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Conserved domains on  [gi|15224310|ref|NP_181886|]
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Chitinase family protein [Arabidopsis thaliana]

Protein Classification

ChtBD1 and chitinase_GH19 domain-containing protein( domain architecture ID 10445992)

ChtBD1 and chitinase_GH19 domain-containing protein

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
chitinase_GH19 cd00325
Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the ...
73-265 4.32e-71

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.


:

Pssm-ID: 381595 [Multi-domain]  Cd Length: 224  Bit Score: 217.68  E-value: 4.32e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310  73 VTQIFFNNIINQAGNgcAGKSFYTRDSFINATNTFPSFANTVT----RREIATMFAHFTYETG------------HFCYI 136
Cdd:cd00325   1 VTEDLFNELFPHRND--PAKGFYTYDAFLAAAGSFPGFGNTGTddirKRELAAFLAHIAHETGggwaaaggpyawGLCYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310 137 EEINGASRVmCDQNNRQYPCAPAKSYHGRGPLLLSWNFNYGACGQSLG--LDLLRQPELVSSNPVVAFRTALWFWMKSVR 214
Cdd:cd00325  79 EEIGCASDD-CCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGgkDDLLNNPDLVATDPTLAFKTAIWFWMTPQG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224310 215 P---------------VLNQGFGATIRAISG-FDCDGRNLGGVNARIGYYRDYCGQLGLDPGANITC 265
Cdd:cd00325 158 PkpschdvilsadraaGRGPGFGATINIINGgLECGGGNNAQVQNRIGYYKRFCDILGVSPGDNLDC 224
Chitin_bind_1 pfam00187
Chitin recognition protein;
29-55 1.26e-10

Chitin recognition protein;


:

Pssm-ID: 459705  Cd Length: 38  Bit Score: 55.25  E-value: 1.26e-10
                          10        20
                  ....*....|....*....|....*..
gi 15224310    29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:pfam00187  11 CPNNLCCSQYGYCGTTSDYCGDGCQSG 37
 
Name Accession Description Interval E-value
chitinase_GH19 cd00325
Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the ...
73-265 4.32e-71

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.


Pssm-ID: 381595 [Multi-domain]  Cd Length: 224  Bit Score: 217.68  E-value: 4.32e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310  73 VTQIFFNNIINQAGNgcAGKSFYTRDSFINATNTFPSFANTVT----RREIATMFAHFTYETG------------HFCYI 136
Cdd:cd00325   1 VTEDLFNELFPHRND--PAKGFYTYDAFLAAAGSFPGFGNTGTddirKRELAAFLAHIAHETGggwaaaggpyawGLCYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310 137 EEINGASRVmCDQNNRQYPCAPAKSYHGRGPLLLSWNFNYGACGQSLG--LDLLRQPELVSSNPVVAFRTALWFWMKSVR 214
Cdd:cd00325  79 EEIGCASDD-CCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGgkDDLLNNPDLVATDPTLAFKTAIWFWMTPQG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224310 215 P---------------VLNQGFGATIRAISG-FDCDGRNLGGVNARIGYYRDYCGQLGLDPGANITC 265
Cdd:cd00325 158 PkpschdvilsadraaGRGPGFGATINIINGgLECGGGNNAQVQNRIGYYKRFCDILGVSPGDNLDC 224
Glyco_hydro_19 pfam00182
Chitinase class I;
72-265 3.82e-52

Chitinase class I;


Pssm-ID: 459702  Cd Length: 232  Bit Score: 169.65  E-value: 3.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310    72 IVTQIFFNNII-NQAGNGCAGKSFYTRDSFINATNTFPSFANT----VTRREIATMFAHFTYET-------------GHF 133
Cdd:pfam00182   1 IVSRSLFDQMLkHRNDDACPAKGFYTYDAFIAAANSFPGFGTTgddtARKKEIAAFFAQTSHETtggwatapdgpyaWGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310   134 CYIEEiNGASRVMCdQNNRQYPCAPAKSYHGRGPLLLSWNFNYGACGQSLGLDLLRQPELVSSNPVVAFRTALWFWMKSV 213
Cdd:pfam00182  81 CFVRE-QGSPGDYC-APSAQWPCAPGKKYYGRGPIQLSYNYNYGPAGQAIGQDLLNNPDLVATDAVVSFKTAIWFWMTPQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224310   214 RP-------VLNQ--------------GFGATIRAISG-FDCDGRNLGGVNARIGYYRDYCGQLGLDPGANITC 265
Cdd:pfam00182 159 SPkpschdvITGQwtpsaadraanrvpGYGVITNIINGgLECGRGQNARVEDRIGFYRRYCGILGVPPGDNLDC 232
GH19 COG3179
Chitinase, GH19 family [Carbohydrate transport and metabolism];
72-249 2.97e-28

