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Conserved domains on  [gi|4758092|ref|NP_004379|]
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di-N-acetylchitobiase precursor [Homo sapiens]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 10120845)

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_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
39-378 0e+00

Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.


:

Pssm-ID: 119354 [Multi-domain]  Cd Length: 358  Bit Score: 646.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092   39 TDCPCPEPELCRPIRHHPDFEVFVFDVGQKTWKSYDWSQITTVATFGKYDSELMCYAHSKGARVVLKGDVSLKDIIDPAF 118
Cdd:cd02875  17 YECPCIEPELCEPIEIGPRFEFLVFSVNSTNYPNYDWSKVTTIAIFGDIDDELLCYAHSKGVRLVLKGDVPLEQISNPTY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  119 RASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRCYNYTGIA 198
Cdd:cd02875  97 RTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYYALTELVKETTKAFKKENPGYQISFDVAWSPSCIDKRCYDYTGIA 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  199 DACDFLFVMSYDEQSQIWS-ECIAAANAPYNQTLTGYNDYIKMSINPKKLVMGVPWYGYDYTCLNLS-EDHVCTIAKVPF 276
Cdd:cd02875 177 DASDFLVVMDYDEQSQIWGkECIAGANSPYSQTLSGYNNFTKLGIDPKKLVMGLPWYGYDYPCLNGNlEDVVCTIPKVPF 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  277 RGAPCSDAAGRQVPYKTIMKQINSSISGNLWDKDQRAPYYNYKDPAGHFHQVWYDNPQSISLKATYIQNYRLRGIGMWNA 356
Cdd:cd02875 257 RGANCSDAAGRQIPYSEIMKQINSSIGGRLWDSEQKSPFYNYKDKQGNLHQVWYDNPQSLSIKVAYAKNLGLKGIGMWNG 336
                       330       340
                ....*....|....*....|..
gi 4758092  357 NCLDYSGDAVAKQQTEEMWEVL 378
Cdd:cd02875 337 DLLDYSGLPIAEKQTEDMWNAL 358
 
Name Accession Description Interval E-value
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
39-378 0e+00

Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.


Pssm-ID: 119354 [Multi-domain]  Cd Length: 358  Bit Score: 646.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092   39 TDCPCPEPELCRPIRHHPDFEVFVFDVGQKTWKSYDWSQITTVATFGKYDSELMCYAHSKGARVVLKGDVSLKDIIDPAF 118
Cdd:cd02875  17 YECPCIEPELCEPIEIGPRFEFLVFSVNSTNYPNYDWSKVTTIAIFGDIDDELLCYAHSKGVRLVLKGDVPLEQISNPTY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  119 RASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRCYNYTGIA 198
Cdd:cd02875  97 RTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYYALTELVKETTKAFKKENPGYQISFDVAWSPSCIDKRCYDYTGIA 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  199 DACDFLFVMSYDEQSQIWS-ECIAAANAPYNQTLTGYNDYIKMSINPKKLVMGVPWYGYDYTCLNLS-EDHVCTIAKVPF 276
Cdd:cd02875 177 DASDFLVVMDYDEQSQIWGkECIAGANSPYSQTLSGYNNFTKLGIDPKKLVMGLPWYGYDYPCLNGNlEDVVCTIPKVPF 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  277 RGAPCSDAAGRQVPYKTIMKQINSSISGNLWDKDQRAPYYNYKDPAGHFHQVWYDNPQSISLKATYIQNYRLRGIGMWNA 356
Cdd:cd02875 257 RGANCSDAAGRQIPYSEIMKQINSSIGGRLWDSEQKSPFYNYKDKQGNLHQVWYDNPQSLSIKVAYAKNLGLKGIGMWNG 336
                       330       340
                ....*....|....*....|..
gi 4758092  357 NCLDYSGDAVAKQQTEEMWEVL 378
Cdd:cd02875 337 DLLDYSGLPIAEKQTEDMWNAL 358
Glyco_18 smart00636
Glyco_18 domain;
115-358 1.27e-44

