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Conserved domains on  [gi|505960957|ref|WP_015728939|]
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glycosyltransferase family 4 protein [Staphylococcus pseudintermedius]

Protein Classification

glycosyltransferase family 4 protein( domain architecture ID 10133406)

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
5-317 1.12e-43

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: 156.35  E-value: 1.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957   5 KLLIITQNFYPELGSAANRMKMLFKHFTKESVMTYVLTTQPSYPNhelfqddSYFDDDVINRYENNRIIRMKmLCEKQNK 84
Cdd:cd03794    1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPL-------GRIFAGATETKDGIRVIRVK-LGPIKKN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  85 NLIARLFYYIEQYLRVRYFIFKHKNDFDYIYVTSPNIFIAWATLFMKKAKRPDYILEVRDLWPDSVNSIKGINLKLTWPL 164
Cdd:cd03794   73 GLIRRLLNYLSFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 165 LKRLEKIMYNRADKIVINNKGFREHIQQMLDKAVPIEFIPNSVSqEERFTEEKYED----------FRVIYTGNIGYAQD 234
Cdd:cd03794  153 LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWAD-LEEFKPPPKDElrkklglddkFVVVYAGNIGKAQG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 235 VDHLIELFSLLNDYKiNVTAIVYGVKAPKfrEAVQHLEF------VTLKHAMSRERCLQEISRHHVALSILNENDTFLNV 308
Cdd:cd03794  232 LETLLEAAERLKRRP-DIRFLFVGDGDEK--ERLKELAKargldnVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGS 308

                 ....*....
gi 505960957 309 LPGKIVDAI 317
Cdd:cd03794  309 SPSKLFEYM 317
 
Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
5-317 1.12e-43

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: 156.35  E-value: 1.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957   5 KLLIITQNFYPELGSAANRMKMLFKHFTKESVMTYVLTTQPSYPNhelfqddSYFDDDVINRYENNRIIRMKmLCEKQNK 84
Cdd:cd03794    1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPL-------GRIFAGATETKDGIRVIRVK-LGPIKKN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  85 NLIARLFYYIEQYLRVRYFIFKHKNDFDYIYVTSPNIFIAWATLFMKKAKRPDYILEVRDLWPDSVNSIKGINLKLTWPL 164
Cdd:cd03794   73 GLIRRLLNYLSFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 165 LKRLEKIMYNRADKIVINNKGFREHIQQMLDKAVPIEFIPNSVSqEERFTEEKYED----------FRVIYTGNIGYAQD 234
Cdd:cd03794  153 LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWAD-LEEFKPPPKDElrkklglddkFVVVYAGNIGKAQG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 235 VDHLIELFSLLNDYKiNVTAIVYGVKAPKfrEAVQHLEF------VTLKHAMSRERCLQEISRHHVALSILNENDTFLNV 308
Cdd:cd03794  232 LETLLEAAERLKRRP-DIRFLFVGDGDEK--ERLKELAKargldnVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGS 308

                 ....*....
gi 505960957 309 LPGKIVDAI 317
Cdd:cd03794  309 SPSKLFEYM 317
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
110-205 4.66e-05

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 43.16  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  110 DFDYIYVTSPniFIAWATLFMKKAKRPDYILEVRDLWPDSVNSIKGinlkltwPLLKRLEKIMYNRADKIVINNKGFREH 189
Cdd:pfam13579  71 RPDVVHAHSP--TAGLAARLARRRRGVPLVVTVHGLALDYGSGWKR-------RLARALERRLLRRADAVVVVSEAEAEL 141
                          90
                  ....*....|....*.
gi 505960957  190 IQQMLDKAVPIEFIPN 205
Cdd:pfam13579 142 LRALGVPAARVVVVPN 157
 
Name Accession Description Interval E-value
GT4_WbuB-like cd03794
Escherichia coli WbuB and similar proteins; This family is most closely related to the GT1 ...
5-317 1.12e-43