Chitinase, GH19 family [Carbohydrate transport and metabolism];


Pssm-ID: 442412  Cd Length: 193  Bit Score: 106.54  E-value: 2.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310  72 IVTQIFFNNIINQAgngcagkSFYTRDSFINATN-TFPSFANTvTRREIATMFAHFTYETGHFCYIEEINGASRV----- 145
Cdd:COG3179   3 LITEAQLRAIFPGA-------SFALAQGYAPALNaALPEFGIT-TPLRLAHFLAQIAHESGGLRYLEENLNYSALqvfgr 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310 146 MCDQNNRQYPC------------APA--KSYHGRGPLLLSWNFNYGACGQSLGLDLLRQPELVsSNPVVAFRTALWFWM- 210
Cdd:COG3179  75 YPDGAPEAIANrvyggrkdlgntAPGdgWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLL-ADPEVAARSAAWFWAt 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15224310 211 KSVRPVLNQG-FGATIRAISGfdcdGRNlgGVNARIGYYR 249
Cdd:COG3179 154 RGLNALADAGdFGEVTRRING----GLN--GLDDRRARYQ 187
Chitin_bind_1 pfam00187
Chitin recognition protein;
29-55 1.26e-10

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 55.25  E-value: 1.26e-10
                          10        20
                  ....*....|....*....|....*..
gi 15224310    29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:pfam00187  11 CPNNLCCSQYGYCGTTSDYCGDGCQSG 37
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
29-55 1.16e-08

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.


Pssm-ID: 211311  Cd Length: 39  Bit Score: 49.69  E-value: 1.16e-08
                        10        20
                ....*....|....*....|....*..
gi 15224310  29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:cd00035  11 CPNNLCCSQYGYCGTGDDYCGEGCQSQ 37
ChtBD1 smart00270
Chitin binding domain;
29-55 2.71e-08

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 48.90  E-value: 2.71e-08
                           10        20
                   ....*....|....*....|....*..
gi 15224310     29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:smart00270  11 CPNNLCCSQFGYCGSGDEYCGRGCQSQ 37
 
Name Accession Description Interval E-value
chitinase_GH19 cd00325
Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the ...
73-265 4.32e-71

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.


Pssm-ID: 381595 [Multi-domain]  Cd Length: 224  Bit Score: 217.68  E-value: 4.32e-71
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310  73 VTQIFFNNIINQAGNgcAGKSFYTRDSFINATNTFPSFANTVT----RREIATMFAHFTYETG------------HFCYI 136
Cdd:cd00325   1 VTEDLFNELFPHRND--PAKGFYTYDAFLAAAGSFPGFGNTGTddirKRELAAFLAHIAHETGggwaaaggpyawGLCYI 78
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310 137 EEINGASRVmCDQNNRQYPCAPAKSYHGRGPLLLSWNFNYGACGQSLG--LDLLRQPELVSSNPVVAFRTALWFWMKSVR 214
Cdd:cd00325  79 EEIGCASDD-CCSSSTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGgkDDLLNNPDLVATDPTLAFKTAIWFWMTPQG 157
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 15224310 215 P---------------VLNQGFGATIRAISG-FDCDGRNLGGVNARIGYYRDYCGQLGLDPGANITC 265
Cdd:cd00325 158 PkpschdvilsadraaGRGPGFGATINIINGgLECGGGNNAQVQNRIGYYKRFCDILGVSPGDNLDC 224
Glyco_hydro_19 pfam00182
Chitinase class I;
72-265 3.82e-52

Chitinase class I;


