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Conserved domains on  [gi|1949865553|ref|XP_038213592|]
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phosphatidylinositol N-acetylglucosaminyltransferase subunit A isoform X2 [Zerene cesonia]

Protein Classification

glycosyltransferase family protein( domain architecture ID 56)

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
Glycosyltransferase_GTB-type super family cl10013
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
16-283 1.04e-163

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


The actual alignment was detected with superfamily member cd03796:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 398  Bit Score: 460.17  E-value: 1.04e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMICNIAIVR 95
Cdd:cd03796     2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILIRERIQIVHGHSAFSVLAHEVSIIGKLMGLKTVFTDHSLFGFADMSAVLTNKYLQMCLCECDHCICVSHTGKENTVL 175
Cdd:cd03796    82 NILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 176 RAKVKAHKVSVIPNAVDAYTFTPDPSQRDPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQE 255
Cdd:cd03796   162 RASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241
                         250       260
                  ....*....|....*....|....*...
gi 1949865553 256 VRERKGFQHCVTLLGSLKHSEVRDVLVK 283
Cdd:cd03796   242 MREKYQLQDRVELLGAVPHEEVRDVLVQ 269
 
Name Accession Description Interval E-value
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
16-283 1.04e-163

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: 460.17  E-value: 1.04e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMICNIAIVR 95
Cdd:cd03796     2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILIRERIQIVHGHSAFSVLAHEVSIIGKLMGLKTVFTDHSLFGFADMSAVLTNKYLQMCLCECDHCICVSHTGKENTVL 175
Cdd:cd03796    82 NILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 176 RAKVKAHKVSVIPNAVDAYTFTPDPSQRDPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQE 255
Cdd:cd03796   162 RASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241
                         250       260
                  ....*....|....*....|....*...
gi 1949865553 256 VRERKGFQHCVTLLGSLKHSEVRDVLVK 283
Cdd:cd03796   242 MREKYQLQDRVELLGAVPHEEVRDVLVQ 269
PIGA pfam08288
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ...
53-142 2.14e-48

PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.


Pssm-ID: 400541  Cd Length: 90  Bit Score: 155.88  E-value: 2.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  53 HCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMICNIAIVRYILIRERIQIVHGHSAFSVLAHEVSIIGKLMGLKTVF 132
Cdd:pfam08288   1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80
                          90
                  ....*....|
gi 1949865553 133 TDHSLFGFAD 142
Cdd:pfam08288  81 TDHSLFGFAD 90
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
27-247 5.19e-07

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 50.48  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  27 TGGVEEHIYNLSQCLIKRGHKVVVITHCY-----------------------EDRVGVRYLTG-GLKVYYL--------- 73
Cdd:COG0297    16 TGGLADVVGALPKALAKLGHDVRVVLPGYpsiddklkdlevvaslevplggrTYYARVLEGPDdGVPVYFIdnpelfdrp 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  74 -------------PIR-VFYSQCALpTMICNIAIvryilireRIQIVHGH---SAF-SVLAHEVSIIGKLMGLKTVFTDH 135
Cdd:COG0297    96 gpygdpdrdypdnAERfAFFSRAAL-ELLKGLDW--------KPDIIHCHdwqTGLiPALLKTRYADDPFKRIKTVFTIH 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 136 SL-----FGFADMSAV-LTNKYLQMCLCECDHCIC--------------VSHT------------GKENtVLRAKvkAHK 183
Cdd:COG0297   167 NLayqgiFPAEILELLgLPPELFTPDGLEFYGQINflkagivyadrvttVSPTyareiqtpefgeGLDG-LLRAR--SGK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 184 VSVIPNAVDAYTFTP--DPS--------------------QR------DPNVITVIIVSRLVYRKGVDLMAAVIADMCPR 235
Cdd:COG0297   244 LSGILNGIDYDVWNPatDPYlpanysaddlegkaankaalQEelglpvDPDAPLIGMVSRLTEQKGLDLLLEALDELLEE 323
                         330
                  ....*....|..
gi 1949865553 236 ypNLRFIIGGDG 247
Cdd:COG0297   324 --DVQLVVLGSG 333
 
Name Accession Description Interval E-value
GT4_PIG-A-like cd03796
phosphatidylinositol N-acetylglucosaminyltransferase subunit A and similar proteins; This ...
16-283 1.04e-163

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: 460.17  E-value: 1.04e-163
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMICNIAIVR 95
Cdd:cd03796     2 ICMVSDFFYPNLGGVETHIYQLSQCLIKRGHKVIVITHAYGNRVGVRYLTNGLKVYYLPFKVFYNQSTLPTLFSTFPLLR 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILIRERIQIVHGHSAFSVLAHEVSIIGKLMGLKTVFTDHSLFGFADMSAVLTNKYLQMCLCECDHCICVSHTGKENTVL 175
Cdd:cd03796    82 NILIRERIQIVHGHQAFSSLAHEALFHARTLGLKTVFTDHSLFGFADASSILTNKLLRFSLADIDHVICVSHTSKENTVL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 176 RAKVKAHKVSVIPNAVDAYTFTPDPSQRDPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQE 255
Cdd:cd03796   162 RASLDPRIVSVIPNAVDSSDFTPDPSKPDPNKITIVVISRLVYRKGIDLLVGIIPRICKKHPNVRFIIGGDGPKRIELEE 241
                         250       260
                  ....*....|....*....|....*...
gi 1949865553 256 VRERKGFQHCVTLLGSLKHSEVRDVLVK 283
Cdd:cd03796   242 MREKYQLQDRVELLGAVPHEEVRDVLVQ 269
PIGA pfam08288
PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol ...
53-142 2.14e-48

PIGA (GPI anchor biosynthesis); This domain is found on phosphatidylinositol n-acetylglucosaminyltransferase proteins. These proteins are involved in GPI anchor biosynthesis and are associated with disease the paroxysmal nocturnal haemoglobinuria.


