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Conserved domains on  [gi|1056828536|ref|WP_068248030|]
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glycosyltransferase family 4 protein [Hydrotalea flava]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133453)

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

CAZY:  GT4
EC:  2.4.-.-
Gene Ontology:  GO:0016757|GO:0006486
PubMed:  12691742|10521532|16037492
SCOP:  3001586

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-338 4.52e-22

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: 96.07  E-value: 4.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536   4 LALISYKVFPAQMGGQKGIAQFYEYLAKQ-DNVIIVAaknnqLSDIPFPKKYNCLFPQGKGILNILKLFFVIKLIRR--- 79
Cdd:cd03801     2 ILLLSPELPPPVGGAERHVRELARALAARgHDVTVLT-----PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRElrp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  80 ----ENIDVIVIEHSYWGWYGYLLHVLTKKPFIIHSHNIEAERFN-IQKRKYWKIYELyeKWAHQRCSHNFFKCEEDAAY 154
Cdd:cd03801    77 llrlRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLlLLAAERRLLARA--EALLRRADAVIAVSEALRDE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 155 AVKQWNINPSKVTIIRYGTDVQSsptaaekqaARSQLIQQVNLPASACLLLFNGTLNYAPNVEVLTEitgsIIPILRKNK 234
Cdd:cd03801   155 LRALGGIPPEKIVVIPNGVDLER---------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLE----ALAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 235 FNFSLIICGK---MLPEEWLQKLTQYPEIHFLGFV--ENIAAINAGVDALIQPgSMGTGIKTKLVEALAQNTTVITTHNG 309
Cdd:cd03801   222 PDVRLVIVGGdgpLRAELEELELGLGDRVRFLGFVpdEELPALYAAADVFVLP-SRYEGFGLVVLEAMAAGLPVVATDVG 300

                         330       340       350
                  ....*....|....*....|....*....|
gi 1056828536 310 arGIPQKIAQSK-LILIPDYNPVAFAEKIL 338
Cdd:cd03801   301 --GLPEVVEDGEgGLVVPPDDVEALADALL 328
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-338 4.52e-22

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: 96.07  E-value: 4.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536   4 LALISYKVFPAQMGGQKGIAQFYEYLAKQ-DNVIIVAaknnqLSDIPFPKKYNCLFPQGKGILNILKLFFVIKLIRR--- 79
Cdd:cd03801     2 ILLLSPELPPPVGGAERHVRELARALAARgHDVTVLT-----PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRElrp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  80 ----ENIDVIVIEHSYWGWYGYLLHVLTKKPFIIHSHNIEAERFN-IQKRKYWKIYELyeKWAHQRCSHNFFKCEEDAAY 154
Cdd:cd03801    77 llrlRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLlLLAAERRLLARA--EALLRRADAVIAVSEALRDE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 155 AVKQWNINPSKVTIIRYGTDVQSsptaaekqaARSQLIQQVNLPASACLLLFNGTLNYAPNVEVLTEitgsIIPILRKNK 234
Cdd:cd03801   155 LRALGGIPPEKIVVIPNGVDLER---------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLE----ALAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 235 FNFSLIICGK---MLPEEWLQKLTQYPEIHFLGFV--ENIAAINAGVDALIQPgSMGTGIKTKLVEALAQNTTVITTHNG 309
Cdd:cd03801   222 PDVRLVIVGGdgpLRAELEELELGLGDRVRFLGFVpdEELPALYAAADVFVLP-SRYEGFGLVVLEAMAAGLPVVATDVG 300

                         330       340       350
                  ....*....|....*....|....*....|
gi 1056828536 310 arGIPQKIAQSK-LILIPDYNPVAFAEKIL 338
Cdd:cd03801   301 --GLPEVVEDGEgGLVVPPDDVEALADALL 328
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
203-339 2.98e-17

