|
Name |
Accession |
Description |
Interval |
E-value |
| GH18_chitolectin_chitotriosidase |
cd02872 |
This conserved domain family includes a large number of catalytically inactive chitinase-like ... |
24-387 |
0e+00 |
|
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: 679.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNWAQYRPGLGSFKPDDINPCLCTHLIYAFAGMQN--NQITTIEWND--VTLYKAFNDLKNRNSKLKTLLAIGGW 99
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 100 NFGTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSPPQDKHLFTVLVKELREAFEQEAiesnrPRLM 179
Cdd:cd02872 81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 180 VTAAVAAGISNIQAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPTETGSNAYLNVDYVMNYWKDNGAPAEK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 260 LIVGFPEYGHTYILSNPSDTGIGAPTSGNGPAGPYTRQAGFWAYYEICTFLRNGATQDWDAPQEVPYAYKGNEWVGYDNI 339
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 46485462 340 KSFSVKAQWLKQNNFGGAMIWAIDLDDFTGsFCDQGKFPLTSTLNKAL 387
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
24-365 |
5.76e-149 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 427.87 E-value: 5.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNWAQYRPglgSFKPDDINPCLCTHLIYAFAGMQNNQITTI--EWNDVTLYKAFNDLKNRNSKLKTLLAIGGWNF 101
Cdd:smart00636 2 VVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIgdEWADIGNFGQLKALKKKNPGLKVLLSIGGWTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 102 GTaPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGsppQDKHLFTVLVKELREAFEQEaiESNRPRLMVT 181
Cdd:smart00636 79 SD-NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG---DDRENYTALLKELREALDKE--GAEGKGYLLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 182 AAVAAGISNIQAGYE-IPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPTETGsnaYLNVDYVMNYWKDNGAPAEKL 260
Cdd:smart00636 153 IAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPE---KYNVDYAVKYYLCKGVPPSKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 261 IVGFPEYGHTYILSNPSDTGIGAPTSGNGPAGPYTRQAGFWAYYEICTFLrnGATQDWDAPQEVPYAYKGN--EWVGYDN 338
Cdd:smart00636 230 VLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL--GATVVYDDTAKAPYAYNPGtgQWVSYDD 307
|
330 340
....*....|....*....|....*..
gi 46485462 339 IKSFSVKAQWLKQNNFGGAMIWAIDLD 365
Cdd:smart00636 308 PRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
23-365 |
7.59e-122 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 357.92 E-value: 7.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 23 NLVCYFTNWAQYRPGlgsfkpDDINPCLCTHLIYAFAGM--QNNQITTIEWnDVTLYKAFNDLKN-RNSKLKTLLAIGGW 99
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIdgSDGTLFIGDW-DLGNFEQLKKLKKqKNPGVKVLLSIGGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 100 NFGTaPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRgspPQDKHLFTVLVKELREAFEQEaieSNRPRLM 179
Cdd:pfam00704 74 TDST-GFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGN---PEDKENYDLLLRELRAALDEA---KGGKKYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 180 VTAAVAAGISNIQAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKlptetgsNAYLNVDYVMNYWKDNGAPAEK 259
Cdd:pfam00704 147 LSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG-------GGSYNVDYAVKYYLKQGVPASK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 260 LIVGFPEYGHTYILSNPSDTgigaptsgngpagpyTRQAGFWAYYEICTFLR-NGATQDWDAPQEVPYAYKGNEWVGYDN 338
Cdd:pfam00704 220 LVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLLKdNGATVVWDDVAKAPYVYDGDQFITYDD 284
|
330 340
....*....|....*....|....*..
