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Conserved domains on  [gi|1663468062|ref|XP_029140943|]
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cytosolic endo-beta-N-acetylglucosaminidase [Protobothrops mucrosquamatus]

Protein Classification

endo-beta-N-acetylglucosaminidase( domain architecture ID 10158478)

cytosolic endo-beta-N-acetylglucosaminidase (ENGase) that hydrolyzes the N-N'-diacetylchitobiosyl core of N-glycosylproteins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
76-386 9.35e-153

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: 445.97  E-value: 9.35e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  76 LVCHDMRGGYLEDRFIQGAKVRDPYVFYHWCYIDIFVYFSHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGEKMCESF 155
Cdd:cd06547     1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 156 LAGEEEAYLAVAKQLAAIAEFYRFDGWLVNIENSLHVSA-AQKMPHFLQQLTAEVHRLVPGGQVLWYDSVLKSGELKWQN 234
Cdd:cd06547    81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELGDAEkAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 235 ELNEQNKVYFDVCDGFFTNYNWREEHLLRTR---EAASSRQTDVYVGVDVFGRGDVVGSGFDTKKSLQMIREQGLSVALF 311
Cdd:cd06547   161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVqlaEGLGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 312 APGWVYEHLGPRDF---------------LNNEDKFWALLSQLLSIHHIV-SLPFCTSFNLGVGNRHFSHGQETRTEPWY 375
Cdd:cd06547   241 APGWTYESFEEPDFfvknesrfgesgdpfLTNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                         330
                  ....*....|.
gi 1663468062 376 NLSAQEIQPIY 386
Cdd:cd06547   321 NLSLQDILPTY 331
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
76-386 9.35e-153

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: 445.97  E-value: 9.35e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  76 LVCHDMRGGYLEDRFIQGAKVRDPYVFYHWCYIDIFVYFSHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGEKMCESF 155
Cdd:cd06547     1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 156 LAGEEEAYLAVAKQLAAIAEFYRFDGWLVNIENSLHVSA-AQKMPHFLQQLTAEVHRLVPGGQVLWYDSVLKSGELKWQN 234
Cdd:cd06547    81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELGDAEkAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 235 ELNEQNKVYFDVCDGFFTNYNWREEHLLRTR---EAASSRQTDVYVGVDVFGRGDVVGSGFDTKKSLQMIREQGLSVALF 311
Cdd:cd06547   161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVqlaEGLGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 312 APGWVYEHLGPRDF---------------LNNEDKFWALLSQLLSIHHIV-SLPFCTSFNLGVGNRHFSHGQETRTEPWY 375
Cdd:cd06547   241 APGWTYESFEEPDFfvknesrfgesgdpfLTNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                         330
                  ....*....|.
gi 1663468062 376 NLSAQEIQPIY 386
Cdd:cd06547   321 NLSLQDILPTY 331
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
93-359 1.79e-133

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: 394.73  E-value: 1.79e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  93 GAKVRDPYVFYHWCYIDIFVYFSHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGEKMCESFLAGEEEAYLAVAKQLAA 172
Cdd:pfam03644   1 GGNDFDAYTFYYWQYVDTFVYFSHSRVTIPPPGWINAAHRNGVPVLGTFIFEWDEGGEWLEELLEKDEDGAFPVADKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 173 IAEFYRFDGWLVNIENSLHVSA--AQKMPHFLQQLTAEVHRLVPGGQVLWYDSVLKSGELKWQNELNEQNKVYFDVCDGF 250
Cdd:pfam03644  81 IAKYYGFDGWLINIETAFLLDPelAENLKEFLRYLREELHERVPGSEVIWYDSVTTDGKLSWQNELNEKNAPFFQAADSI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 251 FTNYNWREEHLLRTREAASS---RQTDVYVGVDVFGRGDVVGSGFDTKKSLQMIREQGLSVALFAPGWVYEHLGP---RD 324
Cdd:pfam03644 161 FLNYWWTESNLESSAELAGSlgrRPYDVYVGIDVFGRGTVGGGGFNTNVALDLIAKAGLSAALFAPGWTYETFQSgstPD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1663468062 325 FLNNEDKFWALLSQLLSIHH-----------------IVSLPFCTSFNLGVG 359
Cdd:pfam03644 241 FLERERRFWVGPKGDPDPDSsdnswkgianyvaersaISSLPFYTNFNTGSG 292
COG4724 COG4724
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];
19-470 3.23e-72

Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];


