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Conserved domains on  [gi|384367990|ref|NP_001244933|]
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acidic mammalian chitinase isoform b [Homo sapiens]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 10297124)

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_chitinase-like super family cl10447
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 1-226 2.76e-141

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.


The actual alignment was detected with superfamily member cd02872:

Pssm-ID: 471972 [Multi-domain]  Cd Length: 362  Bit Score: 403.09  E-value: 2.76e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   1 MREAFEQEAkqinkPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYL 80
Cdd:cd02872  143 LREAFEPEA-----PRLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  81 NVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAP 160
Cdd:cd02872  218 NVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDE 297

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384367990 161 QEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTfCNQGKFPLISTLKKAL 226
Cdd:cd02872  298 QKVPYAYKGNQWVGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGT-CGQGKYPLLNAINRAL 362
ChtBD2 smart00494
Chitin-binding domain type 2;
268-315 2.33e-11

Chitin-binding domain type 2;


:

Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 57.84  E-value: 2.33e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 384367990   268 FCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA 315
Cdd:smart00494   2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 1-226 2.76e-141

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: 403.09  E-value: 2.76e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   1 MREAFEQEAkqinkPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYL 80
Cdd:cd02872  143 LREAFEPEA-----PRLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  81 NVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAP 160
Cdd:cd02872  218 NVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDE 297

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384367990 161 QEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTfCNQGKFPLISTLKKAL 226
Cdd:cd02872  298 QKVPYAYKGNQWVGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGT-CGQGKYPLLNAINRAL 362
Glyco_18 smart00636
Glyco_18 domain;
1-204 1.60e-77

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 239.89  E-value: 1.60e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990     1 MREAFEQEAKqiNKPRLMVTAAVAAGISNIQSGYE-IPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGsnaY 79
Cdd:smart00636 135 LREALDKEGA--EGKGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPE---K 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990    80 LNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLknGATQGWDA 159
Cdd:smart00636 210 YNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL--GATVVYDD 287

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 384367990   160 PQEVPYAYQGN--VWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLD 204
Cdd:smart00636 288 TAKAPYAYNPGtgQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
1-204 5.87e-61

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 196.52  E-value: 5.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990    1 MREAFEqeaKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKyptdtgsNAYL 80
Cdd:pfam00704 132 LRAALD---EAKGGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG-------GGSY 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   81 NVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTgigaptsgagpagpyAKESGIWAYYEICTFLK-NGATQGWDA 159
Cdd:pfam00704 202 NVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLLKdNGATVVWDD 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 384367990  160 PQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLD 204
Cdd:pfam00704 267 VAKAPYVYDGDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
2-226 6.37e-55

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 183.19  E-value: 6.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   2 REAFEQEAKQINKPrLMVTAAVAAGISNIQsGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYlN 81
Cdd:COG3325  177 RAQLDALGAETGKH-YLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQGY-S 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  82 VDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPaGPYakESGIWAYYEICTFL--KNGATQGWDA 159
Cdd:COG3325  254 VDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGPAP-GTW--EAGVNDYKDLKALYlgSNGYTRYWDD 330

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384367990 160 PQEVPYAYQGN--VWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTfcnqgkfpLISTLKKAL 226
Cdd:COG3325  331 VAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT--------LLNAIGEGL 391
ChtBD2 smart00494
Chitin-binding domain type 2;
268-315 2.33e-11

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 57.84  E-value: 2.33e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 384367990   268 FCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA 315
Cdd:smart00494   2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 269-315 2.02e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 49.72  E-value: 2.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 384367990  269 CAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA 315
Cdd:pfam01607   1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 1-226 2.76e-141

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: 403.09  E-value: 2.76e-141
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   1 MREAFEQEAkqinkPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYL 80
Cdd:cd02872  143 LREAFEPEA-----PRLLLTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYL 217

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  81 NVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLKNGATQGWDAP 160
Cdd:cd02872  218 NVDYAIKYWLSKGAPPEKLVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDE 297

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 384367990 161 QEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTfCNQGKFPLISTLKKAL 226
Cdd:cd02872  298 QKVPYAYKGNQWVGYDDEESIALKVQYLKSKGLGGAMVWSIDLDDFRGT-CGQGKYPLLNAINRAL 362
Glyco_18 smart00636
Glyco_18 domain;
1-204 1.60e-77