gi 46485462 339 IKSFSVKAQWLKQNNFGGAMIWAIDLD 365
Cdd:pfam00704 285 PRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
20-387 |
4.26e-101 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 307.99 E-value: 4.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 20 SAYNLVCYFTNWAQYRPGlgsFKPDDINPCLCTHLIYAFAGMQNN--------------QITTIEWNDV--TLYKAFNDL 83
Cdd:COG3325 17 SGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDgkcsvgdawakpsvDGAADDWDQPlkGNFNQLKKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 84 KNRNSKLKTLLAIGGWNfGTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSP-----PQDKHLFTVL 158
Cdd:COG3325 94 KAKNPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPgnvyrPEDKANFTAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 159 VKELREAFEQEAIESNRPrLMVTAAVAAGISNIqAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPTETGSN 238
Cdd:COG3325 173 LKELRAQLDALGAETGKH-YLLTAAAPAGPDKL-DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 239 AYlNVDYVMNYWKDNGAPAEKLIVGFPEYGHTYILSNPSDTGIGAPTSGngpAGPYTRQAGFWAYYEICTFL--RNGATQ 316
Cdd:COG3325 251 GY-SVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTWEAGVNDYKDLKALYlgSNGYTR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46485462 317 DWDAPQEVPYAYKGN--EWVGYDNIKSFSVKAQWLKQNNFGGAMIWAIDLDDFTGSfcdqgkfpLTSTLNKAL 387
Cdd:COG3325 327 YWDDVAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT--------LLNAIGEGL 391
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
426-473 |
1.21e-11 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 59.38 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 46485462 426 FCAGKADGLYPVADDRNAFWHCINGITYQQHCQAGLVFDTSCNCCNWP 473
Cdd:smart00494 2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
427-473 |
3.20e-10 |
|
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: 55.50 E-value: 3.20e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 46485462 427 CAGKADGLYPVADDRNAFWHCINGITYQQHCQAGLVFDTSCNCCNWP 473
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 ... |
24-387 |
0e+00 |
|
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: 679.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNWAQYRPGLGSFKPDDINPCLCTHLIYAFAGMQN--NQITTIEWND--VTLYKAFNDLKNRNSKLKTLLAIGGW 99
Cdd:cd02872 1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 100 NFGTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSPPQDKHLFTVLVKELREAFEQEAiesnrPRLM 179
Cdd:cd02872 81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 180 VTAAVAAGISNIQAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPTETGSNAYLNVDYVMNYWKDNGAPAEK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 260 LIVGFPEYGHTYILSNPSDTGIGAPTSGNGPAGPYTRQAGFWAYYEICTFLRNGATQDWDAPQEVPYAYKGNEWVGYDNI 339
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 46485462 340 KSFSVKAQWLKQNNFGGAMIWAIDLDDFTGsFCDQGKFPLTSTLNKAL 387
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
|
|
| Glyco_18 |
smart00636 |
Glyco_18 domain; |
24-365 |
5.76e-149 |
|
Glyco_18 domain;
Pssm-ID: 214753 [Multi-domain] Cd Length: 334 Bit Score: 427.87 E-value: 5.76e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNWAQYRPglgSFKPDDINPCLCTHLIYAFAGMQNNQITTI--EWNDVTLYKAFNDLKNRNSKLKTLLAIGGWNF 101
Cdd:smart00636 2 VVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIgdEWADIGNFGQLKALKKKNPGLKVLLSIGGWTE 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 102 GTaPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGsppQDKHLFTVLVKELREAFEQEaiESNRPRLMVT 181
Cdd:smart00636 79 SD-NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG---DDRENYTALLKELREALDKE--GAEGKGYLLT 152
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 182 AAVAAGISNIQAGYE-IPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPTETGsnaYLNVDYVMNYWKDNGAPAEKL 260
Cdd:smart00636 153 IAVPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPE---KYNVDYAVKYYLCKGVPPSKL 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 261 IVGFPEYGHTYILSNPSDTGIGAPTSGNGPAGPYTRQAGFWAYYEICTFLrnGATQDWDAPQEVPYAYKGN--EWVGYDN 338
Cdd:smart00636 230 VLGIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL--GATVVYDDTAKAPYAYNPGtgQWVSYDD 307
|
330 340
....*....|....*....|....*..
gi 46485462 339 IKSFSVKAQWLKQNNFGGAMIWAIDLD 365
Cdd:smart00636 308 PRSIKAKADYVKDKGLGGVMIWELDAD 334
|
|
| Glyco_hydro_18 |
pfam00704 |
Glycosyl hydrolases family 18; |
23-365 |
7.59e-122 |
|
Glycosyl hydrolases family 18;
Pssm-ID: 425828 [Multi-domain] Cd Length: 311 Bit Score: 357.92 E-value: 7.59e-122
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 23 NLVCYFTNWAQYRPGlgsfkpDDINPCLCTHLIYAFAGM--QNNQITTIEWnDVTLYKAFNDLKN-RNSKLKTLLAIGGW 99
Cdd:pfam00704 1 RIVGYYTSWGVYRNG------NFLPSDKLTHIIYAFANIdgSDGTLFIGDW-DLGNFEQLKKLKKqKNPGVKVLLSIGGW 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 100 NFGTaPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRgspPQDKHLFTVLVKELREAFEQEaieSNRPRLM 179
Cdd:pfam00704 74 TDST-GFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGGN---PEDKENYDLLLRELRAALDEA---KGGKKYL 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 180 VTAAVAAGISNIQAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKlptetgsNAYLNVDYVMNYWKDNGAPAEK 259
Cdd:pfam00704 147 LSAAVPASYPDLDKGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYG-------GGSYNVDYAVKYYLKQGVPASK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 260 LIVGFPEYGHTYILSNPSDTgigaptsgngpagpyTRQAGFWAYYEICTFLR-NGATQDWDAPQEVPYAYKGNEWVGYDN 338
Cdd:pfam00704 220 LVLGVPFYGRSWTLVNGSGN---------------TWEDGVLAYKEICNLLKdNGATVVWDDVAKAPYVYDGDQFITYDD 284
|
330 340
....*....|....*....|....*..
