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Conserved domains on  [gi|51315803|sp|O35744|]
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RecName: Full=Chitinase-like protein 3; AltName: Full=Beta-N-acetylhexosaminidase Ym1; AltName: Full=Chitinase-3-like protein 3; AltName: Full=ECF-L; AltName: Full=Eosinophil chemotactic cytokine; AltName: Full=Secreted protein Ym1; Flags: Precursor

Protein Classification

GH18_chitolectin_chitotriosidase domain-containing protein (domain architecture ID 10120809)

GH18_chitolectin_chitotriosidase domain-containing protein

Graphical summary

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List of domain hits

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: 596.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  24 LMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQN--NEITYTHEQD--LRDYEALNGLKDKNTELKTLLAIGGW 99
Cdd:cd02872   1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 100 KFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESvekdiPRLL 179
Cdd:cd02872  81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 180 LTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 260 LIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNV 339
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 51315803 340 RSFKLKAQWLKDNNLGGAVVWPLDMDDFSGsFCHQRHFPLTSTLKGDL 387
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
 
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: 596.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  24 LMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQN--NEITYTHEQD--LRDYEALNGLKDKNTELKTLLAIGGW 99
Cdd:cd02872   1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 100 KFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESvekdiPRLL 179
Cdd:cd02872  81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 180 LTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 260 LIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNV 339
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 51315803 340 RSFKLKAQWLKDNNLGGAVVWPLDMDDFSGsFCHQRHFPLTSTLKGDL 387
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
Glyco_18 smart00636
Glyco_18 domain;
26-365 6.67e-126

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 366.23  E-value: 6.67e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803     26 CYYTSWAKDRPiegSFKPGNIDPCLCTHLIYAFAGMQNNEITY--THEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGP 103
Cdd:smart00636   4 GYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTigDEWADIGNFGQLKALKKKNPGLKVLLSIGGWTESD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    104 aPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGsppKDKHLFSVLVKEMRKAFEEESVEKdiPRLLLTST 183
Cdd:smart00636  81 -NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG---DDRENYTALLKELREALDKEGAEG--KGYLLTIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    184 GAGIIDVIKSGYK-IPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKsadLNVDSIISYWKDHGAASEKLIV 262
Cdd:smart00636 155 VPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK---YNVDYAVKYYLCKGVPPSKLVL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    263 GFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLneGATEVWDAPQEVPYAYQGN--EWVGYDNVR 340
Cdd:smart00636 232 GIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL--GATVVYDDTAKAPYAYNPGtgQWVSYDDPR 309
                          330       340
                   ....*....|....*....|....*
gi 51315803    341 SFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:smart00636 310 SIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
23-365 1.52e-103

Glycosyl hydrolases family 18;


Pssm-ID: 395573 [Multi-domain]  Cd Length: 307  Bit Score: 308.60  E-value: 1.52e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    23 QLMCYYTSWAKDRPIEGsfkpgnIDPCLCTHLIYAFAGM--QNNEITyTHEQDLRDYEALNGLKD-KNTELKTLLAIGGW 99
Cdd:pfam00704   1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIdgSDGTLV-IGDWDLGNFEQLKKLKKqKNPGVKVLLSIGGW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803   100 KFGpAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRgspPKDKHLFSVLVKEMRKAFEEesvekdiPRLL 179
Cdd:pfam00704  74 TDS-TGFSLMASNPASRKKFADSIISFLRKYGFDGIDIDWEYPGGN---PEDKENYDLLLRELRAALDE-------KKYL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803   180 LTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYdigksadLNVDSIISYWKDHGAASEK 259
Cdd:pfam00704 143 LSAAVPASYPDLDIGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYGGGS-------YNVDYAVKYYLKKGVPASK 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803   260 LIVGFPAYGHTFILSDPSKTgigaptistgppgkyTDESGLLAYYEVCTFLN-EGATEVWDAPQEVPYAYQGNEWVGYDN 338
Cdd:pfam00704 216 LVLGVPFYGRSWTLVNGSNN---------------TWEDGVLAYKEICNNLGkNGATPVWDDVAKAPYVYDGDQFITYDD 280
                         330       340
                  ....*....|....*....|....*..
gi 51315803   339 VRSFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:pfam00704 281 PRSIATKVDYVKAKGLGGVMIWSLDAD 307
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
27-365 8.19e-59