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 77.55  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 203 LLLFNGTLNYAP-NVEVLTEItgsiIPILRKNKFNFSLIICGKMlPEEWLQKLTQ--YPEIHFLGFVENIAAINAGVDAL 279
Cdd:pfam13692   3 VILFVGRLHPNVkGVDYLLEA----VPLLRKRDNDVRLVIVGDG-PEEELEELAAglEDRVIFTGFVEDLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 280 IQPgSMGTGIKTKLVEALAQNTTVITTHNGarGIPQKIAQSKLILIPDYNPVAFAEKILQ 339
Cdd:pfam13692  78 VLP-SLYEGFGLKLLEAMAAGLPVVATDVG--GIPELVDGENGLLVPPGDPEALAEAILR 134
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 269-371 2.76e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 46.14  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 269 IAAINAGVDALIQPGSMGtGIKTKLVEALAQNTTVITTHNGarGIPQKIAQSKL-ILIPDYNPVAFAEKILQFNNSID-- 345
Cdd:COG0438    14 LEALLAAADVFVLPSRSE-GFGLVLLEAMAAGLPVIATDVG--GLPEVIEDGETgLLVPPGDPEALAEAILRLLEDPElr 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1056828536 346 -----NIPNSFYHEFYWGNIAKQTHAVLENL 371
Cdd:COG0438    91 rrlgeAARERAEERFSWEAIAERLLALYEEL 121
 
Name Accession Description Interval E-value
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 4-338 4.52e-22

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: 96.07  E-value: 4.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536   4 LALISYKVFPAQMGGQKGIAQFYEYLAKQ-DNVIIVAaknnqLSDIPFPKKYNCLFPQGKGILNILKLFFVIKLIRR--- 79
Cdd:cd03801     2 ILLLSPELPPPVGGAERHVRELARALAARgHDVTVLT-----PADPGEPPEELEDGVIVPLLPSLAALLRARRLLRElrp 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  80 ----ENIDVIVIEHSYWGWYGYLLHVLTKKPFIIHSHNIEAERFN-IQKRKYWKIYELyeKWAHQRCSHNFFKCEEDAAY 154
Cdd:cd03801    77 llrlRKFDVVHAHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLlLLAAERRLLARA--EALLRRADAVIAVSEALRDE 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 155 AVKQWNINPSKVTIIRYGTDVQSsptaaekqaARSQLIQQVNLPASACLLLFNGTLNYAPNVEVLTEitgsIIPILRKNK 234
Cdd:cd03801   155 LRALGGIPPEKIVVIPNGVDLER---------FSPPLRRKLGIPPDRPVLLFVGRLSPRKGVDLLLE----ALAKLLRRG 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 235 FNFSLIICGK---MLPEEWLQKLTQYPEIHFLGFV--ENIAAINAGVDALIQPgSMGTGIKTKLVEALAQNTTVITTHNG 309
Cdd:cd03801   222 PDVRLVIVGGdgpLRAELEELELGLGDRVRFLGFVpdEELPALYAAADVFVLP-SRYEGFGLVVLEAMAAGLPVVATDVG 300

                         330       340       350
                  ....*....|....*....|....*....|
gi 1056828536 310 arGIPQKIAQSK-LILIPDYNPVAFAEKIL 338
Cdd:cd03801   301 --GLPEVVEDGEgGLVVPPDDVEALADALL 328
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
203-339 2.98e-17

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 77.55  E-value: 2.98e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 203 LLLFNGTLNYAP-NVEVLTEItgsiIPILRKNKFNFSLIICGKMlPEEWLQKLTQ--YPEIHFLGFVENIAAINAGVDAL 279
Cdd:pfam13692   3 VILFVGRLHPNVkGVDYLLEA----VPLLRKRDNDVRLVIVGDG-PEEELEELAAglEDRVIFTGFVEDLAELLAAADVF 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 280 IQPgSMGTGIKTKLVEALAQNTTVITTHNGarGIPQKIAQSKLILIPDYNPVAFAEKILQ 339
Cdd:pfam13692  78 VLP-SLYEGFGLKLLEAMAAGLPVVATDVG--GIPELVDGENGLLVPPGDPEALAEAILR 134
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
 17-337 4.77e-12

