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Conserved domains on  [gi|2462502499|ref|XP_054189969|]
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chitinase-3-like protein 1 isoform X7 [Homo sapiens]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 248)

glycoside hydrolase family 18 protein such as chitinase, which catalyzes the random endo-hydrolysis of the 1,4-beta-linkages of N-acetylglucosamine in chitin and chitodextrins

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
GH18_chitinase-like super family cl10447
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 24-196 6.25e-100

The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant polymer of beta-1,4-linked N-acetylglucosamine (GlcNAc) which is a major component of the cell wall of fungi and the exoskeleton of arthropods. Chitinases have been identified in viruses, bacteria, fungi, protozoan parasites, insects, and plants. The structure of the GH18 domain is an eight-stranded beta/alpha barrel with a pronounced active-site cleft at the C-terminal end of the beta-barrel. The GH18 family includes chitotriosidase, chitobiase, hevamine, zymocin-alpha, narbonin, SI-CLP (stabilin-1 interacting chitinase-like protein), IDGF (imaginal disc growth factor), CFLE (cortical fragment-lytic enzyme) spore hydrolase, the type III and type V plant chitinases, the endo-beta-N-acetylglucosaminidases, and the chitolectins. The GH85 (glycosyl hydrolase, family 85) ENGases (endo-beta-N-acetylglucosaminidases) are closely related to the GH18 chitinases and are included in this alignment model.


The actual alignment was detected with superfamily member cd02872:

Pssm-ID: 471972 [Multi-domain]  Cd Length: 362  Bit Score: 296.01  E-value: 6.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  24 LVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISND--HIDTWEWND--VTLYGMLNTLKNRNPNLKTLLSVGGW 99
Cdd:cd02872     1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDgnIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 100 NFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG-RG----DKQHFTTLIKEMKAEFIKEAQPgkkqLLL 174
Cdd:cd02872    81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGqRGgppeDKENFVTLLKELREAFEPEAPR----LLL 156

                         170       180
                  ....*....|....*....|..
gi 2462502499 175 SAALSAGKVTIDSSYDIAKISQ 196
Cdd:cd02872   157 TAAVSAGKETIDAAYDIPEISK 178
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 24-196 6.25e-100

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: 296.01  E-value: 6.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  24 LVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISND--HIDTWEWND--VTLYGMLNTLKNRNPNLKTLLSVGGW 99
Cdd:cd02872     1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDgnIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 100 NFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG-RG----DKQHFTTLIKEMKAEFIKEAQPgkkqLLL 174
Cdd:cd02872    81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGqRGgppeDKENFVTLLKELREAFEPEAPR----LLL 156

                         170       180
                  ....*....|....*....|..
gi 2462502499 175 SAALSAGKVTIDSSYDIAKISQ 196
Cdd:cd02872   157 TAAVSAGKETIDAAYDIPEISK 178
Glyco_18 smart00636
Glyco_18 domain;
23-196 6.44e-66

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 208.30  E-value: 6.44e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499   23 KLVCYYTSWSQYREgdgSCFPDALDRFLCTHIIYSFANISNDHIDTW--EWNDVTLYGMLNTLKNRNPNLKTLLSVGGWN 100
Cdd:smart00636   1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIgdEWADIGNFGQLKALKKKNPGLKVLLSIGGWT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  101 FgSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG--RGDKQHFTTLIKEMKAEFIKEAQPGkKQLLLSAAL 178
Cdd:smart00636  78 E-SDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGgrGDDRENYTALLKELREALDKEGAEG-KGYLLTIAV 155

                          170
                   ....*....|....*....
gi 2462502499  179 SAGKVTIDSSYD-IAKISQ 196
Cdd:smart00636 156 PAGPDKIDKGYGdLPAIAK 174
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
23-196 6.89e-60

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 191.90  E-value: 6.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  23 KLVCYYTSWSQYREGDgscfpdALDRFLCTHIIYSFANI--SNDHIDTWEWnDVTLYGMLNTLKN-RNPNLKTLLSVGGW 99
Cdd:pfam00704   1 RIVGYYTSWGVYRNGN------FLPSDKLTHIIYAFANIdgSDGTLFIGDW-DLGNFEQLKKLKKqKNPGVKVLLSIGGW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 100 NfGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG--RGDKQHFTTLIKEMKAEFikEAQPGKKQLLLSAA 177
Cdd:pfam00704  74 T-DSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGgnPEDKENYDLLLRELRAAL--DEAKGGKKYLLSAA 150

