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Conserved domains on  [gi|1757988590|dbj|BBN80394|]
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hypothetical protein PA25_03790 [Pseudoalteromonas sp. A25]

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 ...
 108-288 2.32e-15

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 cd03794:

Pssm-ID: 471961 [Multi-domain]  Cd Length: 391  Bit Score: 76.61  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 108 EINTDTDMEISLEKSRSIKGFATYIYNALTKAFyqrrlAGAVSVTKEL-----SGSVSTQQVAVIPNSIAVEGFNYRKSV 182
Cdd:cd03794   132 DLWPESLIALGVLKKGSLLKLLKKLERKLYRLA-----DAIIVLSPGLkeyllRKGVPKEKIIVIPNWADLEEFKPPPKD 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 183 D-----KLDSKLSVLFVGTPGLmWHGIDILNQLARETKGR--LEFHVVG-------MEQSVLSEPSENIHFYGYLPVEQY 248
Cdd:cd03794   207 ElrkklGLDDKFVVVYAGNIGK-AQGLETLLEAAERLKRRpdIRFLFVGdgdekerLKELAKARGLDNVTFLGRVPKEEV 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1757988590 249 AAIAQSCSVGLGTLAlHRKGMKEACPLKVREYLAAGLPVI 288
Cdd:cd03794   286 PELLSAADVGLVPLK-DNPANRGSSPSKLFEYMAAGKPIL 324
 
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 ...
 108-288 2.32e-15

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: 76.61  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 108 EINTDTDMEISLEKSRSIKGFATYIYNALTKAFyqrrlAGAVSVTKEL-----SGSVSTQQVAVIPNSIAVEGFNYRKSV 182
Cdd:cd03794   132 DLWPESLIALGVLKKGSLLKLLKKLERKLYRLA-----DAIIVLSPGLkeyllRKGVPKEKIIVIPNWADLEEFKPPPKD 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 183 D-----KLDSKLSVLFVGTPGLmWHGIDILNQLARETKGR--LEFHVVG-------MEQSVLSEPSENIHFYGYLPVEQY 248
Cdd:cd03794   207 ElrkklGLDDKFVVVYAGNIGK-AQGLETLLEAAERLKRRpdIRFLFVGdgdekerLKELAKARGLDNVTFLGRVPKEEV 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1757988590 249 AAIAQSCSVGLGTLAlHRKGMKEACPLKVREYLAAGLPVI 288
Cdd:cd03794   286 PELLSAADVGLVPLK-DNPANRGSSPSKLFEYMAAGKPIL 324
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
191-288 1.89e-05

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 44.04  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 191 VLFVGTPGLMWHGIDILNQ---LARETKGRLEFHVVGME-----QSVLSEPSENIHFYGYlpVEQYAAIAQSCSVGLgtL 262
Cdd:pfam13692   4 ILFVGRLHPNVKGVDYLLEavpLLRKRDNDVRLVIVGDGpeeelEELAAGLEDRVIFTGF--VEDLAELLAAADVFV--L 79

                          90       100
                  ....*....|....*....|....*.
gi 1757988590 263 ALHRKGMkeacPLKVREYLAAGLPVI 288
Cdd:pfam13692  80 PSLYEGF----GLKLLEAMAAGLPVV 101
 
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 ...
 108-288 2.32e-15

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: 76.61  E-value: 2.32e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 108 EINTDTDMEISLEKSRSIKGFATYIYNALTKAFyqrrlAGAVSVTKEL-----SGSVSTQQVAVIPNSIAVEGFNYRKSV 182
Cdd:cd03794   132 DLWPESLIALGVLKKGSLLKLLKKLERKLYRLA-----DAIIVLSPGLkeyllRKGVPKEKIIVIPNWADLEEFKPPPKD 206

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 183 D-----KLDSKLSVLFVGTPGLmWHGIDILNQLARETKGR--LEFHVVG-------MEQSVLSEPSENIHFYGYLPVEQY 248
Cdd:cd03794   207 ElrkklGLDDKFVVVYAGNIGK-AQGLETLLEAAERLKRRpdIRFLFVGdgdekerLKELAKARGLDNVTFLGRVPKEEV 285

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1757988590 249 AAIAQSCSVGLGTLAlHRKGMKEACPLKVREYLAAGLPVI 288
Cdd:cd03794   286 PELLSAADVGLVPLK-DNPANRGSSPSKLFEYMAAGKPIL 324
GT4_PimA-like cd03801
phosphatidyl-myo-inositol mannosyltransferase; This family is most closely related to the GT4 ...
 54-288 2.07e-11