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 225862 [Multi-domain]  Cd Length: 441  Bit Score: 197.65  E-value: 8.19e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  27 YYTSWAK-DRPiegSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRD-----------------------YEALNG 82
Cdd:COG3325  43 YYTSWSQyDRQ---DYFPGDIPLDQLTHINYAFLDINSDGKSIESWVADEAalygvpniegveldpwsdplkghFGALFD 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  83 LKDKNTELKTLLAIGGWKFGPaPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGS-----PPKDKHLFSV 157
Cdd:COG3325 120 LKATYPDLKTLISIGGWSDSG-GFSDMAADDASRENFAKSAVEFMRTYGFDGVDIDWEYPGSGGDagncgRPKDKANYVL 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 158 LVKEMRKAFEEESVEkDIPRLLLTsTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDI-- 235
Cdd:COG3325 199 LLQELRKKLDKAGVE-DGRHYQLT-IAAPASKDKLEGLNHAEIAQYVDYINIMTYDFHGAWNETLGHHAALYGTPKDPpl 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 236 ---GKSADLNVDSII-SYWKDHGAASE-KLIVGFPAYGHTF----ILSDPSKTGIGAPTISTGPP-GKYTDESGLLAY-- 303
Cdd:COG3325 277 angGFYVDAEVDGIDwLEEGFAGDVPPsKLVLGMPFYGRGWngvdGGSLGTCPGLYQGLDNSGIPkGTWEAGNGDKDYgk 356
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51315803 304 YEVCTFLNEGA---TEVWDAPQEVPYAY--QGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:COG3325 357 AYDLDANNAGKngyERYWDDVAKAPYLYnpEKGVFISYDDPRSVKAKAEYVADNNLGGMMFWEISGD 423
 
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: 596.08  E-value: 0e+00
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  24 LMCYYTSWAKDRPIEGSFKPGNIDPCLCTHLIYAFAGMQN--NEITYTHEQD--LRDYEALNGLKDKNTELKTLLAIGGW 99
Cdd:cd02872   1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPdgNIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 100 KFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDKHLFSVLVKEMRKAFEEESvekdiPRLL 179
Cdd:cd02872  81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGQRGGPPEDKENFVTLLKELREAFEPEA-----PRLL 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 180 LTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISYWKDHGAASEK 259
Cdd:cd02872 156 LTAAVSAGKETIDAAYDIPEISKYLDFINVMTYDFHGSWEGVTGHNSPLYAGSADTGDQKYLNVDYAIKYWLSKGAPPEK 235
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 260 LIVGFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLNEGATEVWDAPQEVPYAYQGNEWVGYDNV 339
Cdd:cd02872 236 LVLGIPTYGRSFTLASPSNTGVGAPASGPGTAGPYTREAGFLAYYEICEFLKSGWTVVWDDEQKVPYAYKGNQWVGYDDE 315
                       330       340       350       360
                ....*....|....*....|....*....|....*....|....*...
gi 51315803 340 RSFKLKAQWLKDNNLGGAVVWPLDMDDFSGsFCHQRHFPLTSTLKGDL 387
Cdd:cd02872 316 ESIALKVQYLKSKGLGGAMVWSIDLDDFRG-TCGQGKYPLLNAINRAL 362
Glyco_18 smart00636
Glyco_18 domain;
26-365 6.67e-126