Pssm-ID: 400541  Cd Length: 90  Bit Score: 155.88  E-value: 2.14e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  53 HCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMICNIAIVRYILIRERIQIVHGHSAFSVLAHEVSIIGKLMGLKTVF 132
Cdd:pfam08288   1 HAYGDRTGVRYLTNGLKVYYVPFLVIYRQSTFPTVFGTFPLFRNILLRERIDIVHGHGSFSTLAHEAILHARTMGLKTVF 80
                          90
                  ....*....|
gi 1949865553 133 TDHSLFGFAD 142
Cdd:pfam08288  81 TDHSLFGFAD 90
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
16-281 1.25e-34

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


Pssm-ID: 340831 [Multi-domain]  Cd Length: 366  Bit Score: 128.42  E-value: 1.25e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALptmicnIAIVR 95
Cdd:cd03801     2 ILLLSPELPPPVGGAERHVRELARALAARGHDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRL------LRELR 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILIRERIQIVHGHSAFSVLAheVSIIGKLMGLKTVFTDHSLFGF------ADMSAVLTNKYLQmcLCECDHCICVSHTG 169
Cdd:cd03801    76 PLLRLRKFDVVHAHGLLAALL--AALLALLLGAPLVVTLHGAEPGrlllllAAERRLLARAEAL--LRRADAVIAVSEAL 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 170 KENTVLRAKVKAHKVSVIPNAVDAYTFTPDPSQR---DPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRF-IIGG 245
Cdd:cd03801   152 RDELRALGGIPPEKIVVIPNGVDLERFSPPLRRKlgiPPDRPVLLFVGRLSPRKGVDLLLEALAKLLRRGPDVRLvIVGG 231
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1949865553 246 DGPkmWLLQEVRERKGFQHCVTLLGSLKHSEVRDVL 281
Cdd:cd03801   232 DGP--LRAELEELELGLGDRVRFLGFVPDEELPALY 265
GT4_WavL-like cd03819
Vibrio cholerae WavL and similar sequences; This family is most closely related to the GT4 ...
16-270 1.82e-26

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: 105.90  E-value: 1.82e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPntGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYsqcalptmicNIAIVR 95
Cdd:cd03819     1 ILMLTPALEI--GGAETYILDLARALAERGHRVLVVTAGGPLLPRLRQIGIGLPGLKVPLLRAL----------LGNVRL 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILI-RERIQIVHGHSAFSVLAheVSIIGKLMGLKTVFTDHSL----FGFADMS-AVLTNKylqmclcecDHCICVSHTG 169
Cdd:cd03819    69 ARLIrRERIDLIHAHSRAPAWL--GWLASRLTGVPLVTTVHGSylatYHPKDFAlAVRARG---------DRVIAVSELV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 170 KENTVLRAKVKAHKVSVIPNAVDAYTFTPDPSQR-------DPNVITVIIVSRLVYRKGVDL---MAAVIADMcpryPNL 239
Cdd:cd03819   138 RDHLIEALGVDPERIRVIPNGVDTDRFPPEAEAEeraqlglPEGKPVVGYVGRLSPEKGWLLlvdAAAELKDE----PDF 213
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1949865553 240 RFIIGGDGPKMWLLQEVRERKGFQHCVTLLG 270
Cdd:cd03819   214 RLLVAGDGPERDEIRRLVERLGLRDRVTFTG 244
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
28-192 2.93e-23

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 93.37  E-value: 2.93e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  28 GGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTgglkVYYLPIRVFYSQCALPTMICNIAIVRYILIRERIQIVH 107
Cdd:pfam13439   1 GGVERYVLELARALARRGHEVTVVTPGGPGPLAEEVVR----VVRVPRVPLPLPPRLLRSLAFLRRLRRLLRRERPDVVH 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 108 GHSAFSvLAHEVSIIGKLMGLKTVFTDHSLF-------GFADMSAVLTNKYLQMCLCECDHCICVSHTGKENTVLRAKVK 180
Cdd:pfam13439  77 AHSPFP-LGLAALAARLRLGIPLVVTYHGLFpdykrlgARLSPLRRLLRRLERRLLRRADRVIAVSEAVADELRRLYGVP 155
                         170
                  ....*....|..
gi 1949865553 181 AHKVSVIPNAVD 192
Cdd:pfam13439 156 PEKIRVIPNGVD 167
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
15-277 1.24e-19

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: 87.33  E-value: 1.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  15 IICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVIT------HCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTmi 88
Cdd:cd03817     1 KIAIFTDTYLPQVNGVATSVRNLARALEKRGHEVYVITpsdpgaEDEEEVVRYRSFSIPIRKYHRQHIPFPFKKAVID-- 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  89 cniaivryILIRERIQIVHGHSAFSV--LAHEvsiIGKLMGLKTVFTDHSL---------FGFADMSAVLTNKYLQMCLc 157
Cdd:cd03817    79 --------RIKELGPDIIHTHTPFSLgkLGLR---IARKLKIPIVHTYHTMyedylhyipKGKLLVKAVVRKLVRRFYN- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 158 ECDHCICVSHtGKENTVLRAKVKAHKVsVIPNAVDAYTFTPDPSQR-------DPNVITVIIVSRLVYRKGVDLMAAVIA 230
Cdd:cd03817   147 HTDAVIAPSE-KIKDTLREYGVKGPIE-VIPNGIDLDKFEKPLNTEerrklglPPDEPILLYVGRLAKEKNIDFLLRAFA 224
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1949865553 231 DMcPRYPNLRFIIGGDGPKMWLLQEVRERKGFQHCVTLLGSLKHSEV 277
Cdd:cd03817   225 EL-KKEPNIKLVIVGDGPEREELKELARELGLADKVIFTGFVPREEL 270
GT4_WlbH-like cd03798
Bordetella parapertussis WlbH and similar proteins; This family is most closely related to the ...
22-281 4.24e-19