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 239.89  E-value: 1.60e-77
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990     1 MREAFEQEAKqiNKPRLMVTAAVAAGISNIQSGYE-IPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGsnaY 79
Cdd:smart00636 135 LREALDKEGA--EGKGYLLTIAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPE---K 209

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990    80 LNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPAGPYAKESGIWAYYEICTFLknGATQGWDA 159
Cdd:smart00636 210 YNVDYAVKYYLCKGVPPSKLVLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL--GATVVYDD 287

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 384367990   160 PQEVPYAYQGN--VWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLD 204
Cdd:smart00636 288 TAKAPYAYNPGtgQWVSYDDPRSIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
1-204 5.87e-61

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 196.52  E-value: 5.87e-61
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990    1 MREAFEqeaKQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKyptdtgsNAYL 80
Cdd:pfam00704 132 LRAALD---EAKGGKKYLLSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG-------GGSY 201

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   81 NVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTgigaptsgagpagpyAKESGIWAYYEICTFLK-NGATQGWDA 159
Cdd:pfam00704 202 NVDYAVKYYLKQGVPASKLVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLLKdNGATVVWDD 266

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 384367990  160 PQEVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLD 204
Cdd:pfam00704 267 VAKAPYVYDGDQFITYDDPRSIATKVDYVKAKGLGGVMIWSLDAD 311
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
2-226 6.37e-55

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 183.19  E-value: 6.37e-55
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   2 REAFEQEAKQINKPrLMVTAAVAAGISNIQsGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNAYlN 81
Cdd:COG3325  177 RAQLDALGAETGKH-YLLTAAAPAGPDKLD-GIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQGY-S 253

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  82 VDYVMNYWKDNGAPAEKLIVGFPTYGHNFILSNPSNTGIGAPTSGAGPaGPYakESGIWAYYEICTFL--KNGATQGWDA 159
Cdd:COG3325  254 VDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATGPAP-GTW--EAGVNDYKDLKALYlgSNGYTRYWDD 330

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 384367990 160 PQEVPYAYQGN--VWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTfcnqgkfpLISTLKKAL 226
Cdd:COG3325  331 VAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT--------LLNAIGEGL 391
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 1-204 5.20e-40

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: 142.38  E-value: 5.20e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   1 MREAFEQEAKQINKPRLmVTAAVAAGISNIQsGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPTDTGSNayL 80
Cdd:cd06548  161 LREALDALGAETGRKYL-LTIAAPAGPDKLD-KLEVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPADPPGG--Y 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  81 NVDYVMNYWKDNGAPAEKLIVGFPTYGHNFilsnpsnTGigaptsgagpagpyakesgiWAYYeictflkngatqgWDAP 160
Cdd:cd06548  237 SVDAAVNYYLSAGVPPEKLVLGVPFYGRGW-------TG--------------------YTRY-------------WDEV 276

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 384367990 161 QEVPYAYQGN--VWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLD 204
Cdd:cd06548  277 AKAPYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
 34-226 5.11e-36

The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects that include at least five members, some of which are encoded by genes in a tight cluster. The IDGF's have an eight-stranded alpha/beta barrel fold and are related to the glycosyl hydrolase family 18 (GH18) chitinases, but they have an amino acid substitution known to abolish chitinase catalytic activity. IDGFs may have evolved from chitinases to gain new functions as growth factors, interacting with cell surface glycoproteins involved in growth-promoting processes.


Pssm-ID: 119352 [Multi-domain]  Cd Length: 413  Bit Score: 133.98  E-value: 5.11e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  34 YEIPQLSQYLDYIHVMTYDLhgswegYTGENSPL---YKYPTD--TGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPTYGH 108
Cdd:cd02873  203 FDVPAIANNVDFVNLATFDF------LTPERNPEeadYTAPIYelYERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGR 276

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990 109 NFILSnpSNTGI-GAP----TSGAGPAGPYAKESGIWAYYEICTFLKNGATQ-GWDAP-QEV--------PYAYQ---GN 170
Cdd:cd02873  277 AWKLT--KDSGItGVPpvleTDGPGPAGPQTKTPGLLSWPEICSKLPNPANLkGADAPlRKVgdptkrfgSYAYRpadEN 354

