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Conserved domains on  [gi|2098438818|ref|NP_001382981|]
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cytosolic endo-beta-N-acetylglucosaminidase isoform 1 [Homo sapiens]

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 ...
126-444 9.87e-174

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: 503.37  E-value: 9.87e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 126 LLCHDMMGGYLDDRFIQGSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAF 205
Cdd:cd06547     1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 206 LAGDERSYQAVADRLVQITQFFRFDGWLINIENSL-SLAAVGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQD 284
Cdd:cd06547    81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELgDAEKAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 285 ELNQHNRVFFDSCDGFFTNYNWREEHLERMLGQA---GERRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALF 361
Cdd:cd06547   161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAeglGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 362 APGWVYECLEKKDFFQ---------------NQDKFWGRLERYLPTHSIC-SLPFVTSFCLGMGARRVCYGQEEAVGPWY 425
Cdd:cd06547   241 APGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                         330
                  ....*....|....*....
gi 2098438818 426 HLSAQEIQPLFGEHRLGGD 444
Cdd:cd06547   321 NLSLQDILPTYRWIVSSNG 339
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
126-444 9.87e-174

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: 503.37  E-value: 9.87e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 126 LLCHDMMGGYLDDRFIQGSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAF 205
Cdd:cd06547     1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 206 LAGDERSYQAVADRLVQITQFFRFDGWLINIENSL-SLAAVGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQD 284
Cdd:cd06547    81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELgDAEKAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 285 ELNQHNRVFFDSCDGFFTNYNWREEHLERMLGQA---GERRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALF 361
Cdd:cd06547   161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAeglGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 362 APGWVYECLEKKDFFQ---------------NQDKFWGRLERYLPTHSIC-SLPFVTSFCLGMGARRVCYGQEEAVGPWY 425
Cdd:cd06547   241 APGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                         330
                  ....*....|....*....
gi 2098438818 426 HLSAQEIQPLFGEHRLGGD 444
Cdd:cd06547   321 NLSLQDILPTYRWIVSSNG 339
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
143-409 9.67e-144

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: 424.78  E-value: 9.67e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 143 GSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAFLAGDERSYQAVADRLVQ 222
Cdd:pfam03644   1 GGNDFDAYTFYYWQYVDTFVYFSHSRVTIPPPGWINAAHRNGVPVLGTFIFEWDEGGEWLEELLEKDEDGAFPVADKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 223 ITQFFRFDGWLINIENSLSLAA--VGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQDELNQHNRVFFDSCDGF 300
Cdd:pfam03644  81 IAKYYGFDGWLINIETAFLLDPelAENLKEFLRYLREELHERVPGSEVIWYDSVTTDGKLSWQNELNEKNAPFFQAADSI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 301 FTNYNWREEHLERMLGQAGE---RRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALFAPGWVYECLEK---KD 374
Cdd:pfam03644 161 FLNYWWTESNLESSAELAGSlgrRPYDVYVGIDVFGRGTVGGGGFNTNVALDLIAKAGLSAALFAPGWTYETFQSgstPD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098438818 375 FFQNQDKFW----------------GRLERYLPTHS-ICSLPFVTSFCLGMG 409
Cdd:pfam03644 241 FLERERRFWvgpkgdpdpdssdnswKGIANYVAERSaISSLPFYTNFNTGSG 292
COG4724 COG4724
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];
62-516 9.37e-68

