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CHI6_ORYSJ
ID   CHI6_ORYSJ              Reviewed;         271 AA.
AC   Q6K8R2; A0A0P0VLJ2;
DT   22-SEP-2009, integrated into UniProtKB/Swiss-Prot.
DT   05-JUL-2004, sequence version 1.
DT   03-AUG-2022, entry version 114.
DE   RecName: Full=Chitinase 6;
DE            EC=3.2.1.14;
DE   AltName: Full=Pathogenesis related (PR)-3 chitinase 6;
DE   Flags: Precursor;
GN   Name=Cht6; OrderedLocusNames=Os02g0605900, LOC_Os02g39330;
GN   ORFNames=OJ1058_F07.19, OsJ_07447;
OS   Oryza sativa subsp. japonica (Rice).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; Liliopsida; Poales; Poaceae; BOP clade;
OC   Oryzoideae; Oryzeae; Oryzinae; Oryza; Oryza sativa.
OX   NCBI_TaxID=39947;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=16100779; DOI=10.1038/nature03895;
RG   International rice genome sequencing project (IRGSP);
RT   "The map-based sequence of the rice genome.";
RL   Nature 436:793-800(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=18089549; DOI=10.1093/nar/gkm978;
RG   The rice annotation project (RAP);
RT   "The rice annotation project database (RAP-DB): 2008 update.";
RL   Nucleic Acids Res. 36:D1028-D1033(2008).
RN   [3]
RP   GENOME REANNOTATION.
RC   STRAIN=cv. Nipponbare;
RX   PubMed=24280374; DOI=10.1186/1939-8433-6-4;
RA   Kawahara Y., de la Bastide M., Hamilton J.P., Kanamori H., McCombie W.R.,
RA   Ouyang S., Schwartz D.C., Tanaka T., Wu J., Zhou S., Childs K.L.,
RA   Davidson R.M., Lin H., Quesada-Ocampo L., Vaillancourt B., Sakai H.,
RA   Lee S.S., Kim J., Numa H., Itoh T., Buell C.R., Matsumoto T.;
RT   "Improvement of the Oryza sativa Nipponbare reference genome using next
RT   generation sequence and optical map data.";
RL   Rice 6:4-4(2013).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=15685292; DOI=10.1371/journal.pbio.0030038;
RA   Yu J., Wang J., Lin W., Li S., Li H., Zhou J., Ni P., Dong W., Hu S.,
RA   Zeng C., Zhang J., Zhang Y., Li R., Xu Z., Li S., Li X., Zheng H., Cong L.,
RA   Lin L., Yin J., Geng J., Li G., Shi J., Liu J., Lv H., Li J., Wang J.,
RA   Deng Y., Ran L., Shi X., Wang X., Wu Q., Li C., Ren X., Wang J., Wang X.,
RA   Li D., Liu D., Zhang X., Ji Z., Zhao W., Sun Y., Zhang Z., Bao J., Han Y.,
RA   Dong L., Ji J., Chen P., Wu S., Liu J., Xiao Y., Bu D., Tan J., Yang L.,
RA   Ye C., Zhang J., Xu J., Zhou Y., Yu Y., Zhang B., Zhuang S., Wei H.,
RA   Liu B., Lei M., Yu H., Li Y., Xu H., Wei S., He X., Fang L., Zhang Z.,
RA   Zhang Y., Huang X., Su Z., Tong W., Li J., Tong Z., Li S., Ye J., Wang L.,
RA   Fang L., Lei T., Chen C.-S., Chen H.-C., Xu Z., Li H., Huang H., Zhang F.,
RA   Xu H., Li N., Zhao C., Li S., Dong L., Huang Y., Li L., Xi Y., Qi Q.,
RA   Li W., Zhang B., Hu W., Zhang Y., Tian X., Jiao Y., Liang X., Jin J.,
RA   Gao L., Zheng W., Hao B., Liu S.-M., Wang W., Yuan L., Cao M.,
RA   McDermott J., Samudrala R., Wang J., Wong G.K.-S., Yang H.;
RT   "The genomes of Oryza sativa: a history of duplications.";
RL   PLoS Biol. 3:266-281(2005).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=cv. Nipponbare;
RX   PubMed=12869764; DOI=10.1126/science.1081288;
RG   The rice full-length cDNA consortium;
RT   "Collection, mapping, and annotation of over 28,000 cDNA clones from
RT   japonica rice.";
RL   Science 301:376-379(2003).
RN   [6]
RP   GENE FAMILY, NOMENCLATURE, AND TISSUE SPECIFICITY.
RX   PubMed=16936841; DOI=10.1139/g06-020;
RA   Nakazaki T., Tsukiyama T., Okumoto Y., Kageyama D., Naito K., Inouye K.,
RA   Tanisaka T.;
RT   "Distribution, structure, organ-specific expression, and phylogenic
RT   analysis of the pathogenesis-related protein-3 chitinase gene family in
RT   rice (Oryza sativa L.).";
RL   Genome 49:619-630(2006).
