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Basic endochitinase A (EC 3.2.1.14) (Rye seed chitinase-a) (RSC-a)

 CHIA_SECCE              Reviewed;         321 AA.
Q9FRV1;
25-OCT-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
10-OCT-2018, entry version 76.
RecName: Full=Basic endochitinase A;
EC=3.2.1.14;
AltName: Full=Rye seed chitinase-a;
Short=RSC-a;
Flags: Precursor;
Name=rsca {ECO:0000312|EMBL:BAB18519.1};
Secale cereale (Rye).
Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
Spermatophyta; Magnoliophyta; Liliopsida; Poales; Poaceae; BOP clade;
Pooideae; Triticodae; Triticeae; Hordeinae; Secale.
NCBI_TaxID=4550;
[1] {ECO:0000305, ECO:0000312|EMBL:BAB18519.1}
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 20-24, FUNCTION,
CATALYTIC ACTIVITY, AND MUTAGENESIS OF TRP-42 AND GLU-145.
TISSUE=Seed {ECO:0000269|PubMed:14981295};
PubMed=14981295; DOI=10.1271/bbb.68.324;
Ohnuma T., Taira T., Yamagami T., Aso Y., Ishiguro M.;
"Molecular cloning, functional expression, and mutagenesis of cDNA
encoding class I chitinase from rye (Secale cereale) seeds.";
Biosci. Biotechnol. Biochem. 68:324-332(2004).
[2] {ECO:0000305}
PROTEIN SEQUENCE OF 20-321.
PubMed=7764543; DOI=10.1271/bbb.58.322;
Yamagami T., Funatsu G.;
"The complete amino acid sequence of chitinase-a from the seeds of rye
(Secale cereal).";
Biosci. Biotechnol. Biochem. 58:322-329(1994).
[3] {ECO:0000305}
PROTEIN SEQUENCE OF 20-26, FUNCTION, CATALYTIC ACTIVITY, AND
BIOPHYSICOCHEMICAL PROPERTIES.
PubMed=7763659; DOI=10.1271/bbb.57.643;
Yamagami T., Funatsu G.;
"Purification and some properties of three chitinases from the seeds
of rye (Secale cereale).";
Biosci. Biotechnol. Biochem. 57:643-647(1993).
[4] {ECO:0000305}
DISULFIDE BONDS.
PubMed=10923812; DOI=10.1271/bbb.64.1313;
Yamagami T., Funatsu G., Ishiguro M.;
"Positions of disulfide bonds in rye (Secale cereale) seed chitinase-
a.";
Biosci. Biotechnol. Biochem. 64:1313-1316(2000).
[5] {ECO:0000305}
FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, AND DEVELOPMENTAL
STAGE.
PubMed=11826968; DOI=10.1271/bbb.65.2710;
Taira T., Yamagami T., Aso Y., Ishiguro M., Ishihara M.;
"Localization, accumulation, and antifungal activity of chitinases in
rye (Secale cereale) seed.";
Biosci. Biotechnol. Biochem. 65:2710-2718(2001).
[6] {ECO:0000305}
FUNCTION.
PubMed=12092848; DOI=10.1271/bbb.66.970;
Taira T., Ohnuma T., Yamagami T., Aso Y., Ishiguro M., Ishihara M.;
"Antifungal activity of rye (Secale cereale) seed chitinases: the
different binding manner of class I and class II chitinases to the
fungal cell walls.";
Biosci. Biotechnol. Biochem. 66:970-977(2002).
-!- FUNCTION: Defense against chitin-containing fungal pathogens.
Binds the hyphal tips, lateral walls and septa of fungi and
degrades mature chitin. {ECO:0000269|PubMed:11826968,
ECO:0000269|PubMed:12092848, ECO:0000269|PubMed:14981295,
ECO:0000269|PubMed:7763659}.
-!- CATALYTIC ACTIVITY: Random endo-hydrolysis of N-acetyl-beta-D-
glucosaminide (1->4)-beta-linkages in chitin and chitodextrins.
{ECO:0000269|PubMed:11826968, ECO:0000269|PubMed:14981295,
ECO:0000269|PubMed:7763659}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
pH dependence:
Optimum pH is about 5.0. Stable between pH 4-8.
