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Q7DNA1

- CHI2_ORYSJ

UniProt

Q7DNA1 - CHI2_ORYSJ

Protein

Chitinase 2

Gene

Cht2

Organism
Oryza sativa subsp. japonica (Rice)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 69 (01 Oct 2014)
      Sequence version 1 (05 Jul 2004)
      Previous versions | rss
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    Functioni

    Hydrolyzes chitin and plays a role in defense against fungal pathogens containing chitin. Its overexpression confers enhanced resistance to sheath blight pathogen (R.solani).3 Publications

    Catalytic activityi

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

    GO - Molecular functioni

    1. chitinase activity Source: UniProtKB
    2. chitin binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell wall macromolecule catabolic process Source: InterPro
    2. chitin catabolic process Source: UniProtKB-KW
    3. defense response to fungus Source: UniProtKB
    4. polysaccharide catabolic process Source: UniProtKB-KW

    Keywords - Molecular functioni

    Glycosidase, Hydrolase

    Keywords - Biological processi

    Carbohydrate metabolism, Chitin degradation, Plant defense, Polysaccharide degradation

    Keywords - Ligandi

    Chitin-binding

    Protein family/group databases

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

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Chitinase 2 (EC:3.2.1.14)
    Alternative name(s):
    Class I chitinase b
    Short name:
    OsChia1b
    Pathogenesis related (PR)-3 chitinase 2
    Gene namesi
    Name:Cht2
    Synonyms:RC7
    Ordered Locus Names:Os05g0399300, LOC_Os05g33130
    ORF Names:OsJ_18467
    OrganismiOryza sativa subsp. japonica (Rice)
    Taxonomic identifieri39947 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaLiliopsidaPoalesPoaceaeBEP cladeEhrhartoideaeOryzeaeOryza
    ProteomesiUP000000763: Chromosome 5

    Organism-specific databases

    GrameneiQ7DNA1.

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi159 – 1591W → A: Increased activity. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3232Sequence AnalysisAdd
    BLAST
    Chaini33 – 340308Chitinase 2PRO_5000139669Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi35 ↔ 501 PublicationPROSITE-ProRule annotation
    Disulfide bondi44 ↔ 561 PublicationPROSITE-ProRule annotation
    Disulfide bondi47 ↔ 741 PublicationPROSITE-ProRule annotation
    Disulfide bondi49 ↔ 631 PublicationPROSITE-ProRule annotation
    Disulfide bondi67 ↔ 711 PublicationPROSITE-ProRule annotation
    Disulfide bondi110 ↔ 1721 PublicationPROSITE-ProRule annotation
    Disulfide bondi184 ↔ 1921 PublicationPROSITE-ProRule annotation
    Disulfide bondi291 ↔ 3231 PublicationPROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Tissue specificityi

    Expressed in roots, sheaths and meristems.1 Publication

    Structurei

    Secondary structure

    1
    340
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Turni37 – 415
    Helixi45 – 473
    Beta strandi54 – 596
    Helixi60 – 634
    Helixi89 – 913
    Helixi95 – 1017
    Turni102 – 1065
    Turni111 – 1144
    Helixi118 – 1269
    Turni129 – 1324
    Beta strandi134 – 1363
    Helixi137 – 15519
    Helixi166 – 1683
    Beta strandi188 – 1903
    Turni202 – 2054
    Helixi209 – 21911
    Turni223 – 2253
    Helixi229 – 2324
    Helixi234 – 24613
    Helixi255 – 2595
    Helixi267 – 2715
    Helixi278 – 29013
    Beta strandi291 – 2944
    Helixi297 – 31216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DKVX-ray2.00A33-340[»]
    3IWRX-ray2.57A/B33-340[»]
    ProteinModelPortaliQ7DNA1.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ7DNA1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini33 – 7341Chitin-binding type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Contains 1 chitin-binding type-1 domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Signal

    Phylogenomic databases

    HOGENOMiHOG000231411.
    KOiK01183.
    OMAiNCLCCSR.

    Family and domain databases

    Gene3Di3.30.60.10. 1 hit.
    InterProiIPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    IPR016283. Glyco_hydro_19.
    IPR000726. Glyco_hydro_19_cat.
    IPR023346. Lysozyme-like_dom.
    [Graphical view]
    PfamiPF00187. Chitin_bind_1. 1 hit.
    PF00182. Glyco_hydro_19. 1 hit.
    [Graphical view]
    PIRSFiPIRSF001060. Endochitinase. 1 hit.
    PRINTSiPR00451. CHITINBINDNG.
    ProDomiPD000609. Chitin_bd_1. 1 hit.
    [Graphical view] [Entries sharing at least one domain]
    SMARTiSM00270. ChtBD1. 1 hit.
    [Graphical view]
    SUPFAMiSSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 1 hit.
    PROSITEiPS00026. 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.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    Q7DNA1-1 [UniParc]FASTAAdd to Basket

    « Hide

    MSTPRAAASL AKKAALVALA VLAAALATAA RAEQCGAQAG GARCPNCLCC    50
    SRWGWCGTTS DFCGDGCQSQ CSGCGPTPTP TPPSPSDGVG SIVPRDLFER 100
    LLLHRNDGAC PARGFYTYEA FLAAAAAFPA FGGTGNTETR KREVAAFLGQ 150
    TSHETTGGWP TAPDGPFSWG YCFKQEQNPP SDYCQPSPEW PCAPGRKYYG 200
    RGPIQLSFNF NYGPAGRAIG VDLLSNPDLV ATDATVSFKT ALWFWMTPQG 250
    NKPSSHDVIT GRWAPSPADA AAGRAPGYGV ITNIVNGGLE CGHGPDDRVA 300
    NRIGFYQRYC GAFGIGTGGN LDCYNQRPFN SGSSVGLAEQ 340
    Length:340
    Mass (Da):35,587
    Last modified:July 5, 2004 - v1
    Checksum:i642F13E3928CA7BE
    GO

    Sequence cautioni

    The sequence BAF17390.1 differs from that shown. Reason: Erroneous gene model prediction.

