ID A0A5A7Q5F1_STRAF Unreviewed; 569 AA. AC A0A5A7Q5F1; DT 13-NOV-2019, integrated into UniProtKB/TrEMBL. DT 13-NOV-2019, sequence version 1. DT 27-NOV-2024, entry version 15. DE SubName: Full=Chitinase {ECO:0000313|EMBL:GER40459.1}; GN ORFNames=STAS_17132 {ECO:0000313|EMBL:GER40459.1}; OS Striga asiatica (Asiatic witchweed) (Buchnera asiatica). OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta; OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae; OC asterids; lamiids; Lamiales; Orobanchaceae; Buchnereae; Striga. OX NCBI_TaxID=4170 {ECO:0000313|EMBL:GER40459.1, ECO:0000313|Proteomes:UP000325081}; RN [1] {ECO:0000313|Proteomes:UP000325081} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=cv. UVA1 {ECO:0000313|Proteomes:UP000325081}; RX PubMed=31522940; DOI=10.1016/j.cub.2019.07.086; RA Yoshida S., Kim S., Wafula E.K., Tanskanen J., Kim Y.M., Honaas L., RA Yang Z., Spallek T., Conn C.E., Ichihashi Y., Cheong K., Cui S., Der J.P., RA Gundlach H., Jiao Y., Hori C., Ishida J.K., Kasahara H., Kiba T., Kim M.S., RA Koo N., Laohavisit A., Lee Y.H., Lumba S., McCourt P., Mortimer J.C., RA Mutuku J.M., Nomura T., Sasaki-Sekimoto Y., Seto Y., Wang Y., Wakatake T., RA Sakakibara H., Demura T., Yamaguchi S., Yoneyama K., Manabe R.I., RA Nelson D.C., Schulman A.H., Timko M.P., dePamphilis C.W., Choi D., RA Shirasu K.; RT "Genome Sequence of Striga asiatica Provides Insight into the Evolution of RT Plant Parasitism."; RL Curr. Biol. 29:3041-3052.e4(2019). CC -!- FUNCTION: Defense against chitin-containing fungal pathogens. CC {ECO:0000256|ARBA:ARBA00003102}. CC -!- SUBCELLULAR LOCATION: Vacuole {ECO:0000256|ARBA:ARBA00004116}. CC -!- CAUTION: Lacks conserved residue(s) required for the propagation of CC feature annotation. {ECO:0000256|PROSITE-ProRule:PRU00261}. CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ CC whole genome shotgun (WGS) entry which is preliminary data. CC {ECO:0000313|EMBL:GER40459.1}. 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; BKCP01005883; GER40459.1; -; Genomic_DNA. DR AlphaFoldDB; A0A5A7Q5F1; -. DR Proteomes; UP000325081; Unassembled WGS sequence. DR GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell. DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule. DR GO; GO:0004568; F:chitinase activity; IEA:InterPro. 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 CDD; cd00325; chitinase_GH19; 2. DR CDD; cd00035; ChtBD1; 2. DR FunFam; 3.30.20.10:FF:000001; Endochitinase (Chitinase); 2. DR Gene3D; 1.10.530.10; -; 2. DR Gene3D; 3.30.20.10; Endochitinase, domain 2; 2. DR Gene3D; 3.30.60.10; Endochitinase-like; 2. DR InterPro; IPR001002; Chitin-bd_1. DR InterPro; IPR018371; Chitin-binding_1_CS. DR InterPro; IPR036861; Endochitinase-like_sf. DR InterPro; IPR000726; Glyco_hydro_19_cat. DR InterPro; IPR023346; Lysozyme-like_dom_sf. DR PANTHER; PTHR22595; CHITINASE-RELATED; 1. DR PANTHER; PTHR22595:SF193; ENDOCHITINASE EP3; 1. DR Pfam; PF00187; Chitin_bind_1; 2. DR Pfam; PF00182; Glyco_hydro_19; 2. DR SMART; SM00270; ChtBD1; 2. DR SUPFAM; SSF53955; Lysozyme-like; 2. DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 2. DR PROSITE; PS00026; CHIT_BIND_I_1; 2. DR PROSITE; PS50941; CHIT_BIND_I_2; 2. DR PROSITE; PS00773; CHITINASE_19_1; 2. DR PROSITE; PS00774; CHITINASE_19_2; 2. PE 4: Predicted; KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023024}; KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024}; KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE- KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261}; KW Plant defense {ECO:0000256|ARBA:ARBA00022821}; KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023024}; KW Reference proteome {ECO:0000313|Proteomes:UP000325081}; KW Signal {ECO:0000256|SAM:SignalP}; Vacuole {ECO:0000256|ARBA:ARBA00022554}. FT SIGNAL 1..32 FT /evidence="ECO:0000256|SAM:SignalP" FT CHAIN 33..569 FT /evidence="ECO:0000256|SAM:SignalP" FT /id="PRO_5023029845" FT DOMAIN 32..67 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000259|PROSITE:PS50941" FT DOMAIN 331..366 FT /note="Chitin-binding type-1" FT /evidence="ECO:0000259|PROSITE:PS50941" FT DISULFID 37..49 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261" FT DISULFID 42..56 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261" FT DISULFID 336..348 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261" FT DISULFID 341..355 FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261" SQ SEQUENCE 569 AA; 61548 MW; B30CAACFDFBA3152 CRC64; MNFLTTKKSL PPISGLLALA LLLVAGAQWA SAQNCGCTNN LCCSRWGYCG TGDAYCGAGC QAGPCYGSQG GGNLANIVTD AFFNRIVNRA PANCPGRGFY TRSAFLQAAR SYPQFGTGAS DVARREVAAF FAHVTHETGE EIGGASRDYC DENNREYPCA PGRGYYGRGP LQLSWNYNYG PAGRSIGFDG LNNPDIVARD PVISFRTALW FWMNNCHNRI TSGQGFGSTI RAINSMECNG RNPNAVSARV NYFRDYCNQL RVDPGANLRR WLKLGSNTLN TNINILSSLP LQSHTQTHNM NSLTTKKSLP PINGLLALAF LLVAGAQWTS AQNCGCTNNL CCSRFGYCGT GDAYCGDGCQ AGPCYASQGG GNLANIVTDA FFNGIANRAA ANCPGRGFYT RSAFLQAARS YPQFGTGASD VARREVAAFF AHVTHETGEE IGGASRDYCD ENNREYPCAP GRGYYGRGPL QLSWNYNYGP AGRSIGFDGL NNPDIVARDP VISFRTALWF WMNNCHNRII SGQGFGSTIR AINSMECNGG NPNTVTARVN YFRDYCNQLR VDPGANLRC //