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 366.23  E-value: 6.67e-126
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803     26 CYYTSWAKDRPiegSFKPGNIDPCLCTHLIYAFAGMQNNEITY--THEQDLRDYEALNGLKDKNTELKTLLAIGGWKFGP 103
Cdd:smart00636   4 GYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTigDEWADIGNFGQLKALKKKNPGLKVLLSIGGWTESD 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    104 aPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGsppKDKHLFSVLVKEMRKAFEEESVEKdiPRLLLTST 183
Cdd:smart00636  81 -NFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGGRG---DDRENYTALLKELREALDKEGAEG--KGYLLTIA 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    184 GAGIIDVIKSGYK-IPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDIGKsadLNVDSIISYWKDHGAASEKLIV 262
Cdd:smart00636 155 VPAGPDKIDKGYGdLPAIAKYLDFINLMTYDFHGAWSNPTGHNAPLYAGPGDPEK---YNVDYAVKYYLCKGVPPSKLVL 231
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    263 GFPAYGHTFILSDPSKTGIGAPTISTGPPGKYTDESGLLAYYEVCTFLneGATEVWDAPQEVPYAYQGN--EWVGYDNVR 340
Cdd:smart00636 232 GIPFYGRGWTLVDGSNNGPGAPFTGPATGGPGTWEGGVVDYREICKLL--GATVVYDDTAKAPYAYNPGtgQWVSYDDPR 309
                          330       340
                   ....*....|....*....|....*
gi 51315803    341 SFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:smart00636 310 SIKAKADYVKDKGLGGVMIWELDAD 334
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
23-365 1.52e-103

Glycosyl hydrolases family 18;


Pssm-ID: 395573 [Multi-domain]  Cd Length: 307  Bit Score: 308.60  E-value: 1.52e-103
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803    23 QLMCYYTSWAKDRPIEGsfkpgnIDPCLCTHLIYAFAGM--QNNEITyTHEQDLRDYEALNGLKD-KNTELKTLLAIGGW 99
Cdd:pfam00704   1 RIVGYYTSWGVYRNGNF------LPSDKLTHIIYAFANIdgSDGTLV-IGDWDLGNFEQLKKLKKqKNPGVKVLLSIGGW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803   100 KFGpAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRgspPKDKHLFSVLVKEMRKAFEEesvekdiPRLL 179
Cdd:pfam00704  74 TDS-TGFSLMASNPASRKKFADSIISFLRKYGFDGIDIDWEYPGGN---PEDKENYDLLLRELRAALDE-------KKYL 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803   180 LTSTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYdigksadLNVDSIISYWKDHGAASEK 259
Cdd:pfam00704 143 LSAAVPASYPDLDIGYDLPKIAKYLDFINVMTYDFHGSWDNVTGHHAPLYGGGS-------YNVDYAVKYYLKKGVPASK 215
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803   260 LIVGFPAYGHTFILSDPSKTgigaptistgppgkyTDESGLLAYYEVCTFLN-EGATEVWDAPQEVPYAYQGNEWVGYDN 338
Cdd:pfam00704 216 LVLGVPFYGRSWTLVNGSNN---------------TWEDGVLAYKEICNNLGkNGATPVWDDVAKAPYVYDGDQFITYDD 280
                         330       340
                  ....*....|....*....|....*..
gi 51315803   339 VRSFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:pfam00704 281 PRSIATKVDYVKAKGLGGVMIWSLDAD 307
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
25-365 6.62e-77

