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UniProtKB - P29059 (CHI3_TOBAC)

Entry version 116 (02 Dec 2020)
Sequence version 1 (01 Dec 1992)
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Protein

Endochitinase 3

Gene

CHN14

Organism
Nicotiana tabacum (Common tobacco)
Status
Reviewed-Annotation score:

Annotation score:4 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Protein inferred from homologyi <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Defense against chitin-containing fungal pathogens.

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide (1->4)-beta-linkages in chitin and chitodextrins. EC:3.2.1.14

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section is used for enzymes and indicates the residues directly involved in catalysis.<p><a href='/help/act_site' target='_top'>More...</a></p>Active sitei150Proton donorBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • chitinase activity Source: GO_Central
  • chitin binding Source: UniProtKB-KW
Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGlycosidase, Hydrolase
Biological processCarbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation
LigandChitin-binding

Protein family/group databases

Carbohydrate-Active enZymes

More...CAZyi		CBM18, Carbohydrate-Binding Module Family 18
GH19, Glycoside Hydrolase Family 19

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Endochitinase 3 (EC:3.2.1.14)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:CHN14
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiNicotiana tabacum (Common tobacco)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri4097 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Viridiplantae › Streptophyta › Embryophyta › Tracheophyta › Spermatophyta › Magnoliopsida › eudicotyledons › Gunneridae › Pentapetalae › asterids › lamiids › Solanales › Solanaceae › Nicotianoideae › Nicotianeae › Nicotiana
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000084051 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Genome assembly

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Vacuole

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section denotes the presence of an N-terminal signal peptide.<p><a href='/help/signal' target='_top'>More...</a></p>Signal peptidei1 – 23Add BLAST23
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_000000533424 – 327Endochitinase 3Add BLAST304
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_0000005335328 – 334Removed in mature formCurated7

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the PTM / Processing":/help/ptm_processing_section section describes the positions of cysteine residues participating in disulfide bonds.<p><a href='/help/disulfid' target='_top'>More...</a></p>Disulfide bondi26 ↔ 41PROSITE-ProRule annotation
Disulfide bondi35 ↔ 47PROSITE-ProRule annotation
Disulfide bondi40 ↔ 54PROSITE-ProRule annotation
Disulfide bondi59 ↔ 63PROSITE-ProRule annotation
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei734-hydroxyprolineBy similarity1
Modified residuei744-hydroxyprolineBy similarity1
Modified residuei764-hydroxyprolineBy similarity1
Disulfide bondi106 ↔ 168PROSITE-ProRule annotation
Disulfide bondi180 ↔ 188PROSITE-ProRule annotation
Disulfide bondi287 ↔ 319PROSITE-ProRule annotation

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

The 4-hydroxyproline residues are not glycosylated in this plant vacuolar protein.By similarity

Keywords - PTMi

Disulfide bond, Hydroxylation

Proteomic databases

PRoteomics IDEntifications database

More...PRIDEi		P29059

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P29059

Database of comparative protein structure models

More...ModBasei		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini24 – 65Chitin-binding type-1PROSITE-ProRule annotationAdd BLAST42

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the glycosyl hydrolase 19 family. Chitinase class I subfamily.Curated

Keywords - Domaini

Signal

Phylogenomic databases

Identification of Orthologs from Complete Genome Data

More...OMAi		YCFKREL

Database of Orthologous Groups

More...OrthoDBi		1132954at2759

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		3.30.60.10, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR001002, Chitin-bd_1
IPR018371, Chitin-binding_1_CS
IPR036861, Endochitinase-like_sf
IPR016283, Glyco_hydro_19
IPR000726, Glyco_hydro_19_cat
IPR023346, Lysozyme-like_dom_sf

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00187, Chitin_bind_1, 1 hit
PF00182, Glyco_hydro_19, 1 hit

PIRSF; a whole-protein classification database

More...PIRSFi		PIRSF001060, Endochitinase, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00451, CHITINBINDNG

Simple Modular Architecture Research Tool; a protein domain database

More...SMARTi		View protein in SMART
SM00270, ChtBD1, 1 hit

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF53955, SSF53955, 1 hit
SSF57016, SSF57016, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00026, CHIT_BIND_I_1, 1 hit
PS50941, CHIT_BIND_I_2, 1 hit
PS00773, CHITINASE_19_1, 1 hit
PS00774, CHITINASE_19_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P29059-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MRLLEFTALS SLLVLFLLLA VSAEQCGKQA GGARCPSGMC CSNFGWCGNT 
        60         70         80         90        100
QDYCGPGKCQ SQCPSGPGPT PRPPTPTPGP STGDISNIIS SSMFDQMLKH 
       110        120        130        140        150
RNDNTCQGKS FYTYNAFITA ARSFRGFGTT GDTTRRKREV AAFFAQTSHE 
       160        170        180        190        200
TTGGWDTAPD GRYAWGYCYL REQGNPPSYC VQSSQWPCAP GQKYYGRGPI 
       210        220        230        240        250
QISYNYNYGP CGRAIGQNLL NNPDLVATNA VVSFKSAIWF WMTAQSPKPS 
       260        270        280        290        300
CHDVITGRWT PSAADRAANR LPGYGVITNI INGGLECGHG SDARVQDRIG 
       310        320        330 
FYRRYCSILG VSPGDNIDCG NQKSFNSGLL LETM
Length:334
Mass (Da):36,221
Last modified:December 1, 1992 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i4F684CE1FBD432FB
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
X64518 Genomic DNA Translation: CAA45821.1

Protein sequence database of the Protein Information Resource

More...PIRi		S20982

NCBI Reference Sequences

More...RefSeqi		XP_016461053.1, XM_016605567.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...GeneIDi		107784434

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		nta:107784434

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X64518 Genomic DNA Translation: CAA45821.1
PIRiS20982
RefSeqiXP_016461053.1, XM_016605567.1

3D structure databases

SMRiP29059
ModBaseiSearch...

Protein family/group databases

CAZyiCBM18, Carbohydrate-Binding Module Family 18
GH19, Glycoside Hydrolase Family 19

Proteomic databases

PRIDEiP29059

Genome annotation databases

GeneIDi107784434
KEGGinta:107784434

Phylogenomic databases

OMAiYCFKREL
OrthoDBi1132954at2759

Family and domain databases

Gene3Di3.30.60.10, 1 hit
InterProiView protein in InterPro
IPR001002, Chitin-bd_1
IPR018371, Chitin-binding_1_CS
IPR036861, Endochitinase-like_sf
IPR016283, Glyco_hydro_19
IPR000726, Glyco_hydro_19_cat
IPR023346, Lysozyme-like_dom_sf
PfamiView protein in Pfam
PF00187, Chitin_bind_1, 1 hit
PF00182, Glyco_hydro_19, 1 hit
PIRSFiPIRSF001060, Endochitinase, 1 hit
PRINTSiPR00451, CHITINBINDNG
SMARTiView protein in SMART
SM00270, ChtBD1, 1 hit
SUPFAMiSSF53955, SSF53955, 1 hit
SSF57016, SSF57016, 1 hit
PROSITEiView protein in PROSITE
PS00026, CHIT_BIND_I_1, 1 hit
PS50941, CHIT_BIND_I_2, 1 hit
PS00773, CHITINASE_19_1, 1 hit
PS00774, CHITINASE_19_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiCHI3_TOBAC
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P29059
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: December 1, 1992
Last modified: December 2, 2020
This is version 116 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programPlant Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Reference proteome

Documents

  1. Glycosyl hydrolases
    Classification of glycosyl hydrolase families and list of entries
  2. SIMILARITY comments
    Index of protein domains and families
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