gi 46485462 339 IKSFSVKAQWLKQNNFGGAMIWAIDLD 365
Cdd:pfam00704 285 PRSIATKVDYVKAKGLGGVMIWSLDAD 311
|
|
| ChiA |
COG3325 |
Chitinase, GH18 family [Carbohydrate transport and metabolism]; |
20-387 |
4.26e-101 |
|
Chitinase, GH18 family [Carbohydrate transport and metabolism];
Pssm-ID: 442554 [Multi-domain] Cd Length: 391 Bit Score: 307.99 E-value: 4.26e-101
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 20 SAYNLVCYFTNWAQYRPGlgsFKPDDINPCLCTHLIYAFAGMQNN--------------QITTIEWNDV--TLYKAFNDL 83
Cdd:COG3325 17 SGKRVVGYFTQWGIYGRN---YLVKDIPASKLTHINYAFANVDPDgkcsvgdawakpsvDGAADDWDQPlkGNFNQLKKL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 84 KNRNSKLKTLLAIGGWNfGTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSP-----PQDKHLFTVL 158
Cdd:COG3325 94 KAKNPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGGAPgnvyrPEDKANFTAL 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 159 VKELREAFEQEAIESNRPrLMVTAAVAAGISNIqAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPTETGSN 238
Cdd:COG3325 173 LKELRAQLDALGAETGKH-YLLTAAAPAGPDKL-DGIELPKVAQYLDYVNVMTYDFHGAWSPTTGHQAPLYDSPKDPEAQ 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 239 AYlNVDYVMNYWKDNGAPAEKLIVGFPEYGHTYILSNPSDTGIGAPTSGngpAGPYTRQAGFWAYYEICTFL--RNGATQ 316
Cdd:COG3325 251 GY-SVDSAVQAYLAAGVPASKLVLGVPFYGRGWTGVTGGNNGLYQPATG---PAPGTWEAGVNDYKDLKALYlgSNGYTR 326
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 46485462 317 DWDAPQEVPYAYKGN--EWVGYDNIKSFSVKAQWLKQNNFGGAMIWAIDLDDFTGSfcdqgkfpLTSTLNKAL 387
Cdd:COG3325 327 YWDDVAKAPYLYNGDtgTFISYDDPRSIAAKADYVKDKGLGGVMFWELSGDTADGT--------LLNAIGEGL 391
|
|
| GH18_chitinase |
cd06548 |
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ... |
25-365 |
4.41e-91 |
|
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: 279.90 E-value: 4.41e-91
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 25 VCYFTNWAQYrpGLGSFKPDDINPCLCTHLIYAFAGMQNN---QITTIEWNDVTLY-----------------KAFNDLK 84
Cdd:cd06548 2 VGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGDggvVTSDDEAADEAAQsvdggadtddqplkgnfGQLRKLK 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 85 NRNSKLKTLLAIGGWNFGTaPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSP-----PQDKHLFTVLV 159
Cdd:cd06548 80 QKNPHLKILLSIGGWTWSG-GFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPgnvarPEDKENFTLLL 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 160 KELREAFEQEAIESNRPRLmVTAAVAAGISNIQAGyEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYklPTETGSNA 239
Cdd:cd06548 159 KELREALDALGAETGRKYL-LTIAAPAGPDKLDKL-EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLY--ASPADPPG 234
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 240 YLNVDYVMNYWKDNGAPAEKLIVGFPEYGHtyilsnpsdtgigaptsgnGPAGpytrqagfWAYYeictflrngatqdWD 319
Cdd:cd06548 235 GYSVDAAVNYYLSAGVPPEKLVLGVPFYGR-------------------GWTG--------YTRY-------------WD 274
|
330 340 350 360
....*....|....*....|....*....|....*....|....*...