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: 240.61  E-value: 6.62e-77
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  25 MCYYTSWAKdrPIEGSFKPGNIDPCLCTHLIYAFAGMQNNEI--------------------TYTHEQDLRDYEALNGLK 84
Cdd:cd06548   2 VGYFTNWGI--YGRNYFVTDDIPADKLTHINYAFADIDGDGGvvtsddeaadeaaqsvdggaDTDDQPLKGNFGQLRKLK 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  85 DKNTELKTLLAIGGWKFGPaPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSP-----PKDKHLFSVLV 159
Cdd:cd06548  80 QKNPHLKILLSIGGWTWSG-GFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGGAPgnvarPEDKENFTLLL 158
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 160 KEMRKAFEEESVEKDIPRLLLTSTGAG--IIDVIksgyKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDigK 237
Cdd:cd06548 159 KELREALDALGAETGRKYLLTIAAPAGpdKLDKL----EVAEIAKYLDFINLMTYDFHGAWSNTTGHHSNLYASPAD--P 232
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 238 SADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFilsdpsktgigaptistgppgkytdesgllayyevctflnEGATEV 317
Cdd:cd06548 233 PGGYSVDAAVNYYLSAGVPPEKLVLGVPFYGRGW----------------------------------------TGYTRY 272
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|
gi 51315803 318 WDAPQEVPYAYQGN--EWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:cd06548 273 WDEVAKAPYLYNPStkTFISYDDPRSIKAKADYVKDKGLGGVMFWELSGD 322
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
27-365 8.19e-59

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 225862 [Multi-domain]  Cd Length: 441  Bit Score: 197.65  E-value: 8.19e-59
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  27 YYTSWAK-DRPiegSFKPGNIDPCLCTHLIYAFAGMQNNEITYTHEQDLRD-----------------------YEALNG 82
Cdd:COG3325  43 YYTSWSQyDRQ---DYFPGDIPLDQLTHINYAFLDINSDGKSIESWVADEAalygvpniegveldpwsdplkghFGALFD 119
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  83 LKDKNTELKTLLAIGGWKFGPaPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGS-----PPKDKHLFSV 157
Cdd:COG3325 120 LKATYPDLKTLISIGGWSDSG-GFSDMAADDASRENFAKSAVEFMRTYGFDGVDIDWEYPGSGGDagncgRPKDKANYVL 198
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 158 LVKEMRKAFEEESVEkDIPRLLLTsTGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPYDI-- 235
Cdd:COG3325 199 LLQELRKKLDKAGVE-DGRHYQLT-IAAPASKDKLEGLNHAEIAQYVDYINIMTYDFHGAWNETLGHHAALYGTPKDPpl 276
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 236 ---GKSADLNVDSII-SYWKDHGAASE-KLIVGFPAYGHTF----ILSDPSKTGIGAPTISTGPP-GKYTDESGLLAY-- 303
Cdd:COG3325 277 angGFYVDAEVDGIDwLEEGFAGDVPPsKLVLGMPFYGRGWngvdGGSLGTCPGLYQGLDNSGIPkGTWEAGNGDKDYgk 356
                       330       340       350       360       370       380
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 51315803 304 YEVCTFLNEGA---TEVWDAPQEVPYAY--QGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:COG3325 357 AYDLDANNAGKngyERYWDDVAKAPYLYnpEKGVFISYDDPRSVKAKAEYVADNNLGGMMFWEISGD 423
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
23-387 1.76e-58

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: 196.00  E-value: 1.76e-58
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  23 QLMCYYTSWAKDRPIEGSFKPGNIDPCL--CTHLIYAFAGMQ--NNEItYTHEQDL----RDYEALNGLKDKNTELKTLL 94
Cdd:cd02873   1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGIDadTYKI-KSLNEDLdldkSHYRAITSLKRKYPHLKVLL 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  95 AIGGWKF-----GPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYP-----------GS---------RGSPP 149
Cdd:cd02873  80 SVGGDRDtdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPknkpkkvrgtfGSawhsfkklfTGDSV 159
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 150 KD------KHLFSVLVKEMRKAFEEESvekdiprLLLTSTgagIIDVIKSG--YKIPELSQSLDYIQVMTYD----LHDP 217
Cdd:cd02873 160 VDekaaehKEQFTALVRELKNALRPDG-------LLLTLT---VLPHVNSTwyFDVPAIANNVDFVNLATFDfltpERNP 229
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 218 KDG-YTgenSPLYKsPYDigKSADLNVDSIISYWKDHGAASEKLIVGFPAYGHTFILSDPS-KTGIgAPTIST---GPPG 292
Cdd:cd02873 230 EEAdYT---APIYE-LYE--RNPHHNVDYQVKYWLNQGTPASKLNLGIATYGRAWKLTKDSgITGV-PPVLETdgpGPAG 302
                       330       340       350       360       370       380       390       400
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 293 KYTDESGLLAYYEVCTFL-NEGATEVWDAP-QEV--------PYAY-----QGNE--WVGYDNVRSFKLKAQWLKDNNLG 355
Cdd:cd02873 303 PQTKTPGLLSWPEICSKLpNPANLKGADAPlRKVgdptkrfgSYAYrpadeNGEHgiWVSYEDPDTAANKAGYAKAKGLG 382
                       410       420       430
                ....*....|....*....|....*....|..
gi 51315803 356 GAVVWPLDMDDFSGSfCHQRHFPLTSTLKGDL 387
Cdd:cd02873 383 GVALFDLSLDDFRGQ-CTGDKFPILRSAKYRL 413
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
27-366 1.12e-56