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 157.07  E-value: 1.27e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092     115 DPAFRASWIAQKLNLAKTQYMDGINIDIEQeVNCLSPEYDALTALVKETTDSFHRE---IEGSQVTFDVAWSPKNIDRRC 191
Cdd:smart00636  88 DPASRKKFIDSIVSFLKKYGFDGIDIDWEY-PGGRGDDRENYTALLKELREALDKEgaeGKGYLLTIAVPAGPDKIDKGY 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092     192 YNYTGIADACDFLFVMSYDEQSqIWSEcIAAANAPYNQTLT---------GYNDYIKMSINPKKLVMGVPWYGYDYTCLN 262
Cdd:smart00636 167 GDLPAIAKYLDFINLMTYDFHG-AWSN-PTGHNAPLYAGPGdpekynvdyAVKYYLCKGVPPSKLVLGIPFYGRGWTLVD 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092     263 LSEDHVCTIAKVPFRGAPCSDAAGrQVPYKTIMKQINSSISgnlWDKDQRAPyYNYKDPAGHFhqVWYDNPQSISLKATY 342
Cdd:smart00636 245 GSNNGPGAPFTGPATGGPGTWEGG-VVDYREICKLLGATVV---YDDTAKAP-YAYNPGTGQW--VSYDDPRSIKAKADY 317
                          250
                   ....*....|....*.
gi 4758092     343 IQNYRLRGIGMWNANC 358
Cdd:smart00636 318 VKDKGLGGVMIWELDA 333
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
115-357 3.37e-31

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 120.64  E-value: 3.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092    115 DPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNCLSpEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRC-YN 193
Cdd:pfam00704  85 NPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPE-DKENYDLLLRELRAALDEAKGGKKYLLSAAVPASYPDLDKgYD 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092    194 YTGIADACDFLFVMSYDEQSQIWSECIAAANAPYNQTLT---GYNDYIKMSINPKKLVMGVPWYGYDYTCLNlsedhvct 270
Cdd:pfam00704 164 LPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYGGGSYNvdyAVKYYLKQGVPASKLVLGVPFYGRSWTLVN-------- 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092    271 iakvpfrGAPCSDAAGrQVPYKTIMKQINSSISGNLWDKDQRAPY-YNYKdpaghfHQVWYDNPQSISLKATYIQNYRLR 349
Cdd:pfam00704 236 -------GSGNTWEDG-VLAYKEICNLLKDNGATVVWDDVAKAPYvYDGD------QFITYDDPRSIATKVDYVKAKGLG 301

                  ....*...
gi 4758092    350 GIGMWNAN 357
Cdd:pfam00704 302 GVMIWSLD 309
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
136-378 6.30e-21

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 93.44  E-value: 6.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  136 DGINIDIE------QEVNCLSPE-YDALTALVKE---------TTDSFHREIegsqvTFDVAWSPKNIDRrcYNYTGIAD 199
Cdd:COG3325 142 DGIDIDWEypgsggAPGNVYRPEdKANFTALLKElraqldalgAETGKHYLL-----TAAAPAGPDKLDG--IELPKVAQ 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  200 ACDFLFVMSYDeQSQIWSECI-------AAANAPYNQTLT---GYNDYIKMSINPKKLVMGVPWYGYDYTCLNLSEDHVC 269
Cdd:COG3325 215 YLDYVNVMTYD-FHGAWSPTTghqaplyDSPKDPEAQGYSvdsAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLY 293
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  270 TiakvPFRGAPCSDAAGRQVPYKTIMKQINSSISGNL-WDKDQRAPY-YNykdpaGHFHQVW-YDNPQSISLKATYIQNY 346
Cdd:COG3325 294 Q----PATGPAPGTWEAGVNDYKDLKALYLGSNGYTRyWDDVAKAPYlYN-----GDTGTFIsYDDPRSIAAKADYVKDK 364
                       250       260       270
                ....*....|....*....|....*....|..
gi 4758092  347 RLRGIGMWnanclDYSGDAVAKQQTEEMWEVL 378
Cdd:COG3325 365 GLGGVMFW-----ELSGDTADGTLLNAIGEGL 391
 