gi 46485462 320 APQEVPYAYKGN--EWVGYDNIKSFSVKAQWLKQNNFGGAMIWAIDLD 365
Cdd:cd06548 275 EVAKAPYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
|
|
| GH18_IDGF |
cd02873 |
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ... |
23-380 |
4.07e-74 |
|
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: 239.14 E-value: 4.07e-74
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 23 NLVCYFTNWAQYRPGLGSFKPDDINPCL--CTHLIYAFAGMQ--NNQITTIEWN---DVTLYKAFNDLKNRNSKLKTLLA 95
Cdd:cd02873 1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGIDadTYKIKSLNEDldlDKSHYRAITSLKRKYPHLKVLLS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 96 IGGWNF-----GTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYP-----------GS---------RGSPPQ 150
Cdd:cd02873 81 VGGDRDtdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPknkpkkvrgtfGSawhsfkklfTGDSVV 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 151 D------KHLFTVLVKELREAFEQEAiesnrprLMVTAAVAAGIsNIQAGYEIPELSQYLDFIHVMTYDLhgswdgYTGE 224
Cdd:cd02873 161 DekaaehKEQFTALVRELKNALRPDG-------LLLTLTVLPHV-NSTWYFDVPAIANNVDFVNLATFDF------LTPE 226
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 225 N--------SPLYKLpteTGSNAYLNVDYVMNYWKDNGAPAEKLIVGFPEYGHTYILSnpSDTGI-GAP----TSGNGPA 291
Cdd:cd02873 227 RnpeeadytAPIYEL---YERNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLT--KDSGItGVPpvleTDGPGPA 301
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 292 GPYTRQAGFWAYYEICTFLRNGATQDWDAP--QEV--------PYAY-----KGNE--WVGYDNIKSFSVKAQWLKQNNF 354
Cdd:cd02873 302 GPQTKTPGLLSWPEICSKLPNPANLKGADAplRKVgdptkrfgSYAYrpadeNGEHgiWVSYEDPDTAANKAGYAKAKGL 381
|
410 420
....*....|....*....|....*.
gi 46485462 355 GGAMIWAIDLDDFTGSfCDQGKFPLT 380
Cdd:cd02873 382 GGVALFDLSLDDFRGQ-CTGDKFPIL 406
|
|
| GH18_plant_chitinase_class_V |
cd02879 |
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ... |
36-366 |
6.40e-63 |
|
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: 206.45 E-value: 6.40e-63
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 36 PGLGSFKPDDINPCLCTHLIYAFAGMQNNQIT-TIEWNDVTLYKAF-NDLKNRNSKLKTLLAIGGWNFGTAPFTTMVSTS 113
Cdd:cd02879 11 AWSEEFPPSNIDSSLFTHLFYAFADLDPSTYEvVISPSDESEFSTFtETVKRKNPSVKTLLSIGGGGSDSSAFAAMASDP 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 114 QNRQTFITSVIKFLRQYGFDGLDLDWEYPgsrgSPPQDKHLFTVLVKELREAFEQEAIESNRPRLMVTAAV----AAGIS 189
Cdd:cd02879 91 TARKAFINSSIKVARKYGFDGLDLDWEFP----SSQVEMENFGKLLEEWRAAVKDEARSSGRPPLLLTAAVyfspILFLS 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 190 NIQAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPLYKLPtetgsNAYLNVDYVMNYWKDNGAPAEKLIVGFPEYGH 269
Cdd:cd02879 167 DDSVSYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDP-----NSNVSTDYGIKSWIKAGVPAKKLVLGLPLYGR 241
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 270 TYILSNPSdtgigapTSGNgpagpytrqagfwayyeictflrngatqdwdapqevpYAYKGNEWVGYDNIKSFSVKAQWL 349
Cdd:cd02879 242 AWTLYDTT-------TVSS-------------------------------------YVYAGTTWIGYDDVQSIAVKVKYA 277
|
330
....*....|....*..
gi 46485462 350 KQNNFGGAMIWAIDLDD 366
Cdd:cd02879 278 KQKGLLGYFAWAVGYDD 294
|
|
| GH18_chitinase-like |
cd00598 |
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ... |
24-214 |
1.04e-51 |
|
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: 174.10 E-value: 1.04e-51
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNWAQYRPglgsFKPDDINPCLCTHLIYAFAGMQ--NNQITTIEWNDVTLYKAFNDLKNRNSKLKTLLAIGGWNF 101
Cdd:cd00598 1 VICYYDGWSSGRG----PDPTDIPLSLCTHIIYAFAEISsdGSLNLFGDKSEEPLKGALEELASKKPGLKVLISIGGWTD 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 102 GtaPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSppQDKHLFTVLVKELREAFEQEaiesnrpRLMVT 181
Cdd:cd00598 77 S--SPFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADN--SDRENFITLLRELRSALGAA-------NYLLT 145
|
170 180 190
....*....|....*....|....*....|...