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990 171 ----VWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTGTfCNQGKFPLISTLKKAL 226
Cdd:cd02873  355 gehgIWVSYEDPDTAANKAGYAKAKGLGGVALFDLSLDDFRGQ-CTGDKFPILRSAKYRL 413
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 2-205 1.51e-23

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: 97.82  E-value: 1.51e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   2 REAFEQEAKQINKPRLMVTAAV----AAGISNIQSGYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPLYKYPtdtgsN 77
Cdd:cd02879  136 RAAVKDEARSSGRPPLLLTAAVyfspILFLSDDSVSYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDP-----N 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  78 AYLNVDYVMNYWKDNGAPAEKLIVGFPTYGHNFILsnpsntgigaptsgagpagpYAKESGiwayyeictflkngatqgw 157
Cdd:cd02879  211 SNVSTDYGIKSWIKAGVPAKKLVLGLPLYGRAWTL--------------------YDTTTV------------------- 251

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 384367990 158 dapqeVPYAYQGNVWVGYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDD 205
Cdd:cd02879  252 -----SSYVYAGTTWIGYDDVQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
 33-204 3.37e-18

Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle progression. The zymocin alpha subunit has a chitinase activity that is essential for holoenzyme action from the cell exterior while the gamma subunit contains the intracellular toxin responsible for G1 phase cell cycle arrest. The zymocin alpha and beta subunits are thought to act from the cell's exterior by docking to the cell wall-associated chitin, thus mediating gamma-toxin translocation. The alpha subunit has an eight-stranded TIM barrel fold similar to that of family 18 glycosyl hydrolases such as hevamine, chitolectin, and chitobiase.


Pssm-ID: 119357 [Multi-domain]  Cd Length: 345  Bit Score: 83.51  E-value: 3.37e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  33 GYEIPQLSQYLDYIHVMTYDLHGSWEGYTGENSPlyKYPTDTGSNAYLNVDYVMNYWK---DNGAPAEKLIVGFPTYGHN 109
Cdd:cd02878  167 GFPIKDMAKYVDYIVYMTYDLHGQWDYGNKWASP--GCPAGNCLRSHVNKTETLDALSmitKAGVPSNKVVVGVASYGRS 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990 110 FILSNPSNTGIGAPTSGAG---PAGPYAKESGIWAYYEICTFLKNGATQG--WDAPQEVPYA-YQGNVWVGYDNIKSFDI 183
Cdd:cd02878  245 FKMADPGCTGPGCTFTGPGsgaEAGRCTCTAGYGAISEIEIIDISKSKNKrwYDTDSDSDILvYDDDQWVAYMSPATKAA 324

                        170       180
                 ....*....|....*....|.
gi 384367990 184 KAQWLKHNKFGGAMVWAIDLD 204
Cdd:cd02878  325 RIEWYKGLNFGGTSDWAVDLQ 345
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 2-205 1.14e-14

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: 73.07  E-value: 1.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   2 REAFEQ---EAKQ-INKPRLMVTAAVAAGISNIQSG-----YEIPQLSQYLDYIHVMTYDLHGSWegytgensplykypT 72
Cdd:cd02874  119 REAYTQflrELSDrLHPAGYTLSTAVVPKTSADQFGnwsgaYDYAAIGKIVDFVVLMTYDWHWRG--------------G 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  73 DTGSNAYLN-----VDYVMNywkdnGAPAEKLIVGFPTYGHNFILsnPSNTGIGAPTSGAGPAGPYAKEsgiwayyeict 147
Cdd:cd02874  185 PPGPVAPIGwvervLQYAVT-----QIPREKILLGIPLYGYDWTL--PYKKGGKASTISPQQAINLAKR----------- 246

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 384367990 148 flkNGATQGWDAPQEVP-YAY---QGN---VWvgYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDD 205
Cdd:cd02874  247 ---YGAEIQYDEEAQSPfFRYvdeQGRrheVW--FEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
 19-208 8.70e-12