                         170
                  ....*....|....*....
gi 2462502499 178 LSAGKVTIDSSYDIAKISQ 196
Cdd:pfam00704 151 VPASYPDLDKGYDLPKIAK 169
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
20-196 2.95e-43

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 151.22  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  20 SAYKLVCYYTSWSQYregDGSCFPDALDRFLCTHIIYSFANISND----HIDTWEWNDVTLYGM------------LNTL 83
Cdd:COG3325    17 SGKRVVGYFTQWGIY---GRNYLVKDIPASKLTHINYAFANVDPDgkcsVGDAWAKPSVDGAADdwdqplkgnfnqLKKL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  84 KNRNPNLKTLLSVGGWNfGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRG----------DKQHFTTL 153
Cdd:COG3325    94 KAKNPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGgapgnvyrpeDKANFTAL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462502499 154 IKEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDsSYDIAKISQ 196
Cdd:COG3325   173 LKELRAQLDALGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQ 214
 
Name Accession Description Interval E-value
GH18_chitolectin_chitotriosidase cd02872
This conserved domain family includes a large number of catalytically inactive chitinase-like ...
 24-196 6.25e-100

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: 296.01  E-value: 6.25e-100
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  24 LVCYYTSWSQYREGDGSCFPDALDRFLCTHIIYSFANISND--HIDTWEWND--VTLYGMLNTLKNRNPNLKTLLSVGGW 99
Cdd:cd02872     1 VVCYFTNWAQYRPGNGKFVPENIDPFLCTHIIYAFAGLNPDgnIIILDEWNDidLGLYERFNALKEKNPNLKTLLAIGGW 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 100 NFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG-RG----DKQHFTTLIKEMKAEFIKEAQPgkkqLLL 174
Cdd:cd02872    81 NFGSAKFSAMAASPENRKTFIKSAIAFLRKYGFDGLDLDWEYPGqRGgppeDKENFVTLLKELREAFEPEAPR----LLL 156

                         170       180
                  ....*....|....*....|..
gi 2462502499 175 SAALSAGKVTIDSSYDIAKISQ 196
Cdd:cd02872   157 TAAVSAGKETIDAAYDIPEISK 178
Glyco_18 smart00636
Glyco_18 domain;
23-196 6.44e-66

Glyco_18 domain;


Pssm-ID: 214753 [Multi-domain]  Cd Length: 334  Bit Score: 208.30  E-value: 6.44e-66
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499   23 KLVCYYTSWSQYREgdgSCFPDALDRFLCTHIIYSFANISNDHIDTW--EWNDVTLYGMLNTLKNRNPNLKTLLSVGGWN 100
Cdd:smart00636   1 RVVGYFTNWGVYGR---NFPVDDIPASKLTHIIYAFANIDPDGTVTIgdEWADIGNFGQLKALKKKNPGLKVLLSIGGWT 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  101 FgSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG--RGDKQHFTTLIKEMKAEFIKEAQPGkKQLLLSAAL 178
Cdd:smart00636  78 E-SDNFSSMLSDPASRKKFIDSIVSFLKKYGFDGIDIDWEYPGgrGDDRENYTALLKELREALDKEGAEG-KGYLLTIAV 155

                          170
                   ....*....|....*....
gi 2462502499  179 SAGKVTIDSSYD-IAKISQ 196
Cdd:smart00636 156 PAGPDKIDKGYGdLPAIAK 174
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
23-196 6.89e-60

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 191.90  E-value: 6.89e-60
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  23 KLVCYYTSWSQYREGDgscfpdALDRFLCTHIIYSFANI--SNDHIDTWEWnDVTLYGMLNTLKN-RNPNLKTLLSVGGW 99
Cdd:pfam00704   1 RIVGYYTSWGVYRNGN------FLPSDKLTHIIYAFANIdgSDGTLFIGDW-DLGNFEQLKKLKKqKNPGVKVLLSIGGW 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 100 NfGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG--RGDKQHFTTLIKEMKAEFikEAQPGKKQLLLSAA 177
Cdd:pfam00704  74 T-DSTGFSLMASNPASRKKFADSIVSFLRKYGFDGIDIDWEYPGgnPEDKENYDLLLRELRAAL--DEAKGGKKYLLSAA 150

                         170
                  ....*....|....*....
gi 2462502499 178 LSAGKVTIDSSYDIAKISQ 196
Cdd:pfam00704 151 VPASYPDLDKGYDLPKIAK 169
GH18_chitinase cd06548
The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant ...
 25-196 4.57e-46