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: 156.35  E-value: 1.12e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957   5 KLLIITQNFYPELGSAANRMKMLFKHFTKESVMTYVLTTQPSYPNhelfqddSYFDDDVINRYENNRIIRMKmLCEKQNK 84
Cdd:cd03794    1 KILLISQYYPPPKGAAAARVYELAKELVRRGHEVTVLTPSPNYPL-------GRIFAGATETKDGIRVIRVK-LGPIKKN 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  85 NLIARLFYYIEQYLRVRYFIFKHKNDFDYIYVTSPNIFIAWATLFMKKAKRPDYILEVRDLWPDSVNSIKGINLKLTWPL 164
Cdd:cd03794   73 GLIRRLLNYLSFALAALLKLLVREERPDVIIAYSPPITLGLAALLLKKLRGAPFILDVRDLWPESLIALGVLKKGSLLKL 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 165 LKRLEKIMYNRADKIVINNKGFREHIQQMLDKAVPIEFIPNSVSqEERFTEEKYED----------FRVIYTGNIGYAQD 234
Cdd:cd03794  153 LKKLERKLYRLADAIIVLSPGLKEYLLRKGVPKEKIIVIPNWAD-LEEFKPPPKDElrkklglddkFVVVYAGNIGKAQG 231
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 235 VDHLIELFSLLNDYKiNVTAIVYGVKAPKfrEAVQHLEF------VTLKHAMSRERCLQEISRHHVALSILNENDTFLNV 308
Cdd:cd03794  232 LETLLEAAERLKRRP-DIRFLFVGDGDEK--ERLKELAKargldnVTFLGRVPKEEVPELLSAADVGLVPLKDNPANRGS 308

                 ....*....
gi 505960957 309 LPGKIVDAI 317
Cdd:cd03794  309 SPSKLFEYM 317
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
5-395 2.02e-09

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: 58.70  E-value: 2.02e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957   5 KLLIITQNFYPELGSAANRMKMLFKHFTKE--SVMTYVLTTQPSYPNHELFQDDSYFDDDVINRYENNRIIRmkmlcekq 82
Cdd:cd03801    1 KILLLSPELPPPVGGAERHVRELARALAARghDVTVLTPADPGEPPEELEDGVIVPLLPSLAALLRARRLLR-------- 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  83 nknliarlfyyieqylRVRYFIFKHknDFDYIYVTspNIFIAWATLFMKKAKRPDYILEVRDLWPDSvnsikgiNLKLTW 162
Cdd:cd03801   73 ----------------ELRPLLRLR--KFDVVHAH--GLLAALLAALLALLLGAPLVVTLHGAEPGR-------LLLLLA 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 163 PLLKRLEKI--MYNRADKIVINNKGFREHIQQML-DKAVPIEFIPNSVSQEERFTEEKYE------DFRVIYTGNIGYAQ 233
Cdd:cd03801  126 AERRLLARAeaLLRRADAVIAVSEALRDELRALGgIPPEKIVVIPNGVDLERFSPPLRRKlgippdRPVLLFVGRLSPRK 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 234 DVDHLIELFSLLNDYKINVTAIVYGVKAPKFREAVQHlefvtLKHAMSRERCLQEISRHHVAlSILNENDTFLNV----- 308
Cdd:cd03801  206 GVDLLLEALAKLLRRGPDVRLVIVGGDGPLRAELEEL-----ELGLGDRVRFLGFVPDEELP-ALYAAADVFVLPsryeg 279
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 309 LPGKIVDAI--GvntLPV--TNIGGKM---AEDINAFRIGFAEKKAtpqiLLEKIIAYRDNPSHFESQLVNVRRYRNQFL 381
Cdd:cd03801  280 FGLVVLEAMaaG---LPVvaTDVGGLPevvEDGEGGLVVPPDDVEA----LADALLRLLADPELRARLGRAARERVAERF 352
                        410
                 ....*....|....
gi 505960957 382 NWETNIKALIRFLK 395
Cdd:cd03801  353 SWERVAERLLDLYR 366
GT4_AmsD-like cd03820
amylovoran biosynthesis glycosyltransferase AmsD and similar proteins; This family is most ...
81-245 1.03e-05