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


Pssm-ID: 443759 [Multi-domain]  Cd Length: 662  Bit Score: 237.28  E-value: 9.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818  62 VVSFSPDPLPVRYYDKDTTKPISFYLSsLEELLAWKPRLE--DGFNVALEPLACRQPPLSSQRPRTL------LCHDMMG 133
Cdd:COG4724    15 ATSILFPSANEEYSQKIANQPYSSYWF-PEDLLNWSPETDpdARYNRSRVPLAPRFTGSATQINPTLspdakvMSLAIDN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 134 GYLDDRFIQGSVVQTPYAFYHWQCIDVFVYF----SHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNE-GGRL--CEAFL 206
Cdd:COG4724    94 PNTSGNPSQGGSDFNVYTFTYWQYIDYLVYWggsaGEGIIVPPSPDVIDAAHKNGVKVLGTVFFPPGAyGGKIewVDAFL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 207 AGDERSYQAVADRLVQITQFFRFDGWLINIENSLSLAAVGN-MPPFLRYLTTQLhrqvPGGLVL-WYDSVVQSGQLKWQD 284
Cdd:COG4724   174 EKDEDGSFPVADKLIEIAQYYGFDGWFINQETNGTDPELAKkMKEFLEYLKEKS----PENMEImWYDSMLENGSVSWQN 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 285 ELNQHNRVFFD-----SCDGFFTNYNW-REEHLER---MLGQAGERRADVYVGVDVFARGNVVGGRFDTDksLELIRKHG 355
Cdd:COG4724   250 ALNEKNDAFLQdgnkkVSDSMFLNFWWtGGSLLEKsrdTAKSLGRSPYDLYAGIDVQQNGYNTRINWDAL--LDDNKKPP 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 356 FSVALFAPGWVY--EClEKKDFFQNQDKFWGR----------------LERYLPTHS-ICSLPFVTSFCLGMGARRVCYG 416
Cdd:COG4724   328 TSLGLYCPNWTFnsSK-NPDDFYDNEQKFWVGpdgdpanttdsngwkgISTYVVEKSpVTSLPFVTNFNTGHGYKFYING 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 417 QEEAVGPWYHLSAQEIQPLFgehRLGGDGRG-WVRTHCCLEDAWHGGSSLLVRGVIppEVGN-VAVRLFSLQAPVPPKIY 494
Cdd:COG4724   407 QQVSDGEWNNRSLQDVLPTW---QWIVDSEGnSLTPSFDYTDAYNGGSSLKLEGKL--KAGGeTTIKLYKTDLPITDDTK 481
                         490       500
                  ....*....|....*....|..
gi 2098438818 495 LSMVYKLEGPTDVTVALELTTG 516
Cdd:COG4724   482 LSVVYKTDAKVKLSLGLTFKDG 503
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
126-444 9.87e-174

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: 503.37  E-value: 9.87e-174
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 126 LLCHDMMGGYLDDRFIQGSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAF 205
Cdd:cd06547     1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 206 LAGDERSYQAVADRLVQITQFFRFDGWLINIENSL-SLAAVGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQD 284
Cdd:cd06547    81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELgDAEKAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 285 ELNQHNRVFFDSCDGFFTNYNWREEHLERMLGQA---GERRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALF 361
Cdd:cd06547   161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAeglGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 362 APGWVYECLEKKDFFQ---------------NQDKFWGRLERYLPTHSIC-SLPFVTSFCLGMGARRVCYGQEEAVGPWY 425
Cdd:cd06547   241 APGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                         330
                  ....*....|....*....
gi 2098438818 426 HLSAQEIQPLFGEHRLGGD 444
Cdd:cd06547   321 NLSLQDILPTYRWIVSSNG 339
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
143-409 9.67e-144

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: 424.78  E-value: 9.67e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 143 GSVVQTPYAFYHWQCIDVFVYFSHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNEGGRLCEAFLAGDERSYQAVADRLVQ 222
Cdd:pfam03644   1 GGNDFDAYTFYYWQYVDTFVYFSHSRVTIPPPGWINAAHRNGVPVLGTFIFEWDEGGEWLEELLEKDEDGAFPVADKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 223 ITQFFRFDGWLINIENSLSLAA--VGNMPPFLRYLTTQLHRQVPGGLVLWYDSVVQSGQLKWQDELNQHNRVFFDSCDGF 300
Cdd:pfam03644  81 IAKYYGFDGWLINIETAFLLDPelAENLKEFLRYLREELHERVPGSEVIWYDSVTTDGKLSWQNELNEKNAPFFQAADSI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 301 FTNYNWREEHLERMLGQAGE---RRADVYVGVDVFARGNVVGGRFDTDKSLELIRKHGFSVALFAPGWVYECLEK---KD 374
Cdd:pfam03644 161 FLNYWWTESNLESSAELAGSlgrRPYDVYVGIDVFGRGTVGGGGFNTNVALDLIAKAGLSAALFAPGWTYETFQSgstPD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2098438818 375 FFQNQDKFW----------------GRLERYLPTHS-ICSLPFVTSFCLGMG 409
Cdd:pfam03644 241 FLERERRFWvgpkgdpdpdssdnswKGIANYVAERSaISSLPFYTNFNTGSG 292
COG4724 COG4724
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];
62-516 9.37e-68

