG---YEVTI---PKR--VIPTGIPLEKYirDDITAEEVTNLKAELGIAGdetmllslsRISYEKNIQAIINQMP 230
Cdd:cd03813   248 IISLYEGnrrRQIRLgadPDKtrVIPNGIDIQRF--APAREERPEKEPPVVGLVG---------RVVPIKDVKTFIRAFK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 231 AILAENAKIKLIIVG----DGPYLQDLKHLAMQLEVDKHVTFTGMVShdkVALYYKACDFFISASTSETQGLTYIESLAS 306
Cdd:cd03813   317 LVRRAMPDAEGWLIGpedeDPEYAQECKRLVASLGLENKVKFLGFQN---IKEYYPKLGLLVLTSISEGQPLVILEAMAS 393

                  ....*.
gi 1622294796 307 GTPIIA 312
Cdd:cd03813   394 GVPVVA 399
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
23-370 7.94e-10

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: 59.99  E-value: 7.94e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  23 TLKEELEKEGHEVYIFTTTDRDVKRFEDPTIIRLPSVPFVSFTDrrVVYRGLISSYKIAKHYNLDIIHTQTEFSLGLLGK 102
Cdd:cd03802    26 ALTEGLVRRGHEVTLFAPGDSHTSAPLVAVIPRALRLDPIPQES--KLAELLEALEVQLRASDFDVIHNHSYDWLPPFAP 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 103 MIGKalriPVVHTYHTQYEDYVSYIAngkiirpSMVKPLLRGYLKDLDGVICPsrivlnllegyevTIPKR-VIPTGIPL 181
Cdd:cd03802   104 LIGT----PFVTTLHGPSIPPSLAIY-------AAEPPVNYVSISDAQRAATP-------------PIDYLtVVHNGLDP 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 182 EKYIRDDitaeevtnlkaelgiaGDETMLLSLSRISYEKNIQAiinqmpAI-LAENAKIKLIIVGDGPYlQDLKHLAMQL 260
Cdd:cd03802   160 ADYRFQP----------------DPEDYLAFLGRIAPEKGLED------AIrVARRAGLPLKIAGKVRD-EDYFYYLQEP 216
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 261 EVDKHVTFTGMVSHD-KVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMFGTLyyaeTDLTD 339
Cdd:cd03802   217 LPGPRIEFIGEVGHDeKQELLGGARALLFPINWDEPFGLVMIEAMACGTPVIAYRRGGLPEVIQHGETGFL----VDSVE 292
                         330       340       350
                  ....*....|....*....|....*....|....
gi 1622294796 340 AIIDAILKTPVMDK---RLLAKKRYeiSAQHFGK 370
Cdd:cd03802   293 EMAEAIANIDRIDRaacRRYAEDRF--SAARMAD 324
GT4_WcaC-like cd03825
putative colanic acid biosynthesis glycosyl transferase WcaC and similar proteins; This family ...
170-378 9.87e-10

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: 60.04  E-value: 9.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 170 IPKRVIPTGIPLEKYIRDDITAeevtnLKAELGIAGDETMLLSLSRiSYE---KNIQAIINQMpAILAENAKIKLIIVG- 245
Cdd:cd03825   161 LPVVVIPNGIDTEIFAPVDKAK-----ARKRLGIPQDKKVILFGAE-SVTkprKGFDELIEAL-KLLATKDDLLLVVFGk 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 246 DGPYLQDLKHLAMQLEVDKHVTftgmvshdKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDK 325
Cdd:cd03825   234 NDPQIVILPFDIISLGYIDDDE--------QLVDIYSAADLFVHPSLADNLPNTLLEAMACGTPVVAFDTGGSPEIVQHG 305
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 326 MFGTLY--YAETDLTDAiIDAILKTPVMDKRLLAKKRYEISAQHFGKSIYTFYLD 378
Cdd:cd03825   306 VTGYLVppGDVQALAEA-IEWLLANPKERESLGERARALAENHFDQRVQAQRYLE 359
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
2-347 1.68e-09