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: 47.23  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  81 KQNKNLIARLFYYIEQYLRVRYFIFKHKNDFDYIYVTSPNIFIAWATLFMKkakrpdYILEVRdlwpdsvNSIKGINLKL 160
Cdd:cd03820   60 DRKYSHFKLLLKYFKKVRRLRKYLKNNKPDVVISFRTSLLTFLALIGLKSK------LIVWEH-------NNYEAYNKGL 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 161 TWPLLKRLekiMYNRADKIVINNKGFREHIQQMLDKavPIEFIPNSVSQEERFTEEKYEDFRVIYTGNIGYAQDVDHLIE 240
Cdd:cd03820  127 RRLLLRRL---LYKRADKIVVLTEADKLKKYKQPNS--NVVVIPNPLSFPSEEPSTNLKSKRILAVGRLTYQKGFDLLIE 201

                 ....*
gi 505960957 241 LFSLL 245
Cdd:cd03820  202 AWALI 206
Glyco_trans_4_4 pfam13579
Glycosyl transferase 4-like domain;
110-205 4.66e-05

Glycosyl transferase 4-like domain;


Pssm-ID: 433325 [Multi-domain]  Cd Length: 158  Bit Score: 43.16  E-value: 4.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957  110 DFDYIYVTSPniFIAWATLFMKKAKRPDYILEVRDLWPDSVNSIKGinlkltwPLLKRLEKIMYNRADKIVINNKGFREH 189
Cdd:pfam13579  71 RPDVVHAHSP--TAGLAARLARRRRGVPLVVTVHGLALDYGSGWKR-------RLARALERRLLRRADAVVVVSEAEAEL 141
                          90
                  ....*....|....*.
gi 505960957  190 IQQMLDKAVPIEFIPN 205
Cdd:pfam13579 142 LRALGVPAARVVVVPN 157
Glyco_transf_4 pfam13439
Glycosyltransferase Family 4;
86-207 5.19e-04

Glycosyltransferase Family 4;


Pssm-ID: 463877 [Multi-domain]  Cd Length: 169  Bit Score: 40.59  E-value: 5.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957   86 LIARLFYYIEQYLRVRYFIFKHKndFDYIYVTSPNIFIAWATLFMKKAKRPdYILEVRDLWPDsvNSIKGINLKLTWPLL 165
Cdd:pfam13439  49 LPPRLLRSLAFLRRLRRLLRRER--PDVVHAHSPFPLGLAALAARLRLGIP-LVVTYHGLFPD--YKRLGARLSPLRRLL 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 505960957  166 KRLEKIMYNRADKIVINNKGFREHIQQMLD-KAVPIEFIPNSV 207
Cdd:pfam13439 124 RRLERRLLRRADRVIAVSEAVADELRRLYGvPPEKIRVIPNGV 166
GT4_UGDG-like cd03817
UDP-Glc:1,2-diacylglycerol 3-a-glucosyltransferase and similar proteins; This family is most ...
163-258 1.68e-03

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: 40.34  E-value: 1.68e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 505960957 163 PLLKRLEKIMYNRADKIVINNKGFREHIQQMLDKaVPIEFIPNSV-------SQEERFTEEKY---EDFRVIYTGNIGYA 232
Cdd:cd03817  135 AVVRKLVRRFYNHTDAVIAPSEKIKDTLREYGVK-GPIEVIPNGIdldkfekPLNTEERRKLGlppDEPILLYVGRLAKE 213
                         90       100
                 ....*....|....*....|....*.
gi 505960957 233 QDVDHLIELFSLLNdYKINVTAIVYG 258
Cdd:cd03817  214 KNIDFLLRAFAELK-KEPNIKLVIVG 238
 
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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