gi 46485462 182 AAVAAGISNIQAGYEIPELSQYLDFIHVMTYDL 214
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDL 178
|
|
| GH18_zymocin_alpha |
cd02878 |
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ... |
25-365 |
7.18e-42 |
|
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: 152.08 E-value: 7.18e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 25 VCYFTNWAQYRPGLgSFKPDDINPCLCTHLIYAFAGmqnnqITTIEWNDVTLYKA-FNDLKNRnSKLKTLLAIGGWNFGT 103
Cdd:cd02878 3 IAYFEAYNLDRPCL-NMDVTQIDTSKYTHIHFAFAN-----ITSDFSVDVSSVQEqFSDFKKL-KGVKKILSFGGWDFST 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 104 APFTTMV----STSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSP------PQDKHLFTVLVKELREAFeqeaies 173
Cdd:cd02878 76 SPSTYQIfrdaVKPANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDIPgipagdPDDGKNYLEFLKLLKSKL------- 148
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 174 nrPRLMvTAAVAAGISN-IQAGYEIPELSQYLDFIHVMTYDLHGSWDGYTGENSPlyKLPTETGSNAYLNVDYVMNYWK- 251
Cdd:cd02878 149 --PSGK-SLSIAAPASYwYLKGFPIKDMAKYVDYIVYMTYDLHGQWDYGNKWASP--GCPAGNCLRSHVNKTETLDALSm 223
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 252 --DNGAPAEKLIVGFPEYGHTYILSNPSDTGIGAPTSG---NGPAGPYTRQAGFWAYYEICTFLRNGATQD--WDAPQEV 324
Cdd:cd02878 224 itKAGVPSNKVVVGVASYGRSFKMADPGCTGPGCTFTGpgsGAEAGRCTCTAGYGAISEIEIIDISKSKNKrwYDTDSDS 303
|
330 340 350 360
....*....|....*....|....*....|....*....|..
gi 46485462 325 PYA-YKGNEWVGYDNIKSFSVKAQWLKQNNFGGAMIWAIDLD 365
Cdd:cd02878 304 DILvYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
|
|
| GH18_CFLE_spore_hydrolase |
cd02874 |
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ... |
96-366 |
2.47e-28 |
|
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: 114.28 E-value: 2.47e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 96 IGGWNFGTAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYpgsrgSPPQDKHLFTVLVKELREAFeqeaiesNR 175
Cdd:cd02874 68 LTNGNFDSELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDFEN-----VPPEDREAYTQFLRELSDRL-------HP 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 176 PRLMVTAAVAAGISNIQAG-----YEIPELSQYLDFIHVMTYDLHGSWdgytgensplyklpTETGSNAYLN-----VDY 245
Cdd:cd02874 136 AGYTLSTAVVPKTSADQFGnwsgaYDYAAIGKIVDFVVLMTYDWHWRG--------------GPPGPVAPIGwvervLQY 201
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 246 VMnywkdNGAPAEKLIVGFPEYGhtYILSNPSDTGIGAPTSGNGpagpytrQAGFWAyyeictfLRNGATQDWDAPQEVP 325
Cdd:cd02874 202 AV-----TQIPREKILLGIPLYG--YDWTLPYKKGGKASTISPQ-------QAINLA-------KRYGAEIQYDEEAQSP 260
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 46485462 326 -YAY----KGNEWVGYDNIKSFSVKAQWLKQNNFGGAMIWAIDLDD 366
Cdd:cd02874 261 fFRYvdeqGRRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
|
|
| GH18_chitobiase |
cd02875 |
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ... |
110-369 |
1.01e-19 |
|
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: 90.18 E-value: 1.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 110 VSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSPPQDkhLFTVLVKELREAFEQEaiesnRPRLMVTAAVAAGIS 189
Cdd:cd02875 91 ISNPTYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYY--ALTELVKETTKAFKKE-----NPGYQISFDVAWSPS 163
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 190 NI-QAGYEIPELSQYLDFIHVMTYDlhgswdgytgENSPLYKLPTETGSNA-YLNVDYVMNYWKDNGAPAEKLIVGFPEY 267
Cdd:cd02875 164 CIdKRCYDYTGIADASDFLVVMDYD----------EQSQIWGKECIAGANSpYSQTLSGYNNFTKLGIDPKKLVMGLPWY 233
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 268 GHTYIL--SNPSDTGIGAPTSGNGPAgPYTRQAGFWAYYEICTFLRN---GATQdWDAPQEVPYAY----KGN-EWVGYD 337
Cdd:cd02875 234 GYDYPClnGNLEDVVCTIPKVPFRGA-NCSDAAGRQIPYSEIMKQINssiGGRL-WDSEQKSPFYNykdkQGNlHQVWYD 311
|
250 260 270
....*....|....*....|....*....|..