Name Accession Description Interval E-value
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
39-378 0e+00

Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes the reducing-end N-acetylglucosamine from the chitobiose core of oligosaccharides during the ordered degradation of asparagine-linked glycoproteins in eukaryotes. Chitobiase can only do so if the asparagine that joins the oligosaccharide to protein is previously removed by a glycosylasparaginase. Chitobiase is therefore the final step in the lysosomal degradation of the protein/carbohydrate linkage component of asparagine-linked glycoproteins. The catalytic domain of chitobiase is an eight-stranded alpha/beta barrel fold similar to that of other family 18 glycosyl hydrolases such as hevamine and chitotriosidase.


Pssm-ID: 119354 [Multi-domain]  Cd Length: 358  Bit Score: 646.03  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092   39 TDCPCPEPELCRPIRHHPDFEVFVFDVGQKTWKSYDWSQITTVATFGKYDSELMCYAHSKGARVVLKGDVSLKDIIDPAF 118
Cdd:cd02875  17 YECPCIEPELCEPIEIGPRFEFLVFSVNSTNYPNYDWSKVTTIAIFGDIDDELLCYAHSKGVRLVLKGDVPLEQISNPTY 96
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  119 RASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRCYNYTGIA 198
Cdd:cd02875  97 RTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYYALTELVKETTKAFKKENPGYQISFDVAWSPSCIDKRCYDYTGIA 176
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  199 DACDFLFVMSYDEQSQIWS-ECIAAANAPYNQTLTGYNDYIKMSINPKKLVMGVPWYGYDYTCLNLS-EDHVCTIAKVPF 276
Cdd:cd02875 177 DASDFLVVMDYDEQSQIWGkECIAGANSPYSQTLSGYNNFTKLGIDPKKLVMGLPWYGYDYPCLNGNlEDVVCTIPKVPF 256
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  277 RGAPCSDAAGRQVPYKTIMKQINSSISGNLWDKDQRAPYYNYKDPAGHFHQVWYDNPQSISLKATYIQNYRLRGIGMWNA 356
Cdd:cd02875 257 RGANCSDAAGRQIPYSEIMKQINSSIGGRLWDSEQKSPFYNYKDKQGNLHQVWYDNPQSLSIKVAYAKNLGLKGIGMWNG 336
                       330       340
                ....*....|....*....|..
gi 4758092  357 NCLDYSGDAVAKQQTEEMWEVL 378
Cdd:cd02875 337 DLLDYSGLPIAEKQTEDMWNAL 358
Glyco_18 smart00636
Glyco_18 domain;
115-358 1.27e-44

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 157.07  E-value: 1.27e-44
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092     115 DPAFRASWIAQKLNLAKTQYMDGINIDIEQeVNCLSPEYDALTALVKETTDSFHRE---IEGSQVTFDVAWSPKNIDRRC 191
Cdd:smart00636  88 DPASRKKFIDSIVSFLKKYGFDGIDIDWEY-PGGRGDDRENYTALLKELREALDKEgaeGKGYLLTIAVPAGPDKIDKGY 166
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092     192 YNYTGIADACDFLFVMSYDEQSqIWSEcIAAANAPYNQTLT---------GYNDYIKMSINPKKLVMGVPWYGYDYTCLN 262
Cdd:smart00636 167 GDLPAIAKYLDFINLMTYDFHG-AWSN-PTGHNAPLYAGPGdpekynvdyAVKYYLCKGVPPSKLVLGIPFYGRGWTLVD 244
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092     263 LSEDHVCTIAKVPFRGAPCSDAAGrQVPYKTIMKQINSSISgnlWDKDQRAPyYNYKDPAGHFhqVWYDNPQSISLKATY 342
Cdd:smart00636 245 GSNNGPGAPFTGPATGGPGTWEGG-VVDYREICKLLGATVV---YDDTAKAP-YAYNPGTGQW--VSYDDPRSIKAKADY 317
                          250
                   ....*....|....*.
gi 4758092     343 IQNYRLRGIGMWNANC 358
Cdd:smart00636 318 VKDKGLGGVMIWELDA 333
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
55-354 4.96e-34

