NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1153159111|gb|AQX12625|]
View 

endo-beta-N-acetylglucosaminidase [Elizabethkingia meningoseptica]

Protein Classification

endo-beta-N-acetylglucosaminidase family protein( domain architecture ID 10158430)

endo-beta-N-acetylglucosaminidase family protein is a bacterial chitinase that hydrolyzes the chitin core of various asparagine (N)-linked glycans and glycoproteins; belongs to the glycoside hydrolase 18 (GH18) protein family

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
60-324 1.85e-58

Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.


:

Pssm-ID: 119359  Cd Length: 255  Bit Score: 189.13  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111  60 IKLFSFMEVNDTNPLNNLNfTLKKSGkPLVDMVVLFSANINYDAVNDkvivsnnsnVQHLLTNKAKYLKPLRDKGMKVIL 139
Cdd:cd06542     1 PISFGYFEVWDDKGASLQE-SLLNLP-DSVDMVSLFAANINLDAATA---------VQFLLTNKETYIRPLQAKGTKVLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 140 GILGNHDRSGVA-NLSTERAKQFAQELKKTCELYDLDGVFFDDEYSAYETPPPAgfvTPSNNAAARLAYETKQAMP--DK 216
Cdd:cd06542    70 SILGNHLGAGFAnNLSDAAAKAYAKAIVDTVDKYGLDGVDFDDEYSGYGKNGTS---QPSNEAFVRLIKELRKYMGptDK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 217 LVTVYVYSRTSSFpnpvDGVQAGKFVDYAIHDYGGTWDLSS------NYPGLPKSGM----AMASQEFNLNRYASAQTLK 286
Cdd:cd06542   147 LLTIDGYGQALSN----DGEEVSPYVDYVIYQYYGSSSSSTqrnwntNSPKIPPEKMvyteSFEEENGGNSGSSAEQYAR 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1153159111 287 NLRT-SGYGAHMIFAMDPNRSnfttkqLPAMKLIAKELY 324
Cdd:cd06542   223 WTPAkGGKGGIGTYALDRDYY------RPYDSAVSKALK 255
 
Name Accession Description Interval E-value
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
60-324 1.85e-58

Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.


Pssm-ID: 119359  Cd Length: 255  Bit Score: 189.13  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111  60 IKLFSFMEVNDTNPLNNLNfTLKKSGkPLVDMVVLFSANINYDAVNDkvivsnnsnVQHLLTNKAKYLKPLRDKGMKVIL 139
Cdd:cd06542     1 PISFGYFEVWDDKGASLQE-SLLNLP-DSVDMVSLFAANINLDAATA---------VQFLLTNKETYIRPLQAKGTKVLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 140 GILGNHDRSGVA-NLSTERAKQFAQELKKTCELYDLDGVFFDDEYSAYETPPPAgfvTPSNNAAARLAYETKQAMP--DK 216
Cdd:cd06542    70 SILGNHLGAGFAnNLSDAAAKAYAKAIVDTVDKYGLDGVDFDDEYSGYGKNGTS---QPSNEAFVRLIKELRKYMGptDK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 217 LVTVYVYSRTSSFpnpvDGVQAGKFVDYAIHDYGGTWDLSS------NYPGLPKSGM----AMASQEFNLNRYASAQTLK 286
Cdd:cd06542   147 LLTIDGYGQALSN----DGEEVSPYVDYVIYQYYGSSSSSTqrnwntNSPKIPPEKMvyteSFEEENGGNSGSSAEQYAR 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1153159111 287 NLRT-SGYGAHMIFAMDPNRSnfttkqLPAMKLIAKELY 324
Cdd:cd06542   223 WTPAkGGKGGIGTYALDRDYY------RPYDSAVSKALK 255
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
88-254 1.47e-08

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 55.15  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111  88 LVDMVVLFSANINYDavnDKVIVSNNSNVQHLltNKAKYLKPLRDKGMKVILGILGNHDRSGVANL--STERAKQFAQEL 165
Cdd:pfam00704  22 KLTHIIYAFANIDGS---DGTLFIGDWDLGNF--EQLKKLKKQKNPGVKVLLSIGGWTDSTGFSLMasNPASRKKFADSI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 166 KKTCELYDLDGVFFDDEYSAYETPPPAGFVTpsnnaaarLAYETKQAM------PDKLVTVYVYSRTSSFPNPVDGVQAG 239
Cdd:pfam00704  97 VSFLRKYGFDGIDIDWEYPGGNPEDKENYDL--------LLRELRAALdeakggKKYLLSAAVPASYPDLDKGYDLPKIA 168
                         170
                  ....*....|....*....
gi 1153159111 240 KFVDYaIH----DYGGTWD 254
Cdd:pfam00704 169 KYLDF-INvmtyDFHGSWD 186
 
Name Accession Description Interval E-value
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
60-324 1.85e-58

Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.