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: 59.32  E-value: 1.68e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796   2 RIGLFTdTYFPQVSGVATSIRTLKEELEKEGHEVY--IFTTTDRDVKRFEDPTIIRLPSVPFVSFtdrrvvYRGLISSYK 79
Cdd:cd03822     1 KIAVLG-TLPPRKCGIATYTDDLVEGLRKGGPVVIvvIVSPQDEILKDDDFEVPNEIKSWNSNEY------FRLLDHLNF 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  80 IAkhynLDIIHTQTEFSLGLlGKMIGKAL------RIPVVHTYHTqyedYVSYIANGKIIRPSMVKPLLRgylkdLDGVI 153
Cdd:cd03822    74 KK----PDVVHIQHEFGIFG-GKYGLYALglllhlRIPVITTLHT----VLDLSDPGKQALKVLFRIATL-----SERVV 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 154 CPSRIVLNLLEGYEVtIPKR---VIPTGIPlekyirdDITAEEVTNLKAELGIAGdETMLLSLSRISYEKNIQAIINQMP 230
Cdd:cd03822   140 VMAPISRFLLVRIKL-IPAVnieVIPHGVP-------EVPQDPTTALKRLLLPEG-KKVILTFGFIGPGKGLEILLEALP 210
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 231 AILAENAKIKLIIVG-DGPYLQD------LKHLAMQLEVDKHVTF-TGMVSHDKVALYYKACDFFISA--STSETQGLTY 300
Cdd:cd03822   211 ELKAEFPDVRLVIAGeLHPSLARyegeryRKAAIEELGLQDHVDFhNNFLPEEEVPRYISAADVVVLPylNTEQSSSGTL 290
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*..
gi 1622294796 301 IESLASGTPIIAHGNPYLDDVVTDkmfGTLYYAETDLTDAIIDAILK 347
Cdd:cd03822   291 SYAIACGKPVISTPLRHAEELLAD---GRGVLVPFDDPSAIAEAILR 334
GT4_WbaZ-like cd03804
mannosyltransferase WbaZ and similar proteins; This family is most closely related to the GT4 ...
211-372 2.25e-09

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: 58.84  E-value: 2.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 211 LSLSRISYEKNIQAII---NQMPAilaenakiKLIIVGDGPYLQDLKHLAmqlevDKHVTFTGMVSHDKVALYYKACDFF 287
Cdd:cd03804   203 LTASRLVPYKRIDLAVeafNELPK--------RLVVIGDGPDLDRLRAMA-----SPNVEFLGYQPDEVLKELLSKARAF 269
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 288 ISASTsETQGLTYIESLASGTPIIAHGNPYLDDVVTDKMFGTLYYAETdlTDAIIDAIL----KTPVMDKRLLAKKRYEI 363
Cdd:cd03804   270 VFAAE-EDFGIVPVEAQACGTPVIAFGKGGALETVRPGPTGILFGEQT--VESLKAAVEefeqNFDRFKPQAIRANAERF 346

                  ....*....
gi 1622294796 364 SAQHFGKSI 372
Cdd:cd03804   347 SRARFRQEI 355
GT4_AmsK-like cd04946
amylovoran biosynthesis glycosyltransferase AmsK and similar proteins; This family is most ...
134-312 1.51e-08

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: 56.31  E-value: 1.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 134 RPSMVKPLLRGYLKDLDGVICPSRIVLNLLEGyevTIP-----KRVIPTGIPlekyirddiTAEEVTNLKAELGIAgdet 208
Cdd:cd04946   163 YGSYYLPLREYLVSYLDAVFLISKEGKDYLQK---CYPaykekIFVSRLGVS---------DKEQYSKVKKEGDLR---- 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 209 mLLSLSRISYEKNIQAIIN--QMPAILAENAKIKLIIVGDGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYK--AC 284
Cdd:cd04946   227 -LVSCSSIVPVKRIDLIIEtlNSLCVAHPSICISWTHIGGGPLKERLEKLAENKLENVKVNFTGEVSNKEVKQLYKenDV 305
                         170       180
                  ....*....|....*....|....*...
gi 1622294796 285 DFFISASTSETQGLTYIESLASGTPIIA 312
Cdd:cd04946   306 DVFVNVSESEGIPVSIMEAISFGIPVIA 333
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
86-368 5.69e-08

