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Conserved domains on  [gi|255740203|gb|ACU31858|]
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acidic endochitinase [Nepenthes ampullaria]

Protein Classification

glycoside hydrolase family 18 protein( domain architecture ID 10120849)

glycoside hydrolase family 18 protein similar to Candida albicans chitinase 3 that catalyzes random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
GH18_hevamine_XipI_class_III cd02877
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant ...
27-290 8.57e-132

This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.


:

Pssm-ID: 119356 [Multi-domain]  Cd Length: 280  Bit Score: 375.04  E-value: 8.57e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  27 SGIAVYWGQNGNEGTLSDTCATGNYNYVLVSFLTTFGNGQTPVLNLAGHCDPSSN-GCTGLSTDITSCQNQGIKVLLSLG 105
Cdd:cd02877    1 GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGSTYpNCPQLGADIKHCQSKGKKVLLSIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 106 GASGSYSLVSTDDADQVAAYLWNNYLGGQ--SDSRPLGSAVLDGIDFDIESGSDNYWGDLATALKNYSQS-----VLVSA 178
Cdd:cd02877   81 GAGGSYSLSSDADAKDFADYLWNAFGGGTdsGVPRPFGDAVVDGFDFDIEHGSPENYDALAKRLRSLFASdpskkYYLTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 179 APQCPYPDAHLDLAIATGIFDYVWVQFYNNEQCEYVTDDA-NLLSAWNQWTSSQANV----VFLGLPASTDAASSGYISP 253
Cdd:cd02877  161 APQCPYPDASLGDAIATGLFDFIFVQFYNNPCCSYASGNAsGFNFNWDTWTSWAKATsnakVFLGLPASPEAAGSGYVDP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 255740203 254 DVLISQVLPSIKASSKYGGVMLWSKYYD---NGYSSAIKD 290
Cdd:cd02877  241 SELASLVLPVKQKSPNFGGVMLWDASQDkqgTGYSSKIKD 280
 
Name Accession Description Interval E-value
GH18_hevamine_XipI_class_III cd02877
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant ...
27-290 8.57e-132

This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.


Pssm-ID: 119356 [Multi-domain]  Cd Length: 280  Bit Score: 375.04  E-value: 8.57e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  27 SGIAVYWGQNGNEGTLSDTCATGNYNYVLVSFLTTFGNGQTPVLNLAGHCDPSSN-GCTGLSTDITSCQNQGIKVLLSLG 105
Cdd:cd02877    1 GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGSTYpNCPQLGADIKHCQSKGKKVLLSIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 106 GASGSYSLVSTDDADQVAAYLWNNYLGGQ--SDSRPLGSAVLDGIDFDIESGSDNYWGDLATALKNYSQS-----VLVSA 178
Cdd:cd02877   81 GAGGSYSLSSDADAKDFADYLWNAFGGGTdsGVPRPFGDAVVDGFDFDIEHGSPENYDALAKRLRSLFASdpskkYYLTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 179 APQCPYPDAHLDLAIATGIFDYVWVQFYNNEQCEYVTDDA-NLLSAWNQWTSSQANV----VFLGLPASTDAASSGYISP 253
Cdd:cd02877  161 APQCPYPDASLGDAIATGLFDFIFVQFYNNPCCSYASGNAsGFNFNWDTWTSWAKATsnakVFLGLPASPEAAGSGYVDP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 255740203 254 DVLISQVLPSIKASSKYGGVMLWSKYYD---NGYSSAIKD 290
Cdd:cd02877  241 SELASLVLPVKQKSPNFGGVMLWDASQDkqgTGYSSKIKD 280
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
29-281 1.53e-23