Pssm-ID: 443759 [Multi-domain]  Cd Length: 662  Bit Score: 246.91  E-value: 3.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  19 PLPARQYDRQTTE-PISFYLSgLEELLAWKPTKD--DAFNVSTEPLAKR--QPPLDSH---RPRT-LVCHDMRGGYLEDR 89
Cdd:COG4724    21 PSANEEYSQKIANqPYSSYWF-PEDLLNWSPETDpdARYNRSRVPLAPRftGSATQINptlSPDAkVMSLAIDNPNTSGN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  90 FIQGAKVRDPYVFYHWCYIDIFVYF----SHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGE---KMCESFLAGEEEA 162
Cdd:COG4724   100 PSQGGSDFNVYTFTYWQYIDYLVYWggsaGEGIIVPPSPDVIDAAHKNGVKVLGTVFFPPGAYGgkiEWVDAFLEKDEDG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 163 YLAVAKQLAAIAEFYRFDGWLVNIENSLHVSA-AQKMPHFLQQLTAEVhrlvPGGQVL-WYDSVLKSGELKWQNELNEQN 240
Cdd:COG4724   180 SFPVADKLIEIAQYYGFDGWFINQETNGTDPElAKKMKEFLEYLKEKS----PENMEImWYDSMLENGSVSWQNALNEKN 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 241 KVYFD-----VCDGFFTNYNWREEHLLRtreaaSSRQT---------DVYVGVDVFGRgdvvgsGFDTK-KSLQMIREQG 305
Cdd:COG4724   256 DAFLQdgnkkVSDSMFLNFWWTGGSLLE-----KSRDTakslgrspyDLYAGIDVQQN------GYNTRiNWDALLDDNK 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 306 ---LSVALFAPGWVYEH-LGPRDFLNNEDKFWALLSQLLSI-----------HHIV------SLPFCTSFNLGVGNRHFS 364
Cdd:COG4724   325 kppTSLGLYCPNWTFNSsKNPDDFYDNEQKFWVGPDGDPANttdsngwkgisTYVVekspvtSLPFVTNFNTGHGYKFYI 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 365 HGQETRTEPWYNLSAQEIQPIYashrmpdRGWV-------RTRCCLQEAWCGGSSLLLEGAIPAKAEdVTTRLFSFQMP- 436
Cdd:COG4724   405 NGQQVSDGEWNNRSLQDVLPTW-------QWIVdsegnslTPSFDYTDAYNGGSSLKLEGKLKAGGE-TTIKLYKTDLPi 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1663468062 437 -------------APSRLFLVLIFKHDYRLQaTALAPLLTTRESWSR 470
Cdd:COG4724   477 tddtklsvvyktdAKVKLSLGLTFKDGPTEF-ITFDLGTTSNNGWTT 522
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
76-386 9.35e-153

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: 445.97  E-value: 9.35e-153
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  76 LVCHDMRGGYLEDRFIQGAKVRDPYVFYHWCYIDIFVYFSHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGEKMCESF 155
Cdd:cd06547     1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 156 LAGEEEAYLAVAKQLAAIAEFYRFDGWLVNIENSLHVSA-AQKMPHFLQQLTAEVHRLVPGGQVLWYDSVLKSGELKWQN 234
Cdd:cd06547    81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELGDAEkAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 235 ELNEQNKVYFDVCDGFFTNYNWREEHLLRTR---EAASSRQTDVYVGVDVFGRGDVVGSGFDTKKSLQMIREQGLSVALF 311
Cdd:cd06547   161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVqlaEGLGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 312 APGWVYEHLGPRDF---------------LNNEDKFWALLSQLLSIHHIV-SLPFCTSFNLGVGNRHFSHGQETRTEPWY 375
Cdd:cd06547   241 APGWTYESFEEPDFfvknesrfgesgdpfLTNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                         330
                  ....*....|.
gi 1663468062 376 NLSAQEIQPIY 386
Cdd:cd06547   321 NLSLQDILPTY 331
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
93-359 1.79e-133

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: 394.73  E-value: 1.79e-133
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  93 GAKVRDPYVFYHWCYIDIFVYFSHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGEKMCESFLAGEEEAYLAVAKQLAA 172
Cdd:pfam03644   1 GGNDFDAYTFYYWQYVDTFVYFSHSRVTIPPPGWINAAHRNGVPVLGTFIFEWDEGGEWLEELLEKDEDGAFPVADKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 173 IAEFYRFDGWLVNIENSLHVSA--AQKMPHFLQQLTAEVHRLVPGGQVLWYDSVLKSGELKWQNELNEQNKVYFDVCDGF 250
Cdd:pfam03644  81 IAKYYGFDGWLINIETAFLLDPelAENLKEFLRYLREELHERVPGSEVIWYDSVTTDGKLSWQNELNEKNAPFFQAADSI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 251 FTNYNWREEHLLRTREAASS---RQTDVYVGVDVFGRGDVVGSGFDTKKSLQMIREQGLSVALFAPGWVYEHLGP---RD 324
Cdd:pfam03644 161 FLNYWWTESNLESSAELAGSlgrRPYDVYVGIDVFGRGTVGGGGFNTNVALDLIAKAGLSAALFAPGWTYETFQSgstPD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1663468062 325 FLNNEDKFWALLSQLLSIHH-----------------IVSLPFCTSFNLGVG 359
Cdd:pfam03644 241 FLERERRFWVGPKGDPDPDSsdnswkgianyvaersaISSLPFYTNFNTGSG 292
COG4724 COG4724
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];
19-470 3.23e-72

Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];


Pssm-ID: 443759 [Multi-domain]  Cd Length: 662  Bit Score: 246.91  E-value: 3.23e-72
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  19 PLPARQYDRQTTE-PISFYLSgLEELLAWKPTKD--DAFNVSTEPLAKR--QPPLDSH---RPRT-LVCHDMRGGYLEDR 89
Cdd:COG4724    21 PSANEEYSQKIANqPYSSYWF-PEDLLNWSPETDpdARYNRSRVPLAPRftGSATQINptlSPDAkVMSLAIDNPNTSGN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  90 FIQGAKVRDPYVFYHWCYIDIFVYF----SHHLVTIPPVVWTNAAHRNGVLMLGTFITEWIEGE---KMCESFLAGEEEA 162
Cdd:COG4724   100 PSQGGSDFNVYTFTYWQYIDYLVYWggsaGEGIIVPPSPDVIDAAHKNGVKVLGTVFFPPGAYGgkiEWVDAFLEKDEDG 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 163 YLAVAKQLAAIAEFYRFDGWLVNIENSLHVSA-AQKMPHFLQQLTAEVhrlvPGGQVL-WYDSVLKSGELKWQNELNEQN 240
Cdd:COG4724   180 SFPVADKLIEIAQYYGFDGWFINQETNGTDPElAKKMKEFLEYLKEKS----PENMEImWYDSMLENGSVSWQNALNEKN 255
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 241 KVYFD-----VCDGFFTNYNWREEHLLRtreaaSSRQT---------DVYVGVDVFGRgdvvgsGFDTK-KSLQMIREQG 305
Cdd:COG4724   256 DAFLQdgnkkVSDSMFLNFWWTGGSLLE-----KSRDTakslgrspyDLYAGIDVQQN------GYNTRiNWDALLDDNK 324
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 306 ---LSVALFAPGWVYEH-LGPRDFLNNEDKFWALLSQLLSI-----------HHIV------SLPFCTSFNLGVGNRHFS 364
Cdd:COG4724   325 kppTSLGLYCPNWTFNSsKNPDDFYDNEQKFWVGPDGDPANttdsngwkgisTYVVekspvtSLPFVTNFNTGHGYKFYI 404
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 365 HGQETRTEPWYNLSAQEIQPIYashrmpdRGWV-------RTRCCLQEAWCGGSSLLLEGAIPAKAEdVTTRLFSFQMP- 436
Cdd:COG4724   405 NGQQVSDGEWNNRSLQDVLPTW-------QWIVdsegnslTPSFDYTDAYNGGSSLKLEGKLKAGGE-TTIKLYKTDLPi 476
                         490       500       510       520
                  ....*....|....*....|....*....|....*....|....*..
gi 1663468062 437 -------------APSRLFLVLIFKHDYRLQaTALAPLLTTRESWSR 470
Cdd:COG4724   477 tddtklsvvyktdAKVKLSLGLTFKDGPTEF-ITFDLGTTSNNGWTT 522
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
81-255 1.62e-07

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: 52.38  E-value: 1.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062  81 MRGGYLEDRFIQGAKVRDPYVFYHWCYIDIFVYFSHHLVTIPPVVW----------TNAAHRNGVLMLGTFITEWIEGEK 150
Cdd:cd00598     1 VICYYDGWSSGRGPDPTDIPLSLCTHIIYAFAEISSDGSLNLFGDKseeplkgaleELASKKPGLKVLISIGGWTDSSPF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1663468062 151 mcesFLAGEEEAYLAVAKQLAAIAEFYRFDGWLVNIEN--SLHVSAAQKMPHFLQQLTAEVHRLvpggQVLWYDSVLKSG 228
Cdd:cd00598    81 ----TLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYpgAADNSDRENFITLLRELRSALGAA----NYLLTIAVPASY 152
                         170       180
                  ....*....|....*....|....*..
gi 1663468062 229 ELKWQNELNEQNKVYFDvcDGFFTNYN 255
Cdd:cd00598   153 FDLGYAYDVPAIGDYVD--FVNVMTYD 177
 
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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