gi 46485462 338 NIKSFSVKAQWLKQNNFGGAMIWAIDLDDFTG 369
Cdd:cd02875 312 NPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
|
|
| GH18_3CO4_chitinase |
cd06545 |
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ... |
44-271 |
2.07e-14 |
|
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: 72.87 E-value: 2.07e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 44 DDINPCLCTHLIYAFAGMQNNQITTIEWNDVTLYKAFNDLKNRNSKLKTLLAIGGWNFGTAPFTTmvstSQNRQTFITSV 123
Cdd:cd06545 16 PTIDFSKLTHINLAFANPDANGTLNANPVRSELNSVVNAAHAHNVKILISLAGGSPPEFTAALND----PAKRKALVDKI 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 124 IKFLRQYGFDGLDLDWEYPGSRGSPpqdkhlFTVLVKELREAFEQEAiesnrprLMVTAAVAAGISNiqagyEIPELS-Q 202
Cdd:cd06545 92 INYVVSYNLDGIDVDLEGPDVTFGD------YLVFIRALYAALKKEG-------KLLTAAVSSWNGG-----AVSDSTlA 153
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 46485462 203 YLDFIHVMTYDLHGSWDGYT-GENSPlyklptetgsnaYLNVDYVMNYWKDNG-APAEKLIVGFPEYGHTY 271
Cdd:cd06545 154 YFDFINIMSYDATGPWWGDNpGQHSS------------YDDAVNDLNYWNERGlASKDKLVLGLPFYGYGF 212
|
|
| GH18_chitinase_D-like |
cd02871 |
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ... |
24-369 |
2.79e-12 |
|
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins. The domain architecture of ChiD includes a catalytic glycosyl hydrolase family 18 (GH18) domain, a chitin-binding domain, and a fibronectin type III domain. The chitin-binding and fibronectin type III domains are located either N-terminal or C-terminal to the catalytic domain. This family includes exochitinase Chi36 from Bacillus cereus.
Pssm-ID: 119350 [Multi-domain] Cd Length: 312 Bit Score: 67.36 E-value: 2.79e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNWAQYRpglGSFKPD-DINPCLCTHLIYAFAGMQNNQITTIEWNDVTLYKAFN------DLKNRNSK-LKTLLA 95
Cdd:cd02871 3 LVGYWHNWDNGA---GSGRQDlDDVPSKYNVINVAFAEPTSDGGGEVTFNNGSSPGGYSpaefkaDIKALQAKgKKVLIS 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 96 IGGwnfgtAPFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEY-PGSRGSPPQDKHLfTVLVKELREAFeqeaiesn 174
Cdd:cd02871 80 IGG-----ANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLESgSNPLNATPVITNL-ISALKQLKDHY-------- 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 175 RPRLMVTAA-----VAAGISN---IQAGYE--IPELSQYLDFIHVMTYDlHGSWDGYTGensplyklptetGSNAYLNVD 244
Cdd:cd02871 146 GPNFILTMApetpyVQGGYAAyggIWGAYLplIDNLRDDLTWLNVQYYN-SGGMGGCDG------------QSYSQGTAD 212
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 245 YVMnywkdngAPAEKLIVGFPEYGHTYILSNPSD-TGIGAPTSGNGPAGPYTrqagfwayyeictflrngatqdwdAPQE 323
Cdd:cd02871 213 FLV-------ALADMLLTGFPIAGNDRFPPLPADkVVIGLPASPSAAGGGYV------------------------SPSE 261
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 46485462 324 VPYAY----KGNEWVGYDNIKSFSvkaqwlkqnNFGGAMIWAIDLDDFTG 369
Cdd:cd02871 262 VIKALdclmKGTNCGSYYPAGGYP---------SLRGLMTWSINWDATNN 302
|
|
| ChtBD2 |
smart00494 |
Chitin-binding domain type 2; |
426-473 |
1.21e-11 |
|
Chitin-binding domain type 2;
Pssm-ID: 214696 [Multi-domain] Cd Length: 49 Bit Score: 59.38 E-value: 1.21e-11
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 46485462 426 FCAGKADGLYPVADDRNAFWHCINGITYQQHCQAGLVFDTSCNCCNWP 473