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 97.53  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203   29 IAVYWGQNGNEGtLSDTCATGNYNYVLVSFLTTFG-NGQTPVLNLAghcdpssNGCTGLSTDITSCQNQGIKVLLSLGGA 107
Cdd:pfam00704   2 IVGYYTSWGVYR-NGNFLPSDKLTHIIYAFANIDGsDGTLFIGDWD-------LGNFEQLKKLKKQKNPGVKVLLSIGGW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  108 SGS--YSLVSTDDAD--QVAAYLWNNYlggqsdsRPLGsavLDGIDFDIESGSDNY-----WGDLATALKN------YSQ 172
Cdd:pfam00704  74 TDStgFSLMASNPASrkKFADSIVSFL-------RKYG---FDGIDIDWEYPGGNPedkenYDLLLRELRAaldeakGGK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  173 SVLVSAAPQCPYPDAH--LDLAIATGIFDYVWVQFYN-NEQCEYVTDDANLLSAWNQWTSS-----------QANVVFLG 238
Cdd:pfam00704 144 KYLLSAAVPASYPDLDkgYDLPKIAKYLDFINVMTYDfHGSWDNVTGHHAPLYGGGSYNVDyavkyylkqgvPASKLVLG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  239 LPAST-------------------------------------DAASSGYI----------SPDVLISQVlPSIKAsSKYG 271
Cdd:pfam00704 224 VPFYGrswtlvngsgntwedgvlaykeicnllkdngatvvwdDVAKAPYVydgdqfitydDPRSIATKV-DYVKA-KGLG 301
                         330
                  ....*....|
gi 255740203  272 GVMLWSKYYD 281
Cdd:pfam00704 302 GVMIWSLDAD 311
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
50-292 1.20e-11

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 64.77  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  50 NYNYVLVSFLTTFGNGQ-TPVLNLaghcDPSSNGCTGLS-----TDITSCQNQGIKVLLSLGGASGSYSLVSTDDADQVA 123
Cdd:COG3469  239 KYDVINVAFAEPTGATNgTVTFTL----DPGSSSPGGYTdaqfkADIAALQAQGKKVLLSIGGANGTVQLNTAAAADNFV 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 124 AylwnnylggqSDSRPLGSAVLDGIDFDIESGSDNYWGD---------LATALK----NYSQSVLVSAAPQCPY------ 184
Cdd:COG3469  315 N----------SVIALIDEYGFDGLDIDLEGGSNSLNAGdtdtpvitnLISALKqlkaKYGPGFVLTMAPETPYvqggyv 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 185 -----PDAHLDLAIAT-GIFDYVWVQFYNNeQCEYVTDDAN---------------LLSAWNQWTSSQ------ANVVFL 237
Cdd:COG3469  385 ayggiWGAYLPVILALrDILTLLHVQYYNS-GSMLGLDGQVysqgtvdflvamadmLLEGFPVAGNSNgfpglrPDQVAI 463
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255740203 238 GLPASTDAASSGYISPDVLIS--------QVLPSIKASSKY---GGVMLWSKYYDNGYSSAIKDSV 292
Cdd:COG3469  464 GLPASPSAAGGGYVSPANVNKaldcltkgTNCGSYKPRGTYpglRGLMTWSINWDASNGYEFSNNV 529
 
Name Accession Description Interval E-value
GH18_hevamine_XipI_class_III cd02877
This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant ...
27-290 8.57e-132

This conserved domain family includes xylanase inhibitor Xip-I, and the class III plant chitinases such as hevamine, concanavalin B, and PPL2, all of which have a glycosyl hydrolase family 18 (GH18) domain. Hevamine is a class III endochitinase that hydrolyzes the linear polysaccharide chains of chitin and peptidoglycan and is important for defense against pathogenic bacteria and fungi. PPL2 (Parkia platycephala lectin 2) is a class III chitinase from Parkia platycephala seeds that hydrolyzes beta(1-4) glycosidic bonds linking 2-acetoamido-2-deoxy-beta-D-glucopyranose units in chitin.


