ID G1UH28_PUNGR Unreviewed; 299 AA. AC G1UH28; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 25-OCT-2017, entry version 30. DE SubName: Full=Class III chitinase {ECO:0000313|EMBL:BAK68869.1}; DE EC=3.2.1.14 {ECO:0000313|EMBL:BAK68869.1}; GN Name=PSC {ECO:0000313|EMBL:BAK68869.1}; GN ORFNames=CDL15_Pgr011527 {ECO:0000313|EMBL:OWM64072.1}; OS Punica granatum (Pomegranate). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae; OC Pentapetalae; rosids; malvids; Myrtales; Lythraceae; Punica. OX NCBI_TaxID=22663 {ECO:0000313|EMBL:BAK68869.1}; RN [1] {ECO:0000313|EMBL:BAK68869.1} RP NUCLEOTIDE SEQUENCE. RX PubMed=21790816; DOI=10.1111/j.1365-313X.2011.04727.x; RA Yang H., Zhang T., Masuda T., Lv C., Sun L., Qu G., Zhao G.; RT "Chitinase III in pomegranate seeds (Punica granatum Linn.): a high- RT capacity calcium-binding protein in amyloplasts."; RL Plant J. 68:765-776(2011). RN [2] {ECO:0000213|PDB:4TOQ} RP X-RAY CRYSTALLOGRAPHY (1.60 ANGSTROMS) OF 27-299, AND DISULFIDE BONDS. RX PubMed=25252615; DOI=10.1080/09168451.2014.962475; RA Masuda T., Zhao G., Mikami B.; RT "Crystal structure of class III chitinase from pomegranate provides RT the insight into its metal storage capacity."; RL Biosci. Biotechnol. Biochem. 79:45-50(2015). RN [3] {ECO:0000313|Proteomes:UP000197138} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. Dabenzi {ECO:0000313|Proteomes:UP000197138}; RX PubMed=28654223; DOI=10.1111/tpj.13625; RA Qin G., Xu C., Ming R., Tang H., Guyot R., Kramer E.M., Hu Y., Yi X., RA Qi Y., Xu X., Gao Z., Pan H., Jian J., Tian Y., Yue Z., Xu Y.; RT "The pomegranate (Punica granatum L.) genome and the genomics of RT punicalagin biosynthesis."; RL Plant J. 0:0-0(2017). RN [4] {ECO:0000313|EMBL:OWM64072.1} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC TISSUE=Fresh leaf {ECO:0000313|EMBL:OWM64072.1}; RA Xu C.; RT "The pomegranate genome and the genomics of punicalagin RT biosynthesis."; RL Submitted (JUN-2017) to the EMBL/GenBank/DDBJ databases. CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. CC {ECO:0000256|RuleBase:RU004453}. 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; AB605773; BAK68869.1; -; mRNA. DR EMBL; MTKT01005817; OWM64072.1; -; Genomic_DNA. DR PDB; 4TOQ; X-ray; 1.60 A; A/B/C/D=27-299. DR PDBsum; 4TOQ; -. DR Allergome; 11786; Pun g 14. DR Proteomes; UP000197138; Unassembled WGS sequence. DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR001579; Glyco_hydro_18_chit_AS. DR InterPro; IPR017853; Glycoside_hydrolase_SF. DR Pfam; PF00704; Glyco_hydro_18; 1. DR SUPFAM; SSF51445; SSF51445; 1. DR PROSITE; PS01095; CHITINASE_18; 1. PE 1: Evidence at protein level; KW 3D-structure {ECO:0000213|PDB:4TOQ}; KW Complete proteome {ECO:0000313|Proteomes:UP000197138}; KW Glycosidase {ECO:0000256|RuleBase:RU000489, KW ECO:0000313|EMBL:BAK68869.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000489, KW ECO:0000313|EMBL:BAK68869.1}; Magnesium {ECO:0000213|PDB:4TOQ}; KW Metal-binding {ECO:0000213|PDB:4TOQ}; KW Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 299 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5011090758. FT DOMAIN 29 254 Glyco_hydro_18. {ECO:0000259|Pfam: FT PF00704}. FT METAL 234 234 Magnesium. {ECO:0000213|PDB:4TOQ}. FT METAL 274 274 Magnesium. {ECO:0000213|PDB:4TOQ}. FT DISULFID 46 93 {ECO:0000213|PDB:4TOQ}. FT DISULFID 76 83 {ECO:0000213|PDB:4TOQ}. FT DISULFID 185 216 {ECO:0000213|PDB:4TOQ}. SQ SEQUENCE 299 AA; 31747 MW; D5D28157AA92D0B1 CRC64; MAKTLPFSRA LLLSLSILLV ARAISAGDIA IYWGQNGGEG TLASTCDTGR YAYVIVSFVT TFGNFRAPVV NLAGHCDPAA GTCTGLSDEI RSCQGKDIKV LMSIGGGAGD YSLVSEADAD NFADYLWNNF LGGQSSSRPL GDAVLDGIDF DIELGTTTFY DTLARALSSR STQAAKVYLT AAPQCPHPDS HLDAALNTGL FDNVWIQFYN NPLAQCQYSS GNTNDILSSW NTWTSSTTAG KIFLGLPAAP EAAGSGYIPP DVLTGQILPQ IKTSAKYGGV MLYSKFYDTT YSTTIKDQV //