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: 66.22  E-value: 4.77e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  17 GGQKGIAQFYEYLAKQDNVIIVAAknNQLSDIPFPKKYNCLFP-QGKGILNILKLFFVIK-LIRRENIDVIVIEHSYWGW 94
Cdd:cd03819    12 GAETYILDLARALAERGHRVLVVT--AGGPLLPRLRQIGIGLPgLKVPLLRALLGNVRLArLIRRERIDLIHAHSRAPAW 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  95 YGYLLHVLTKKPFIIHSHNIEAERFNIqkrKYWKIYELYeKWAHQRCSHNFFKCEEDAAYAVkqwniNPSKVTIIRYGTD 174
Cdd:cd03819    90 LGWLASRLTGVPLVTTVHGSYLATYHP---KDFALAVRA-RGDRVIAVSELVRDHLIEALGV-----DPERIRVIPNGVD 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 175 VQSSPTAAEKQAARsqliqQVNLPASACLLLFNGTLNYAPNVEVLTEitgsIIPILRKNKfNFSLIICGKMLPEEWLQK- 253
Cdd:cd03819   161 TDRFPPEAEAEERA-----QLGLPEGKPVVGYVGRLSPEKGWLLLVD----AAAELKDEP-DFRLLVAGDGPERDEIRRl 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 254 -----LTQYpeIHFLGFVENIAAINAGVDALIQPGSMGTGIKTkLVEALAQNTTVITT-HNGARGIPQKIAQSklILIPD 327
Cdd:cd03819   231 verlgLRDR--VTFTGFREDVPAALAASDVVVLPSLHEEFGRV-ALEAMACGTPVVATdVGGAREIVVHGRTG--LLVPP 305

                         330
                  ....*....|
gi 1056828536 328 YNPVAFAEKI 337
Cdd:cd03819   306 GDAEALADAI 315
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
17-176 9.57e-12

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 62.94  E-value: 9.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  17 GGQKGIAQFYEYLAKQD-NVIIVA------AKNNQLSDIPFPKKYNCLFPqgKGILNILKLFFVIKLIRRENIDVIVIEH 89
Cdd:pfam13439   2 GVERYVLELARALARRGhEVTVVTpggpgpLAEEVVRVVRVPRVPLPLPP--RLLRSLAFLRRLRRLLRRERPDVVHAHS 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  90 SYWGWYGYL-LHVLTKKPFI--IHSHNIEAERFNIQKRKYWKIYELYEKWAHQRCSHNFFKCEEDAAYAVKQWNINPSKV 166
Cdd:pfam13439  80 PFPLGLAALaARLRLGIPLVvtYHGLFPDYKRLGARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVPPEKI 159

                         170
                  ....*....|
gi 1056828536 167 TIIRYGTDVQ 176
Cdd:pfam13439 160 RVIPNGVDLE 169
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
 34-306 4.12e-11

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: 63.53  E-value: 4.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  34 NVIIVAAKNNQLSDIPFPKKYNCLFPQGKGILNI----LKLFFVIK-LIRRENIDVIvieHSYWGWYGYLLHVL--TKKP 106
Cdd:cd03811    31 DVTLVLLRDEGDLDKQLNGDVKLIRLLIRVLKLIklglLKAILKLKrILKRAKPDVV---ISFLGFATYIVAKLaaARSK 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 107 FIIHSHNIeaerFNIQKRKYWKIYELYEKWahQRCSHNFFKCEEDAAYAVKQWNINPSKVTIIRYGTDVQSSPTAAEKQA 186
Cdd:cd03811   108 VIAWIHSS----LSKLYYLKKKLLLKLKLY--KKADKIVCVSKGIKEDLIRLGPSPPEKIEVIYNPIDIDRIRALAKEPI 181

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 187 arsqliqqVNLPASACLLLFNGTLNYAPNVEVLTEItgsiIPILRKNKFNFSLIICGKMLPEEWLQKLTQY----PEIHF 262
Cdd:cd03811   182 --------LNEPEDGPVILAVGRLDPQKGHDLLIEA----FAKLRKKYPDVKLVILGDGPLREELEKLAKElglaERVIF 249