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: 65.15  E-value: 8.70e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  19 VTAAVAAGISNI-QSGYEIPQLSQYLDYIHVMTYDlhgswegytgENSPLYKYPTDTGSNA-YLNVDYVMNYWKDNGAPA 96
Cdd:cd02875  154 ISFDVAWSPSCIdKRCYDYTGIADASDFLVVMDYD----------EQSQIWGKECIAGANSpYSQTLSGYNNFTKLGIDP 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  97 EKLIVGFPTYGHNFILSN----------PSNTGIGAPTSGAgpagpyakeSGIWAYYEICTFLKNGATQG--WDAPQEVP 164
Cdd:cd02875  224 KKLVMGLPWYGYDYPCLNgnledvvctiPKVPFRGANCSDA---------AGRQIPYSEIMKQINSSIGGrlWDSEQKSP 294

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 384367990 165 YAY----QGN---VWvgYDNIKSFDIKAQWLKHNKFGGAMVWAIDLDDFTG 208
Cdd:cd02875  295 FYNykdkQGNlhqVW--YDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
ChtBD2 smart00494
Chitin-binding domain type 2;
268-315 2.33e-11

Chitin-binding domain type 2;


Pssm-ID: 214696 [Multi-domain]  Cd Length: 49  Bit Score: 57.84  E-value: 2.33e-11
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 384367990   268 FCAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA 315
Cdd:smart00494   2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
CBM_14 pfam01607
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ...
 269-315 2.02e-08

Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is found in chitin binding proteins particularly peritrophic matrix proteins of insects and animal chitinases. Copies of the domain are also found in some baculoviruses. Relevant references that describe proteins with this domain include. It is an extracellular domain that contains six conserved cysteines that probably form three disulphide bridges. Chitin binding has been demonstrated for a protein containing only two of these domains.


Pssm-ID: 426342 [Multi-domain]  Cd Length: 53  Bit Score: 49.72  E-value: 2.02e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 384367990  269 CAVRANGLYPVANNRNAFWHCVNGVTYQQNCQAGLVFDTSCDCCNWA 315
Cdd:pfam01607   1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 10-53 1.25e-06

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: 48.53  E-value: 1.25e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 384367990  10 KQINKPRLMVTAAVAAGISNIQSGYEIPQLSQYLDYIHVMTYDL 53
Cdd:cd00598  135 SALGAANYLLTIAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDL 178
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
 3-110 6.33e-06

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: 46.68  E-value: 6.33e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990   3 EAFEQEAKQINKPR-LMVTAAVAAGISNiqsgyEIPQLS-QYLDYIHVMTYDLHGSWEGYT-GENSPLYKYPTDtgsnay 79
Cdd:cd06545  118 LVFIRALYAALKKEgKLLTAAVSSWNGG-----AVSDSTlAYFDFINIMSYDATGPWWGDNpGQHSSYDDAVND------ 186

                         90       100       110
                 ....*....|....*....|....*....|..
gi 384367990  80 lnvdyvMNYWKDNG-APAEKLIVGFPTYGHNF 110
Cdd:cd06545  187 ------LNYWNERGlASKDKLVLGLPFYGYGF 212
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
 38-122 1.51e-03

Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein of unknown function that interacts with the endocytic/sorting transmembrane receptor stabilin-1 and is secreted from the lysosome. SI-CLP has a glycosyl hydrolase family 18 (GH18) domain but lacks a chitin-binding domain. The catalytic amino acids of the GH18 domain are not conserved in SI-CLP, similar to the chitolectins YKL-39, YKL-40, and YM1/2. Human SI-CLP is sorted to late endosomes and secretory lysosomes in alternatively activated macrophages.


Pssm-ID: 119355 [Multi-domain]  Cd Length: 318  Bit Score: 39.60  E-value: 1.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 384367990  38 QLSQYLDYIHVMTYDlhgswegYTGENSPlykyptdtGSNAYL-----NVDYVMnywKDNGAPAEKLIVGFPTYGHNFIL 112
Cdd:cd02876  174 KLAPHVDGFSLMTYD-------YSSPQRP--------GPNAPLswvrsCLELLL---PESGKKRAKILLGLNFYGNDYTL 235

                         90
                 ....*....|
gi 384367990 113 SNPSNTGIGA 122
Cdd:cd02876  236 PGGGGAITGS 245
 
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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