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Basic 30 kDa endochitinase (EC 3.2.1.14)

 CHIC_SOLLC              Reviewed;         322 AA.
Q05538; P80800;
01-JUN-1994, integrated into UniProtKB/Swiss-Prot.
01-JUN-1994, sequence version 1.
16-JAN-2019, entry version 130.
RecName: Full=Basic 30 kDa endochitinase;
EC=3.2.1.14;
Flags: Precursor;
Name=CHI9;
Solanum lycopersicum (Tomato) (Lycopersicon esculentum).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; eudicotyledons; Gunneridae;
Pentapetalae; asterids; lamiids; Solanales; Solanaceae; Solanoideae;
Solaneae; Solanum; Lycopersicon.
NCBI_TaxID=4081;
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
STRAIN=cv. Moneymaker;
PubMed=8400122; DOI=10.1007/BF00028974;
Danhash N., Wagemakers C.A.M., van Kan J.A.L., de Wit P.J.G.M.;
"Molecular characterization of four chitinase cDNAs obtained from
Cladosporium fulvum-infected tomato.";
Plant Mol. Biol. 22:1017-1029(1993).
[2]
PROTEIN SEQUENCE OF 23-38, AND SUBCELLULAR LOCATION.
PubMed=9188482; DOI=10.1074/jbc.272.25.15841;
Robertson D., Mitchell G.P., Gilroy J.S., Gerrish C., Bolwell G.P.,
Slabas A.R.;
"Differential extraction and protein sequencing reveals major
differences in patterns of primary cell wall proteins from plants.";
J. Biol. Chem. 272:15841-15848(1997).
[3]
PROTEIN SEQUENCE OF 97-124; 160-180; 187-223 AND 259-282.
Almagro L., Briceno Z., Pedreno M.A.;
Submitted (JUL-2008) to UniProtKB.
-!- FUNCTION: Defense against chitin-containing fungal pathogens.
-!- CATALYTIC ACTIVITY:
Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
(1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
-!- SUBCELLULAR LOCATION: Vacuole {ECO:0000269|PubMed:9188482}.
Secreted, cell wall {ECO:0000269|PubMed:9188482}. Note=Vacuolar,
protoplast and cell wall.
-!- INDUCTION: By fungal infection.
-!- PTM: The 4-hydroxyproline residues are not glycosylated in this
plant vacuolar protein. {ECO:0000250}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
class I subfamily. {ECO:0000305}.
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EMBL; Z15140; CAA78845.1; -; mRNA.
PIR; S37344; S37344.
RefSeq; NP_001234403.1; NM_001247474.2.
UniGene; Les.3406; -.
ProteinModelPortal; Q05538; -.
SMR; Q05538; -.
STRING; 4081.Solyc10g055810.1.1; -.
CAZy; CBM18; Carbohydrate-Binding Module Family 18.
CAZy; GH19; Glycoside Hydrolase Family 19.
PaxDb; Q05538; -.
EnsemblPlants; Solyc10g055810.1.1; Solyc10g055810.1.1; Solyc10g055810.1.
GeneID; 544148; -.
Gramene; Solyc10g055810.1.1; Solyc10g055810.1.1; Solyc10g055810.1.
KEGG; sly:544148; -.
eggNOG; KOG4742; Eukaryota.
eggNOG; COG3979; LUCA.
InParanoid; Q05538; -.
KO; K20547; -.
OMA; SPEWPCA; -.
OrthoDB; 1132954at2759; -.
Proteomes; UP000004994; Chromosome 10.
GO; GO:0005618; C:cell wall; IEA:UniProtKB-SubCell.
GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
GO; GO:0005773; C:vacuole; IEA:UniProtKB-SubCell.
GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
GO; GO:0004568; F:chitinase activity; IBA:GO_Central.
GO; GO:0030247; F:polysaccharide binding; IBA:GO_Central.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IEA:InterPro.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IBA:GO_Central.
GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
CDD; cd00325; chitinase_glyco_hydro_19; 1.
Gene3D; 3.30.60.10; -; 1.
InterPro; IPR001002; Chitin-bd_1.
InterPro; IPR018371; Chitin-binding_1_CS.
InterPro; IPR036861; Endochitinase-like_sf.
InterPro; IPR016283; Glyco_hydro_19.
InterPro; IPR000726; Glyco_hydro_19_cat.
InterPro; IPR023346; Lysozyme-like_dom_sf.
Pfam; PF00187; Chitin_bind_1; 1.
Pfam; PF00182; Glyco_hydro_19; 1.
PIRSF; PIRSF001060; Endochitinase; 1.
PRINTS; PR00451; CHITINBINDNG.
ProDom; PD000609; Chitin_bd_1; 1.
SMART; SM00270; ChtBD1; 1.
SUPFAM; SSF53955; SSF53955; 1.
SUPFAM; SSF57016; SSF57016; 1.
PROSITE; PS00026; CHIT_BIND_I_1; 1.
PROSITE; PS50941; CHIT_BIND_I_2; 1.
PROSITE; PS00773; CHITINASE_19_1; 1.
PROSITE; PS00774; CHITINASE_19_2; 1.
1: Evidence at protein level;
Carbohydrate metabolism; Cell wall; Chitin degradation;
Chitin-binding; Complete proteome; Direct protein sequencing;
Disulfide bond; Glycosidase; Hydrolase; Hydroxylation; Plant defense;
Polysaccharide degradation; Reference proteome; Secreted; Signal;
Vacuole.
SIGNAL 1 22 {ECO:0000269|PubMed:9188482}.
CHAIN 23 315 Basic 30 kDa endochitinase.
/FTId=PRO_0000005301.
PROPEP 316 322 Removed in mature form.
/FTId=PRO_0000005302.
DOMAIN 23 64 Chitin-binding type-1.
{ECO:0000255|PROSITE-ProRule:PRU00261}.
ACT_SITE 138 138 Proton donor.
{ECO:0000250|UniProtKB:P29022}.
MOD_RES 66 66 4-hydroxyproline. {ECO:0000250}.
MOD_RES 68 68 4-hydroxyproline. {ECO:0000250}.
DISULFID 25 40 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 34 46 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 39 53 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 58 62 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 93 156 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 168 176 {ECO:0000255|PROSITE-ProRule:PRU00261}.
DISULFID 275 307 {ECO:0000255|PROSITE-ProRule:PRU00261}.
CONFLICT 34 34 C -> R (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 36 36 Missing (in Ref. 2; AA sequence).
{ECO:0000305}.
CONFLICT 106 106 V -> I (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 107 107 T -> N (in Ref. 3; AA sequence).
{ECO:0000305}.
CONFLICT 107 107 T -> S (in Ref. 3; AA sequence).
{ECO:0000305}.
SEQUENCE 322 AA; 34345 MW; D13A9191AEE8FC5A CRC64;
MRLSEFTTLF LLFSVLLLSA SAEQCGSQAG GALCASGLCC SKFGWCGNTN EYCGPGNCQS
QCPGGPGPSG DLGGVISNSM FDQMLNHRND NACQGKNNFY SYNAFVTAAG SFPGFGTTGD
ITARKREIAA FLAQTSHETT GGWPTAPDGP YAWGYCFLRE QGSPGDYCTP SSQWPCAPGR
KYFGRGPIQI SHNYNYGPCG RAIGVDLLNN PDLVATDPVI SFKSAIWFWM TPQSPKPSCH
DVITGRWQPS GADQAANRVP GFGVITNIIN GGLECGHGSD SRVQDRIGFY RRYCGILGVS
PGENLDCGNQ RSFGNGLLVD IM


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