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....
gi 1056828536 263 LGFVENIAAINAGVDALIQPgSMGTGIKTKLVEALAQNTTVITT 306
Cdd:cd03811   250 LGFQSNPYPYLKKADLFVLS-SRYEGFPNVLLEAMALGTPVVST 292
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 65-345 1.71e-09

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: 58.76  E-value: 1.71e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  65 LNILK----LFFVIKLIRRENIDVIvieHSYW---GWYGYLLHVLTKKPFIIHshNIEAERFNIQKRKY-WKIYELYEKW 136
Cdd:cd03808    61 INPLKdlkaLFKLYKLLKKEKPDIV---HCHTpkpGILGRLAARLAGVPKVIY--TVHGLGFVFTEGKLlRLLYLLLEKL 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 137 AHQRCSHNFFKCEEDAAYAVKQWNINPSKVTIIRyGTDV-QSSPTAAEKQAARSQLIqqvnlpasaclLLFNGTLNYAPN 215
Cdd:cd03808   136 ALLFTDKVIFVNEDDRDLAIKKGIIKKKKTVLIP-GSGVdLDRFQYSPESLPSEKVV-----------FLFVARLLKDKG 203

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 216 VEVLTEITGsiipILRKNKFNFSLIICGKMLPEE----WLQKLTQYPEIHFLGFVENIAAINAGVDALIQPgSMGTGIKT 291
Cdd:cd03808   204 IDELIEAAK----ILKKKGPNVRFLLVGDGELENpseiLIEKLGLEGRIEFLGFRSDVPELLAESDVFVLP-SYREGLPR 278

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1056828536 292 KLVEALAQNTTVITTHNGarGIPQKIAQSK-LILIPDYNPVAFAEKILQFNNSID 345
Cdd:cd03808   279 SLLEAMAAGRPVITTDVP--GCRELVIDGVnGFLVPPGDVEALADAIEKLIEDPE 331
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
 203-340 3.40e-08

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: 52.28  E-value: 3.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 203 LLLFNGTLNYAPNVEVLTEItgsiIPILRKNKFNFSLIICGKMLPEEWLQKLTQ----YPEIHFLGFV--ENIAAINAGV 276
Cdd:pfam00534   4 IILFVGRLEPEKGLDLLIKA----FALLKEKNPNLKLVIAGDGEEEKRLKKLAEklglGDNVIFLGFVsdEDLPELLKIA 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1056828536 277 DALIQPGSM-GTGIktKLVEALAQNTTVITTHNGarGIPQKIAQSKL-ILIPDYNPVAFAEKILQF 340
Cdd:pfam00534  80 DVFVLPSRYeGFGI--VLLEAMACGLPVIASDVG--GPPEVVKDGETgFLVKPNNAEALAEAIDKL 141
RfaB COG0438
Glycosyltransferase involved in cell wall bisynthesis [Cell wall/membrane/envelope biogenesis]; ...
 269-371 2.76e-06

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


Pssm-ID: 440207 [Multi-domain]  Cd Length: 123  Bit Score: 46.14  E-value: 2.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 269 IAAINAGVDALIQPGSMGtGIKTKLVEALAQNTTVITTHNGarGIPQKIAQSKL-ILIPDYNPVAFAEKILQFNNSID-- 345
Cdd:COG0438    14 LEALLAAADVFVLPSRSE-GFGLVLLEAMAAGLPVIATDVG--GLPEVIEDGETgLLVPPGDPEALAEAILRLLEDPElr 90

                          90       100       110
                  ....*....|....*....|....*....|.
gi 1056828536 346 -----NIPNSFYHEFYWGNIAKQTHAVLENL 371
Cdd:COG0438    91 rrlgeAARERAEERFSWEAIAERLLALYEEL 121
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
 66-347 5.82e-06