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: 54.38  E-value: 5.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  86 LDIIHTQTEFSlGLLGKMIGKALRIPVVHTYHTqYEDYVS--YIANGKIIRpsMVKPLLRGYL-KDLDGVICPSRivlnl 162
Cdd:cd05844    82 PALVHAHFGRD-GVYALPLARALGVPLVVTFHG-FDITTSraWLAASPGWP--SQFQRHRRALqRPAALFVAVSG----- 152
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 163 legyevTIPKRVIPTGIPLEKYIRDDITAEevTNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLI 242
Cdd:cd05844   153 ------FIRDRLLARGLPAERIHVHYIGID--PAKFAPRDPAERAPTILFVGRLVEKKGCDVLIEAFRRLAARHPTARLV 224
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 243 IVGDGPYLQDLKHLAMQLEvdkHVTFTGMVSHDKVALYYKACDFFISAST------SETQGLTYIESLASGTPIIAHGNP 316
Cdd:cd05844   225 IAGDGPLRPALQALAAALG---RVRFLGALPHAEVQDWMRRAEIFCLPSVtaasgdSEGLGIVLLEAAACGVPVVSSRHG 301
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 317 YLDDVVTDKMFGtLYYAETD---LTDAiIDAILKTPVMDKRLLAKKRyEISAQHF 368
Cdd:cd05844   302 GIPEAILDGETG-FLVPEGDvdaLADA-LQALLADRALADRMGGAAR-AFVCEQF 353
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
32-330 9.26e-07

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: 50.53  E-value: 9.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796  32 GHEVYIFTTTD-RDVKRFEDPTIIRLPSVPFVSftdrrvVYRGLISsykiAKHYnlDIIHTQtefsLGLLGKMIGKALRI 110
Cdd:cd03799    28 GHEVDIYAVNPgDLVKRHPDVEKYNVPSLNLLY------AIVGLNK----KGAY--DIIHCQ----FGPLGALGALLRRL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 111 PV-------------VHTYHTQY--EDYVSYIANGKIIRPSMvkpllRGYLKDLDGVICPsrivlnllegyevtiPKRVI 175
Cdd:cd03799    92 KVlkgklvtsfrgydISMYVILEgnKVYPQLFAQGDLFLPNC-----ELFKHRLIALGCD---------------EKKII 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 176 PT--GIPLEKYirdditaeevtNLKAELGIAGDETMLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDL 253
Cdd:cd03799   152 VHrsGIDCNKF-----------RFKPRYLPLDGKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQL 220
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 254 KHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQG------LTYIESLASGTPIIAHGNPYLDDVVTDKMF 327
Cdd:cd03799   221 QQLIQELNIGDCVKLLGWKPQEEIIEILDEADIFIAPSVTAADGdqdgppNTLKEAMAMGLPVISTEHGGIPELVEDGVS 300

                  ...
gi 1622294796 328 GTL 330
Cdd:cd03799   301 GFL 303
GT4_ALG11-like cd03806
alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related ...
192-371 1.33e-06

alpha-1,2-mannosyltransferase ALG11 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG11 in yeast is involved in adding the final 1,2-linked Man to the Man5GlcNAc2-PP-Dol synthesized on the cytosolic face of the ER. The deletion analysis of ALG11 was shown to block the early steps of core biosynthesis that takes place on the cytoplasmic face of the ER and lead to a defect in the assembly of lipid-linked oligosaccharides.