Cdd:smart00494 2 ECPGRGDGLYPHPTDCSKYYQCSNGRPIVGSCPAGLVFNPATQTCDWP 49
|
|
| CBM_14 |
pfam01607 |
Chitin binding Peritrophin-A domain; This domain is called the Peritrophin-A domain and is ... |
427-473 |
3.20e-10 |
|
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: 55.50 E-value: 3.20e-10
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 46485462 427 CAGKADGLYPVADDRNAFWHCINGITYQQHCQAGLVFDTSCNCCNWP 473
Cdd:pfam01607 1 CAGKEDGYYADPGDCSKYYVCSNGEAVEFTCPNGLVFDPTLGICDYP 47
|
|
| Chi1 |
COG3469 |
Chitinase [Carbohydrate transport and metabolism]; |
91-369 |
2.00e-09 |
|
Chitinase [Carbohydrate transport and metabolism];
Pssm-ID: 442692 [Multi-domain] Cd Length: 534 Bit Score: 59.77 E-value: 2.00e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 91 KTLLAIGGWNfGTapftTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWE-----YPGSRGSPPQDKHLFTVLvKELREA 165
Cdd:COG3469 290 KVLLSIGGAN-GT----VQLNTAAAADNFVNSVIALIDEYGFDGLDIDLEggsnsLNAGDTDTPVITNLISAL-KQLKAK 363
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 166 FEqeaiesnrPRLMVTAA-----VAAGI---SNIQAGYE--IPELSQYLDFIHVMTYDlHGSWDGYTGENsplyklptet 235
Cdd:COG3469 364 YG--------PGFVLTMApetpyVQGGYvayGGIWGAYLpvILALRDILTLLHVQYYN-SGSMLGLDGQV---------- 424
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 236 gsNAYLNVDYVMnywkdngAPAEKLIVGFPEYGHTYILSN--PSDTGIGAPTSGNGPAGPYTrqagfwayyeictflrng 313
Cdd:COG3469 425 --YSQGTVDFLV-------AMADMLLEGFPVAGNSNGFPGlrPDQVAIGLPASPSAAGGGYV------------------ 477
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 314 atqdwdAPQEVPYAY----KGNewvgydNIKSFSVKAQWlkqNNFGGAMIWAIDLDDFTG 369
Cdd:COG3469 478 ------SPANVNKALdcltKGT------NCGSYKPRGTY---PGLRGLMTWSINWDASNG 522
|
|
| GH18_SI-CLP |
cd02876 |
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ... |
82-283 |
3.57e-06 |
|
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: 48.84 E-value: 3.57e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 82 DLKNRNSKLKTL--LAIGGWNFGTapFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLD-WEYPGSRGSPPQDKHLFTvL 158
Cdd:cd02876 59 EVRKANKNIKILprVLFEGWSYQD--LQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQLAAYGVPDKRKELIQ-L 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 159 VKELREAFEQEAIESnrpRLMVTAAVAAGISNIQAGYEIPE-LSQYLDFIHVMTYDlhgswdgYTGENSPlyklptetGS 237
Cdd:cd02876 136 VIHLGETLHSANLKL---ILVIPPPREKGNQNGLFTRKDFEkLAPHVDGFSLMTYD-------YSSPQRP--------GP 197
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 46485462 238 NAYL-----NVDYVMnywKDNGAPAEKLIVGFPEYGHTYILSNPSDTGIGA 283
Cdd:cd02876 198 NAPLswvrsCLELLL---PESGKKRAKILLGLNFYGNDYTLPGGGGAITGS 245
|
|
| GH18_narbonin |
cd06544 |
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ... |
46-140 |
5.99e-05 |
|
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) cotyledons with unknown function. Narbonin has a glycosyl hydrolase family 18 (GH18) domain without the conserved catalytic residues and with no known enzymatic activity. Narbonin amounts to up to 3% of the total seed globulins of mature seeds and was thought to be a storage protein but was found to degrade too slowly during germination. This family also includes the VfNOD32 nodulin from Vicia faba.
