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P05315

- CHIT_SOLTU

UniProt

P05315 - CHIT_SOLTU

Protein

Endochitinase

Gene
N/A
Organism
Solanum tuberosum (Potato)
Status
Reviewed - Annotation score: 3 out of 5- Experimental evidence at transcript leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 1 (01 Nov 1988)
      Previous versions | rss
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    Functioni

    Defense against chitin containing fungal pathogens.

    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-EC
    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 Source: UniProtKB-KW
    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:
    Endochitinase (EC:3.2.1.14)
    OrganismiSolanum tuberosum (Potato)
    Taxonomic identifieri4113 [NCBI]
    Taxonomic lineageiEukaryotaViridiplantaeStreptophytaEmbryophytaTracheophytaSpermatophytaMagnoliophytaeudicotyledonsGunneridaePentapetalaeasteridslamiidsSolanalesSolanaceaeSolanoideaeSolaneaeSolanum
    ProteomesiUP000011115: Unplaced

    Subcellular locationi

    Vacuole By similarity
    Note: Vacuolar and protoplast.By similarity

    GO - Cellular componenti

    1. vacuole Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Vacuole

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2626Add
    BLAST
    Chaini27 – 321295EndochitinasePRO_0000005327Add
    BLAST
    Propeptidei322 – 3287Removed in mature formCuratedPRO_0000005328

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 44PROSITE-ProRule annotation
    Disulfide bondi38 ↔ 50PROSITE-ProRule annotation
    Disulfide bondi43 ↔ 57PROSITE-ProRule annotation
    Disulfide bondi62 ↔ 66PROSITE-ProRule annotation
    Disulfide bondi100 ↔ 162PROSITE-ProRule annotation
    Disulfide bondi174 ↔ 182PROSITE-ProRule annotation
    Disulfide bondi281 ↔ 313PROSITE-ProRule annotation

    Keywords - PTMi

    Disulfide bond

    Expressioni

    Inductioni

    By ethylene.

    Structurei

    Secondary structure

    1
    328
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi79 – 813
    Helixi85 – 917
    Turni92 – 965
    Beta strandi100 – 1045
    Helixi108 – 1169
    Turni119 – 1235
    Helixi127 – 14519
    Helixi156 – 1583
    Beta strandi178 – 1803
    Turni192 – 1954
    Helixi199 – 20911
    Turni213 – 2153
    Helixi219 – 2224
    Helixi224 – 23613
    Helixi245 – 2506
    Helixi257 – 2626
    Helixi268 – 28013
    Beta strandi281 – 2844
    Helixi287 – 30317

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1P3Zmodel-A1-328[»]
    ProteinModelPortaliP05315.
    SMRiP05315. Positions 27-320.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini27 – 6842Chitin-binding type-1PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

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

    Keywords - Domaini

    Signal

    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.

    P05315-1 [UniParc]FASTAAdd to Basket

    « Hide

    MRRHKEVNFV AYLLFSLLVL VSAALAQNCG SQGGGKACAS GQCCSKFGWC    50
    GNTNDYCGSG NCQSQCPGGG PGPGPGGDLG SAISNSMFDQ MLKHRNENSC 100
    QGKNFYSYNA FINAARSFPG FGTSGDINAR KREIAAFFAQ TSHETTGGWA 150
    SAPDGPYAWG YCFLRERGNP GDYCPPSSQW PCAPGRKYFG RGPIQISHNY 200
    NYGPCGRAIG VDLLNNPDLV ATDPVISFKT ALWFWMTPQS PKPSCHDVII 250
    GRWNPSSADR AANRLPGFGV ITNIINGGLE CGRGTDNRVQ DRIGFYRRYC 300
    SILGVTPGDN LDCVNQRWFG NALLVDTL 328
    Length:328
    Mass (Da):35,407
    Last modified:November 1, 1988 - v1
    Checksum:i669B82159BC176EF
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07130 mRNA. Translation: CAA30142.1.
    X15494 Genomic DNA. Translation: CAA33517.1.
    PIRiS05426.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X07130 mRNA. Translation: CAA30142.1 .
    X15494 Genomic DNA. Translation: CAA33517.1 .
    PIRi S05426.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1P3Z model - A 1-328 [» ]
    ProteinModelPortali P05315.
    SMRi P05315. Positions 27-320.
    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...

    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. "Primary structure of an endochitinase mRNA from Solanum tuberosum."
      Gaynor J.J.
      Nucleic Acids Res. 16:5210-5210(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Strain: cv. Russet Burbank-0.
      Tissue: Leaf.
    2. "Sequence analysis of a genomic clone encoding an endochitinase from Solanum tuberosum."
      Gaynor J.J., Unkenholz K.M.
      Nucleic Acids Res. 17:5855-5855(1989) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Strain: cv. Russet Burbank-0.
    3. "Endochitinase [precursor] function as a defense against chitin containing fungal pathogens."
      Rao G.S.
      Submitted (MAY-2003) to the PDB data bank
      Cited for: 3D-STRUCTURE MODELING.

    Entry informationi

    Entry nameiCHIT_SOLTU
    AccessioniPrimary (citable) accession number: P05315
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1988
    Last sequence update: November 1, 1988
    Last modified: October 1, 2014
    This is version 106 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3