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: 187.96  E-value: 1.12e-56
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  27 YYTSWAKDRPiegsfkPGNIDPCLCTHLIYAFAGMQNN----EITYTHEQDLRDYEALngLKDKNTELKTLLAIGGWKFG 102
Cdd:cd02879   8 YWPAWSEEFP------PSNIDSSLFTHLFYAFADLDPStyevVISPSDESEFSTFTET--VKRKNPSVKTLLSIGGGGSD 79
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 103 PAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPgsrgSPPKDKHLFSVLVKEMRKAFEEESVEKDIPRLLLTS 182
Cdd:cd02879  80 SSAFAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFP----SSQVEMENFGKLLEEWRAAVKDEARSSGRPPLLLTA 155
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 183 TGAGIIDVIKSG----YKIPELSQSLDYIQVMTYDLHDPKDGYTGENSPLYKSPydigkSADLNVDSIISYWKDHGAASE 258
Cdd:cd02879 156 AVYFSPILFLSDdsvsYPIEAINKNLDWVNVMAYDYYGSWESNTTGPAAALYDP-----NSNVSTDYGIKSWIKAGVPAK 230
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 259 KLIVGFPAYGHTFILSDPSktgigapTISTgppgkytdesgllayyevctflnegatevwdapqevpYAYQGNEWVGYDN 338
Cdd:cd02879 231 KLVLGLPLYGRAWTLYDTT-------TVSS-------------------------------------YVYAGTTWIGYDD 266
                       330       340
                ....*....|....*....|....*...
gi 51315803 339 VRSFKLKAQWLKDNNLGGAVVWPLDMDD 366
Cdd:cd02879 267 VQSIAVKVKYAKQKGLLGYFAWAVGYDD 294
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
24-214 3.73e-42

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: 147.14  E-value: 3.73e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  24 LMCYYTSWAKDRPiegsFKPGNIDPCLCTHLIYAFAGMQ--NNEITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKF 101
Cdd:cd00598   1 VICYYDGWSSGRG----PDPTDIPLSLCTHIIYAFAEISsdGSLNLFGDKSEEPLKGALEELASKKPGLKVLISIGGWTD 76
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 102 GPAPFsaMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDkhLFSVLVKEMRKAFEEEsvekdipRLLLT 181
Cdd:cd00598  77 SSPFT--LASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGAADNSDRE--NFITLLRELRSALGAA-------NYLLT 145
                       170       180       190
                ....*....|....*....|....*....|...
gi 51315803 182 STGAGIIDVIKSGYKIPELSQSLDYIQVMTYDL 214
Cdd:cd00598 146 IAVPASYFDLGYAYDVPAIGDYVDFVNVMTYDL 178
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
27-365 4.39e-29