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16222 Genomic DNA. Translation: BAA03750.1.
    X56787 mRNA. Translation: CAA40107.1.
    AP008211 Genomic DNA. Translation: BAF17390.1. Sequence problems.
    CM000142 Genomic DNA. Translation: EEE63650.1.
    PIRiS39979.
    S40414.
    RefSeqiNP_001055476.1. NM_001062011.1.
    UniGeneiOs.3374.

    Genome annotation databases

    GeneIDi4338718.
    KEGGiosa:4338718.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D16222 Genomic DNA. Translation: BAA03750.1 .
    X56787 mRNA. Translation: CAA40107.1 .
    AP008211 Genomic DNA. Translation: BAF17390.1 . Sequence problems.
    CM000142 Genomic DNA. Translation: EEE63650.1 .
    PIRi S39979.
    S40414.
    RefSeqi NP_001055476.1. NM_001062011.1.
    UniGenei Os.3374.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DKV X-ray 2.00 A 33-340 [» ]
    3IWR X-ray 2.57 A/B 33-340 [» ]
    ProteinModelPortali Q7DNA1.
    ModBasei Search...
    MobiDBi Search...

    Protein family/group databases

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

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    GeneIDi 4338718.
    KEGGi osa:4338718.

    Organism-specific databases

    Gramenei Q7DNA1.

    Phylogenomic databases

    HOGENOMi HOG000231411.
    KOi K01183.
    OMAi NCLCCSR.

    Miscellaneous databases

    EvolutionaryTracei Q7DNA1.

    Family and domain databases

    Gene3Di 3.30.60.10. 1 hit.
    InterProi IPR001002. Chitin-bd_1.
    IPR018371. Chitin-binding_1_CS.
    IPR016283. Glyco_hydro_19.
    IPR000726. Glyco_hydro_19_cat.
    IPR023346. Lysozyme-like_dom.
    [Graphical view ]
    Pfami PF00187. Chitin_bind_1. 1 hit.
    PF00182. Glyco_hydro_19. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF001060. Endochitinase. 1 hit.
    PRINTSi PR00451. CHITINBINDNG.
    ProDomi PD000609. Chitin_bd_1. 1 hit.
    [Graphical view ] [Entries sharing at least one domain ]
    SMARTi SM00270. ChtBD1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53955. SSF53955. 1 hit.
    SSF57016. SSF57016. 1 hit.
    PROSITEi 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.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Sequence variation, differential expression and chromosomal location of rice chitinase genes."
      Nishizawa Y., Kishimoto N., Saito A., Hibi T.
      Mol. Gen. Genet. 241:1-10(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA].
      Strain: cv. Nipponbare.
    2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    3. "The rice annotation project database (RAP-DB): 2008 update."
      The rice annotation project (RAP)
      Nucleic Acids Res. 36:D1028-D1033(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENOME REANNOTATION.
      Strain: cv. Nipponbare.
    4. "The genomes of Oryza sativa: a history of duplications."
      Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S., Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.
      , Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J., Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X., Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y., Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L., Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H., Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z., Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L., Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F., Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q., Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J., Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M., McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.
      PLoS Biol. 3:266-281(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
      Strain: cv. Nipponbare.
    5. "Enhanced resistance to sheath blight by constitutive expression of infection-related rice chitinase in transgenic elite indica rice cultivars."
      Datta K., Tu J., Oliva N., Ona I., Velazhahan R., Mew T.W., Muthukrishnan S., Datta S.K.
      Plant Sci. 160:405-414(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    6. "Distribution, structure, organ-specific expression, and phylogenic analysis of the pathogenesis-related protein-3 chitinase gene family in rice (Oryza sativa L.)."
      Nakazaki T., Tsukiyama T., Okumoto Y., Kageyama D., Naito K., Inouye K., Tanisaka T.
      Genome 49:619-630(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: GENE FAMILY, NOMENCLATURE, TISSUE SPECIFICITY.
    7. "Purification and characterization of a rice class I chitinase, OsChia1b, produced in Esherichia coli."
      Mizuno R., Itoh Y., Nishizawa Y., Kezuka Y., Suzuki K., Nonaka T., Watanabe T.
      Biosci. Biotechnol. Biochem. 72:893-895(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION.
    8. "Role of the loop structure of the catalytic domain in rice class I chitinase."
      Mizuno R., Fukamizo T., Sugiyama S., Nishizawa Y., Kezuka Y., Nonaka T., Suzuki K., Watanabe T.
      J. Biochem. 143:487-495(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF TRP-159.
    9. "Crystallization and preliminary X-ray analysis of plant class I chitinase from rice."
      Kezuka Y., Kitazaki K., Itoh Y., Watanabe J., Takaha O., Watanabe T., Nishizawa Y., Nonaka T.
      Protein Pept. Lett. 11:401-405(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 33-340, DISULFIDE BONDS.

    Entry informationi

    Entry nameiCHI2_ORYSJ
    AccessioniPrimary (citable) accession number: Q7DNA1
    Secondary accession number(s): Q0DID3, Q43294
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 22, 2009
    Last sequence update: July 5, 2004
    Last modified: October 1, 2014
    This is version 69 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programPlant Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Glycosyl hydrolases
      Classification of glycosyl hydrolase families and list of entries
    2. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    3. Oryza sativa (rice)
      Index of Oryza sativa entries and their corresponding gene designations
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3