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: 128.15  E-value: 4.96e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092   55 HPDFEVFVFDVGQKTWKSYDWSQITTVATF-GKYDSELMCYAHSKGARVVL-----KGDVSLKDII-----DPAFRASWI 123
Cdd:cd02874  13 GSDYESLRANAPYLTYIAPFWYGVDADGTLtGLPDERLIEAAKRRGVKPLLvitnlTNGNFDSELAhavlsNPEARQRLI 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  124 AQKLNLAKTQYMDGINIDIEQevncLSPE-YDALTALVKETTDSFHREieGSQVTFDVA----WSPKNIDRRCYNYTGIA 198
Cdd:cd02874  93 NNILALAKKYGYDGVNIDFEN----VPPEdREAYTQFLRELSDRLHPA--GYTLSTAVVpktsADQFGNWSGAYDYAAIG 166
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  199 DACDFLFVMSYDEQSQiWSECIAAA-NAPYNQTLtgynDYIKMSINPKKLVMGVPWYGYDYTclnlsedhvctiakVPFR 277
Cdd:cd02874 167 KIVDFVVLMTYDWHWR-GGPPGPVApIGWVERVL----QYAVTQIPREKILLGIPLYGYDWT--------------LPYK 227
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 4758092  278 GAPCSDAAGRQVPYKTIMKQiNSSIsgnLWDKDQRAPYYNYKDPAGHFHQVWYDNPQSISLKATYIQNYRLRGIGMW 354
Cdd:cd02874 228 KGGKASTISPQQAINLAKRY-GAEI---QYDEEAQSPFFRYVDEQGRRHEVWFEDARSLQAKFELAKEYGLRGVSYW 300
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
115-357 3.37e-31

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 120.64  E-value: 3.37e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092    115 DPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNCLSpEYDALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRC-YN 193
Cdd:pfam00704  85 NPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGNPE-DKENYDLLLRELRAALDEAKGGKKYLLSAAVPASYPDLDKgYD 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092    194 YTGIADACDFLFVMSYDEQSQIWSECIAAANAPYNQTLT---GYNDYIKMSINPKKLVMGVPWYGYDYTCLNlsedhvct 270
Cdd:pfam00704 164 LPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYGGGSYNvdyAVKYYLKQGVPASKLVLGVPFYGRSWTLVN-------- 235
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092    271 iakvpfrGAPCSDAAGrQVPYKTIMKQINSSISGNLWDKDQRAPY-YNYKdpaghfHQVWYDNPQSISLKATYIQNYRLR 349
Cdd:pfam00704 236 -------GSGNTWEDG-VLAYKEICNLLKDNGATVVWDDVAKAPYvYDGD------QFITYDDPRSIATKVDYVKAKGLG 301

                  ....*...
gi 4758092    350 GIGMWNAN 357
Cdd:pfam00704 302 GVMIWSLD 309
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
49-210 7.37e-22

