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Conserved domains on  [gi|15224319|ref|NP_181889|]
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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 ...
 92-281 8.75e-79

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: 238.10  E-value: 8.75e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319  92 ITPAFFNSIMSKVGSgcPAKGFYTRQAFIAAAESFAAYKGT----VAKREIAAMLAQFSHESG------------SFCYK 155
Cdd:cd00325   1 VTEDLFNELFPHRND--PAKGFYTYDAFLAAAGSFPGFGNTgtddIRKRELAAFLAHIAHETGggwaaaggpyawGLCYI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319 156 EEIARGRYCSPS--TTYPCQPGKNYYGRGPIQITWNYNYGAAGKFLG--LPLLKDPDMVARSPTVAFQCAMWFWNKNVRP 231
Cdd:cd00325  79 EEIGCASDDCCSssTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGgkDDLLNNPDLVATDPTLAFKTAIWFWMTPQGP 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224319 232 ---------------VLSQGFGATTRRINGG-ECNGGRPAAVQSRVNHYLDFCKKLGVTPGTNLSC 281
Cdd:cd00325 159 kpschdvilsadraaGRGPGFGATINIINGGlECGGGNNAQVQNRIGYYKRFCDILGVSPGDNLDC 224
Chitin_bind_1 pfam00187
Chitin recognition protein;
30-62 2.49e-11

Chitin recognition protein;


:

Pssm-ID: 459705  Cd Length: 38  Bit Score: 57.17  E-value: 2.49e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 15224319    30 NCGTNG----CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:pfam00187   1 RCGKQAggatCPNNLCCSQYGYCGTTSDYCGDGCQSG 37
 
Name Accession Description Interval E-value
chitinase_GH19 cd00325
Glycoside hydrolase family 19, chitinase domain; Chitinases are enzymes that catalyze the ...
 92-281 8.75e-79

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: 238.10  E-value: 8.75e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319  92 ITPAFFNSIMSKVGSgcPAKGFYTRQAFIAAAESFAAYKGT----VAKREIAAMLAQFSHESG------------SFCYK 155
Cdd:cd00325   1 VTEDLFNELFPHRND--PAKGFYTYDAFLAAAGSFPGFGNTgtddIRKRELAAFLAHIAHETGggwaaaggpyawGLCYI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319 156 EEIARGRYCSPS--TTYPCQPGKNYYGRGPIQITWNYNYGAAGKFLG--LPLLKDPDMVARSPTVAFQCAMWFWNKNVRP 231
Cdd:cd00325  79 EEIGCASDDCCSssTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGgkDDLLNNPDLVATDPTLAFKTAIWFWMTPQGP 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224319 232 ---------------VLSQGFGATTRRINGG-ECNGGRPAAVQSRVNHYLDFCKKLGVTPGTNLSC 281
Cdd:cd00325 159 kpschdvilsadraaGRGPGFGATINIINGGlECGGGNNAQVQNRIGYYKRFCDILGVSPGDNLDC 224
Glyco_hydro_19 pfam00182
Chitinase class I;
91-281 8.37e-59

Chitinase class I;


Pssm-ID: 459702  Cd Length: 232  Bit Score: 187.37  E-value: 8.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319    91 VITPAFFNSIMS-KVGSGCPAKGFYTRQAFIAAAESFAAYKGT----VAKREIAAMLAQFSHE-------------SGSF 152
Cdd:pfam00182   1 IVSRSLFDQMLKhRNDDACPAKGFYTYDAFIAAANSFPGFGTTgddtARKKEIAAFFAQTSHEttggwatapdgpyAWGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319   153 CYKEE-IARGRYCSPSTTYPCQPGKNYYGRGPIQITWNYNYGAAGKFLGLPLLKDPDMVARSPTVAFQCAMWFWNKNVRP 231
Cdd:pfam00182  81 CFVREqGSPGDYCAPSAQWPCAPGKKYYGRGPIQLSYNYNYGPAGQAIGQDLLNNPDLVATDAVVSFKTAIWFWMTPQSP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224319   232 VLS---------------------QGFGATTRRINGG-ECNGGRPAAVQSRVNHYLDFCKKLGVTPGTNLSC 281
Cdd:pfam00182 161 KPSchdvitgqwtpsaadraanrvPGYGVITNIINGGlECGRGQNARVEDRIGFYRRYCGILGVPPGDNLDC 232
GH19 COG3179
Chitinase, GH19 family [Carbohydrate transport and metabolism];
89-271 5.18e-41

