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Conserved domains on  [gi|2261231199|emb|CAH2572223|]
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hypothetical protein PRNO82_01625 [Planktothrix rubescens]

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 ...
 172-412 3.13e-18

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


The actual alignment was detected with superfamily member COG0763:

Pssm-ID: 471961  Cd Length: 378  Bit Score: 85.50  E-value: 3.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 172 SEDIIIGLLPGSKASKLTQGMALALAISEYLHQKRPEIRLVIPVAPTLDLQTLAKF-ADAESNPIIaqfggISGKlnlgn 250
Cdd:COG0763   183 PDKPVIALLPGSRRSEIKRLLPVFLEAAKLLAARRPDLQFVVPLAPSLRRELIEAAlADWPLPVTL-----VDGQ----- 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 251 pAYletqngvkielytqfpacDLLSKCQICLTTVGANTAQLGALAVPMIVllptqqldAMRswdgipgilanlpgFGAIF 330
Cdd:COG0763   253 -TY------------------DAMAAADAALVASGTATLEAALLGVPMVV--------AYK--------------VSPLT 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 331 AKIINRLVlKQgKLFAWPNIWAKQEIVPELVGE-LKAEDIGNLVLNYLDHPEKLEAMRQRLRQVR---GNPGATQKLANI 406
Cdd:COG0763   292 YWIAKRLV-KV-PYISLPNLLAGREVVPELLQDdATPENLAAALLRLLDDPAARAAQLAAFAELRqllGEGGASERAAEA 369


                  ....*.
gi 2261231199 407 VIELLS 412
Cdd:COG0763   370 ILELLE 375
 
Name Accession Description Interval E-value
LpxB COG0763
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
 172-412 3.13e-18

Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440526  Cd Length: 378  Bit Score: 85.50  E-value: 3.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 172 SEDIIIGLLPGSKASKLTQGMALALAISEYLHQKRPEIRLVIPVAPTLDLQTLAKF-ADAESNPIIaqfggISGKlnlgn 250
Cdd:COG0763   183 PDKPVIALLPGSRRSEIKRLLPVFLEAAKLLAARRPDLQFVVPLAPSLRRELIEAAlADWPLPVTL-----VDGQ----- 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 251 pAYletqngvkielytqfpacDLLSKCQICLTTVGANTAQLGALAVPMIVllptqqldAMRswdgipgilanlpgFGAIF 330
Cdd:COG0763   253 -TY------------------DAMAAADAALVASGTATLEAALLGVPMVV--------AYK--------------VSPLT 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 331 AKIINRLVlKQgKLFAWPNIWAKQEIVPELVGE-LKAEDIGNLVLNYLDHPEKLEAMRQRLRQVR---GNPGATQKLANI 406
Cdd:COG0763   292 YWIAKRLV-KV-PYISLPNLLAGREVVPELLQDdATPENLAAALLRLLDDPAARAAQLAAFAELRqllGEGGASERAAEA 369


                  ....*.
gi 2261231199 407 VIELLS 412
Cdd:COG0763   370 ILELLE 375
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 355-411 2.04e-04

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 43.20  E-value: 2.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2261231199 355 EIVPElvGELKAEDIGNLVLNYLDHPEKLEAMRQRLRQVrGNPGATQKLANIVIELL 411
Cdd:PRK00726  302 LLIPQ--SDLTPEKLAEKLLELLSDPERLEAMAEAARAL-GKPDAAERLADLIEELA 355
 
Name Accession Description Interval E-value
LpxB COG0763
Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide ...
 172-412 3.13e-18

Lipid A disaccharide synthetase [Cell wall/membrane/envelope biogenesis]; Lipid A disaccharide synthetase is part of the Pathway/BioSystem: Lipid A biosynthesis


Pssm-ID: 440526  Cd Length: 378  Bit Score: 85.50  E-value: 3.13e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 172 SEDIIIGLLPGSKASKLTQGMALALAISEYLHQKRPEIRLVIPVAPTLDLQTLAKF-ADAESNPIIaqfggISGKlnlgn 250
Cdd:COG0763   183 PDKPVIALLPGSRRSEIKRLLPVFLEAAKLLAARRPDLQFVVPLAPSLRRELIEAAlADWPLPVTL-----VDGQ----- 252

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 251 pAYletqngvkielytqfpacDLLSKCQICLTTVGANTAQLGALAVPMIVllptqqldAMRswdgipgilanlpgFGAIF 330
Cdd:COG0763   253 -TY------------------DAMAAADAALVASGTATLEAALLGVPMVV--------AYK--------------VSPLT 291

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2261231199 331 AKIINRLVlKQgKLFAWPNIWAKQEIVPELVGE-LKAEDIGNLVLNYLDHPEKLEAMRQRLRQVR---GNPGATQKLANI 406
Cdd:COG0763   292 YWIAKRLV-KV-PYISLPNLLAGREVVPELLQDdATPENLAAALLRLLDDPAARAAQLAAFAELRqllGEGGASERAAEA 369


                  ....*.
gi 2261231199 407 VIELLS 412
Cdd:COG0763   370 ILELLE 375
MurG COG0707
UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope ...
 363-412 7.16e-05

UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase [Cell wall/membrane/envelope biogenesis]; UDP-N-acetylglucosamine:LPS N-acetylglucosamine transferase is part of the Pathway/BioSystem: Mureine biosynthesis


Pssm-ID: 440471 [Multi-domain]  Cd Length: 363  Bit Score: 44.73  E-value: 7.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2261231199 363 ELKAEDIGNLVLNYLDHPEKLEAMRQRLRQVrGNPGATQKLANIVIELLS 412
Cdd:COG0707   314 ELTPEKLAEALEELLEDPERLAKMAEAARAL-ARPDAAERIADLILELAK 362
murG PRK00726
undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional
 355-411 2.04e-04

undecaprenyldiphospho-muramoylpentapeptide beta-N- acetylglucosaminyltransferase; Provisional


Pssm-ID: 234825 [Multi-domain]  Cd Length: 357  Bit Score: 43.20  E-value: 2.04e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2261231199 355 EIVPElvGELKAEDIGNLVLNYLDHPEKLEAMRQRLRQVrGNPGATQKLANIVIELL 411
Cdd:PRK00726  302 LLIPQ--SDLTPEKLAEKLLELLSDPERLEAMAEAARAL-GKPDAAERLADLIEELA 355
 
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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