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: 92.44  E-value: 7.37e-22
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092   49 CRPIRHHPDFEVFVFDVGQKTWKSYDWSQITTV-----------ATFGKYDSELMcyAHSKGARVVL----KGDVSLKDI 113
Cdd:cd00598   5 YDGWSSGRGPDPTDIPLSLCTHIIYAFAEISSDgslnlfgdkseEPLKGALEELA--SKKPGLKVLIsiggWTDSSPFTL 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  114 I-DPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYDALTALVKETTDSFHReiEGSQVTFDVAWSPKNIDRRcY 192
Cdd:cd00598  83 AsDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADNSDRENFITLLRELRSALGA--ANYLLTIAVPASYFDLGYA-Y 159
                       170
                ....*....|....*...
gi 4758092  193 NYTGIADACDFLFVMSYD 210
Cdd:cd00598 160 DVPAIGDYVDFVNVMTYD 177
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
136-378 6.30e-21

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 93.44  E-value: 6.30e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  136 DGINIDIE------QEVNCLSPE-YDALTALVKE---------TTDSFHREIegsqvTFDVAWSPKNIDRrcYNYTGIAD 199
Cdd:COG3325 142 DGIDIDWEypgsggAPGNVYRPEdKANFTALLKElraqldalgAETGKHYLL-----TAAAPAGPDKLDG--IELPKVAQ 214
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  200 ACDFLFVMSYDeQSQIWSECI-------AAANAPYNQTLT---GYNDYIKMSINPKKLVMGVPWYGYDYTCLNLSEDHVC 269
Cdd:COG3325 215 YLDYVNVMTYD-FHGAWSPTTghqaplyDSPKDPEAQGYSvdsAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLY 293
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  270 TiakvPFRGAPCSDAAGRQVPYKTIMKQINSSISGNL-WDKDQRAPY-YNykdpaGHFHQVW-YDNPQSISLKATYIQNY 346
Cdd:COG3325 294 Q----PATGPAPGTWEAGVNDYKDLKALYLGSNGYTRyWDDVAKAPYlYN-----GDTGTFIsYDDPRSIAAKADYVKDK 364
                       250       260       270
                ....*....|....*....|....*....|..
gi 4758092  347 RLRGIGMWnanclDYSGDAVAKQQTEEMWEVL 378
Cdd:COG3325 365 GLGGVMFW-----ELSGDTADGTLLNAIGEGL 391
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
115-354 4.89e-18

This conserved domain family includes a large number of catalytically inactive chitinase-like lectins (chitolectins) including YKL-39, YKL-40 (HCGP39), YM1, oviductin, and AMCase (acidic mammalian chitinase), as well as catalytically active chitotriosidases. The conserved domain is an eight-stranded alpha/beta barrel fold belonging to the family 18 glycosyl hydrolases. The fold has a pronounced active-site cleft at the C-terminal end of the beta-barrel. The chitolectins lack a key active site glutamate (the proton donor required for hydrolytic activity) but retain highly conserved residues involved in oligosaccharide binding. Chitotriosidase is a chitinolytic enzyme expressed in maturing macrophages, which suggests that it plays a part in antimicrobial defense. Chitotriosidase hydrolyzes chitotriose, as well as colloidal chitin to yield chitobiose and is therefore considered an exochitinase. Chitotriosidase occurs in two major forms, the large form being converted to the small form by either RNA or post-translational processing. Although the small form, containing the chitinase domain alone, is sufficient for the chitinolytic activity, the additional C-terminal chitin-binding domain of the large form plays a role in processing colloidal chitin. The chitotriosidase gene is nonessential in humans, as about 35% of the population are heterozygous and 6% homozygous for an inactivated form of the gene. HCGP39 is a 39-kDa human cartilage glycoprotein thought to play a role in connective tissue remodeling and defense against pathogens.