Chitinase, GH19 family [Carbohydrate transport and metabolism];


Pssm-ID: 442412  Cd Length: 193  Bit Score: 140.06  E-value: 5.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319  89 ASVITPAFFNSIMskvgsgcPAKGFYTRQAFIAAAES-FAAYkGTVAKREIAAMLAQFSHESGSFCYKEEIARGRYCSPS 167
Cdd:COG3179   1 GFLITEAQLRAIF-------PGASFALAQGYAPALNAaLPEF-GITTPLRLAHFLAQIAHESGGLRYLEENLNYSALQVF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319 168 TTYPCQ----------------------PGKNYYGRGPIQITWNYNYGAAGKFLGLPLLKDPDMVArSPTVAFQCAMWFW 225
Cdd:COG3179  73 GRYPDGapeaianrvyggrkdlgntapgDGWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLLA-DPEVAARSAAWFW 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15224319 226 NKN--VRPVLSQGFGATTRRINGGEcNGgrpaaVQSRVNHYLDFCKKL 271
Cdd:COG3179 152 ATRglNALADAGDFGEVTRRINGGL-NG-----LDDRRARYQRAKAVL 193
Chitin_bind_1 pfam00187
Chitin recognition protein;
30-62 2.49e-11

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 57.17  E-value: 2.49e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 15224319    30 NCGTNG----CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:pfam00187   1 RCGKQAggatCPNNLCCSQYGYCGTTSDYCGDGCQSG 37
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
 31-62 5.92e-09

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: 50.85  E-value: 5.92e-09
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15224319  31 CGTNG----CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:cd00035   2 CGSQAggppCPNNLCCSQYGYCGTGDDYCGEGCQSQ 37
ChtBD1 smart00270
Chitin binding domain;
36-62 9.96e-08

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 47.36  E-value: 9.96e-08
                           10        20
                   ....*....|....*....|....*..
gi 15224319     36 CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
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 ...
 92-281 8.75e-79

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: 238.10  E-value: 8.75e-79
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319  92 ITPAFFNSIMSKVGSgcPAKGFYTRQAFIAAAESFAAYKGT----VAKREIAAMLAQFSHESG------------SFCYK 155
Cdd:cd00325   1 VTEDLFNELFPHRND--PAKGFYTYDAFLAAAGSFPGFGNTgtddIRKRELAAFLAHIAHETGggwaaaggpyawGLCYI 78

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319 156 EEIARGRYCSPS--TTYPCQPGKNYYGRGPIQITWNYNYGAAGKFLG--LPLLKDPDMVARSPTVAFQCAMWFWNKNVRP 231
Cdd:cd00325  79 EEIGCASDDCCSssTGYPCAPGKSYYGRGPIQLSWNYNYGAASEALGgkDDLLNNPDLVATDPTLAFKTAIWFWMTPQGP 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224319 232 ---------------VLSQGFGATTRRINGG-ECNGGRPAAVQSRVNHYLDFCKKLGVTPGTNLSC 281
Cdd:cd00325 159 kpschdvilsadraaGRGPGFGATINIINGGlECGGGNNAQVQNRIGYYKRFCDILGVSPGDNLDC 224
Glyco_hydro_19 pfam00182
Chitinase class I;
91-281 8.37e-59

Chitinase class I;


Pssm-ID: 459702  Cd Length: 232  Bit Score: 187.37  E-value: 8.37e-59
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319    91 VITPAFFNSIMS-KVGSGCPAKGFYTRQAFIAAAESFAAYKGT----VAKREIAAMLAQFSHE-------------SGSF 152
Cdd:pfam00182   1 IVSRSLFDQMLKhRNDDACPAKGFYTYDAFIAAANSFPGFGTTgddtARKKEIAAFFAQTSHEttggwatapdgpyAWGY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319   153 CYKEE-IARGRYCSPSTTYPCQPGKNYYGRGPIQITWNYNYGAAGKFLGLPLLKDPDMVARSPTVAFQCAMWFWNKNVRP 231
Cdd:pfam00182  81 CFVREqGSPGDYCAPSAQWPCAPGKKYYGRGPIQLSYNYNYGPAGQAIGQDLLNNPDLVATDAVVSFKTAIWFWMTPQSP 160

