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Conserved domains on  [gi|2231611316|ref|NP_001392430|]
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xylanase inhibitor protein 1 precursor [Triticum aestivum]

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 ...
36-302 1.30e-115

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: 334.59  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316  36 GQVTVFWGRNKAEGSLREACDSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSS-------VGADIKHCQSKGVPVSLSIG 108
Cdd:cd02877     1 GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGStypncpqLGADIKHCQSKGKKVLLSIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 109 GYGTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWLDGVDLFLEHGTPAdRYDVLALELAKHNiRGGPGKPLHL 188
Cdd:cd02877    81 GAGGSYSLSSDADAKDFADYLWNAFGGGTDSGVPRPFGDAVVDGFDFDIEHGSPE-NYDALAKRLRSLF-ASDPSKKYYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 189 TATVRCGYPPaAHVGRALATGIFERVHVRTYESDKWCN---QNLGWEGSWDKWTAAYPAT---RFYVGLTADDK--SHQW 260
Cdd:cd02877   159 TAAPQCPYPD-ASLGDAIATGLFDFIFVQFYNNPCCSYasgNASGFNFNWDTWTSWAKATsnaKVFLGLPASPEaaGSGY 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2231611316 261 VHPKNVYYGVAPVAQKKDNYGGIMLWDRYFDKQ-TNYSSLIKY 302
Cdd:cd02877   238 VDPSELASLVLPVKQKSPNFGGVMLWDASQDKQgTGYSSKIKD 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 ...
36-302 1.30e-115

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: 334.59  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316  36 GQVTVFWGRNKAEGSLREACDSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSS-------VGADIKHCQSKGVPVSLSIG 108
Cdd:cd02877     1 GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGStypncpqLGADIKHCQSKGKKVLLSIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 109 GYGTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWLDGVDLFLEHGTPAdRYDVLALELAKHNiRGGPGKPLHL 188
Cdd:cd02877    81 GAGGSYSLSSDADAKDFADYLWNAFGGGTDSGVPRPFGDAVVDGFDFDIEHGSPE-NYDALAKRLRSLF-ASDPSKKYYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 189 TATVRCGYPPaAHVGRALATGIFERVHVRTYESDKWCN---QNLGWEGSWDKWTAAYPAT---RFYVGLTADDK--SHQW 260
Cdd:cd02877   159 TAAPQCPYPD-ASLGDAIATGLFDFIFVQFYNNPCCSYasgNASGFNFNWDTWTSWAKATsnaKVFLGLPASPEaaGSGY 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2231611316 261 VHPKNVYYGVAPVAQKKDNYGGIMLWDRYFDKQ-TNYSSLIKY 302
Cdd:cd02877   238 VDPSELASLVLPVKQKSPNFGGVMLWDASQDKQgTGYSSKIKD 280
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
56-271 2.33e-13

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 69.02  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316  56 DSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSSVGADIKHCQSKGVPVSLSIGGY--GTGYSLP-SNRSALDLF-DHLWN 131
Cdd:pfam00704  19 PSDKLTHIIYAFANIDGSDGTLFIGDWDLGNFEQLKKLKKQKNPGVKVLLSIGGWtdSTGFSLMaSNPASRKKFaDSIVS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 132 SYfggskpsvpRPFGdawLDGVDLFLE--HGTPADR--YDVLALELAKHNIRGGPGKPLHLTATVRCGYPPaAHVGRALA 207
Cdd:pfam00704  99 FL---------RKYG---FDGIDIDWEypGGNPEDKenYDLLLRELRAALDEAKGGKKYLLSAAVPASYPD-LDKGYDLP 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2231611316 208 TgIFER---VHVRTYesdkwcnqNLGweGSWDKWTAAYPATRFYVGLTADDKSHQW----VHPKNVYYGVA 271
Cdd:pfam00704 166 K-IAKYldfINVMTY--------DFH--GSWDNVTGHHAPLYGGGSYNVDYAVKYYlkqgVPASKLVLGVP 225
 
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 ...
36-302 1.30e-115

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: 334.59  E-value: 1.30e-115
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316  36 GQVTVFWGRNKAEGSLREACDSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSS-------VGADIKHCQSKGVPVSLSIG 108
Cdd:cd02877     1 GNIAVYWGQNSDEGSLREYCDTGNYDIVNISFLNVFGSGGTPGLNFAGHCGGStypncpqLGADIKHCQSKGKKVLLSIG 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 109 GYGTGYSLPSNRSALDLFDHLWNSYFGGSKPSVPRPFGDAWLDGVDLFLEHGTPAdRYDVLALELAKHNiRGGPGKPLHL 188
Cdd:cd02877    81 GAGGSYSLSSDADAKDFADYLWNAFGGGTDSGVPRPFGDAVVDGFDFDIEHGSPE-NYDALAKRLRSLF-ASDPSKKYYL 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 189 TATVRCGYPPaAHVGRALATGIFERVHVRTYESDKWCN---QNLGWEGSWDKWTAAYPAT---RFYVGLTADDK--SHQW 260
Cdd:cd02877   159 TAAPQCPYPD-ASLGDAIATGLFDFIFVQFYNNPCCSYasgNASGFNFNWDTWTSWAKATsnaKVFLGLPASPEaaGSGY 237
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 2231611316 261 VHPKNVYYGVAPVAQKKDNYGGIMLWDRYFDKQ-TNYSSLIKY 302
Cdd:cd02877   238 VDPSELASLVLPVKQKSPNFGGVMLWDASQDKQgTGYSSKIKD 280
Glyco_hydro_18 pfam00704
Glycosyl hydrolases family 18;
56-271 2.33e-13

Glycosyl hydrolases family 18;


Pssm-ID: 425828 [Multi-domain]  Cd Length: 311  Bit Score: 69.02  E-value: 2.33e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316  56 DSGMYTMVTMSFLDVFGANGKYHLDLSGHDLSSVGADIKHCQSKGVPVSLSIGGY--GTGYSLP-SNRSALDLF-DHLWN 131
Cdd:pfam00704  19 PSDKLTHIIYAFANIDGSDGTLFIGDWDLGNFEQLKKLKKQKNPGVKVLLSIGGWtdSTGFSLMaSNPASRKKFaDSIVS 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2231611316 132 SYfggskpsvpRPFGdawLDGVDLFLE--HGTPADR--YDVLALELAKHNIRGGPGKPLHLTATVRCGYPPaAHVGRALA 207
Cdd:pfam00704  99 FL---------RKYG---FDGIDIDWEypGGNPEDKenYDLLLRELRAALDEAKGGKKYLLSAAVPASYPD-LDKGYDLP 165
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2231611316 208 TgIFER---VHVRTYesdkwcnqNLGweGSWDKWTAAYPATRFYVGLTADDKSHQW----VHPKNVYYGVA 271
Cdd:pfam00704 166 K-IAKYldfINVMTY--------DFH--GSWDNVTGHHAPLYGGGSYNVDYAVKYYlkqgVPASKLVLGVP 225
 
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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