Pssm-ID: 119351 [Multi-domain]  Cd Length: 362  Bit Score: 84.53  E-value: 4.89e-18
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  115 DPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNCLSPEYD--ALTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRRcY 192
Cdd:cd02872  93 SPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDkeNFVTLLKELREAFEPEAPRLLLTAAVSAGKETIDAA-Y 171
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  193 NYTGIADACDFLFVMSYDEQSQiWsECIAAANAP--YNQTLTGYNDY--IKMSIN--------PKKLVMGVPWYGYDYTC 260
Cdd:cd02872 172 DIPEISKYLDFINVMTYDFHGS-W-EGVTGHNSPlyAGSADTGDQKYlnVDYAIKywlskgapPEKLVLGIPTYGRSFTL 249
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  261 LNLSEDHVctiakvpfrGAPCSdAAGRQVPYkTimKQ--------INSSISGNL---WDKDQRAPyYNYKDpaghfhQVW 329
Cdd:cd02872 250 ASPSNTGV---------GAPAS-GPGTAGPY-T--REagflayyeICEFLKSGWtvvWDDEQKVP-YAYKG------NQW 309
                       250       260
                ....*....|....*....|....*..
gi 4758092  330 --YDNPQSISLKATYIQNYRLRGIGMW 354
Cdd:cd02872 310 vgYDDEESIALKVQYLKSKGLGGAMVW 336
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
115-364 2.69e-13

The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. The structure of this domain is an eight-stranded alpha/beta barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel.


Pssm-ID: 119365 [Multi-domain]  Cd Length: 322  Bit Score: 69.97  E-value: 2.69e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  115 DPAFRASWIAQKLNLAKTQYMDGINIDIE------QEVNCLSPE-YDALTALVKETTDSF--HREIEGS--QVTFDVAWS 183
Cdd:cd06548 106 TEASRAKFADSAVDFIRKYGFDGIDIDWEypgsggAPGNVARPEdKENFTLLLKELREALdaLGAETGRkyLLTIAAPAG 185
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  184 PKNIDRrcYNYTGIADACDFLFVMSYD----------EQSQIWSecIAAANAPYNQTLTGYNDYIKMSINPKKLVMGVPW 253
Cdd:cd06548 186 PDKLDK--LEVAEIAKYLDFINLMTYDfhgawsnttgHHSNLYA--SPADPPGGYSVDAAVNYYLSAGVPPEKLVLGVPF 261
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  254 YGydytclnlsedhvctiakvpfRGapcsdAAGRQVpyktimkqinssisgnLWDKDQRAPYYnYKDPAGHFhqVWYDNP 333
Cdd:cd06548 262 YG---------------------RG-----WTGYTR----------------YWDEVAKAPYL-YNPSTKTF--ISYDDP 296
                       250       260       270
                ....*....|....*....|....*....|.
gi 4758092  334 QSISLKATYIQNYRLRGIGMWnanclDYSGD 364
Cdd:cd06548 297 RSIKAKADYVKDKGLGGVMFW-----ELSGD 322
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
95-259 2.88e-10

The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an uncharacterized bacterial member of the family 18 glycosyl hydrolases with homologs found in Flavobacterium, Stigmatella, and Pseudomonas.


Pssm-ID: 119362 [Multi-domain]  Cd Length: 253  Bit Score: 60.16  E-value: 2.88e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092   95 AHSKGARV---VLKGDVS--LKDIIDPAFRASWIAQKLNLAKTQYMDGINIDIEQEVNcLSPEYDaltALVKETTDSFHR 169
Cdd:cd06545  55 AHAHNVKIlisLAGGSPPefTAALNDPAKRKALVDKIINYVVSYNLDGIDVDLEGPDV-TFGDYL---VFIRALYAALKK 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  170 eiEGSQVTFDVAwspknidrrCYNYTGIADAC----DFLFVMSYDeQSQIWSECIAAANAPYNQTLTGYNDYIKMSINPK 245
Cdd:cd06545 131 --EGKLLTAAVS---------SWNGGAVSDSTlayfDFINIMSYD-ATGPWWGDNPGQHSSYDDAVNDLNYWNERGLASK 198
                       170
                ....*....|....*
gi 4758092  246 -KLVMGVPWYGYDYT 259
Cdd:cd06545 199 dKLVLGLPFYGYGFY 213
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
115-357 3.92e-08