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: 85.89  E-value: 4.24e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  22 FFYPNT--GGVEEHIYNLSQCLIKRGHKVVVIT-------------HCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALpt 86
Cdd:cd03798     6 NIYPNAnsPGRGIFVRRQVRALSRRGVDVEVLApapwgpaaarllrKLLGEAVPPRDGRRLLPLKPRLRLLAPLRAPS-- 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  87 micnIAIVRYILIRERIQIVHGHSAFS--VLAHevsIIGKLMGLKTVFTDHS--LFGFADMSAVLtnKYLQMCLCECDHC 162
Cdd:cd03798    84 ----LAKLLKRRRRGPPDLIHAHFAYPagFAAA---LLARLYGVPYVVTEHGsdINVFPPRSLLR--KLLRWALRRAARV 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 163 ICVSHTGKEnTVLRAKVKAHKVSVIPNAVDAYTFTPDPSQRD--PNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLR 240
Cdd:cd03798   155 IAVSKALAE-ELVALGVPRDRVDVIPNGVDPARFQPEDRGLGlpLDAFVILFVGRLIPRKGIDLLLEAFARLAKARPDVV 233
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 1949865553 241 FIIGGDGPKMWLLQEVRERKGFQHCVTLLGSLKHSEVRDVL 281
Cdd:cd03798   234 LLIVGDGPLREALRALAEDLGLGDRVTFTGRLPHEQVPAYY 274
GT4_GT28_WabH-like cd03811
family 4 and family 28 glycosyltransferases similar to Klebsiella WabH; This family is most ...
22-270 4.26e-18

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: 82.79  E-value: 4.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  22 FFYPNT--GGVEEHIYNLSQCLIKRGHKVVVITHC----YEDRVGVRYLTGGLKVYYLPIRVFysqcALPTMICNIaivR 95
Cdd:cd03811     4 FVIPSLsgGGAERVLLNLANALDKRGYDVTLVLLRdegdLDKQLNGDVKLIRLLIRVLKLIKL----GLLKAILKL---K 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILIRERIQIVHGHSAFSVLaheVSIIGKLMGLKTVFTDHSLFGFADMsavLTNKYLQMCLC--ECDHCICVSHTGKENT 173
Cdd:cd03811    77 RILKRAKPDVVISFLGFATY---IVAKLAAARSKVIAWIHSSLSKLYY---LKKKLLLKLKLykKADKIVCVSKGIKEDL 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 174 VLRAKVKAHKVSVIPNAVDAYTFTPDPSQR----DPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPK 249
Cdd:cd03811   151 IRLGPSPPEKIEVIYNPIDIDRIRALAKEPilnePEDGPVILAVGRLDPQKGHDLLIEAFAKLRKKYPDVKLVILGDGPL 230
                         250       260
                  ....*....|....*....|.
gi 1949865553 250 MWLLQEVRERKGFQHCVTLLG 270
Cdd:cd03811   231 REELEKLAKELGLAERVIFLG 251
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
16-284 1.39e-17

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: 81.62  E-value: 1.39e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCY-----EDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMIC- 89
Cdd:cd03794     2 ILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPnyplgRIFAGATETKDGIRVIRVKLGPIKKNGLIRRLLNy 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  90 ---NIAIVRYILIR-ERIQIVHGHSAFSVLAHEVSIIGKLMGLKTVFTDHSLFGFADMSA-VLTNKYL--------QMCL 156
Cdd:cd03794    82 lsfALAALLKLLVReERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALgVLKKGSLlkllkkleRKLY 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 157 CECDHCICVSHTGKENtVLRAKVKAHKVSVIPNAVDAYTFTPDPSQR------DPNVITVIIVSRLVYRKGVDLMAAVIA 230
Cdd:cd03794   162 RLADAIIVLSPGLKEY-LLRKGVPKEKIIVIPNWADLEEFKPPPKDElrkklgLDDKFVVVYAGNIGKAQGLETLLEAAE 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1949865553 231 DMcPRYPNLRFIIGGDGPKMWLLQEVRERKGFQHcVTLLGSLKHSEVRDVLVKV 284
Cdd:cd03794   241 RL-KRRPDIRFLFVGDGDEKERLKELAKARGLDN-VTFLGRVPKEEVPELLSAA 292
GT4_WbnK-like cd03807
Shigella dysenteriae WbnK and similar proteins; This family is most closely related to the GT4 ...
14-270 4.22e-16

