ID CHI5_ORYSJ Reviewed; 288 AA. AC Q7Y1Z0; A0A0P0WC98; Q7XT47; DT 22-SEP-2009, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 27-MAR-2024, entry version 128. DE RecName: Full=Chitinase 5; DE EC=3.2.1.14; DE AltName: Full=Class IV chitinase a; DE Short=OsChia4a; DE AltName: Full=Pathogenesis related (PR)-3 chitinase 5; DE Flags: Precursor; GN Name=Cht5; OrderedLocusNames=Os04g0494100, LOC_Os04g41680; GN ORFNames=OsJ_15308, OSJNBb0091E11.12; 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 [MRNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12834284; DOI=10.1271/bbb.67.1063; RA Truong N.-H., Park S.-M., Nishizawa Y., Watanabe T., Sasaki T., Itoh Y.; RT "Structure, heterologous expression, and properties of rice (Oryza sativa RT L.) family 19 chitinases."; RL Biosci. Biotechnol. Biochem. 67:1063-1070(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Nipponbare; RX PubMed=12447439; DOI=10.1038/nature01183; RA Feng Q., Zhang Y., Hao P., Wang S., Fu G., Huang Y., Li Y., Zhu J., Liu Y., RA Hu X., Jia P., Zhang Y., Zhao Q., Ying K., Yu S., Tang Y., Weng Q., RA Zhang L., Lu Y., Mu J., Lu Y., Zhang L.S., Yu Z., Fan D., Liu X., Lu T., RA Li C., Wu Y., Sun T., Lei H., Li T., Hu H., Guan J., Wu M., Zhang R., RA Zhou B., Chen Z., Chen L., Jin Z., Wang R., Yin H., Cai Z., Ren S., Lv G., RA Gu W., Zhu G., Tu Y., Jia J., Zhang Y., Chen J., Kang H., Chen X., Shao C., RA Sun Y., Hu Q., Zhang X., Zhang W., Wang L., Ding C., Sheng H., Gu J., RA Chen S., Ni L., Zhu F., Chen W., Lan L., Lai Y., Cheng Z., Gu M., Jiang J., RA Li J., Hong G., Xue Y., Han B.; RT "Sequence and analysis of rice chromosome 4."; RL Nature 420:316-320(2002). RN [3] 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 [4] 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 [5] 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 [6] 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 [7] 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 [8] 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 sheaths and meristems and at lower CC levels in roots and leaves. {ECO:0000269|PubMed:16936841}. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase CC class IV subfamily. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AB096140; BAC76691.1; -; mRNA. DR EMBL; AL606629; CAE01675.2; -; Genomic_DNA. DR EMBL; AP008210; BAF15100.1; -; Genomic_DNA. DR EMBL; AP014960; BAS89869.1; -; Genomic_DNA. DR EMBL; CM000141; EEE61251.1; -; Genomic_DNA. DR EMBL; AK071013; BAG92259.1; -; mRNA. DR EMBL; AK104242; BAG96537.1; -; mRNA. DR EMBL; AK104426; BAG96672.1; -; mRNA. DR RefSeq; XP_015636326.1; XM_015780840.1. DR AlphaFoldDB; Q7Y1Z0; -. DR SMR; Q7Y1Z0; -. DR STRING; 39947.Q7Y1Z0; -. DR CAZy; CBM18; Carbohydrate-Binding Module Family 18. DR CAZy; GH19; Glycoside Hydrolase Family 19. DR PaxDb; 39947-Q7Y1Z0; -. DR EnsemblPlants; Os04t0494100-02; Os04t0494100-02; Os04g0494100. DR GeneID; 4336265; -. DR Gramene; Os04t0494100-02; Os04t0494100-02; Os04g0494100. DR KEGG; osa:4336265; -. DR eggNOG; KOG4742; Eukaryota. DR HOGENOM; CLU_045506_1_1_1; -. DR InParanoid; Q7Y1Z0; -. DR OMA; YYNDYCT; -. DR OrthoDB; 997724at2759; -. DR Proteomes; UP000000763; Chromosome 4. DR Proteomes; UP000007752; Chromosome 4. DR Proteomes; UP000059680; Chromosome 4. 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 CDD; cd00325; chitinase_GH19; 1. DR CDD; cd00035; ChtBD1; 1. DR Gene3D; 1.10.530.10; -; 1. DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 1. DR Gene3D; 3.30.60.10; Endochitinase-like; 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 PANTHER; PTHR22595; CHITINASE-RELATED; 1. DR PANTHER; PTHR22595:SF147; ENDOCHITINASE CHI; 1. 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; Lysozyme-like; 1. DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1. DR PROSITE; PS00026; CHIT_BIND_I_1; 1. DR PROSITE; PS50941; CHIT_BIND_I_2; 1. DR PROSITE; PS00773; CHITINASE_19_1; 1. DR PROSITE; PS00774; CHITINASE_19_2; 1. DR Genevisible; Q7Y1Z0; OS. PE 2: Evidence at transcript level; KW Carbohydrate metabolism; Chitin degradation; Chitin-binding; KW Disulfide bond; Glycosidase; Hydrolase; Plant defense; KW Polysaccharide degradation; Reference proteome; Signal. FT SIGNAL 1..29 FT /evidence="ECO:0000255" FT CHAIN 30..288 FT /note="Chitinase 5" FT /id="PRO_0000383464" FT DOMAIN 30..64 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT ACT_SITE 151 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:P29022" FT DISULFID 32..40 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 34..46 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 39..53 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 57..62 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 107..156 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 169..178 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" FT DISULFID 256..288 FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00261" SQ SEQUENCE 288 AA; 30487 MW; E988A12134910C52 CRC64; MANSPTPTML AFLALGLALL LSATGQASAQ NCGCQSNMCC SKWGYCGTGK DYCGDGCRSG PCYGGGGGGG GGGGGGGGGG GGSGVSVESV VTEAFFNGIK NQAPNGCAGK NFYTRQSFLN AAHSYSGFAR DRTNDDSKRE IAAFFAHVTH ETGHMCYINE INGASMDYCD KNNKQWPCQP GKKYYGRGPL QISWNYNYGP AGQNIGFDGL RDPDRVAQDP TISFKTALWF WMNNVHQVML QGFGATIRAI NGALECNGKN PGAVNARVNY YKDYCRQFGV DPGGNLYC //