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Conserved domains on  [gi|578831258|ref|XP_006722081|]
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cytosolic endo-beta-N-acetylglucosaminidase isoform X4 [Homo sapiens]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 248)

glycoside hydrolase family 18 protein such as chitinase, which catalyzes the random endo-hydrolysis of the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH18_chitinase-like super family cl10447
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 44-150 2.96e-33

The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.


The actual alignment was detected with superfamily member cd06547:

Pssm-ID: 471972  Cd Length: 339  Bit Score: 128.18  E-value: 2.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831258  44 TGVMPSSLQSLELIRKHGFSVALFAPGWVYECLEKKDFFQ---------------NQDKFWGRLERYLPTHSIC-SLPFV 107
Cdd:cd06547  217 GGGGWNSDKALDEIKKAGLSVALFAPGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFV 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578831258 108 TSFCLGMGARRVCYGQEEAVGPWYHLSAQEIQPLFGEHRLGGD 150
Cdd:cd06547  297 TNFNTGSGYAFYVNGKKVSDSPWNNLSLQDILPTYRWIVSSNG 339
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
 44-150 2.96e-33

Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.


Pssm-ID: 119364  Cd Length: 339  Bit Score: 128.18  E-value: 2.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831258  44 TGVMPSSLQSLELIRKHGFSVALFAPGWVYECLEKKDFFQ---------------NQDKFWGRLERYLPTHSIC-SLPFV 107
Cdd:cd06547  217 GGGGWNSDKALDEIKKAGLSVALFAPGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFV 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578831258 108 TSFCLGMGARRVCYGQEEAVGPWYHLSAQEIQPLFGEHRLGGD 150
Cdd:cd06547  297 TNFNTGSGYAFYVNGKKVSDSPWNNLSLQDILPTYRWIVSSNG 339
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
 52-115 2.11e-18

Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.


Pssm-ID: 461002  Cd Length: 292  Bit Score: 85.03  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831258   52 QSLELIRKHGFSVALFAPGWVYECLEK---KDFFQNQDKFW----------------GRLERYLPTHS-ICSLPFVTSFC 111
Cdd:pfam03644 209 VALDLIAKAGLSAALFAPGWTYETFQSgstPDFLERERRFWvgpkgdpdpdssdnswKGIANYVAERSaISSLPFYTNFN 288


                  ....
gi 578831258  112 LGMG 115
Cdd:pfam03644 289 TGSG 292
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
 44-150 2.96e-33

Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins. The beta-1,4-glycosyl bond located between two N-acetylglucosamine residues is hydrolyzed such that N-acetylglucosamine 1 remains with the protein and N-acetylglucosamine 2 forms the reducing end of the released glycan. ENGase is a key enzyme in the processing of free oligosaccharides in the cytosol of eukaryotes. Oligosaccharides formed in the lumen of the endoplasmic reticulum are transported into the cytosol where they are catabolized by cytosolic ENGases and other enzymes, possibly to maximize the reutilization of the component sugars. ENGases have an eight-stranded alpha/beta barrel topology and are classified as a family 85 glycosyl hydrolase (GH85) domain. The GH85 ENGases are sequence-similar to the family 18 glycosyl hydrolases, also known as GH18 chitinases. An ENGase-like protein is also found in bacteria and is included in this alignment model.


Pssm-ID: 119364  Cd Length: 339  Bit Score: 128.18  E-value: 2.96e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831258  44 TGVMPSSLQSLELIRKHGFSVALFAPGWVYECLEKKDFFQ---------------NQDKFWGRLERYLPTHSIC-SLPFV 107
Cdd:cd06547  217 GGGGWNSDKALDEIKKAGLSVALFAPGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFV 296

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 578831258 108 TSFCLGMGARRVCYGQEEAVGPWYHLSAQEIQPLFGEHRLGGD 150
Cdd:cd06547  297 TNFNTGSGYAFYVNGKKVSDSPWNNLSLQDILPTYRWIVSSNG 339
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
 52-115 2.11e-18

Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work on a broad spectrum of substrates.


Pssm-ID: 461002  Cd Length: 292  Bit Score: 85.03  E-value: 2.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 578831258   52 QSLELIRKHGFSVALFAPGWVYECLEK---KDFFQNQDKFW----------------GRLERYLPTHS-ICSLPFVTSFC 111
Cdd:pfam03644 209 VALDLIAKAGLSAALFAPGWTYETFQSgstPDFLERERRFWvgpkgdpdpdssdnswKGIANYVAERSaISSLPFYTNFN 288


                  ....
gi 578831258  112 LGMG 115
Cdd:pfam03644 289 TGSG 292
 
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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