{ECO:0000269|PubMed:7763659};
Temperature dependence:
Enzyme activity is retained almost fully under 40 degrees
Celsius and completely destroyed at 70 degrees Celsius. At 60
degrees Celsius the activity was over 80% compared to the
untreated enzyme. {ECO:0000269|PubMed:7763659};
-!- TISSUE SPECIFICITY: Localized in the aleurone cells of the seed
endosperm (at protein level). {ECO:0000269|PubMed:11826968}.
-!- DEVELOPMENTAL STAGE: Levels increase from 23 to 40 days after
flowering, and are maintained until maturation (at protein level).
{ECO:0000269|PubMed:11826968}.
-!- SIMILARITY: Belongs to the glycosyl hydrolase 19 family. Chitinase
class I subfamily. {ECO:0000269|PubMed:14981295}.
-----------------------------------------------------------------------
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EMBL; AB051578; BAB18519.1; -; mRNA.
PIR; JC2071; JC2071.
ProteinModelPortal; Q9FRV1; -.
SMR; Q9FRV1; -.
CAZy; CBM18; Carbohydrate-Binding Module Family 18.
CAZy; GH19; Glycoside Hydrolase Family 19.
PRIDE; Q9FRV1; -.
BRENDA; 3.2.1.14; 5654.
GO; GO:0005576; C:extracellular region; IC:UniProtKB.
GO; GO:0008061; F:chitin binding; IDA:UniProtKB.
GO; GO:0004568; F:chitinase activity; IDA:UniProtKB.
GO; GO:0016998; P:cell wall macromolecule catabolic process; IDA:UniProtKB.
GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
GO; GO:0050832; P:defense response to fungus; IDA:UniProtKB.
GO; GO:0031640; P:killing of cells of other organism; IEA:UniProtKB-KW.
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;
Antimicrobial; Carbohydrate metabolism; Chitin degradation;
Chitin-binding; Direct protein sequencing; Disulfide bond; Fungicide;
Glycosidase; Hydrolase; Plant defense; Polysaccharide degradation;
Signal.
SIGNAL 1 19 {ECO:0000269|PubMed:14981295,
ECO:0000269|PubMed:7763659,
ECO:0000269|PubMed:7764543}.
CHAIN 20 321 Basic endochitinase A.
{ECO:0000269|PubMed:14981295}.
/FTId=PRO_0000042670.
DOMAIN 20 60 Chitin-binding type-1.
{ECO:0000255|PROSITE-ProRule:PRU00261}.
REGION 62 79 Hinge region (Gly/Pro/Thr-rich).
{ECO:0000255}.
REGION 80 321 Catalytic. {ECO:0000255}.
ACT_SITE 145 145 Proton donor.
{ECO:0000250|UniProtKB:P29022}.
DISULFID 22 37 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 31 43 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 34 61 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 36 50 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 54 58 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 101 163 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 175 183 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
DISULFID 301 314 {ECO:0000255|PROSITE-ProRule:PRU00261,
ECO:0000269|PubMed:10923812}.
MUTAGEN 42 42 W->A: Reduces chitinase activity towards
soluble chitin to 65.5% and towards
insoluble chitin. Reduces chitin-binding
activity and anti-fungal activity.
{ECO:0000269|PubMed:14981295}.
MUTAGEN 145 145 E->Q: Abolishes chitinase activity
towards insoluble and soluble chitin.
Abolishes chitin-binding activity and
anti-fungal activity.
{ECO:0000269|PubMed:14981295}.
CONFLICT 305 305 R -> G (in Ref. 2; AA sequence).
{ECO:0000305}.
SEQUENCE 321 AA; 33642 MW; 76E5902BBC337C8E CRC64;
MGAFALFAVL AMAVTMAVAE QCGSQAGGAT CPNCLCCSRF GWCGSTSDYC GDGCQSQCAG
CGGGGTPVTP TPTPSGGGGV SSIVSRALFD RMLLHRNDGA CQAKGFYTYD AFVAAAGAFP
GFGTTGSTDT RKREVAAFLA QTSHETTGGW ATAPDGAFAW GYCFKQERGA TSNYCTPSAQ
WPCAPGKSYY GRGPIQLSHN YNYGPAGRAI GVDLLRNPDL VATDPTVSFK TAMWFWMTAQ
APKPSSHAVI TGQWSPSGTD RAAGRVPGFG VITNIVNGGI ECGHGQDSRV ADRIGFYKRY
CDILRVGYGN NLDCYNQRPF A


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