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: 77.36  E-value: 4.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  14 HIIcmasdfFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMIcniai 93
Cdd:cd03807     4 HVI------TGLNVGGAETMLLRLLEHMDKSRFEHVVISLTGDGVLGEELLAAGVPVVCLGLSSGKDPGVLLRLA----- 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  94 vrYILIRERIQIVHGHSAFSVLAhevSIIGKLM--GLKTVFTDHSLFGFADMSAVLTNKYLQMCLCECDhCICVSHTGKE 171
Cdd:cd03807    73 --KLIRKRNPDVVHTWMYHADLI---GGLAAKLagGVKVIWSVRSSNIPQRLTRLVRKLCLLLSKFSPA-TVANSSAVAE 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 172 nTVLRAKVKAHKVSVIPNAVDAYTFTPDPSQRDP---------NVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFI 242
Cdd:cd03807   147 -FHQEQGYAKNKIVVIYNGIDLFKLSPDDASRARarrrlglaeDRRVIGIVGRLHPVKDHSDLLRAAALLVETHPDLRLL 225
                         250       260
                  ....*....|....*....|....*...
gi 1949865553 243 IGGDGPKMWLLQEVRERKGFQHCVTLLG 270
Cdd:cd03807   226 LVGRGPERPNLERLLLELGLEDRVHLLG 253
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
26-285 1.22e-15

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


Pssm-ID: 340837 [Multi-domain]  Cd Length: 358  Bit Score: 75.71  E-value: 1.22e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  26 NTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRV------GVRYLTggLKVYYLPIRVFYSQCALptmicnIAIVRyILI 99
Cdd:cd03808     8 VDGGFQSFRLPLIKALVKKGYEVHVIAPDGDKLSdelkelGVKVID--IPILRRGINPLKDLKAL------FKLYK-LLK 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 100 RERIQIVHGHSAFSVlahevsIIGKLMGL-----KTVFTDHSLfGFADMSavltNKYLQM--CLCE------CDHCICVS 166
Cdd:cd03808    79 KEKPDIVHCHTPKPG------ILGRLAARlagvpKVIYTVHGL-GFVFTE----GKLLRLlyLLLEklallfTDKVIFVN 147
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 167 HTGKENTVLRAKVKAHKVSVIP-NAVDAYTFTPDPSQRDPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGG 245
Cdd:cd03808   148 EDDRDLAIKKGIIKKKKTVLIPgSGVDLDRFQYSPESLPSEKVVFLFVARLLKDKGIDELIEAAKILKKKGPNVRFLLVG 227
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 1949865553 246 DGPKMWLLQEVRERKGFQHCVTLLGSLkhSEVRDVLVKVS 285
Cdd:cd03808   228 DGELENPSEILIEKLGLEGRIEFLGFR--SDVPELLAESD 265
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
26-274 6.14e-15

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: 73.81  E-value: 6.14e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  26 NTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMICNIAIVRYILIRERIQI 105
Cdd:cd03820    11 NAGGAERVAINLANHLAKKGYDVTIISLDSAEKPPFYELDDNIKIKNLGDRKYSHFKLLLKYFKKVRRLRKYLKNNKPDV 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 106 V--HGHSAFSVLAhevsIIGklMGLKTVFTDHSLFgFADMSAVLtnKYLQMCLC--ECDHCICVSHTGKENtvlRAKVKA 181
Cdd:cd03820    91 VisFRTSLLTFLA----LIG--LKSKLIVWEHNNY-EAYNKGLR--RLLLRRLLykRADKIVVLTEADKLK---KYKQPN 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 182 HKVSVIPNAVdayTFTPDPSQRDPNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQEVRERKG 261
Cdd:cd03820   159 SNVVVIPNPL---SFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIEAWALIAKKHPDWKLRIYGDGPEREELEKLIDKLG 235
                         250
                  ....*....|...
gi 1949865553 262 FQHCVTLLGSLKH 274
Cdd:cd03820   236 LEDRVKLLGPTKN 248
GT4_ExpE7-like cd03823
glycosyltransferase ExpE7 and similar proteins; This family is most closely related to the GT4 ...
20-284 1.43e-11

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: 63.89  E-value: 1.43e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  20 SDFFYPN-TGGVEEHIYNLSQCLIKRGHKVVVITHCYED-------RVGVRYLTGGLKVYYLPIR-------VFYSQCAL 84
Cdd:cd03823     6 NSLYPPQrVGGAEISVHDLAEALVAEGHEVAVLTAGVGPpgqatvaRSVVRYRRAPDETLPLALKrrgyelfETYNPGLR 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  85 PtmicniaIVRYILIRERIQIVHGHSaFSVLAHEVSIIGKLMGLKTVFTDHSLFGfadmsavltnkylqmclcECDHCIC 164
Cdd:cd03823    86 R-------LLARLLEDFRPDVVHTHN-LSGLGASLLDAARDLGIPVVHTLHDYWL------------------LCPRQFL 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 165 VSHTGK---------ENTVLRAKVKAHKVSVIPNAVDAYTFTPDPSQRDPNVITVIIVSRLVYRKGVDLMAAViADMCPR 235
Cdd:cd03823   140 FKKGGDavlapsrftANLHEANGLFSARISVIPNAVEPDLAPPPRRRPGTERLRFGYIGRLTEEKGIDLLVEA-FKRLPR 218
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1949865553 236 yPNLRFIIGGDGPkmwLLQEVRERKGFQhcVTLLGSLKHSEVRDVLVKV 284
Cdd:cd03823   219 -EDIELVIAGHGP---LSDERQIEGGRR--IAFLGRVPTDDIKDFYEKI 261
GT4-like cd05844
glycosyltransferase family 4 proteins; Glycosyltransferases catalyze the transfer of sugar ...
163-281 6.12e-11

