ID F9FAU4_FUSOF Unreviewed; 432 AA.
AC F9FAU4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 48.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=FOXB_03520 {ECO:0000313|EMBL:EGU85964.1};
OS Fusarium oxysporum (strain Fo5176) (Fusarium vascular wilt).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=660025 {ECO:0000313|EMBL:EGU85964.1};
RN [1] {ECO:0000313|EMBL:EGU85964.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Fo5176 {ECO:0000313|EMBL:EGU85964.1};
RX PubMed=21942452; DOI=10.1094/mpmi-08-11-0212;
RA Thatcher L.F., Gardiner D.M., Kazan K., Manners J.;
RT "A highly conserved effector in Fusarium oxysporum is required for full
RT virulence on Arabidopsis.";
RL Mol. Plant Microbe Interact. 25:180-190(2012).
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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:EGU85964.1}.
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DR EMBL; AFQF01001214; EGU85964.1; -; Genomic_DNA.
DR AlphaFoldDB; F9FAU4; -.
DR STRING; 660025.F9FAU4; -.
DR PaxDb; 5507-FOXG_10748P0; -.
DR GO; GO:0008061; F:chitin binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd11618; ChtBD1_1; 1.
DR Gene3D; 3.30.60.10; Endochitinase-like; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 2.
DR InterPro; IPR001002; Chitin-bd_1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR036861; Endochitinase-like_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF337; CHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS50941; CHIT_BIND_I_2; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Chitin-binding {ECO:0000256|ARBA:ARBA00022669, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Disulfide bond {ECO:0000256|PROSITE-ProRule:PRU00261};
KW Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 18..432
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5003382880"
FT DOMAIN 20..430
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT DOMAIN 304..347
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DISULFID 315..327
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 320..334
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 432 AA; 47427 MW; 87ED4F010CC28453 CRC64;
MRVSTLLGLS AYAVAEASCS RNIIYYDQWH TNDLPPKDVT HSVTHVMMSF ANSSLFTTEP
SGKYEPFQPL KQVRALFDHD IKVCLAIGGW GDNAGFDAGL KTDRSRERFA RNVASTLDRL
GYDCVDIDME YPGGNGADYK QVVNSKKTYE IQAFPKLLKE IKKFIGSKEL SIAVPGLERD
MIAYIPSQTP LIEKSVDFVN VMTYDLMNRR DSYTTHHVSV KGAARAIDKY LSLGFPAHKL
VLGIPFYAKW FTTKQGYKCT NPIGCPTELL ENPKDGSDTG KSGSMTFEAA NFVSAPTNLT
TTPDATCGAG TFFKCATGGC CAASGWCGDT AAHCGTGCQS AYGHCDGIDL SASFHEALDK
GKTDKANGGQ WYWDAPNRIF WSWDTPELIA EKINLLAKTR GVKSVMAWAL ALDSHDWSHL
KAMQQGFDRV NA
//