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


Pssm-ID: 443759 [Multi-domain]  Cd Length: 662  Bit Score: 237.28  E-value: 9.37e-68
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818  62 VVSFSPDPLPVRYYDKDTTKPISFYLSsLEELLAWKPRLE--DGFNVALEPLACRQPPLSSQRPRTL------LCHDMMG 133
Cdd:COG4724    15 ATSILFPSANEEYSQKIANQPYSSYWF-PEDLLNWSPETDpdARYNRSRVPLAPRFTGSATQINPTLspdakvMSLAIDN 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 134 GYLDDRFIQGSVVQTPYAFYHWQCIDVFVYF----SHHTVTIPPVGWTNTAHRHGVCVLGTFITEWNE-GGRL--CEAFL 206
Cdd:COG4724    94 PNTSGNPSQGGSDFNVYTFTYWQYIDYLVYWggsaGEGIIVPPSPDVIDAAHKNGVKVLGTVFFPPGAyGGKIewVDAFL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 207 AGDERSYQAVADRLVQITQFFRFDGWLINIENSLSLAAVGN-MPPFLRYLTTQLhrqvPGGLVL-WYDSVVQSGQLKWQD 284
Cdd:COG4724   174 EKDEDGSFPVADKLIEIAQYYGFDGWFINQETNGTDPELAKkMKEFLEYLKEKS----PENMEImWYDSMLENGSVSWQN 249
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 285 ELNQHNRVFFD-----SCDGFFTNYNW-REEHLER---MLGQAGERRADVYVGVDVFARGNVVGGRFDTDksLELIRKHG 355
Cdd:COG4724   250 ALNEKNDAFLQdgnkkVSDSMFLNFWWtGGSLLEKsrdTAKSLGRSPYDLYAGIDVQQNGYNTRINWDAL--LDDNKKPP 327
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 356 FSVALFAPGWVY--EClEKKDFFQNQDKFWGR----------------LERYLPTHS-ICSLPFVTSFCLGMGARRVCYG 416
Cdd:COG4724   328 TSLGLYCPNWTFnsSK-NPDDFYDNEQKFWVGpdgdpanttdsngwkgISTYVVEKSpVTSLPFVTNFNTGHGYKFYING 406
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 417 QEEAVGPWYHLSAQEIQPLFgehRLGGDGRG-WVRTHCCLEDAWHGGSSLLVRGVIppEVGN-VAVRLFSLQAPVPPKIY 494
Cdd:COG4724   407 QQVSDGEWNNRSLQDVLPTW---QWIVDSEGnSLTPSFDYTDAYNGGSSLKLEGKL--KAGGeTTIKLYKTDLPITDDTK 481
                         490       500
                  ....*....|....*....|..
gi 2098438818 495 LSMVYKLEGPTDVTVALELTTG 516
Cdd:COG4724   482 LSVVYKTDAKVKLSLGLTFKDG 503
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
158-269 2.80e-03

Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.


Pssm-ID: 119353 [Multi-domain]  Cd Length: 313  Bit Score: 40.71  E-value: 2.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2098438818 158 IDVFVYFSHH------TVTIPPVGWTNTAHRHGVCVLGTF--ITEWNEGGRLCEAFLAgDERSYQAVADRLVQITQFFRF 229
Cdd:cd02874    26 LTYIAPFWYGvdadgtLTGLPDERLIEAAKRRGVKPLLVItnLTNGNFDSELAHAVLS-NPEARQRLINNILALAKKYGY 104
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2098438818 230 DGWLINIEnslslaavgNMPP--------FLRYLTTQLHRqvPGGLVL 269
Cdd:cd02874   105 DGVNIDFE---------NVPPedreaytqFLRELSDRLHP--AGYTLS 141
 
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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