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: 47.67  E-value: 5.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  66 NILKLFF-VIKLIRRENIDVIVIEHSYWGWYGYLLHVLTKKPF-IIHSHNIEAerfniQKRKYWKIYELYEKWAHQRCSH 143
Cdd:cd03812    64 NIIKYFIkLLKLIKKEKYDIVHVHGSSSNGIILLLAAKAGVPVrIAHSHNTKD-----SSIKLRKIRKNVLKKLIERLST 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 144 NFFKCEEDAAYAVKQWNINpSKVTIIRYGTDVQS---SPTAAEKQAARSQLiqqvnlpaSACLLLFN-GTLNYAPNVEVL 219
Cdd:cd03812   139 KYLACSEDAGEWLFGEVEN-GKFKVIPNGIDIEKykfNKEKRRKRRKLLIL--------EDKLVLGHvGRFNEQKNHSFL 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 220 TEItgsiIPILRKNKFNFSLIICGKMLPEEWLQKLTQYPEI----HFLGFVENIAAINAGVDALIQPgSMGTGIKTKLVE 295
Cdd:cd03812   210 IDI----FEELKKKNPNVKLVLVGEGELKEKIKEKVKELGLedkvIFLGFRNDVSEILSAMDVFLFP-SLYEGLPLVAVE 284

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1056828536 296 ALAQNTTVITTHNGARG--IPQKIAQSKLILIPDYnpvaFAEKILQFNNSIDNI 347
Cdd:cd03812   285 AQASGLPCLLSDTITKEcdITNNVEFLPLNETPST----WAEKILKLIKRKRRI 334
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
 67-338 2.26e-05

Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. WbuB in E. coli is involved in the biosynthesis of the O26 O-antigen. It has been proposed to function as an N-acetyl-L-fucosamine (L-FucNAc) transferase.


Pssm-ID: 340825 [Multi-domain]  Cd Length: 391  Bit Score: 46.18  E-value: 2.26e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  67 ILKLFFVIkLIRRENIDVIVIEHSY--WGWYGYLLHVLTKKPFIIHSHNIEAERF----NIQKRKYWKIYELYEKWAHQR 140
Cdd:cd03794    85 ALAALLKL-LVREERPDVIIAYSPPitLGLAALLLKKLRGAPFILDVRDLWPESLialgVLKKGSLLKLLKKLERKLYRL 163

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 141 CSHNFFKCEEDAAYAVKQwNINPSKVTIIRYGTDVQS-SPTAAEKQAARSQLIQQVNlpasaclLLFNGTLNYAPNVEVL 219
Cdd:cd03794   164 ADAIIVLSPGLKEYLLRK-GVPKEKIIVIPNWADLEEfKPPPKDELRKKLGLDDKFV-------VVYAGNIGKAQGLETL 235

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 220 TEitgsIIPILRKNKfNFSLIICGKMLPEEWLQKLTQ---YPEIHFLGFV--ENIAAINAGVDALIQPGS----MGTGIK 290
Cdd:cd03794   236 LE----AAERLKRRP-DIRFLFVGDGDEKERLKELAKargLDNVTFLGRVpkEEVPELLSAADVGLVPLKdnpaNRGSSP 310

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1056828536 291 TKLVEALAQNTTVIttHNGARGIPQKIAQSKL-ILIPDYNPVAFAEKIL 338
Cdd:cd03794   311 SKLFEYMAAGKPIL--ASDDGGSDLAVEINGCgLVVEPGDPEALADAIL 357
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
 28-339 3.62e-05

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: 45.43  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  28 YLAKQDNVIIVAAKNNQLSDIPFPKKYNCL----FPQGKGILNILKLFFVIK-LIRRENIDVIvieHSYwgwYGYLLHVL 102
Cdd:cd03809    26 ALAKNDPDESVLAVPPLPGELLRLLREYPElslgVIKIKLWRELALLRWLQIlLPKKDKPDLL---HSP---HNTAPLLL 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 103 TKKPFIIHSHNIEAERF-NIQKRKYWKIYELYEKWAHQRCSH-----NFFKceEDAAyavKQWNINPSKVTIIRYGTDVQ 176
Cdd:cd03809   100 KGCPQVVTIHDLIPLRYpEFFPKRFRLYYRLLLPISLRRADAiitvsEATR--DDII---KFYGVPPEKIVVIPLGVDPS 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 177 SSPTAAEkqaarSQLIQQVNLPASacLLLFNGTLnyAP--NVEVLTEItgsiIPILRKNKFNFSLIICGKMLPE-----E 249
Cdd:cd03809   175 FFPPESA-----AVLIAKYLLPEP--YFLYVGTL--EPrkNHERLLKA----FALLKKQGGDLKLVIVGGKGWEdeellD 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 250 WLQKLTQYPEIHFLGFV--ENIAAINAGVDALIQPgSM--GTGIKtkLVEALAQNTTVITTHNGARgipQKIAQSKLILI 325
Cdd:cd03809   242 LVKKLGLGGRVRFLGYVsdEDLPALYRGARAFVFP-SLyeGFGLP--VLEAMACGTPVIASNISVL---PEVAGDAALYF 315