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: 62.08  E-value: 6.12e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 163 ICVSHTGKENtVLRAKVKAHKVSVIPNAVDAYTFTP-DPSQRDPnviTVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRF 241
Cdd:cd05844   148 VAVSGFIRDR-LLARGLPAERIHVHYIGIDPAKFAPrDPAERAP---TILFVGRLVEKKGCDVLIEAFRRLAARHPTARL 223
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1949865553 242 IIGGDGPkmwLLQEVRERKGFQHCVTLLGSLKHSEVRDVL 281
Cdd:cd05844   224 VIAGDGP---LRPALQALAAALGRVRFLGALPHAEVQDWM 260
GT4_Bme6-like cd03821
Brucella melitensis Bme6 and similar proteins; This family is most closely related to the GT4 ...
23-273 8.48e-11

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: 61.62  E-value: 8.48e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  23 FYPNTGGVEEHIYNLSQCLIKRGHKVVVITH--CYEDRVGVRYLTGGLKVYYLPIRVFYSQCALPTMIC-NIAIVRYILI 99
Cdd:cd03821     9 ISPKAGGPVKVVLRLAAALAALGHEVTIVSTgdGYESLVVEENGRYIPPQDGFASIPLLRQGAGRTDFSpGLPNWLRRNL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 100 RErIQIVHGHSAFSVLAHEVSIIGKLMGLKTVFTDH-SLFGFA-DMSAVLTNKYLQMCL------CECDHCICVshtgKE 171
Cdd:cd03821    89 RE-YDVVHIHGVWTYTSLAACKLARRRGIPYVVSPHgMLDPWAlQQKHWKKRIALHLIErrnlnnAALVHFTSE----QE 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 172 NTVLRAKVKAHKVSVIPNAVDAYTFTPDPSQRD-----PNVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGD 246
Cdd:cd03821   164 ADELRRFGLEPPIAVIPNGVDIPEFDPGLRDRRkhnglEDRRIILFLGRIHPKKGLDLLIRAARKLAEQGRDWHLVIAGP 243
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1949865553 247 GP-----KMWLLQEvrerKGFQHCVTLLGSLK 273
Cdd:cd03821   244 DDgaypaFLQLQSS----LGLGDRVTFTGPLY 271
GT4_WfcD-like cd03795
Escherichia coli alpha-1,3-mannosyltransferase WfcD and similar proteins; This family is most ...
22-272 7.78e-10

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: 58.82  E-value: 7.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  22 FFYPNTGGVEEHIYNLSQCLIKRGHKVVVIThCYEDRVGVRYLTGGLKVyylpIRVFYSQCALPTMICNIAIVRYILIRE 101
Cdd:cd03795     8 FYYPDIGGIEQVIYDLAEGLKKKGIEVDVLC-FSKEKETPEKEENGIRI----HRVKSFLNVASTPFSPSYIKRFKKLAK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 102 RIQIVHGHSAFSV--LAHEVSIIGKlmglKTVFTDHSlfgfaDmsaVLTNKYL--------QMCLCECDHCICVSHTGKE 171
Cdd:cd03795    83 EYDIIHYHFPNPLadLLLFFSGAKK----PVVVHWHS-----D---IVKQKKLlklykplmTRFLRRADRIIATSPNYVE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 172 NTVLRAKVKaHKVSVIPNAVDAYTFTPDPSQ----RDPNVITVIIVS--RLVYRKGVD-LMAAViadmcpRYPNLRFIIG 244
Cdd:cd03795   151 TSPTLREFK-NKVRVIPLGIDKNVYNIPRVDfeniKREKKGKKIFLFigRLVYYKGLDyLIEAA------QYLNYPIVIG 223
                         250       260
                  ....*....|....*....|....*...
gi 1949865553 245 GDGPKMWLLQEVRErKGFQHCVTLLGSL 272
Cdd:cd03795   224 GEGPLKPDLEAQIE-LNLLDNVKFLGRV 250
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
28-190 1.54e-09

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 55.48  E-value: 1.54e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  28 GGVEEHIYNLSQCLIKRGHKVVVIthCYEDRVGVRYLTG-GLKVYYLPIRVFYSQCALPTMicnIAIVRYILIRERIQIV 106
Cdd:pfam13579   1 GGIGVYVLELARALAALGHEVRVV--TPGGPPGRPELVGdGVRVHRLPVPPRPSPLADLAA---LRRLRRLLRAERPDVV 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 107 HGHSAFSVLAheVSIIGKLMGLKTVFTDHSLfGFADMSAVLTNKYLQM---CLCECDHCICVSHTGKEnTVLRAKVKAHK 183
Cdd:pfam13579  76 HAHSPTAGLA--ARLARRRRGVPLVVTVHGL-ALDYGSGWKRRLARALerrLLRRADAVVVVSEAEAE-LLRALGVPAAR 151

                  ....*..
gi 1949865553 184 VSVIPNA 190
Cdd:pfam13579 152 VVVVPNG 158
Glycosyltransferase_GTB-type cd01635
glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases ...
16-285 2.13e-09

glycosyltransferase family 1 and related proteins with GTB topology; Glycosyltransferases catalyze the transfer of sugar moieties from activated donor molecules to specific acceptor molecules, forming glycosidic bonds. The acceptor molecule can be a lipid, a protein, a heterocyclic compound, or another carbohydrate residue. The structures of the formed glycoconjugates are extremely diverse, reflecting a wide range of biological functions. The members of this family share a common GTB topology, one of the two protein topologies observed for nucleotide-sugar-dependent glycosyltransferases. GTB proteins have distinct N- and C- terminal domains each containing a typical Rossmann fold. The two domains have high structural homology despite minimal sequence homology. The large cleft that separates the two domains includes the catalytic center and permits a high degree of flexibility.