Pssm-ID: 119356 [Multi-domain]  Cd Length: 280  Bit Score: 375.04  E-value: 8.57e-132
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  27 SGIAVYWGQNGNEGTLSDTCATGNYNYVLVSFLTTFGNGQTPVLNLAGHCDPSSN-GCTGLSTDITSCQNQGIKVLLSLG 105
Cdd:cd02877    1 GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGSTYpNCPQLGADIKHCQSKGKKVLLSIG 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 106 GASGSYSLVSTDDADQVAAYLWNNYLGGQ--SDSRPLGSAVLDGIDFDIESGSDNYWGDLATALKNYSQS-----VLVSA 178
Cdd:cd02877   81 GAGGSYSLSSDADAKDFADYLWNAFGGGTdsGVPRPFGDAVVDGFDFDIEHGSPENYDALAKRLRSLFASdpskkYYLTA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 179 APQCPYPDAHLDLAIATGIFDYVWVQFYNNEQCEYVTDDA-NLLSAWNQWTSSQANV----VFLGLPASTDAASSGYISP 253
Cdd:cd02877  161 APQCPYPDASLGDAIATGLFDFIFVQFYNNPCCSYASGNAsGFNFNWDTWTSWAKATsnakVFLGLPASPEAAGSGYVDP 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 255740203 254 DVLISQVLPSIKASSKYGGVMLWSKYYD---NGYSSAIKD 290
Cdd:cd02877  241 SELASLVLPVKQKSPNFGGVMLWDASQDkqgTGYSSKIKD 280
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
29-281 1.53e-23

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 97.53  E-value: 1.53e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203   29 IAVYWGQNGNEGtLSDTCATGNYNYVLVSFLTTFG-NGQTPVLNLAghcdpssNGCTGLSTDITSCQNQGIKVLLSLGGA 107
Cdd:pfam00704   2 IVGYYTSWGVYR-NGNFLPSDKLTHIIYAFANIDGsDGTLFIGDWD-------LGNFEQLKKLKKQKNPGVKVLLSIGGW 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  108 SGS--YSLVSTDDAD--QVAAYLWNNYlggqsdsRPLGsavLDGIDFDIESGSDNY-----WGDLATALKN------YSQ 172
Cdd:pfam00704  74 TDStgFSLMASNPASrkKFADSIVSFL-------RKYG---FDGIDIDWEYPGGNPedkenYDLLLRELRAaldeakGGK 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  173 SVLVSAAPQCPYPDAH--LDLAIATGIFDYVWVQFYN-NEQCEYVTDDANLLSAWNQWTSS-----------QANVVFLG 238
Cdd:pfam00704 144 KYLLSAAVPASYPDLDkgYDLPKIAKYLDFINVMTYDfHGSWDNVTGHHAPLYGGGSYNVDyavkyylkqgvPASKLVLG 223
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  239 LPAST-------------------------------------DAASSGYI----------SPDVLISQVlPSIKAsSKYG 271
Cdd:pfam00704 224 VPFYGrswtlvngsgntwedgvlaykeicnllkdngatvvwdDVAKAPYVydgdqfitydDPRSIATKV-DYVKA-KGLG 301
                         330
                  ....*....|
gi 255740203  272 GVMLWSKYYD 281
Cdd:pfam00704 302 GVMIWSLDAD 311
GH18_chitinase_D-like cd02871
GH18 domain of Chitinase D (ChiD). ChiD, a chitinase found in Bacillus circulans, hydrolyzes ...
51-292 2.65e-18

