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Conserved domains on  [gi|564375407|ref|XP_006247866|]
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cytosolic endo-beta-N-acetylglucosaminidase isoform X2 [Rattus norvegicus]

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 ...
93-403 1.81e-168

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: 486.42  E-value: 1.81e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  93 LLCHDMMGGYLEDRFIQGSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGKLCEAF 172
Cdd:cd06547    1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 173 LAGDERSFQAVADRLVQIAQFFRFDGWLINIENSL-SPAAVRNTPLFLQYLTRQLHQQVPGGLVLWYDSVVQSGQLKWQD 251
Cdd:cd06547   81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELgDAEKAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 252 ELNEQNRVFFDSCDGFFTNYNWREDHLKRMVAQA---GERLADVYVGIDVFARSNVVGGRFDTDKSLELIRKHGFSAALF 328
Cdd:cd06547  161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAeglGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 329 APGWVYECLEKNDFFQ---------------NQDKFWRLLERFLPTHSIC-SLPFVTSFCLGLGTRRVCYGKEQAVGPWY 392
Cdd:cd06547  241 APGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                        330
                 ....*....|.
gi 564375407 393 HPSAQETQPLF 403
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 ...
93-403 1.81e-168

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: 486.42  E-value: 1.81e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  93 LLCHDMMGGYLEDRFIQGSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGKLCEAF 172
Cdd:cd06547    1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 173 LAGDERSFQAVADRLVQIAQFFRFDGWLINIENSL-SPAAVRNTPLFLQYLTRQLHQQVPGGLVLWYDSVVQSGQLKWQD 251
Cdd:cd06547   81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELgDAEKAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 252 ELNEQNRVFFDSCDGFFTNYNWREDHLKRMVAQA---GERLADVYVGIDVFARSNVVGGRFDTDKSLELIRKHGFSAALF 328
Cdd:cd06547  161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAeglGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 329 APGWVYECLEKNDFFQ---------------NQDKFWRLLERFLPTHSIC-SLPFVTSFCLGLGTRRVCYGKEQAVGPWY 392
Cdd:cd06547  241 APGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                        330
                 ....*....|.
gi 564375407 393 HPSAQETQPLF 403
Cdd:cd06547  321 NLSLQDILPTY 331
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
110-376 4.47e-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: 422.47  E-value: 4.47e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  110 GSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGKLCEAFLAGDERSFQAVADRLVQ 189
Cdd:pfam03644   1 GGNDFDAYTFYYWQYVDTFVYFSHSRVTIPPPGWINAAHRNGVPVLGTFIFEWDEGGEWLEELLEKDEDGAFPVADKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  190 IAQFFRFDGWLINIEN--SLSPAAVRNTPLFLQYLTRQLHQQVPGGLVLWYDSVVQSGQLKWQDELNEQNRVFFDSCDGF 267
Cdd:pfam03644  81 IAKYYGFDGWLINIETafLLDPELAENLKEFLRYLREELHERVPGSEVIWYDSVTTDGKLSWQNELNEKNAPFFQAADSI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  268 FTNYNWREDHLKRMVAQAGE---RLADVYVGIDVFARSNVVGGRFDTDKSLELIRKHGFSAALFAPGWVYECLEK---ND 341
Cdd:pfam03644 161 FLNYWWTESNLESSAELAGSlgrRPYDVYVGIDVFGRGTVGGGGFNTNVALDLIAKAGLSAALFAPGWTYETFQSgstPD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564375407  342 FFQNQDKFW----------------RLLERFLPTHS-ICSLPFVTSFCLGLG 376
Cdd:pfam03644 241 FLERERRFWvgpkgdpdpdssdnswKGIANYVAERSaISSLPFYTNFNTGSG 292
COG4724 COG4724
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];
38-483 7.24e-64