The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the chitin-binding domain present in other GH18 enzymes. The GH18 domain of the class V chitinases has endochitinase activity in some cases and no catalytic activity in others. Included in this family is a lectin found in black locust (Robinia pseudoacacia) bark, which binds chitin but lacks chitinase activity. Also included is a chitinase-related receptor-like kinase (CHRK1) from tobacco (Nicotiana tabacum), with an N-terminal GH18 domain and a C-terminal kinase domain, which is thought to be part of a plant signaling pathway. The GH18 domain of CHRK1 is expressed extracellularly where it binds chitin but lacks chitinase activity.


Pssm-ID: 119358 [Multi-domain]  Cd Length: 299  Bit Score: 54.29  E-value: 3.92e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  115 DPAFRASWIAQKLNLAKTQYMDGINIDIEqevnclSPEYDA----LTALVKETTDSFHREIEGSQ-----VTFDVAWSPK 185
Cdd:cd02879  89 DPTARKAFINSSIKVARKYGFDGLDLDWE------FPSSQVemenFGKLLEEWRAAVKDEARSSGrppllLTAAVYFSPI 162
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  186 ---NIDRRCYNYTGIADACDFLFVMSYDEQSQIWSECIAAANAPYNQ-----TLTGYNDYIKMSINPKKLVMGVPWYGYD 257
Cdd:cd02879 163 lflSDDSVSYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDPnsnvsTDYGIKSWIKAGVPAKKLVLGLPLYGRA 242
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  258 YTCLNlsedhvctiakvpfrgapcsdaagrqvpyKTIMkqINSSISGNLWdkdqrapyynykdpaghfhqVWYDNPQSIS 337
Cdd:cd02879 243 WTLYD-----------------------------TTTV--SSYVYAGTTW--------------------IGYDDVQSIA 271
                       250       260
                ....*....|....*....|
gi 4758092  338 LKATYIQNYRLRGIGMWNAN 357
Cdd:cd02879 272 VKVKYAKQKGLLGYFAWAVG 291
GH18_trifunctional cd06549
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ...
115-360 3.35e-06

GH18 domain of an uncharacterized family of bacterial proteins, which share a common three-domain architecture: an N-terminal glycosyl hydrolase family 18 (GH18) domain, a glycosyl transferase family 2 domain, and a C-terminal polysaccharide deacetylase domain.


Pssm-ID: 119366 [Multi-domain]  Cd Length: 298  Bit Score: 48.18  E-value: 3.35e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  115 DPAFRASWIAQKLN-LAKTQYmDGINIDIEQ-EVNCLSPeydaLTALVKETTDSFHREIEGSQVTFDVAWSPKNIDRrcy 192
Cdd:cd06549  85 DPSARAKFIANIAAyLERNQA-DGIVLDFEElPADDLPK----YVAFLSELRRRLPAQGKQLTVTVPADEADWNLKA--- 156
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  193 nytgIADACDFLFVMSYDEQ----------SQIWSE---CIAAANAPynqtltgyndyikmsinPKKLVMGVPWYGYDYT 259
Cdd:cd06549 157 ----LARNADKLILMAYDEHyqggapgpiaSQDWFEsnlAQAVKKLP-----------------PEKLIVALGSYGYDWT 215
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 4758092  260 clnlsedhvctiakvpfrgapcsdAAGRQVPYKTIMKQINSSISGNLWDKDQRA--PYYNYKDPAGHFHQVWYDNPQSIS 337
Cdd:cd06549 216 ------------------------KGGNTKAISSEAAWLLAAHASAAVKFDDKAsnATYFFYDDEGVSHEVWMLDAVTLF 271
                       250       260
                ....*....|....*....|...
gi 4758092  338 LKATYIQNYRLRGIGMWNANCLD 360
Cdd:cd06549 272 NQLKAVQRLGPAGVALWRLGSED 294
 
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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