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: 83.15  E-value: 2.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  51 YNYVLVSFLTTFGNGQTPVLNLAGHCdPSSNGCTGLSTDITSCQNQGIKVLLSLGGASGSYSLVSTDDADQVAaylwnny 130
Cdd:cd02871   28 YNVINVAFAEPTSDGGGEVTFNNGSS-PGGYSPAEFKADIKALQAKGKKVLISIGGANGHVDLNHTAQEDNFV------- 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 131 lggqsDSrpLGSAV----LDGIDFDIESGSDNYWGD-----LATALK----NYSQSVLVSAAPQCPY---------PDAH 188
Cdd:cd02871  100 -----DS--IVAIIkeygFDGLDIDLESGSNPLNATpvitnLISALKqlkdHYGPNFILTMAPETPYvqggyaaygGIWG 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 189 LDLAIATGIFDYVW---VQFYNNEqcEYVTDDANLLS----------AW--NQWTSSQANVVF---------LGLPASTD 244
Cdd:cd02871  173 AYLPLIDNLRDDLTwlnVQYYNSG--GMGGCDGQSYSqgtadflvalADmlLTGFPIAGNDRFpplpadkvvIGLPASPS 250
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 255740203 245 AASSGYISPDVLISQVL--------PSIKASSKYG---GVMLWSKYYDNGYSSAIKDSV 292
Cdd:cd02871  251 AAGGGYVSPSEVIKALDclmkgtncGSYYPAGGYPslrGLMTWSINWDATNNYEFSKNY 309
Chi1 COG3469
Chitinase [Carbohydrate transport and metabolism];
50-292 1.20e-11

Chitinase [Carbohydrate transport and metabolism];


Pssm-ID: 442692 [Multi-domain]  Cd Length: 534  Bit Score: 64.77  E-value: 1.20e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  50 NYNYVLVSFLTTFGNGQ-TPVLNLaghcDPSSNGCTGLS-----TDITSCQNQGIKVLLSLGGASGSYSLVSTDDADQVA 123
Cdd:COG3469  239 KYDVINVAFAEPTGATNgTVTFTL----DPGSSSPGGYTdaqfkADIAALQAQGKKVLLSIGGANGTVQLNTAAAADNFV 314
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 124 AylwnnylggqSDSRPLGSAVLDGIDFDIESGSDNYWGD---------LATALK----NYSQSVLVSAAPQCPY------ 184
Cdd:COG3469  315 N----------SVIALIDEYGFDGLDIDLEGGSNSLNAGdtdtpvitnLISALKqlkaKYGPGFVLTMAPETPYvqggyv 384
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 185 -----PDAHLDLAIAT-GIFDYVWVQFYNNeQCEYVTDDAN---------------LLSAWNQWTSSQ------ANVVFL 237
Cdd:COG3469  385 ayggiWGAYLPVILALrDILTLLHVQYYNS-GSMLGLDGQVysqgtvdflvamadmLLEGFPVAGNSNgfpglrPDQVAI 463
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255740203 238 GLPASTDAASSGYISPDVLIS--------QVLPSIKASSKY---GGVMLWSKYYDNGYSSAIKDSV 292
Cdd:COG3469  464 GLPASPSAAGGGYVSPANVNKaldcltkgTNCGSYKPRGTYpglRGLMTWSINWDASNGYEFSNNV 529
GH18_chitinase-like cd00598
The GH18 (glycosyl hydrolase, family 18) type II chitinases hydrolyze chitin, an abundant ...
29-207 4.24e-07

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: 49.68  E-value: 4.24e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  29 IAVYWGQNGNE-GTLSDTCATGNYNYVLVSFLTTFGNGQTPVlnlaghcdPSSNGCTGLSTDITS--CQNQGIKVLLSLG 105
Cdd:cd00598    1 VICYYDGWSSGrGPDPTDIPLSLCTHIIYAFAEISSDGSLNL--------FGDKSEEPLKGALEElaSKKPGLKVLISIG 72
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 106 GASGSYSLVSTDDADQVAAYLWN--NYLGGQSdsrplgsavLDGIDFDIE-SGSDNYWG---------DLATALKnySQS 173
Cdd:cd00598   73 GWTDSSPFTLASDPASRAAFANSlvSFLKTYG---------FDGVDIDWEyPGAADNSDrenfitllrELRSALG--AAN 141
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 255740203 174 VLVSAAPQCPYpDAHLDLAIATGIFDYV-W--VQFYN 207
Cdd:cd00598  142 YLLTIAVPASY-FDLGYAYDVPAIGDYVdFvnVMTYD 177
GH18_PF-ChiA-like cd06543
PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus ...
47-155 5.80e-05