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: 115.87  E-value: 4.39e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  27 YYTSWAKDRPIEGSfKPGNIDPCLCTHLIYAFAGmqnneITYTHEQDLRDYEALNGLKDKNTELKTLLAIGGWKFgpapf 106
Cdd:cd02878   5 YFEAYNLDRPCLNM-DVTQIDTSKYTHIHFAFAN-----ITSDFSVDVSSVQEQFSDFKKLKGVKKILSFGGWDF----- 73
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 107 SAMVST---------PQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSP------PKDKHLFSVLVKEMRKAF-EEES 170
Cdd:cd02878  74 STSPSTyqifrdavkPANRDTFANNVVNFVNKYNLDGVDFDWEYPGAPDIPgipagdPDDGKNYLEFLKLLKSKLpSGKS 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 171 VEKDIPR----LlltstgagiidvikSGYKIPELSQSLDYIQVMTYDLHDPKDgytgensplYKSPYDIGKSADLN---- 242
Cdd:cd02878 154 LSIAAPAsywyL--------------KGFPIKDMAKYVDYIVYMTYDLHGQWD---------YGNKWASPGCPAGNclrs 210
                       250       260       270       280       290       300       310       320
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 243 -------VDSIISYWKdHGAASEKLIVGFPAYGHTFILSDPSKTGIGAP---TISTGPPGKYTDESGLLAYYEVCTFL-- 310
Cdd:cd02878 211 hvnktetLDALSMITK-AGVPSNKVVVGVASYGRSFKMADPGCTGPGCTftgPGSGAEAGRCTCTAGYGAISEIEIIDis 289
                       330       340       350       360       370
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 51315803 311 NEGATEVWDAPQEVPYA-YQGNEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMD 365
Cdd:cd02878 290 KSKNKRWYDTDSDSDILvYDDDQWVAYMSPATKAARIEWYKGLNFGGTSDWAVDLQ 345
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
72-366 3.73e-24

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: 101.19  E-value: 3.73e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  72 QDLRDYEALNGLKDKNTelKTLLAI---GGWKFGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYpgsrgSP 148
Cdd:cd02874  43 TGLPDERLIEAAKRRGV--KPLLVItnlTNGNFDSELAHAVLSNPEARQRLINNILALAKKYGYDGVNIDFEN-----VP 115
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 149 PKDKHLFSVLVKEMRKAFEEESvekdipRLLLT----STGAGIIDVIKSGYKIPELSQSLDYIQVMTYDLHdpkdgytGE 224
Cdd:cd02874 116 PEDREAYTQFLRELSDRLHPAG------YTLSTavvpKTSADQFGNWSGAYDYAAIGKIVDFVVLMTYDWH-------WR 182
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 225 NSPlyksPydiGKSADLN-VDSIISYwkdhgAAS----EKLIVGFPAYGHTFILsdPSKTGIGAPTIStgppgkYTDESG 299
Cdd:cd02874 183 GGP----P---GPVAPIGwVERVLQY-----AVTqiprEKILLGIPLYGYDWTL--PYKKGGKASTIS------PQQAIN 242
                       250       260       270       280       290       300       310
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 51315803 300 LLAYYevctflneGATEVWDAPQEVP-YAY---QG-NEWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDD 366
Cdd:cd02874 243 LAKRY--------GAEIQYDEEAQSPfFRYvdeQGrRHEVWFEDARSLQAKFELAKEYGLRGVSYWRLGLED 306
GH18_chitobiase cd02875
Chitobiase (also known as di-N-acetylchitobiase) is a lysosomal glycosidase that hydrolyzes ...
110-369 3.61e-17