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


Pssm-ID: 443759 [Multi-domain]  Cd Length: 662  Bit Score: 224.57  E-value: 7.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  38 PARYYDKDTTRPISFYLsTLEELLAWTPLME--DGFNVALEPLECR---QPPLSSPRPRT---LLCHDMMGGYLEDRFIQ 109
Cdd:COG4724   24 NEEYSQKIANQPYSSYW-FPEDLLNWSPETDpdARYNRSRVPLAPRftgSATQINPTLSPdakVMSLAIDNPNTSGNPSQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 110 GSEVQNPYSFYHWQYIDIFVYF----SHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQE-GGKL--CEAFLAGDERSFQA 182
Cdd:COG4724  103 GGSDFNVYTFTYWQYIDYLVYWggsaGEGIIVPPSPDVIDAAHKNGVKVLGTVFFPPGAyGGKIewVDAFLEKDEDGSFP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 183 VADRLVQIAQFFRFDGWLINIENSLSPAAVRNTPL-FLQYLTRQLhqqvPGGLVL-WYDSVVQSGQLKWQDELNEQNRVF 260
Cdd:COG4724  183 VADKLIEIAQYYGFDGWFINQETNGTDPELAKKMKeFLEYLKEKS----PENMEImWYDSMLENGSVSWQNALNEKNDAF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 261 FD-----SCDGFFTNYNWREDHLKRMVAQAGERLA----DVYVGIDVFARSNVVGGRFDTDksLELIRKHGFSAALFAPG 331
Cdd:COG4724  259 LQdgnkkVSDSMFLNFWWTGGSLLEKSRDTAKSLGrspyDLYAGIDVQQNGYNTRINWDAL--LDDNKKPPTSLGLYCPN 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 332 WVY--EClEKNDFFQNQDKFW----------------RLLERFLPTHS-ICSLPFVTSFCLGLGTRRVCYGKEQAVGPWY 392
Cdd:COG4724  337 WTFnsSK-NPDDFYDNEQKFWvgpdgdpanttdsngwKGISTYVVEKSpVTSLPFVTNFNTGHGYKFYINGQQVSDGEWN 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 393 HPSAQETQPLFGEHKLAGGNRgwVKTHCCLVDAWHGGSSLLLRGLIPPEvDSVAVRLFSMHVPVPPKVFLSMVYKFEGST 472
Cdd:COG4724  416 NRSLQDVLPTWQWIVDSEGNS--LTPSFDYTDAYNGGSSLKLEGKLKAG-GETTIKLYKTDLPITDDTKLSVVYKTDAKV 492
                        490
                 ....*....|.
gi 564375407 473 DVQVALELTTG 483
Cdd:COG4724  493 KLSLGLTFKDG 503
 
Name Accession Description Interval E-value
GH85_ENGase cd06547
Endo-beta-N-acetylglucosaminidase (ENGase) hydrolyzes the N-N'-diacetylchitobiosyl core of ...
93-403 1.81e-168

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: 486.42  E-value: 1.81e-168
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  93 LLCHDMMGGYLEDRFIQGSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGKLCEAF 172
Cdd:cd06547    1 LVCHDMMGGYTSDRPSQGSNSFNAYTFSYWQYVDTFVYFSHSAVTIPPADWINAAHRNGVPVLGTFIFEWTGQVEWLEDF 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 173 LAGDERSFQAVADRLVQIAQFFRFDGWLINIENSL-SPAAVRNTPLFLQYLTRQLHQQVPGGLVLWYDSVVQSGQLKWQD 251
Cdd:cd06547   81 LKKDEDGSFPVADKLVEVAKYYGFDGWLINIETELgDAEKAKRLIAFLRYLKAKLHENVPGSLVIWYDSMTEDGKLSWQN 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 252 ELNEQNRVFFDSCDGFFTNYNWREDHLKRMVAQA---GERLADVYVGIDVFARSNVVGGRFDTDKSLELIRKHGFSAALF 328
Cdd:cd06547  161 ELNSKNKPFFDVCDGIFLNYWWTEESLERSVQLAeglGRSPYDVYVGVDVWGRGTKGGGGWNSDKALDEIKKAGLSVALF 240
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 329 APGWVYECLEKNDFFQ---------------NQDKFWRLLERFLPTHSIC-SLPFVTSFCLGLGTRRVCYGKEQAVGPWY 392
Cdd:cd06547  241 APGWTYESFEEPDFFVknesrfgesgdpfltNDDKFWSGLATYVPEKSPItSLPFVTNFNTGSGYAFYVNGKKVSDSPWN 320
                        330
                 ....*....|.
gi 564375407 393 HPSAQETQPLF 403
Cdd:cd06547  321 NLSLQDILPTY 331
Glyco_hydro_85 pfam03644
Glycosyl hydrolase family 85; Family of endo-beta-N-acetylglucosaminidases. These enzymes work ...
110-376 4.47e-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: 422.47  E-value: 4.47e-144
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  110 GSEVQNPYSFYHWQYIDIFVYFSHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQEGGKLCEAFLAGDERSFQAVADRLVQ 189
Cdd:pfam03644   1 GGNDFDAYTFYYWQYVDTFVYFSHSRVTIPPPGWINAAHRNGVPVLGTFIFEWDEGGEWLEELLEKDEDGAFPVADKLVE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  190 IAQFFRFDGWLINIEN--SLSPAAVRNTPLFLQYLTRQLHQQVPGGLVLWYDSVVQSGQLKWQDELNEQNRVFFDSCDGF 267
Cdd:pfam03644  81 IAKYYGFDGWLINIETafLLDPELAENLKEFLRYLREELHERVPGSEVIWYDSVTTDGKLSWQNELNEKNAPFFQAADSI 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  268 FTNYNWREDHLKRMVAQAGE---RLADVYVGIDVFARSNVVGGRFDTDKSLELIRKHGFSAALFAPGWVYECLEK---ND 341
Cdd:pfam03644 161 FLNYWWTESNLESSAELAGSlgrRPYDVYVGIDVFGRGTVGGGGFNTNVALDLIAKAGLSAALFAPGWTYETFQSgstPD 240
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 564375407  342 FFQNQDKFW----------------RLLERFLPTHS-ICSLPFVTSFCLGLG 376
Cdd:pfam03644 241 FLERERRFWvgpkgdpdpdssdnswKGIANYVAERSaISSLPFYTNFNTGSG 292
COG4724 COG4724
Endo-beta-N-acetylglucosaminidase D [Carbohydrate transport and metabolism];
38-483 7.24e-64