                         330
                  ....*....|....
gi 1056828536 326 PDYNPVAFAEKILQ 339
Cdd:cd03809   316 DPLDPESIADAILR 329
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
70-172 6.88e-05

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 42.77  E-value: 6.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  70 LFFVIKLIRRENIDVIVIEHSYWGWYGYLLHVLTKKPFIIHSHNIEAERFNIQKRkywKIYELYEKWAHQRCSHNFFKCE 149
Cdd:pfam13579  60 LRRLRRLLRAERPDVVHAHSPTAGLAARLARRRRGVPLVVTVHGLALDYGSGWKR---RLARALERRLLRRADAVVVVSE 136

                          90       100
                  ....*....|....*....|...
gi 1056828536 150 EDAAYAVkQWNINPSKVTIIRYG 172
Cdd:pfam13579 137 AEAELLR-ALGVPAARVVVVPNG 158
GT4_mannosyltransferase-like cd03822
mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most ...
 21-369 4.32e-04

mannosyltransferases of glycosyltransferase family 4 and similar proteins; This family is most closely related to the GT1 family of glycosyltransferases. ORF704 in E. coli has been shown to be involved in the biosynthesis of O-specific mannose homopolysaccharides.


Pssm-ID: 340849 [Multi-domain]  Cd Length: 370  Bit Score: 41.99  E-value: 4.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  21 GIAQFYEYL----AKQDNVIIVAAKNNQLSDIPFPKKYNclfPQGKGILNILKLFFVIKLIRRENIDVIVIEHSYwGWYG 96
Cdd:cd03822    14 GIATYTDDLveglRKGGPVVIVVIVSPQDEILKDDDFEV---PNEIKSWNSNEYFRLLDHLNFKKPDVVHIQHEF-GIFG 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536  97 -----YLLHVL--TKKPFIIHSHNIEA--ERFNIQKRKYWKIYELYEKwahqrcshNFFKCEEDAAYAVKQWNINPSKVT 167
Cdd:cd03822    90 gkyglYALGLLlhLRIPVITTLHTVLDlsDPGKQALKVLFRIATLSER--------VVVMAPISRFLLVRIKLIPAVNIE 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 168 IIRYGT-DVQSSPTAAEKQAArsqliqqvnLPASACLLLFNGTLNYAPNVEVLTEitgsIIPILRKNKFNFSLIICGKML 246
Cdd:cd03822   162 VIPHGVpEVPQDPTTALKRLL---------LPEGKKVILTFGFIGPGKGLEILLE----ALPELKAEFPDVRLVIAGELH 228

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1056828536 247 PEEWLQKLTQYP--EIHFLGFVENIAAINAGV------------DALIQP------GSMGTgiktkLVEALAQNTTVITT 306
Cdd:cd03822   229 PSLARYEGERYRkaAIEELGLQDHVDFHNNFLpeeevpryisaaDVVVLPylnteqSSSGT-----LSYAIACGKPVIST 303

                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1056828536 307 HngARGIPQKIAQSKLILIPDYNPVAFAEKILQFNNSID------NIPNSFYHEFYWGNIAKQTHAVLE 369
Cdd:cd03822   304 P--LRHAEELLADGRGVLVPFDDPSAIAEAILRLLEDDErrqaiaERAYAYARAMTWESIADRYLRLFN 370
 
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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