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: 82.10  E-value: 3.61e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 110 VSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGSRGSPPKDkhLFSVLVKEMRKAFEEEsvekdIPRLLLTSTGAGIID 189
Cdd:cd02875  91 ISNPTYRTQWIQQKVELAKSQFMDGINIDIEQPITKGSPEYY--ALTELVKETTKAFKKE-----NPGYQISFDVAWSPS 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 190 VI-KSGYKIPELSQSLDYIQVMTYDLHdpKDGYTGE-----NSPLYKSPYDIGKSADLNVDSiisywkdhgaasEKLIVG 263
Cdd:cd02875 164 CIdKRCYDYTGIADASDFLVVMDYDEQ--SQIWGKEciagaNSPYSQTLSGYNNFTKLGIDP------------KKLVMG 229
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 264 FPAYGHTFI-----LSD-----PSKTGIGAPTistgppgkyTDESGL-LAYYEVCTFLNEGATEV-WDAPQEVPYAY--- 328
Cdd:cd02875 230 LPWYGYDYPclngnLEDvvctiPKVPFRGANC---------SDAAGRqIPYSEIMKQINSSIGGRlWDSEQKSPFYNykd 300
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 51315803 329 -QGN-EWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDDFSG 369
Cdd:cd02875 301 kQGNlHQVWYDNPQSLSIKVAYAKNLGLKGIGMWNGDLLDYSG 343
YaaH COG3858
Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning];
101-366 1.99e-13

Spore germination protein YaaH [Cell cycle control, cell division, chromosome partitioning];


Pssm-ID: 226376 [Multi-domain]  Cd Length: 423  Bit Score: 71.31  E-value: 1.99e-13
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 101 FGPAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDWQYPGsrgspPKDKHLFSVLVKEMRKAFEEESVEkdiprlLL 180
Cdd:COG3858 177 FGGELAQLLLNNETAKNRLINNIITLLDARGYRGVNIDFENVG-----PGDRELYTDFLRQVRDALHSGGYT------VS 245
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 181 TSTGAGIIDVIKS----GYKIPELSQSLDYIQVMTYDlhdpkDGYTGeNSPLYKSPYDIGKSADLNVDSIISywkdhgaa 256
Cdd:COG3858 246 IAVAAKTSDLQVGswhgAYDYVALGKIADFVILMTYD-----WHYSG-GPPGPVASIGWVRKVIEYALTVIP-------- 311
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 257 SEKLIVGFPAYGHTFILSDPSKtGIGAPTIStgpPGKYTDESGLLayyevctflneGATEVWDAPQEVPYAYQG-----N 331
Cdd:COG3858 312 AEKVMMGIPLYGYDWTLPYDPL-GYLARAIS---PDEAIDIANRY-----------NATIQYDATSQSPFFYYVdkegrY 376
                       250       260       270
                ....*....|....*....|....*....|....*
gi 51315803 332 EWVGYDNVRSFKLKAQWLKDNNLGGAVVWPLDMDD 366
Cdd:COG3858 377 HEVWFEDARSFQTKLDLIKEYGLRGVSYWVLGQED 411
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
44-286 1.91e-12

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: 66.71  E-value: 1.91e-12
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  44 GNIDPCLCTHLIYAFAGMQNNE--ITYTHEQDLRDYeaLNGLKDKNteLKTLLAIGGWkfGPAPFSAMVSTPQNRQIFIQ 121
Cdd:cd06545  16 PTIDFSKLTHINLAFANPDANGtlNANPVRSELNSV--VNAAHAHN--VKILISLAGG--SPPEFTAALNDPAKRKALVD 89
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 122 SVIRFLRQYNFDGLNLDWQYPGSRGSPpkdkhlFSVLVKEMRKAFEEESvekdiprLLLTS-----TGAGIIDviksgyk 196
Cdd:cd06545  90 KIINYVVSYNLDGIDVDLEGPDVTFGD------YLVFIRALYAALKKEG-------KLLTAavsswNGGAVSD------- 149
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 197 ipELSQSLDYIQVMTYDlhdpKDGYTGENSPLYKSPYDIGKSAdlnvdsiISYWKDHG-AASEKLIVGFPAYGHTFILSd 275
Cdd:cd06545 150 --STLAYFDFINIMSYD----ATGPWWGDNPGQHSSYDDAVND-------LNYWNERGlASKDKLVLGLPFYGYGFYYN- 215
                       250
                ....*....|.
gi 51315803 276 psktgiGAPTI 286
Cdd:cd06545 216 ------GIPTI 220
GH18_SI-CLP cd02876
Stabilin-1 interacting chitinase-like protein (SI-CLP) is a eukaryotic chitinase-like protein ...
106-283 7.17e-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: 47.30  E-value: 7.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 106 FSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLD-WQYPGSRGSPPKDKHLFSvLVKEMRKAFEEESVEkdiprLLLtstg 184
Cdd:cd02876  83 LQSLLNDEQEREKLIKLLVTTAKKNHFDGIVLEvWSQLAAYGVPDKRKELIQ-LVIHLGETLHSANLK-----LIL---- 152
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 185 aGIIDVIKSGYKIPE--------LSQSLDYIQVMTYDlhdpkdgYTGENSPLYKSPYDIgksadlnVDSIISYW-KDHGA 255
Cdd:cd02876 153 -VIPPPREKGNQNGLftrkdfekLAPHVDGFSLMTYD-------YSSPQRPGPNAPLSW-------VRSCLELLlPESGK 217
                       170       180
                ....*....|....*....|....*...
gi 51315803 256 ASEKLIVGFPAYGHTFILSDPSKTGIGA 283
Cdd:cd02876 218 KRAKILLGLNFYGNDYTLPGGGGAITGS 245
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
91-298 9.17e-06