Pssm-ID: 340835 [Multi-domain]  Cd Length: 419  Bit Score: 50.30  E-value: 1.33e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 192 EEVTNLKAELGiaGDETMLLSLSRISYEKN----IQAI---INQMPAILAENakIKLIIVG------DGPYLQDLKHLAM 258
Cdd:cd03806   224 EELTKLPIDEK--TRENQILSIAQFRPEKNhplqLRAFaelLKRLPESIRSN--PKLVLIGscrneeDKERVEALKLLAK 299
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 259 QLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAH--GNPYLDDVVTDKMFGTLYYAET- 335
Cdd:cd03806   300 ELILEDSVEFVVDAPYEELKELLSTASIGLHTMWNEHFGIGVVEYMAAGLIPLAHasAGPLLDIVVPWDGGPTGFLASTp 379
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1622294796 336 ---DLTDAIIDAILKTPVMDKRLLAKKRYEI-SAQHFGKS 371
Cdd:cd03806   380 eeyAEAIEKILTLSEEERLQRREAARSSAERfSDEEFERD 419
PRK15179 PRK15179
Vi polysaccharide biosynthesis protein TviE; Provisional
170-365 1.09e-05

Vi polysaccharide biosynthesis protein TviE; Provisional


Pssm-ID: 185101 [Multi-domain]  Cd Length: 694  Bit Score: 47.72  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 170 IPKRVIP---TGIPLEKYIRDDITAEEVTNLKAElgiAGDETMLL-SLSRISYEKNIQAIINQMPAILAENAKIKLIIVG 245
Cdd:PRK15179  479 VDERRIPvvyNGLAPLKSVQDDACTAMMAQFDAR---TSDARFTVgTVMRVDDNKRPFLWVEAAQRFAASHPKVRFIMVG 555
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 246 DGPYLQDLKHLAMQLEVDKHVTFTGMVSHdkVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVTDK 325
Cdd:PRK15179  556 GGPLLESVREFAQRLGMGERILFTGLSRR--VGYWLTQFNAFLLLSRFEGLPNVLIEAQFSGVPVVTTLAGGAGEAVQEG 633
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1622294796 326 MFGTLYYAET----DLTDA---IIDAILKTPVMDK--RLLAKKRYEISA 365
Cdd:PRK15179  634 VTGLTLPADTvtapDVAEAlarIHDMCAADPGIARkaADWASARFSLNQ 682
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
197-345 1.09e-05

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: 47.56  E-value: 1.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 197 LKAELGIAGDET--MLLSLSRISYEKNIQAIINQMPAILAENAKIKLIIVGDGPYLQDLKHLAMQlevdkhvtftgmvSH 274
Cdd:cd03791   282 LQKELGLPVDPDapLFGFVGRLTEQKGVDLILDALPELLEEGGQLVVLGSGDPEYEQAFRELAER-------------YP 348
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 275 DKVALY-----------YKACDFFISASTSETQGLTYIESLASGTPIIAH---GnpyLDDVVTD----KMFGTLY----Y 332
Cdd:cd03791   349 GKVAVVigfdealahriYAGADFFLMPSRFEPCGLVQMYAMRYGTLPIVRrtgG---LADTVFDydpeTGEGTGFvfedY 425
                         170
                  ....*....|...
gi 1622294796 333 AETDLTDAIIDAI 345
Cdd:cd03791   426 DAEALLAALRRAL 438
PLN02949 PLN02949
transferase, transferring glycosyl groups
234-365 4.08e-05

transferase, transferring glycosyl groups


Pssm-ID: 215511 [Multi-domain]  Cd Length: 463  Bit Score: 45.88  E-value: 4.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 234 AENAKIKLIIVG------DGPYLQDLKHLAMQLEVDKHVTFTGMVSHDKVALYYKACDFFISASTSETQGLTYIESLASG 307
Cdd:PLN02949  299 ADVPRPKLQFVGscrnkeDEERLQKLKDRAKELGLDGDVEFHKNVSYRDLVRLLGGAVAGLHSMIDEHFGISVVEYMAAG 378
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622294796 308 TPIIAH--GNPYLDDVVTDKMFGTLYYAET--DLTDAIIDAIlktpvmdkRLLAKKRYEISA 365
Cdd:PLN02949  379 AVPIAHnsAGPKMDIVLDEDGQQTGFLATTveEYADAILEVL--------RMRETERLEIAA 432
PHA01633 PHA01633
putative glycosyl transferase group 1
259-378 1.05e-04