Pssm-ID: 340816 [Multi-domain]  Cd Length: 235  Bit Score: 56.64  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDrvgvryltgglkvyylpirvfysqcalptmicnIAIVR 95
Cdd:cd01635     1 ILLVTGEYPPLRGGLELHVRALARALAALGHEVTVLALLLLA---------------------------------LRRIL 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  96 YILIRERIQIVHGHSAFSvLAHEVSIIGKLMGLKTVFTDHSLFgfadmsavltnkylqmclcecDHCICVSHTGKENTVL 175
Cdd:cd01635    48 KKLLELKPDVVHAHSPHA-AALAALLAARLLGIPIVVTVHGPD---------------------SLESTRSELLALARLL 105
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 176 RAKVKAHKVSVipnavdaytftpdpsqrdpnvitviivSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQE 255
Cdd:cd01635   106 VSLPLADKVSV---------------------------GRLVPEKGIDLLLEALALLKARLPDLVLVLVGGGGEREEEEA 158
                         250       260       270
                  ....*....|....*....|....*....|
gi 1949865553 256 VRERKGFQHCVTLLGSLKHSEVRDVLVKVS 285
Cdd:cd01635   159 LAAALGLLERVVIIGGLVDDEVLELLLAAA 188
GT4_MtfB-like cd03809
glycosyltransferases MtfB, WbpX, and similar proteins; This family is most closely related to ...
15-249 4.02e-09

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: 56.60  E-value: 4.02e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  15 IICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVRYLtgglKVYYLPIRVFYSQCALPTMICNIAIV 94
Cdd:cd03809     1 KILIDGRSLAQRLTGIGRYTRELLKALAKNDPDESVLAVPPLPGELLRLL----REYPELSLGVIKIKLWRELALLRWLQ 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  95 RYILIRERIQIVHGHSAFSVLahevsiigKLMGLKTVFTDHSLF------GFADMSAVLTNKYLQMCLCECDHCICVSHT 168
Cdd:cd03809    77 ILLPKKDKPDLLHSPHNTAPL--------LLKGCPQVVTIHDLIplrypeFFPKRFRLYYRLLLPISLRRADAIITVSEA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 169 GKENTVLRAKVKAHKVSVIPNAVDAYTFTPDPS--------QRDPnviTVIIVSRLVYRKGVDLMAAVIADMCPRYPNLR 240
Cdd:cd03809   149 TRDDIIKFYGVPPEKIVVIPLGVDPSFFPPESAavliakylLPEP---YFLYVGTLEPRKNHERLLKAFALLKKQGGDLK 225
                         250
                  ....*....|
gi 1949865553 241 -FIIGGDGPK 249
Cdd:cd03809   226 lVIVGGKGWE 235
GT4_sucrose_synthase cd03800
sucrose-phosphate synthase and similar proteins; This family is most closely related to the ...
25-282 1.40e-08

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: 54.94  E-value: 1.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  25 PNTGGVEEHIYNLSQCLIKRGHKVVVITHCYEDRVGVR-YLTGGLKVYYLP--IRVFYSQCALPTMICNIA--IVRYILi 99
Cdd:cd03800    18 ADTGGQNVYVLELARALAELGYQVDIFTRRISPADPEVvEIAPGARVIRVPagPPEYLPKEELWPYLEEFAdgLLRFIA- 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 100 RERIQ--IVHGHSAFSVLAheVSIIGKLMGLKTVFTDHSLfGfadmsavlTNKYLQM-----------------CLCECD 160
Cdd:cd03800    97 REGGRydLIHSHYWDSGLV--GALLARRLGVPLVHTFHSL-G--------RVKYRHLgaqdtyhpslritaeeqILEAAD 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 161 hCIcVSHTGKENTVLRAKVKAH--KVSVIPNAVDAYTFTPDPSQR--------DPNVITVIIVSRLVYRKGVDLMAAVIA 230
Cdd:cd03800   166 -RV-IASTPQEADELISLYGADpsRINVVPPGVDLERFFPVDRAEarrarlllPPDKPVVLALGRLDPRKGIDTLVRAFA 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949865553 231 DMCPRYPNLRFIIGGDGPKMWLLQEVRERKGFQHC------VTLLGSLKHSEV------RDVLV 282
Cdd:cd03800   244 QLPELRELANLVLVGGPSDDPLSMDREELAELAEElglidrVRFPGRVSRDDLpelyraADVFV 307
GT4_CapH-like cd03812
capsular polysaccharide biosynthesis glycosyltransferase CapH and similar proteins; This ...
26-271 2.40e-08

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: 54.22  E-value: 2.40e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  26 NTGGVEEHIYNLSQCLIKRGHKVVVIthCYEDRVGVRY---LTGGLKVYYLPIRVFYsqcalptMICNIAIVRYILIRER 102
Cdd:cd03812    10 NVGGIETFLMNLYRKLDKSKIEFDFL--ATSDDKGEYDeelEELGGKIFYIPPKKKN-------IIKYFIKLLKLIKKEK 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 103 IQIVHGHSAFSVLAHEVSIigKLMGLK--------TVFTDHSLfgfaDMSAVLTNKYLQMCLCecDHCICVSHtgKENTV 174
Cdd:cd03812    81 YDIVHVHGSSSNGIILLLA--AKAGVPvriahshnTKDSSIKL----RKIRKNVLKKLIERLS--TKYLACSE--DAGEW 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 175 LRAKVKAHKVSVIPNAVDAYTFTPDPSQRDP--------NVITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGD 246
Cdd:cd03812   151 LFGEVENGKFKVIPNGIDIEKYKFNKEKRRKrrkllileDKLVLGHVGRFNEQKNHSFLIDIFEELKKKNPNVKLVLVGE 230
                         250       260
                  ....*....|....*....|....*
gi 1949865553 247 GPKMWLLQEVRERKGFQHCVTLLGS 271
Cdd:cd03812   231 GELKEKIKEKVKELGLEDKVIFLGF 255
GT4-like cd03814
glycosyltransferase family 4 proteins; This family is most closely related to the GT4 family ...
16-273 5.07e-08