Pssm-ID: 119359  Cd Length: 255  Bit Score: 189.13  E-value: 1.85e-58
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111  60 IKLFSFMEVNDTNPLNNLNfTLKKSGkPLVDMVVLFSANINYDAVNDkvivsnnsnVQHLLTNKAKYLKPLRDKGMKVIL 139
Cdd:cd06542     1 PISFGYFEVWDDKGASLQE-SLLNLP-DSVDMVSLFAANINLDAATA---------VQFLLTNKETYIRPLQAKGTKVLL 69
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 140 GILGNHDRSGVA-NLSTERAKQFAQELKKTCELYDLDGVFFDDEYSAYETPPPAgfvTPSNNAAARLAYETKQAMP--DK 216
Cdd:cd06542    70 SILGNHLGAGFAnNLSDAAAKAYAKAIVDTVDKYGLDGVDFDDEYSGYGKNGTS---QPSNEAFVRLIKELRKYMGptDK 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 217 LVTVYVYSRTSSFpnpvDGVQAGKFVDYAIHDYGGTWDLSS------NYPGLPKSGM----AMASQEFNLNRYASAQTLK 286
Cdd:cd06542   147 LLTIDGYGQALSN----DGEEVSPYVDYVIYQYYGSSSSSTqrnwntNSPKIPPEKMvyteSFEEENGGNSGSSAEQYAR 222
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1153159111 287 NLRT-SGYGAHMIFAMDPNRSnfttkqLPAMKLIAKELY 324
Cdd:cd06542   223 WTPAkGGKGGIGTYALDRDYY------RPYDSAVSKALK 255
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
88-254 1.47e-08

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 55.15  E-value: 1.47e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111  88 LVDMVVLFSANINYDavnDKVIVSNNSNVQHLltNKAKYLKPLRDKGMKVILGILGNHDRSGVANL--STERAKQFAQEL 165
Cdd:pfam00704  22 KLTHIIYAFANIDGS---DGTLFIGDWDLGNF--EQLKKLKKQKNPGVKVLLSIGGWTDSTGFSLMasNPASRKKFADSI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 166 KKTCELYDLDGVFFDDEYSAYETPPPAGFVTpsnnaaarLAYETKQAM------PDKLVTVYVYSRTSSFPNPVDGVQAG 239
Cdd:pfam00704  97 VSFLRKYGFDGIDIDWEYPGGNPEDKENYDL--------LLRELRAALdeakggKKYLLSAAVPASYPDLDKGYDLPKIA 168
                         170
                  ....*....|....*....
gi 1153159111 240 KFVDYaIH----DYGGTWD 254
Cdd:pfam00704 169 KYLDF-INvmtyDFHGSWD 186
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
88-244 8.47e-05

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.


Pssm-ID: 119349 [Multi-domain]  Cd Length: 210  Bit Score: 43.14  E-value: 8.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111  88 LVDMVVLFSANINYDAVNDKVIVSNNSNVQHLLTNKAKylkplRDKGMKVILGILGNHDRSGVANLSTE-RAKQFAQELK 166
Cdd:cd00598    23 LCTHIIYAFAEISSDGSLNLFGDKSEEPLKGALEELAS-----KKPGLKVLISIGGWTDSSPFTLASDPaSRAAFANSLV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1153159111 167 KTCELYDLDGVFFDDEY-SAYETPPPAGFVTpsnnaaarLAYETKQAMP--DKLVTVYVYSRTSSFPNPVDGVQAGKFVD 243
Cdd:cd00598    98 SFLKTYGFDGVDIDWEYpGAADNSDRENFIT--------LLRELRSALGaaNYLLTIAVPASYFDLGYAYDVPAIGDYVD 169

                  .
gi 1153159111 244 Y 244
Cdd:cd00598   170 F 170
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH