Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688  81 VTPDFFNSILNQRGDcPGKGFYTHDTFMAAANSYPSFGAS----ISKREIAAFFAHVAQETGF------------MCYIE 144
Cdd:cd00325   1 VTEDLFNELFPHRND-PAKGFYTYDAFLAAAGSFPGFGNTgtddIRKRELAAFLAHIAHETGGgwaaaggpyawgLCYIE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688 145 EIDGPAKaasgeYCDTEKPEFPCAQGKGYYGRGAIQLSWNYNYGLCGKAL--DENLLASPEKVAQDQVLAFKTAFWFWTT 222
Cdd:cd00325  80 EIGCASD-----DCCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALggKDDLLNNPDLVATDPTLAFKTAIWFWMT 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20466688 223 NVRT---------------SFKSGFGATIRAVNSR-ECSGGDsTAKAANRIKYFQDYCGKLGVAPGDNLTC 277
Cdd:cd00325 155 PQGPkpschdvilsadraaGRGPGFGATINIINGGlECGGGN-NAQVQNRIGYYKRFCDILGVSPGDNLDC 224

Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688  81 VTPDFFNSILNQRGDcPGKGFYTHDTFMAAANSYPSFGAS----ISKREIAAFFAHVAQETGF------------MCYIE 144
Cdd:cd00325   1 VTEDLFNELFPHRND-PAKGFYTYDAFLAAAGSFPGFGNTgtddIRKRELAAFLAHIAHETGGgwaaaggpyawgLCYIE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688 145 EIDGPAKaasgeYCDTEKPEFPCAQGKGYYGRGAIQLSWNYNYGLCGKAL--DENLLASPEKVAQDQVLAFKTAFWFWTT 222
Cdd:cd00325  80 EIGCASD-----DCCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALggKDDLLNNPDLVATDPTLAFKTAIWFWMT 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20466688 223 NVRT---------------SFKSGFGATIRAVNSR-ECSGGDsTAKAANRIKYFQDYCGKLGVAPGDNLTC 277
Cdd:cd00325 155 PQGPkpschdvilsadraaGRGPGFGATINIINGGlECGGGN-NAQVQNRIGYYKRFCDILGVSPGDNLDC 224

Chitinase, GH19 family [Carbohydrate transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688  81 VTPDFFNSILnqrgdcPGKGFYTHDTFMAAANS-YPSFGASiSKREIAAFFAHVAQETGFMCYIEEIDGPAKAASGEYCD 159
Cdd:COG3179   4 ITEAQLRAIF------PGASFALAQGYAPALNAaLPEFGIT-TPLRLAHFLAQIAHESGGLRYLEENLNYSALQVFGRYP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688 160 TEKPEFPCAQ---------------GKGYYGRGAIQLSWNYNYGLCGKALDENLLASPEKVAQDQVlAFKTAFWFWTTN- 223
Cdd:COG3179  77 DGAPEAIANRvyggrkdlgntapgdGWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLLADPEV-AARSAAWFWATRg 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20466688 224 -VRTSFKSGFGATIRAVNsrecsGGDSTakAANRIKYFQ 261
Cdd:COG3179 156 lNALADAGDFGEVTRRIN-----GGLNG--LDDRRARYQ 187

Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.

                        10        20
                ....*....|....*....|....*
gi 20466688  36 CASDFCCSKYGYCGTTDEFCGEGCQ 60
Cdd:cd00035  11 CPNNLCCSQYGYCGTGDDYCGEGCQ 35

Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Glycoside hydrolase family 19 chitinases are found primarily in plants (classes I, III, and IV), but some are found in bacteria. Class I and II chitinases are similar in their catalytic domains. Class I chitinases have an N-terminal cysteine-rich, chitin-binding domain which is separated from the catalytic domain by a proline and glycine-rich hinge region. Class II chitinases lack both the chitin-binding domain and the hinge region. Class IV chitinases are similar to class I chitinases, but they are smaller in size due to certain deletions. Despite lacking any significant sequence homology with lysozymes, structural analysis reveals that family 19 chitinases, together with family 46 chitosanases, are similar to several lysozymes including those from T4-phage and from goose. The structures reveal that the different enzyme groups arose from a common ancestor glycohydrolase antecedent to the prokaryotic/eukaryotic divergence.

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688  81 VTPDFFNSILNQRGDcPGKGFYTHDTFMAAANSYPSFGAS----ISKREIAAFFAHVAQETGF------------MCYIE 144
Cdd:cd00325   1 VTEDLFNELFPHRND-PAKGFYTYDAFLAAAGSFPGFGNTgtddIRKRELAAFLAHIAHETGGgwaaaggpyawgLCYIE 79

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688 145 EIDGPAKaasgeYCDTEKPEFPCAQGKGYYGRGAIQLSWNYNYGLCGKAL--DENLLASPEKVAQDQVLAFKTAFWFWTT 222
Cdd:cd00325  80 EIGCASD-----DCCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALggKDDLLNNPDLVATDPTLAFKTAIWFWMT 154

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 20466688 223 NVRT---------------SFKSGFGATIRAVNSR-ECSGGDsTAKAANRIKYFQDYCGKLGVAPGDNLTC 277
Cdd:cd00325 155 PQGPkpschdvilsadraaGRGPGFGATINIINGGlECGGGN-NAQVQNRIGYYKRFCDILGVSPGDNLDC 224

Chitinase, GH19 family [Carbohydrate transport and metabolism];

                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688  81 VTPDFFNSILnqrgdcPGKGFYTHDTFMAAANS-YPSFGASiSKREIAAFFAHVAQETGFMCYIEEIDGPAKAASGEYCD 159
Cdd:COG3179   4 ITEAQLRAIF------PGASFALAQGYAPALNAaLPEFGIT-TPLRLAHFLAQIAHESGGLRYLEENLNYSALQVFGRYP 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20466688 160 TEKPEFPCAQ---------------GKGYYGRGAIQLSWNYNYGLCGKALDENLLASPEKVAQDQVlAFKTAFWFWTTN- 223
Cdd:COG3179  77 DGAPEAIANRvyggrkdlgntapgdGWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLLADPEV-AARSAAWFWATRg 155

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 20466688 224 -VRTSFKSGFGATIRAVNsrecsGGDSTakAANRIKYFQ 261
Cdd:COG3179 156 lNALADAGDFGEVTRRIN-----GGLNG--LDDRRARYQ 187

Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins such as hevein, a major IgE-binding allergen in natural rubber latex, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.

                        10        20
                ....*....|....*....|....*
gi 20466688  36 CASDFCCSKYGYCGTTDEFCGEGCQ 60
Cdd:cd00035  11 CPNNLCCSQYGYCGTGDDYCGEGCQ 35

Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl hydrolases or with barwin domains; This subfamily includes Hevein, a major IgE-binding allergen in natural rubber latex. ChtBD1 is a lectin domain found in proteins from plants and fungi that bind N-acetylglucosamine, plant endochitinases, wound-induced proteins, and the alpha subunit of Kluyveromyces lactis killer toxin. This domain is involved in the recognition and/or binding of chitin subunits; it typically occurs N-terminal to glycosyl hydrolase domains in chitinases, together with other carbohydrate-binding domains, or by itself in tandem-repeat arrangements.

                        10        20
                ....*....|....*....|....*.
gi 20466688  36 CASDFCCSKYGYCGTTDEFCGEGCQA 61
Cdd:cd06921  12 CPGGLCCSQWGWCGSTDDYCGDGCQS 37

chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, and endolysin, which are involved in the degradation of 1,4-N-acetyl D-glucosamine linkages in chitin polymers and related activities. Chitinases are enzymes that catalyze the hydrolysis of the beta-1,4-N-acetyl-D-glucosamine linkages in chitin polymers. Chitosanase enzymes hydrolyze chitosan, a biopolymer of beta (1,4)-linked-D-glucosamine (GlcN) residues produced by partial or full deacetylation of chitin. Pesticin (Pst) is a anti-bacterial toxin produced by Yersinia pestis that acts through uptake by the target related bacteria and the hydrolysis of peptidoglycan in the periplasm. The dsDNA phages of eubacteria use endolysins or muralytic enzymes in conjunction with hollin, a small membrane protein, to degrade the peptidoglycan found in bacterial cell walls. Similarly, bacteria produce autolysins to facilitate the biosynthesis of its cell wall heteropolymer peptidoglycan and cell division.

                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*
gi 20466688 166 PCAQGKGYYGRGaIQLSWNYNYGLCGKALDENLLASPEKVAQDQVLAFKTAFWFW 220
Cdd:cd16889  20 GDGKDPRGYTRG-IGVTHGMLRGSTSRFPGVDTSNQTNNGASTDSQLAKLAMEGF 73