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: 53.45  E-value: 5.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  16 ICMASDFFYPNTGGVEEHIYNLSQCLIKRGHKVVVIT----HCYEDRVGVRYLTGGLKvyyLPirvFYSQC--ALPTMic 89
Cdd:cd03814     2 IALVTDTYHPQVNGVVRTLERLVDHLRRRGHEVRVVApgpfDEAESAEGRVVSVPSFP---LP---FYPEYrlALPLP-- 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  90 niAIVRYILIRERIQIVHGHSAFsVLAHEVSIIGKLMGLKTVFTDHSLF-------GFADMSAVLTNKYLQMCLCeCDHC 162
Cdd:cd03814    74 --RRVRRLIKEFQPDIIHIATPG-PLGLAALRAARRLGLPVVTSYHTDFpeylsyyTLGPLSWLAWAYLRWFHNP-FDTT 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 163 ICVSHTgkentvLRAKVKAH---KVSVIPNAVDAYTFtpDPSQRD---------PNVITVIIVSRLVYRKGVDLMAAVIA 230
Cdd:cd03814   150 LVPSPS------IARELEGHgfeRVRLWPRGVDTELF--HPSRRDaalrrrlgpPGRPLLLYVGRLAPEKNLEALLDADL 221
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1949865553 231 DMCPRYPnLRFIIGGDGPkmwllqevrERKGFQH---CVTLLGSLK 273
Cdd:cd03814   222 PLAASPP-VRLVVVGDGP---------ARAELEArgpDVIFTGFLT 257
GT5_Glycogen_synthase_DULL1-like cd03791
Glycogen synthase GlgA and similar proteins; This family is most closely related to the GT5 ...
27-249 1.77e-07

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: 51.80  E-value: 1.77e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  27 TGGVEEHIYNLSQCLIKRGHKVVVITHCYED-----------------------RVGVRYLT-GGLKVYYL--------- 73
Cdd:cd03791    15 TGGLGDVAGALPKALAKLGHDVRVILPRYGQipdeldgylrvlglevkvggrgeEVGVFELPvDGVDYYFLdnpeffdrp 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  74 -------------PIR-VFYSQCALpTMICNIAIvryilireRIQIVHGH---SAF-SVLAHEVSIIGKLMGLKTVFTDH 135
Cdd:cd03791    95 glpgppgydypdnAERfAFFSRAAL-ELLRRLGF--------QPDIIHANdwhTALvPAYLKTRYRGPGFKKIKTVFTIH 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 136 SL-----FGFADMSAVLTN----------KYLQMC-----LCECDHCICVSHT-GKE----------NTVLRAKvkAHKV 184
Cdd:cd03791   166 NLayqglFPLDTLAELGLPpelfhidgleFYGQINflkagIVYADRVTTVSPTyAKEiltpeygeglDGVLRAR--AGKL 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 185 SVIPNAVD------------AYTFTP-DPSQR---------------DPNVITVIIVSRLVYRKGVDLMAAVIADMCPRy 236
Cdd:cd03791   244 SGILNGIDydewnpatdkliPANYSAnDLEGKaenkaalqkelglpvDPDAPLFGFVGRLTEQKGVDLILDALPELLEE- 322
                         330
                  ....*....|...
gi 1949865553 237 pNLRFIIGGDGPK 249
Cdd:cd03791   323 -GGQLVVLGSGDP 334
GlgA COG0297
Glycogen synthase [Carbohydrate transport and metabolism];
27-247 5.19e-07

Glycogen synthase [Carbohydrate transport and metabolism];


Pssm-ID: 440066 [Multi-domain]  Cd Length: 476  Bit Score: 50.48  E-value: 5.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  27 TGGVEEHIYNLSQCLIKRGHKVVVITHCY-----------------------EDRVGVRYLTG-GLKVYYL--------- 73
Cdd:COG0297    16 TGGLADVVGALPKALAKLGHDVRVVLPGYpsiddklkdlevvaslevplggrTYYARVLEGPDdGVPVYFIdnpelfdrp 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  74 -------------PIR-VFYSQCALpTMICNIAIvryilireRIQIVHGH---SAF-SVLAHEVSIIGKLMGLKTVFTDH 135
Cdd:COG0297    96 gpygdpdrdypdnAERfAFFSRAAL-ELLKGLDW--------KPDIIHCHdwqTGLiPALLKTRYADDPFKRIKTVFTIH 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 136 SL-----FGFADMSAV-LTNKYLQMCLCECDHCIC--------------VSHT------------GKENtVLRAKvkAHK 183
Cdd:COG0297   167 NLayqgiFPAEILELLgLPPELFTPDGLEFYGQINflkagivyadrvttVSPTyareiqtpefgeGLDG-LLRAR--SGK 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 184 VSVIPNAVDAYTFTP--DPS--------------------QR------DPNVITVIIVSRLVYRKGVDLMAAVIADMCPR 235
Cdd:COG0297   244 LSGILNGIDYDVWNPatDPYlpanysaddlegkaankaalQEelglpvDPDAPLIGMVSRLTEQKGLDLLLEALDELLEE 323
                         330
                  ....*....|..
gi 1949865553 236 ypNLRFIIGGDG 247
Cdd:COG0297   324 --DVQLVVLGSG 333
GT4_AviGT4-like cd03802
UDP-Glc:tetrahydrobiopterin alpha-glucosyltransferase and similar proteins; This family is ...
28-281 2.71e-06