CC   -!- FUNCTION: May function in reproductive organs during embryogenesis and
CC       seed maturation.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC         (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC   -!- TISSUE SPECIFICITY: Expressed in roots, leaves, sheaths and meristems.
CC       {ECO:0000269|PubMed:16936841}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
CC       class IV subfamily. {ECO:0000305}.
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DR   EMBL; AP004111; BAD19330.1; -; Genomic_DNA.
DR   EMBL; AP008208; BAF09287.1; -; Genomic_DNA.
DR   EMBL; AP014958; BAS79659.1; -; Genomic_DNA.
DR   EMBL; CM000139; EAZ23743.1; -; Genomic_DNA.
DR   EMBL; AK064754; -; NOT_ANNOTATED_CDS; mRNA.
DR   RefSeq; XP_015623420.1; XM_015767934.1.
DR   AlphaFoldDB; Q6K8R2; -.
DR   SMR; Q6K8R2; -.
DR   STRING; 4530.OS02T0605900-01; -.
DR   CAZy; CBM18; Carbohydrate-Binding Module Family 18.
DR   CAZy; GH19; Glycoside Hydrolase Family 19.
DR   PaxDb; Q6K8R2; -.
DR   PRIDE; Q6K8R2; -.
DR   EnsemblPlants; Os02t0605900-01; Os02t0605900-01; Os02g0605900.
DR   GeneID; 4329920; -.
DR   Gramene; Os02t0605900-01; Os02t0605900-01; Os02g0605900.
DR   KEGG; osa:4329920; -.
DR   eggNOG; KOG4742; Eukaryota.
DR   HOGENOM; CLU_045506_1_1_1; -.
DR   InParanoid; Q6K8R2; -.
DR   OMA; NNRVAYY; -.
DR   OrthoDB; 1574413at2759; -.
DR   Proteomes; UP000000763; Chromosome 2.
DR   Proteomes; UP000007752; Chromosome 2.
DR   Proteomes; UP000059680; Chromosome 2.
DR   Genevisible; Q6K8R2; OS.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
DR   GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
DR   GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
DR   GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR   GO; GO:0006952; P:defense response; IEA:UniProtKB-KW.
DR   GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR   Gene3D; 3.30.60.10; -; 1.
DR   InterPro; IPR001002; Chitin-bd_1.
DR   InterPro; IPR018371; Chitin-binding_1_CS.
DR   InterPro; IPR036861; Endochitinase-like_sf.
DR   InterPro; IPR016283; Glyco_hydro_19.
DR   InterPro; IPR000726; Glyco_hydro_19_cat.
DR   InterPro; IPR023346; Lysozyme-like_dom_sf.
DR   Pfam; PF00187; Chitin_bind_1; 1.
DR   Pfam; PF00182; Glyco_hydro_19; 2.
DR   PIRSF; PIRSF001060; Endochitinase; 1.
DR   SMART; SM00270; ChtBD1; 1.
DR   SUPFAM; SSF53955; SSF53955; 1.
DR   SUPFAM; SSF57016; SSF57016; 1.
DR   PROSITE; PS00026; CHIT_BIND_I_1; 1.
DR   PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR   PROSITE; PS00773; CHITINASE_19_1; 1.
PE   2: Evidence at transcript level;
KW   Carbohydrate metabolism; Chitin degradation; Chitin-binding;
KW   Disulfide bond; Glycoprotein; Glycosidase; Hydrolase; Plant defense;
KW   Polysaccharide degradation; Reference proteome; Signal.
FT   SIGNAL          1..20
FT                   /evidence="ECO:0000255"
FT   CHAIN           21..271
FT                   /note="Chitinase 6"
FT                   /id="PRO_0000383465"
FT   DOMAIN          25..60
FT                   /note="Chitin-binding type-1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   ACT_SITE        132
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000250|UniProtKB:P29022"
FT   CARBOHYD        268
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255"
FT   DISULFID        28..36
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        30..42
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        35..49
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        88..137
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        150..159
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   DISULFID        239..271
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00261"
FT   CONFLICT        6
FT                   /note="S -> L (in Ref. 5; AK064754)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        149
FT                   /note="Y -> H (in Ref. 5; AK064754)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   271 AA;  28534 MW;  3AAADD43296111AA CRC64;
     MARRLSLLAV VLAMVAAVSA STAAAQSCGC ASDQCCSKWG FCGTGSDYCG TGCQAGPCDV
     PATNDVSVAS IVTPEFFAAL VAQADDGCAA KGFYTRDAFL TAAGGYPSFG RTGSVDDSKR
     EIAAFFAHAN HETIKFCYIE EIDGPSKNYC DETSTQWPCM AGKGYYGRGP LQISWNFNYG
     PAGQSIGFDG LGDPDAVARS PVLAFQTALW YWTNNVHDAF VSGQGFGATI RAINGALECD
     GKNPTAVSNR VAYYQQFCQQ FGVDPGSNLT C
 
 
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