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  Cd Length: 312  Bit Score: 46.94  E-value: 9.17e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803  91 KTLLAIGGwkfgpAPFSAMVSTPQNRQIFIQSVIRFLRQYNFDGLNLDW-QYPGSRGSPPKDKHLFSVLvKEMRKAFEee 169
Cdd:cd02871  75 KVLISIGG-----ANGHVDLNHTAQEDNFVDSIVAIIKEYGFDGLDIDLeSGSNPLNATPVITNLISAL-KQLKDHYG-- 146
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 170 svekdiPRLLLTStgAGIIDVIKSGYkIPELSQSLDYIQVmtydLHDPKDGYTGENSPLYKSPYDIGKSADLNVDSIISY 249
Cdd:cd02871 147 ------PNFILTM--APETPYVQGGY-AAYGGIWGAYLPL----IDNLRDDLTWLNVQYYNSGGMGGCDGQSYSQGTADF 213
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 51315803 250 wkdHGAASEKLIVGFP-AYGHTFILSDPSKTGIGAPTISTGPPGKYTDES 298
Cdd:cd02871 214 ---LVALADMLLTGFPiAGNDRFPPLPADKVVIGLPASPSAAGGGYVSPS 260
GH18_EndoS-like cd06542
Endo-beta-N-acetylglucosaminidases are bacterial chitinases that hydrolyze the chitin core of ...
129-237 4.15e-03

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: 38.51  E-value: 4.15e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 51315803 129 QYNFDGLNLDWQY-PGSRGSPP-KDKHLFSVLVKEMRKAFEEESvekdipRLLltstgagIIDVIKSGYK--IPELSQSL 204
Cdd:cd06542 102 KYGLDGVDFDDEYsGYGKNGTSqPSNEAFVRLIKELRKYMGPTD------KLL-------TIDGYGQALSndGEEVSPYV 168
                        90       100       110
                ....*....|....*....|....*....|...
gi 51315803 205 DYIQVMTYDLHDPKdgyTGENSPLYKSPYDIGK 237
Cdd:cd06542 169 DYVIYQYYGSSSSS---TQRNWNTNSPKIPPEK 198
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.19
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
  • Marchler-Bauer A et al. (2015), "CDD: NCBI's conserved domain database.", Nucleic Acids Res.43(D)222-6.
  • Marchler-Bauer A et al. (2011), "CDD: a Conserved Domain Database for the functional annotation of proteins.", Nucleic Acids Res.39(D)225-9.
  • Marchler-Bauer A, Bryant SH (2004), "CD-Search: protein domain annotations on the fly.", Nucleic Acids Res.32(W)327-331.
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