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: 156.64  E-value: 4.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  25 VCYYTSWSQYreGDGSCFPDALDRFLCTHIIYSFANISNDHI-----------------DTWEWNDVTLYG---MLNTLK 84
Cdd:cd06548     2 VGYFTNWGIY--GRNYFVTDDIPADKLTHINYAFADIDGDGGvvtsddeaadeaaqsvdGGADTDDQPLKGnfgQLRKLK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  85 NRNPNLKTLLSVGGWNFgSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRG----------DKQHFTTLI 154
Cdd:cd06548    80 QKNPHLKILLSIGGWTW-SGGFSDAAATEASRAKFADSAVDFIRKYGFDGIDIDWEYPGSGgapgnvarpeDKENFTLLL 158

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462502499 155 KEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDSSyDIAKISQ 196
Cdd:cd06548   159 KELREALDALGAETGRKYLLTIAAPAGPDKLDKL-EVAEIAK 199
ChiA COG3325
Chitinase, GH18 family [Carbohydrate transport and metabolism];
20-196 2.95e-43

Chitinase, GH18 family [Carbohydrate transport and metabolism];


Pssm-ID: 442554 [Multi-domain]  Cd Length: 391  Bit Score: 151.22  E-value: 2.95e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  20 SAYKLVCYYTSWSQYregDGSCFPDALDRFLCTHIIYSFANISND----HIDTWEWNDVTLYGM------------LNTL 83
Cdd:COG3325    17 SGKRVVGYFTQWGIY---GRNYLVKDIPASKLTHINYAFANVDPDgkcsVGDAWAKPSVDGAADdwdqplkgnfnqLKKL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  84 KNRNPNLKTLLSVGGWNfGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPGRG----------DKQHFTTL 153
Cdd:COG3325    94 KAKNPNLKVLISIGGWT-WSKGFSDAAATPASRAAFVDSCVDLLRKYNFDGIDIDWEYPGSGgapgnvyrpeDKANFTAL 172

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2462502499 154 IKEMKAEFIKEAQPGKKQLLLSAALSAGKVTIDsSYDIAKISQ 196
Cdd:COG3325   173 LKELRAQLDALGAETGKHYLLTAAAPAGPDKLD-GIELPKVAQ 214
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
 24-194 1.12e-40

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: 139.44  E-value: 1.12e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  24 LVCYYTSWSQYREGDgscfPDALDRFLCTHIIYSFANIS--NDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNF 101
Cdd:cd00598     1 VICYYDGWSSGRGPD----PTDIPLSLCTHIIYAFAEISsdGSLNLFGDKSEEPLKGALEELASKKPGLKVLISIGGWTD 76

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 102 GSqrFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG---RGDKQHFTTLIKEMKAEFikeaqpGKKQLLLSAAL 178
Cdd:cd00598    77 SS--PFTLASDPASRAAFANSLVSFLKTYGFDGVDIDWEYPGaadNSDRENFITLLRELRSAL------GAANYLLTIAV 148

                         170
                  ....*....|....*.
gi 2462502499 179 SAGKVTIDSSYDIAKI 194
Cdd:cd00598   149 PASYFDLGYAYDVPAI 164
GH18_IDGF cd02873
The IDGF's (imaginal disc growth factors) are a family of growth factors identified in insects ...
 23-175 1.26e-26

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: 107.01  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  23 KLVCYYTSWSQYREGDGSCFPDALDRFL--CTHIIYSFANIsndHIDTWEW--------NDVTLYGMLNTLKNRNPNLKT 92
Cdd:cd02873     1 KLVCYYDSKSYLREGLAKMSLEDLEPALqfCTHLVYGYAGI---DADTYKIkslnedldLDKSHYRAITSLKRKYPHLKV 77

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  93 LLSVGGWNF-----GSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG------RGD--------------- 146
Cdd:cd02873    78 LLSVGGDRDtdeegENEKYLLLLESSESRNAFINSAHSLLKTYGFDGLDLAWQFPKnkpkkvRGTfgsawhsfkklftgd 157

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2462502499 147 ----------KQHFTTLIKEMKAEFikeaQPGKKQLLLS 175
Cdd:cd02873   158 svvdekaaehKEQFTALVRELKNAL----RPDGLLLTLT 192
GH18_plant_chitinase_class_V cd02879
The class V plant chitinases have a glycosyl hydrolase family 18 (GH18) domain, but lack the ...
 27-177 2.67e-26

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: 103.98  E-value: 2.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  27 YYTSWSQYREgdgscfPDALDRFLCTHIIYSFANI--SNDHIDTWEWNDVTLYGMLNTLKNRNPNLKTLLSVGGWNFGSQ 104
Cdd:cd02879     8 YWPAWSEEFP------PSNIDSSLFTHLFYAFADLdpSTYEVVISPSDESEFSTFTETVKRKNPSVKTLLSIGGGGSDSS 81

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462502499 105 RFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYP-GRGDKQHFTTLIKEMKAEFIKEAQ-PGKKQLLLSAA 177
Cdd:cd02879    82 AFAAMASDPTARKAFINSSIKVARKYGFDGLDLDWEFPsSQVEMENFGKLLEEWRAAVKDEARsSGRPPLLLTAA 156
GH18_zymocin_alpha cd02878
Zymocin, alpha subunit. Zymocin is a heterotrimeric enzyme that inhibits yeast cell cycle ...
 23-180 2.16e-11

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: 63.10  E-value: 2.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  23 KLVCYYTSWSQYRegdgSCF---PDALDRFLCTHIIYSFANISNDhidtWEWNDVTLYGMLNTLKNRNpNLKTLLSVGGW 99
Cdd:cd02878     1 KNIAYFEAYNLDR----PCLnmdVTQIDTSKYTHIHFAFANITSD----FSVDVSSVQEQFSDFKKLK-GVKKILSFGGW 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499 100 NFGS-----QRFSKiASNTQSRRTFIKSVPPFLRTHGFDGLDLAWLYPG-----------RGDKQHFTTLIKEMKAEFik 163
Cdd:cd02878    72 DFSTspstyQIFRD-AVKPANRDTFANNVVNFVNKYNLDGVDFDWEYPGapdipgipagdPDDGKNYLEFLKLLKSKL-- 148

                         170
                  ....*....|....*..
gi 2462502499 164 eaqPGKKqlLLSAALSA 180
Cdd:cd02878   149 ---PSGK--SLSIAAPA 160
GH18_CFLE_spore_hydrolase cd02874
Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial ...
 89-196 3.23e-04

Cortical fragment-lytic enzyme (CFLE) is a peptidoglycan hydrolase involved in bacterial endospore germination. CFLE is expressed as an inactive preprotein (called SleB) in the forespore compartment of sporulating cells. SleB translocates across the forespore inner membrane and is deposited as a mature enzyme in the cortex layer of the spore. As part of a sensory mechanism capable of initiating germination, CFLE degrades a spore-specific peptidoglycan constituent called muramic-acid delta-lactam that comprises the outer cortex. CFLE has a C-terminal glycosyl hydrolase family 18 (GH18) catalytic domain as well as two N-terminal LysM peptidoglycan-binding domains. In addition to SleB, this family includes YaaH, YdhD, and YvbX from Bacillus subtilis.


Pssm-ID: 119353 [Multi-domain]  Cd Length: 313  Bit Score: 41.48  E-value: 3.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  89 NLKTLLSV---GGWNFGSQRFSKIASNTQSRRTFIKSVPPFLRTHGFDGL--DLAWLYPgrGDKQHFTTLIKEMKAEFik 163
Cdd:cd02874    58 GVKPLLVItnlTNGNFDSELAHAVLSNPEARQRLINNILALAKKYGYDGVniDFENVPP--EDREAYTQFLRELSDRL-- 133

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 2462502499 164 eaqpGKKQLLLSAALSAGKVTIDSS-----YDIAKISQ 196
Cdd:cd02874   134 ----HPAGYTLSTAVVPKTSADQFGnwsgaYDYAAIGK 167
GH18_narbonin cd06544
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ...
 83-165 2.71e-03

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: 38.12  E-value: 2.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462502499  83 LKNRNPNLKTLLSVGGWNFGSQ-RFSKIASNTQSRRTFIKSVPPFLRTHGFDGLDLawlypgrgDKQHFTT--------- 152
Cdd:cd06544    64 IKAQHPNVKVVISIGGRGVQNNpTPFDPSNVDSWVSNAVSSLTSIIQTYNLDGIDI--------DYEHFPAdpdtfveci 135

                          90
                  ....*....|....*.
gi 2462502499 153 --LIKEMKAE-FIKEA 165
Cdd:cd06544   136 gqLITELKNNgVIKVA 151
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
 91-161 6.62e-03

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: 37.31  E-value: 6.62e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462502499  91 KTLLSVGGWNFGSQRFskiasNTQSRRTFIKSVPPFLRTHGFDGLDLAW-----LYPGRGDKQHFTTLIKEMKAEF 161
Cdd:cd02871    75 KVLISIGGANGHVDLN-----HTAQEDNFVDSIVAIIKEYGFDGLDIDLesgsnPLNATPVITNLISALKQLKDHY 145
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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