PF-ChiA is an uncharacterized chitinase found in the hyperthermophilic archaeon Pyrococcus furiosus with a glycosyl hydrolase family 18 (GH18) catalytic domain as well as a cellulose-binding domain. Members of this domain family are found not only in archaea but also in eukaryotes and prokaryotes. PF-ChiA exhibits hydrolytic activity toward both colloidal and crystalline (beta/alpha) chitins at high temperature.


Pssm-ID: 119360  Cd Length: 294  Bit Score: 43.82  E-value: 5.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  47 ATGNYNYVLvSFLTTFGNgqtpvlnlaghCDPSSNGCTGLST------DITSCQNQGIKVLLSLGGASGSYSLVSTDDAD 120
Cdd:cd06543   23 ATGVKAFTL-AFIVASGG-----------CKPAWGGSYPLDQggwiksDIAALRAAGGDVIVSFGGASGTPLATSCTSAD 90
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 255740203 121 Q-VAAYlwnnylggqsdsrplgSAVLD-----GIDFDIESG 155
Cdd:cd06543   91 QlAAAY----------------QKVIDaygltHLDFDIEGG 115
GH18_narbonin cd06544
Narbonin is a plant 2S protein from the globulin fraction of narbon bean (Vicia narbonensis L.) ...
94-277 3.60e-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: 3.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  94 QNQGIKVLLSLGGASGSYSLVSTDDADQvaaylwNNYLGGQSDSrpLGSAV----LDGIDFD---IESGSDNY---WGDL 163
Cdd:cd06544   67 QHPNVKVVISIGGRGVQNNPTPFDPSNV------DSWVSNAVSS--LTSIIqtynLDGIDIDyehFPADPDTFvecIGQL 138
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 164 ATALKNYSQSVLVSAApqcPYPDAHLDLAIA-----TGIFDYVWVQFYNNEQCeyvTDDANLLSAWNQWTSS-QANVVFL 237
Cdd:cd06544  139 ITELKNNGVIKVASIA---PSEDAEQSHYLAlynayGDYIDYVNYQFYNYGVP---TTVAKYVEFYDEVANNyPGKKVLA 212
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 255740203 238 GLpaSTDAASSGYISPDVLISqVLPSIKASSKYGGVMLWS 277
Cdd:cd06544  213 SF--STDGEDGANIPGEIFIG-GCKRLKKNGSLPGVFIWN 249
GH18_3CO4_chitinase cd06545
The Bacteroides thetaiotaomicron protein represented by pdb structure 3CO4 is an ...
85-276 5.86e-03

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: 37.43  E-value: 5.86e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203  85 GLSTDITSCQNQGIKVLLSLGGASGSYSLVSTDDADQVAAYLWN--NYlggqsdsrpLGSAVLDGIDFDIEsGSDNYWGD 162
Cdd:cd06545   47 ELNSVVNAAHAHNVKILISLAGGSPPEFTAALNDPAKRKALVDKiiNY---------VVSYNLDGIDVDLE-GPDVTFGD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255740203 163 LAT-----ALKNYSQSVLVSAAPQCPYPDAHLDLAIATgiFDYVWVQFYNN----------EQCEYvtDDAnlLSAWNQW 227
Cdd:cd06545  117 YLVfiralYAALKKEGKLLTAAVSSWNGGAVSDSTLAY--FDFINIMSYDAtgpwwgdnpgQHSSY--DDA--VNDLNYW 190
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 255740203 228 TSSQ---ANVVFLGLPAstdaasSGYispdVLISQVLPSIKASSK-----YGGVMLW 276
Cdd:cd06545  191 NERGlasKDKLVLGLPF------YGY----GFYYNGIPTIRNKVAfakqnYGGVMIW 237
 
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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