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: 48.05  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  28 GGVEEHIYNLSQCLIKRGHKVVVITHcyEDRVGVRYLtggLKVYYLPIRVfySQCALPTMICNI-AIVRYILIRERIQIV 106
Cdd:cd03802    18 GGTELVVSALTEGLVRRGHEVTLFAP--GDSHTSAPL---VAVIPRALRL--DPIPQESKLAELlEALEVQLRASDFDVI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 107 HGHSAFSVLAHevsiiGKLMGLKTVFTDHSlFGFADMSAVLTNKYLQmclcecdHCICVSHTGKENTVLrakvkAHKVSV 186
Cdd:cd03802    91 HNHSYDWLPPF-----APLIGTPFVTTLHG-PSIPPSLAIYAAEPPV-------NYVSISDAQRAATPP-----IDYLTV 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 187 IPNAVDAYTFTPDPSQRDPnvitVIIVSRLVYRKGVDLmAAVIADMCprypNLR-FIIGGDGPKMW--LLQEVRERKGfq 263
Cdd:cd03802   153 VHNGLDPADYRFQPDPEDY----LAFLGRIAPEKGLED-AIRVARRA----GLPlKIAGKVRDEDYfyYLQEPLPGPR-- 221
                         250
                  ....*....|....*...
gi 1949865553 264 hcVTLLGSLKHSEVRDVL 281
Cdd:cd03802   222 --IEFIGEVGHDEKQELL 237
Glycos_transf_1 pfam00534
Glycosyl transferases group 1; Mutations in this domain of Swiss:P37287 lead to disease ...
204-281 4.43e-06

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: 45.73  E-value: 4.43e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1949865553 204 DPNVItvIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQEVRERKGFQHCVTLLGSLKHSEVRDVL 281
Cdd:pfam00534   1 KKKII--LFVGRLEPEKGLDLLIKAFALLKEKNPNLKLVIAGDGEEEKRLKKLAEKLGLGDNVIFLGFVSDEDLPELL 76
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
209-281 2.93e-05

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 42.88  E-value: 2.93e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1949865553 209 TVIIVSRLV-YRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQEVRerkGFQHCVTLLGSLKhsEVRDVL 281
Cdd:pfam13692   3 VILFVGRLHpNVKGVDYLLEAVPLLRKRDNDVRLVIVGDGPEEELEELAA---GLEDRVIFTGFVE--DLAELL 71
GT4_AmsK-like cd03799
Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases ...
181-281 5.95e-05

Erwinia amylovora AmsK and similar proteins; This is a family of GT4 glycosyltransferases found specifically in certain bacteria. AmsK in Erwinia amylovora, has been reported to be involved in the biosynthesis of amylovoran, a exopolysaccharide acting as a virulence factor.


Pssm-ID: 340829 [Multi-domain]  Cd Length: 350  Bit Score: 43.98  E-value: 5.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 181 AHKVSVIPNAVDAYTFTPDPSQRDPN-VITVIIVSRLVYRKGVDLMAAVIADMCPRYPNLRFIIGGDGPKMWLLQEVRER 259
Cdd:cd03799   147 EKKIIVHRSGIDCNKFRFKPRYLPLDgKIRILTVGRLTEKKGLEYAIEAVAKLAQKYPNIEYQIIGDGDLKEQLQQLIQE 226
                          90       100
                  ....*....|....*....|..
gi 1949865553 260 KGFQHCVTLLGSLKHSEVRDVL 281
Cdd:cd03799   227 LNIGDCVKLLGWKPQEEIIEIL 248
GT4_WbdM_like cd04951
LPS/UnPP-GlcNAc-Gal a-1,4-glucosyltransferase WbdM and similar proteins; This family is most ...
28-279 2.80e-03

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: 38.58  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553  28 GGVEEHIYNLSQCLIKRGHKVVVIthCYEDRVGVRYLTGGLKVYYLPI-RVFYSqcalptMICNIAIVRYILIRERIQIV 106
Cdd:cd04951    12 GGAEKQTVLLADQMFIRGHDVNIV--YLTGEVEVKPLNNNIIIYNLGMdKNPRS------LLKALLKLKKIISAFKPDVV 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 107 HGH----SAFSVLAHEVSIIGKLmglktVFTDHS--LFGFADMSAVLTNKYLqmclceCDHCICVSHTGKENTVLRAKVK 180
Cdd:cd04951    84 HSHmfhaNIFARFLRMLYPIPLL-----ICTAHNknEGGRIRMFIYRLTDFL------CDITTNVSREALDEFIAKKAFS 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1949865553 181 AHKVSVIPNAVDAYTFTPDPSQRDP---------NVITVIIVSRLVYRKG-VDLMAAvIADMCPRYPNLRFIIGGDGPKM 250
Cdd:cd04951   153 KNKSVPVYNGIDLNKFKKDINVRLKirnklnlknDEFVILNVGRLTEAKDyPNLLLA-ISELILSKNDFKLLIAGDGPLR 231
                         250       260
                  ....*....|....*....|....*....
gi 1949865553 251 WLLQEVRERKGFQHCVTLLGSlkHSEVRD 279
Cdd:cd04951   232 NELERLICNLNLVDRVILLGQ--ISNISE 258
 
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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