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: 64.48  E-value: 2.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590  54 HPHVEVIAPDSTIKLIRKLKHAVDCFNPDIVY-HRMWVLSPLLVPLLLSDYKMLAEINTDTDMEISLeksrsikgFATYI 132
Cdd:cd03801    56 PLLPSLAALLRARRLLRELRPLLRLRKFDVVHaHGLLAALLAALLALLLGAPLVVTLHGAEPGRLLL--------LLAAE 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 133 YNALTKAFYQRRLAGA-VSVTKELS------GSVSTQQVAVIPNSIAVEGFN--YRKSVDKLDSKLSVLFVGTpglMW-- 201
Cdd:cd03801   128 RRLLARAEALLRRADAvIAVSEALRdelralGGIPPEKIVVIPNGVDLERFSppLRRKLGIPPDRPVLLFVGR---LSpr 204

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 202 ----HGIDILNQLARETKgRLEFHVVGME-------QSVLSEPSENIHFYGYLPVEQYAAIAQSCSVGLgtLALHRkgmk 270
Cdd:cd03801   205 kgvdLLLEALAKLLRRGP-DVRLVIVGGDgplraelEELELGLGDRVRFLGFVPDEELPALYAAADVFV--LPSRY---- 277

                         250
                  ....*....|....*...
gi 1757988590 271 EACPLKVREYLAAGLPVI 288
Cdd:cd03801   278 EGFGLVVLEAMAAGLPVV 295
Glyco_trans_1_4 pfam13692
Glycosyl transferases group 1;
191-288 1.89e-05

Glycosyl transferases group 1;


Pssm-ID: 463957 [Multi-domain]  Cd Length: 138  Bit Score: 44.04  E-value: 1.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 191 VLFVGTPGLMWHGIDILNQ---LARETKGRLEFHVVGME-----QSVLSEPSENIHFYGYlpVEQYAAIAQSCSVGLgtL 262
Cdd:pfam13692   4 ILFVGRLHPNVKGVDYLLEavpLLRKRDNDVRLVIVGDGpeeelEELAAGLEDRVIFTGF--VEDLAELLAAADVFV--L 79

                          90       100
                  ....*....|....*....|....*.
gi 1757988590 263 ALHRKGMkeacPLKVREYLAAGLPVI 288
Cdd:pfam13692  80 PSLYEGF----GLKLLEAMAAGLPVV 101
GT4_CapM-like cd03808
capsular polysaccharide biosynthesis glycosyltransferase CapM and similar proteins; This ...
 157-288 6.20e-04

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: 41.43  E-value: 6.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 157 GSVSTQQVAVIPNS-IAVEGFNYRKSVDKLDsKLSVLFVGTpgLMWH-GIDILNQLARETKGR---LEFHVVG------- 224
Cdd:cd03808   158 GIIKKKKTVLIPGSgVDLDRFQYSPESLPSE-KVVFLFVAR--LLKDkGIDELIEAAKILKKKgpnVRFLLVGdgelenp 234

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1757988590 225 MEQSVLSEPSE-NIHFYGYlpVEQYAAIAQSCSVGLgtLALHRKGMkeacPLKVREYLAAGLPVI 288
Cdd:cd03808   235 SEILIEKLGLEgRIEFLGF--RSDVPELLAESDVFV--LPSYREGL----PRSLLEAMAAGRPVI 291
GT4_TuaH-like cd04950
teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this ...
 144-288 2.54e-03

teichuronic acid biosynthesis glycosyltransferase TuaH and similar proteins; Members of this family may function in teichuronic acid biosynthesis/cell wall biogenesis. 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.


Pssm-ID: 340856 [Multi-domain]  Cd Length: 373  Bit Score: 39.66  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 144 RLAGAVSVT-KELSGSVSTQQVAV--IPNSIAVEGFN-----YRKSVDKLDSKLSVL-FVGtpglmwhGID------ILN 208
Cdd:cd04950   152 KRADVVFTTsPALYEAKRPLHENVhpIPNGVDVEHFAaarqpLDDPIDLREIPGPVLgFFG-------AIDekldfdLIE 224

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1757988590 209 QLARETKGrLEFHVVGME-----QSVLSEPseNIHFYGYLPVEQYAAIAQSCSVGLGTLAL--HRKGMKeacPLKVREYL 281
Cdd:cd04950   225 ELAKARPQ-WNFVFIGPVvkidpSSLPRAP--NIHWLGPKPYKELPAYLAGFDVALLPFALneYTRFIS---PLKLFEYL 298


                  ....*..
gi 1757988590 282 AAGLPVI 288
Cdd:cd04950   299 AAGKPVV 305
 
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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