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


Pssm-ID: 443759 [Multi-domain]  Cd Length: 662  Bit Score: 224.57  E-value: 7.24e-64
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407  38 PARYYDKDTTRPISFYLsTLEELLAWTPLME--DGFNVALEPLECR---QPPLSSPRPRT---LLCHDMMGGYLEDRFIQ 109
Cdd:COG4724   24 NEEYSQKIANQPYSSYW-FPEDLLNWSPETDpdARYNRSRVPLAPRftgSATQINPTLSPdakVMSLAIDNPNTSGNPSQ 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 110 GSEVQNPYSFYHWQYIDIFVYF----SHHTVTIPPVCWTNAAHRHGVCVLGTFITEWQE-GGKL--CEAFLAGDERSFQA 182
Cdd:COG4724  103 GGSDFNVYTFTYWQYIDYLVYWggsaGEGIIVPPSPDVIDAAHKNGVKVLGTVFFPPGAyGGKIewVDAFLEKDEDGSFP 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 183 VADRLVQIAQFFRFDGWLINIENSLSPAAVRNTPL-FLQYLTRQLhqqvPGGLVL-WYDSVVQSGQLKWQDELNEQNRVF 260
Cdd:COG4724  183 VADKLIEIAQYYGFDGWFINQETNGTDPELAKKMKeFLEYLKEKS----PENMEImWYDSMLENGSVSWQNALNEKNDAF 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 261 FD-----SCDGFFTNYNWREDHLKRMVAQAGERLA----DVYVGIDVFARSNVVGGRFDTDksLELIRKHGFSAALFAPG 331
Cdd:COG4724  259 LQdgnkkVSDSMFLNFWWTGGSLLEKSRDTAKSLGrspyDLYAGIDVQQNGYNTRINWDAL--LDDNKKPPTSLGLYCPN 336
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 332 WVY--EClEKNDFFQNQDKFW----------------RLLERFLPTHS-ICSLPFVTSFCLGLGTRRVCYGKEQAVGPWY 392
Cdd:COG4724  337 WTFnsSK-NPDDFYDNEQKFWvgpdgdpanttdsngwKGISTYVVEKSpVTSLPFVTNFNTGHGYKFYINGQQVSDGEWN 415
                        410       420       430       440       450       460       470       480
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 393 HPSAQETQPLFGEHKLAGGNRgwVKTHCCLVDAWHGGSSLLLRGLIPPEvDSVAVRLFSMHVPVPPKVFLSMVYKFEGST 472
Cdd:COG4724  416 NRSLQDVLPTWQWIVDSEGNS--LTPSFDYTDAYNGGSSLKLEGKLKAG-GETTIKLYKTDLPITDDTKLSVVYKTDAKV 492
                        490
                 ....*....|.
gi 564375407 473 DVQVALELTTG 483
Cdd:COG4724  493 KLSLGLTFKDG 503
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
124-236 1.46e-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: 41.48  E-value: 1.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 564375407 124 YIDIFVYFSHH------TVTIPPVCWTNAAHRHGVCVLGTfITEWQEGGK---LCEAFLAgDERSFQAVADRLVQIAQFF 194
Cdd:cd02874   25 YLTYIAPFWYGvdadgtLTGLPDERLIEAAKRRGVKPLLV-ITNLTNGNFdseLAHAVLS-NPEARQRLINNILALAKKY 102
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 564375407 195 RFDGWLINIENsLSPAAVRNTPLFLQYLTRQLHQqvPGGLVL 236
Cdd:cd02874  103 GYDGVNIDFEN-VPPEDREAYTQFLRELSDRLHP--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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