putative glycosyl transferase group 1


Pssm-ID: 107050 [Multi-domain]  Cd Length: 335  Bit Score: 44.20  E-value: 1.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 259 QLEVDKHVTFT---GMVSHDKVALYYKACDFFISASTSETQGLTYIESLASGTPIIAHGNPYLDDVVT------------ 323
Cdd:PHA01633  196 QLEVPANVHFVaefGHNSREYIFAFYGAMDFTIVPSGTEGFGMPVLESMAMGTPVIHQLMPPLDEFTSwqwnlliksskv 275
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 324 ----DKMFGTLY-YAETDLTDAIIDAILKTPVMDKRLLAKKRYEISAQHFGKSIYTFYLD 378
Cdd:PHA01633  276 eeyyDKEHGQKWkIHKFQIEDMANAIILAFELQDREERSMKLKELAKKYDIRNLYTRFLE 335
GT4_ExpC-like cd03818
Rhizobium meliloti ExpC and similar proteins; This family is most closely related to the GT4 ...
230-346 7.72e-04

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


Pssm-ID: 340845 [Multi-domain]  Cd Length: 396  Bit Score: 41.58  E-value: 7.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 230 PAILAENAKIKLIIVGDG--------PYLQDLK-HLAMQLEVD-KHVTFTGMVSHDKVALYYKACDFFISastsetqgLT 299
Cdd:cd03818   237 PRIQARRPDARVVVVGGDgvsygsppPDGGSWKqKMLAELGVDlERVHFVGKVPYDQYVRLLQLSDAHVY--------LT 308
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622294796 300 Y--------IESLASGTPIIAHGNPYLDDVVTDKMFGTLyyAETDLTDAIIDAIL 346
Cdd:cd03818   309 YpfvlswslLEAMACGCPVIGSDTAPVREVIRDGRNGLL--VDFFDPDALAAAVL 361
GT4_ALG2-like cd03805
alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely ...
181-315 3.70e-03

alpha-1,3/1,6-mannosyltransferase ALG2 and similar proteins; This family is most closely related to the GT4 family of glycosyltransferases. ALG2, a 1,3-mannosyltransferase, in yeast catalyzes the mannosylation of Man(2)GlcNAc(2)-dolichol diphosphate and Man(1)GlcNAc(2)-dolichol diphosphate to form Man(3)GlcNAc(2)-dolichol diphosphate. A deficiency of this enzyme causes an abnormal accumulation of Man1GlcNAc2-PP-dolichol and Man2GlcNAc2-PP-dolichol, which is associated with a type of congenital disorders of glycosylation (CDG), designated CDG-Ii, in humans.


Pssm-ID: 340834 [Multi-domain]  Cd Length: 392  Bit Score: 39.49  E-value: 3.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622294796 181 LEKYIRD------DITAEEVTNLKAELG---IAGDETMLLSLSRISYEKNIQAIINQMpAIL----AENAKIKLIIVG-- 245
Cdd:cd03805   176 LAKNPPEvlypcvDTDSFDSTSEDPDPGdliAKSNKKFFLSINRFERKKNIALAIEAF-AKLkqklPEFENVRLVIAGgy 254
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622294796 246 DG------PYLQDLKHLAMQLE-VDKHVTFTGMVS-HDKVALYyKACDFFISASTSETQGLTYIESLASGTPIIAHGN 315
Cdd:cd03805   255 DPrvaenvEYLEELQRLAEELLnVEDQVLFLRSISdSQKEQLL-SSALALLYTPSNEHFGIVPLEAMYAGKPVIACNS 331
 
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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