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Database: UniProt
Entry: W9IFI0_FUSOX
LinkDB: W9IFI0_FUSOX
Original site: W9IFI0_FUSOX 
ID   W9IFI0_FUSOX            Unreviewed;       432 AA.
AC   W9IFI0;
DT   14-MAY-2014, integrated into UniProtKB/TrEMBL.
DT   14-MAY-2014, sequence version 1.
DT   24-JAN-2024, entry version 35.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=FOYG_08954 {ECO:0000313|EMBL:EWY92050.1};
OS   Fusarium oxysporum NRRL 32931.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC   Fusarium oxysporum species complex.
OX   NCBI_TaxID=660029 {ECO:0000313|EMBL:EWY92050.1, ECO:0000313|Proteomes:UP000030753};
RN   [1] {ECO:0000313|EMBL:EWY92050.1, ECO:0000313|Proteomes:UP000030753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FOSC 3-a {ECO:0000313|Proteomes:UP000030753}, and NRRL 32931
RC   {ECO:0000313|EMBL:EWY92050.1};
RG   The Broad Institute Genome Sequencing Platform;
RA   Ma L.-J., Gale L.R., Schwartz D.C., Zhou S., Corby-Kistler H., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Haas B., Abouelleil A., Alvarado L.,
RA   Arachchi H.M., Berlin A., Brown A., Chapman S.B., Chen Z., Dunbar C.,
RA   Freedman E., Gearin G., Gellesch M., Goldberg J., Griggs A., Gujja S.,
RA   Heiman D., Howarth C., Larson L., Lui A., MacDonald P.J.P., Mehta T.,
RA   Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M., Roberts A.,
RA   Saif S., Shea T., Shenoy N., Sisk P., Stolte C., Sykes S., Wortman J.,
RA   Nusbaum C., Birren B.;
RT   "The Genome Sequence of Fusarium oxysporum FOSC 3-a.";
RL   Submitted (JUN-2011) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:EWY92050.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=NRRL 32931 {ECO:0000313|EMBL:EWY92050.1};
RG   The Broad Institute Genomics Platform;
RA   Ma L.-J., Corby-Kistler H., Broz K., Gale L.R., Jonkers W., O'Donnell K.,
RA   Ploetz R., Steinberg C., Schwartz D.C., VanEtten H., Zhou S., Young S.K.,
RA   Zeng Q., Gargeya S., Fitzgerald M., Abouelleil A., Alvarado L.,
RA   Chapman S.B., Gainer-Dewar J., Goldberg J., Griggs A., Gujja S., Hansen M.,
RA   Howarth C., Imamovic A., Ireland A., Larimer J., McCowan C., Murphy C.,
RA   Pearson M., Poon T.W., Priest M., Roberts A., Saif S., Shea T., Sykes S.,
RA   Wortman J., Nusbaum C., Birren B.;
RT   "Annotation of the Genome Sequence of Fusarium oxysporum NRRL32931.";
RL   Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; JH717843; EWY92049.1; -; Genomic_DNA.
DR   EMBL; JH717843; EWY92050.1; -; Genomic_DNA.
DR   HOGENOM; CLU_031465_1_0_1; -.
DR   OrthoDB; 1449869at2759; -.
DR   Proteomes; UP000030753; Unassembled WGS sequence.
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   Reference proteome {ECO:0000313|Proteomes:UP000030753};
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_5015102701"
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;  47442 MW;  0D2D50038A703D9D CRC64;
     MRVSTLLGLS AYAVAEASCS RNIIYYDQWH TNDLPPKDVT HSVTHVMMSF ANSSLFTTEP
     SGKYEPFQPL KQVRALFDHD IKVCLAIGGW GDNAGFDAGL KTDRSRERFA RNVASTLDRL
     GYDCVDIDME YPGGNGADYK QVVNSKKTYE IQAFPKLLKE IKKFIGSKEL SIAVPGLERD
     MIAYVPSETP LIEKSVDFVN VMTYDLMNRR DSYTTHHVSV KGAARAIDKY LSLGFPAHKL
     VLGIPFYAKW FTTKQGYKCT NPIGCPTELL ENPKDGSDTG KSGSMTFEAA NFVSAPTNLT
     TTPDATCGAG TFFKCATGGC CAASGWCGDT AAHCGTGCQS AYGHCDGIDL SASFHEALDK
     GKTDKVNGGQ WYWDAPNRIF WSWDTPELIA EKINLLAKTR GVKSVMAWAL ALDSHDWSHL
     KAMQQGFDRV NA
//
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