Pssm-ID: 459702  Cd Length: 232  Bit Score: 169.65  E-value: 3.82e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310    72 IVTQIFFNNII-NQAGNGCAGKSFYTRDSFINATNTFPSFANT----VTRREIATMFAHFTYET-------------GHF 133
Cdd:pfam00182   1 IVSRSLFDQMLkHRNDDACPAKGFYTYDAFIAAANSFPGFGTTgddtARKKEIAAFFAQTSHETtggwatapdgpyaWGY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310   134 CYIEEiNGASRVMCdQNNRQYPCAPAKSYHGRGPLLLSWNFNYGACGQSLGLDLLRQPELVSSNPVVAFRTALWFWMKSV 213
Cdd:pfam00182  81 CFVRE-QGSPGDYC-APSAQWPCAPGKKYYGRGPIQLSYNYNYGPAGQAIGQDLLNNPDLVATDAVVSFKTAIWFWMTPQ 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 15224310   214 RP-------VLNQ--------------GFGATIRAISG-FDCDGRNLGGVNARIGYYRDYCGQLGLDPGANITC 265
Cdd:pfam00182 159 SPkpschdvITGQwtpsaadraanrvpGYGVITNIINGgLECGRGQNARVEDRIGFYRRYCGILGVPPGDNLDC 232
GH19 COG3179
Chitinase, GH19 family [Carbohydrate transport and metabolism];
72-249 2.97e-28

Chitinase, GH19 family [Carbohydrate transport and metabolism];


Pssm-ID: 442412  Cd Length: 193  Bit Score: 106.54  E-value: 2.97e-28
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310  72 IVTQIFFNNIINQAgngcagkSFYTRDSFINATN-TFPSFANTvTRREIATMFAHFTYETGHFCYIEEINGASRV----- 145
Cdd:COG3179   3 LITEAQLRAIFPGA-------SFALAQGYAPALNaALPEFGIT-TPLRLAHFLAQIAHESGGLRYLEENLNYSALqvfgr 74
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224310 146 MCDQNNRQYPC------------APA--KSYHGRGPLLLSWNFNYGACGQSLGLDLLRQPELVsSNPVVAFRTALWFWM- 210
Cdd:COG3179  75 YPDGAPEAIANrvyggrkdlgntAPGdgWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLL-ADPEVAARSAAWFWAt 153
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 15224310 211 KSVRPVLNQG-FGATIRAISGfdcdGRNlgGVNARIGYYR 249
Cdd:COG3179 154 RGLNALADAGdFGEVTRRING----GLN--GLDDRRARYQ 187
Chitin_bind_1 pfam00187
Chitin recognition protein;
29-55 1.26e-10

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 55.25  E-value: 1.26e-10
                          10        20
                  ....*....|....*....|....*..
gi 15224310    29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:pfam00187  11 CPNNLCCSQYGYCGTTSDYCGDGCQSG 37
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
29-55 1.16e-08

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.


Pssm-ID: 211311  Cd Length: 39  Bit Score: 49.69  E-value: 1.16e-08
                        10        20
                ....*....|....*....|....*..
gi 15224310  29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:cd00035  11 CPNNLCCSQYGYCGTGDDYCGEGCQSQ 37
ChtBD1 smart00270
Chitin binding domain;
29-55 2.71e-08

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 48.90  E-value: 2.71e-08
                           10        20
                   ....*....|....*....|....*..
gi 15224310     29 CAPNLCCSQFGYCGTTADYCGSTCQSG 55
Cdd:smart00270  11 CPNNLCCSQFGYCGSGDEYCGRGCQSQ 37
ChtBD1_GH19_hevein cd06921
Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl ...
29-54 7.24e-07

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.


Pssm-ID: 211312  Cd Length: 40  Bit Score: 44.79  E-value: 7.24e-07
                        10        20
                ....*....|....*....|....*.
gi 15224310  29 CAPNLCCSQFGYCGTTADYCGSTCQS 54
Cdd:cd06921  12 CPGGLCCSQWGWCGSTDDYCGDGCQS 37
ChtBD1_1 cd11618
Hevein or type 1 chitin binding domain; filamentous ascomycete subfamily; Hevein or type 1 ...
34-55 2.04e-04

Hevein or type 1 chitin binding domain; filamentous ascomycete subfamily; 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.


Pssm-ID: 211316  Cd Length: 44  Bit Score: 38.13  E-value: 2.04e-04
                        10        20
                ....*....|....*....|..
gi 15224310  34 CCSQFGYCGTTADYCGSTCQSG 55
Cdd:cd11618  18 CCSAYGWCGNTSDHCGVGCQPG 39
chitinase-like cd16889
chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, ...
154-215 1.21e-03

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.


Pssm-ID: 381610  Cd Length: 105  Bit Score: 37.55  E-value: 1.21e-03
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224310 154 YPCAPAKSYHGRGPLLlSWNFNYGACGQSLGLDLLRQPELVSSNPVVAFRTALWFWMKSVRP 215
Cdd:cd16889  19 YGDGKDPRGYTRGIGV-THGMLRGSTSRFPGVDTSNQTNNGASTDSQLAKLAMEGFDPAYRA 79
 
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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