ID G1UH28_PUNGR Unreviewed; 299 AA. AC G1UH28; DT 16-NOV-2011, integrated into UniProtKB/TrEMBL. DT 16-NOV-2011, sequence version 1. DT 15-MAR-2017, entry version 25. 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}; 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). 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 PDB; 4TOQ; X-ray; 1.60 A; A/B/C/D=27-299. DR PDBsum; 4TOQ; -. DR SMR; G1UH28; -. DR Allergome; 11786; Pun g 14. DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC. DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro. DR Gene3D; 3.20.20.80; -; 1. DR InterPro; IPR001223; Glyco_hydro18_cat. DR InterPro; IPR001579; Glyco_hydro_18_chit_AS. DR InterPro; IPR013781; Glyco_hydro_catalytic_dom. 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 Glycosidase {ECO:0000256|RuleBase:RU000489, KW ECO:0000313|EMBL:BAK68869.1}; KW Hydrolase {ECO:0000256|RuleBase:RU000489, KW ECO:0000313|EMBL:BAK68869.1}; Signal {ECO:0000256|SAM:SignalP}. FT SIGNAL 1 26 {ECO:0000256|SAM:SignalP}. FT CHAIN 27 299 {ECO:0000256|SAM:SignalP}. FT /FTId=PRO_5003423490. FT DOMAIN 29 254 Glyco_hydro_18. {ECO:0000259|Pfam: FT PF00704}. 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 //