Pssm-ID: 119361 Cd Length: 253 Bit Score: 44.67 E-value: 5.99e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 46 INPCLCTHLIYAFA------GMQNNQITTIEWNDVTLY-KAFNDLKNRNSKLKTLLAIGGWN--FGTAPFTTMVSTS--Q 114
Cdd:cd06544 20 INPKVEFHFILSFAidydteSNPTNGKFNPYWDTENLTpEAVKSIKAQHPNVKVVISIGGRGvqNNPTPFDPSNVDSwvS 99
|
90 100
....*....|....*....|....*.
gi 46485462 115 NRQTFITSVIKflrQYGFDGLDLDWE 140
Cdd:cd06544 100 NAVSSLTSIIQ---TYNLDGIDIDYE 122
|
|
| GH18_EndoS-like |
cd06542 |
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ... |
129-244 |
2.14e-04 |
|
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of various asparagine (N)-linked glycans and glycoproteins. The endo-beta-N-acetylglucosaminidases have a glycosyl hydrolase family 18 (GH18) catalytic domain. Some members also have an additional C-terminal glycosyl hydrolase family 20 (GH20) domain while others have an N-terminal domain of unknown function (pfam08522). Members of this family include endo-beta-N-acetylglucosaminidase S (EndoS) from Streptococcus pyogenes, EndoF1, EndoF2, EndoF3, and EndoH from Flavobacterium meningosepticum, and EndoE from Enterococcus faecalis. EndoS is a secreted endoglycosidase from Streptococcus pyogenes that specifically hydrolyzes the glycan on human IgG between two core N-acetylglucosamine residues. EndoE is a secreted endoglycosidase, encoded by the ndoE gene in Enterococcus faecalis, that hydrolyzes the glycan on human RNase B.
Pssm-ID: 119359 Cd Length: 255 Bit Score: 42.75 E-value: 2.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 129 QYGFDGLDLDWEY-PGSRGSPPQ-DKHLFTVLVKELREAFeqeaieSNRPRLMVTAavaagiSNIQAGY-EIPELSQYLD 205
Cdd:cd06542 102 KYGLDGVDFDDEYsGYGKNGTSQpSNEAFVRLIKELRKYM------GPTDKLLTID------GYGQALSnDGEEVSPYVD 169
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 46485462 206 FIHVMTYDLHGS-----WDGYTGENSPLYKLPTETGSNAYLNVD 244
Cdd:cd06542 170 YVIYQYYGSSSSstqrnWNTNSPKIPPEKMVYTESFEEENGGNS 213
|
|
| GH18_CTS3_chitinase |
cd06546 |
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen ... |
24-194 |
3.05e-04 |
|
GH18 domain of CTS3 (chitinase 3), an uncharacterized protein from the human fungal pathogen Coccidioides posadasii. CTS3 has a chitinase-like glycosyl hydrolase family 18 (GH18) domain; and has homologs in bacteria as well as fungi.
Pssm-ID: 119363 Cd Length: 256 Bit Score: 42.32 E-value: 3.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 24 LVCYFTNwaqYRPGLG----SFKPDDINPCLCTHLIYAFAGMQNNQitTIEWND--------VTLYKAFNDLknRNSKLK 91
Cdd:cd06546 2 LVIYYQT---THPSNGdpisSLLLVTEKGIALTHLIVAALHINDDG--NIHLNDhppdhprfTTLWTELAIL--QSSGVK 74
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 92 TLLAIGGWNFGTapFTTMVSTSQNRQTFITSVIKFLRQYGFDGLDLDWEYPGSRGSppqdkhlFTVLVKELREAFEQEAI 171
Cdd:cd06546 75 VMGMLGGAAPGS--FSRLDDDDEDFERYYGQLRDMIRRRGLDGLDLDVEEPMSLDG-------IIRLIDRLRSDFGPDFI 145
|
170 180
....*....|....*....|...
gi 46485462 172 esnrprlMVTAAVAAGISNIQAG 194
Cdd:cd06546 146 -------ITLAPVASALTGGEAN 161
|
|
| GH18_trifunctional |
cd06549 |
GH18 domain of an uncharacterized family of bacterial proteins, which share a common ... |
116-268 |
9.97e-04 |
|
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: 41.24 E-value: 9.97e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 46485462 116 RQTFITSVIKFLRQYGFDGLDLDWEypgsrGSPPQDKHLFTVLVKELREAFeqeaiESNRPRLMVTAAVAagisniQAGY 195
Cdd:cd06549 89 RAKFIANIAAYLERNQADGIVLDFE-----ELPADDLPKYVAFLSELRRRL-----PAQGKQLTVTVPAD------EADW 152
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 46485462 196 EIPELSQYLDFIHVMTYDLHgsWDGYTgensplyklPTETGSNAYlnvdYVMNYWKDN-GAPAEKLIVGFPEYG 268
Cdd:cd06549 153 NLKALARNADKLILMAYDEH--YQGGA---------PGPIASQDW----FESNLAQAVkKLPPEKLIVALGSYG 211
|
|
| |