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 15224319   232 VLS---------------------QGFGATTRRINGG-ECNGGRPAAVQSRVNHYLDFCKKLGVTPGTNLSC 281
Cdd:pfam00182 161 KPSchdvitgqwtpsaadraanrvPGYGVITNIINGGlECGRGQNARVEDRIGFYRRYCGILGVPPGDNLDC 232
GH19 COG3179
Chitinase, GH19 family [Carbohydrate transport and metabolism];
89-271 5.18e-41

Chitinase, GH19 family [Carbohydrate transport and metabolism];


Pssm-ID: 442412  Cd Length: 193  Bit Score: 140.06  E-value: 5.18e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319  89 ASVITPAFFNSIMskvgsgcPAKGFYTRQAFIAAAES-FAAYkGTVAKREIAAMLAQFSHESGSFCYKEEIARGRYCSPS 167
Cdd:COG3179   1 GFLITEAQLRAIF-------PGASFALAQGYAPALNAaLPEF-GITTPLRLAHFLAQIAHESGGLRYLEENLNYSALQVF 72

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 15224319 168 TTYPCQ----------------------PGKNYYGRGPIQITWNYNYGAAGKFLGLPLLKDPDMVArSPTVAFQCAMWFW 225
Cdd:COG3179  73 GRYPDGapeaianrvyggrkdlgntapgDGWRYRGRGLIQLTGRANYRAAGDALGLDLVNNPDLLA-DPEVAARSAAWFW 151

                       170       180       190       200
                ....*....|....*....|....*....|....*....|....*...
gi 15224319 226 NKN--VRPVLSQGFGATTRRINGGEcNGgrpaaVQSRVNHYLDFCKKL 271
Cdd:COG3179 152 ATRglNALADAGDFGEVTRRINGGL-NG-----LDDRRARYQRAKAVL 193
Chitin_bind_1 pfam00187
Chitin recognition protein;
30-62 2.49e-11

Chitin recognition protein;


Pssm-ID: 459705  Cd Length: 38  Bit Score: 57.17  E-value: 2.49e-11
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 15224319    30 NCGTNG----CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:pfam00187   1 RCGKQAggatCPNNLCCSQYGYCGTTSDYCGDGCQSG 37
ChtBD1 cd00035
Hevein or type 1 chitin binding domain; Hevein or type 1 chitin binding domain (ChtBD1), a ...
 31-62 5.92e-09

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: 50.85  E-value: 5.92e-09
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 15224319  31 CGTNG----CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:cd00035   2 CGSQAggppCPNNLCCSQYGYCGTGDDYCGEGCQSQ 37
ChtBD1 smart00270
Chitin binding domain;
36-62 9.96e-08

Chitin binding domain;


Pssm-ID: 214593  Cd Length: 38  Bit Score: 47.36  E-value: 9.96e-08
                           10        20
                   ....*....|....*....|....*..
gi 15224319     36 CKGNMCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:smart00270  11 CPNNLCCSQFGYCGSGDEYCGRGCQSQ 37
ChtBD1_GH19_hevein cd06921
Hevein or Type 1 chitin binding domain subfamily co-occuring with family 19 glycosyl ...
 36-61 3.44e-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: 45.94  E-value: 3.44e-07
                        10        20
                ....*....|....*....|....*.
gi 15224319  36 CKGNMCCSRWGYCGTTKAYCGTGCQS 61
Cdd:cd06921  12 CPGGLCCSQWGWCGSTDDYCGDGCQS 37
chitinase-like cd16889
chitinase-like domain; This family includes proteins such as chitinases, chitosanase, pesticin, ...
 166-231 8.70e-07

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: 46.41  E-value: 8.70e-07
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 15224319 166 PSTTYPCQPGKNYYGRGpIQITWNYNYGAAGKFLGLPLLKDPDMVARSPTVAFQCAMWFWNKNVRP 231
Cdd:cd16889  15 PTAVYGDGKDPRGYTRG-IGVTHGMLRGSTSRFPGVDTSNQTNNGASTDSQLAKLAMEGFDPAYRA 79
ChtBD1_1 cd11618
Hevein or type 1 chitin binding domain; filamentous ascomycete subfamily; Hevein or type 1 ...
 40-62 1.18e-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: 38.90  E-value: 1.18e-04
                        10        20
                ....*....|....*....|...
gi 15224319  40 MCCSRWGYCGTTKAYCGTGCQSG 62
Cdd:cd11618  17 NCCSAYGWCGNTSDHCGVGCQPG 39
 
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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