ID N4UE48_FUSC1 Unreviewed; 971 AA.
AC N4UE48;
DT 26-JUN-2013, integrated into UniProtKB/TrEMBL.
DT 26-JUN-2013, sequence version 1.
DT 27-MAR-2024, entry version 48.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=FOC1_g10008997 {ECO:0000313|EMBL:ENH73504.1};
OS Fusarium oxysporum f. sp. cubense (strain race 1) (Panama disease fungus).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Nectriaceae; Fusarium;
OC Fusarium oxysporum species complex.
OX NCBI_TaxID=1229664 {ECO:0000313|EMBL:ENH73504.1, ECO:0000313|Proteomes:UP000016928};
RN [1] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RA Fang X., Huang J.;
RT "Genome sequencing and comparative transcriptomics of race 1 and race 4 of
RT banana pathogen: Fusarium oxysporum f. sp. cubense.";
RL Submitted (SEP-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|Proteomes:UP000016928}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 1 {ECO:0000313|Proteomes:UP000016928};
RX PubMed=24743270;
RA Guo L., Han L., Yang L., Zeng H., Fan D., Zhu Y., Feng Y., Wang G.,
RA Peng C., Jiang X., Zhou D., Ni P., Liang C., Liu L., Wang J., Mao C.,
RA Fang X., Peng M., Huang J.;
RT "Genome and Transcriptome Analysis of the Fungal Pathogen Fusarium
RT oxysporum f. sp. cubense Causing Banana Vascular Wilt Disease.";
RL PLoS ONE 9:E95543-E95543(2014).
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; KB730083; ENH73504.1; -; Genomic_DNA.
DR AlphaFoldDB; N4UE48; -.
DR SMR; N4UE48; -.
DR STRING; 1229664.N4UE48; -.
DR VEuPathDB; FungiDB:FOC1_g10008997; -.
DR HOGENOM; CLU_292872_0_0_1; -.
DR OMA; WAQNLYR; -.
DR Proteomes; UP000016928; Unassembled WGS sequence.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW.
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; cd00035; ChtBD1; 1.
DR Gene3D; 3.10.50.10; -; 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; IPR018371; Chitin-binding_1_CS.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
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:SF317; CHITINASE 11; 1.
DR Pfam; PF00187; Chitin_bind_1; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00270; ChtBD1; 2.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR SUPFAM; SSF57016; Plant lectins/antimicrobial peptides; 1.
DR PROSITE; PS00026; CHIT_BIND_I_1; 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};
KW Disulfide bond {ECO:0000256|ARBA:ARBA00023157, ECO:0000256|PROSITE-
KW ProRule:PRU00261}; Reference proteome {ECO:0000313|Proteomes:UP000016928};
KW Secreted {ECO:0000256|ARBA:ARBA00022525}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..16
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 17..971
FT /note="chitinase"
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5004121590"
FT DOMAIN 149..203
FT /note="Chitin-binding type-1"
FT /evidence="ECO:0000259|PROSITE:PS50941"
FT DOMAIN 165..529
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 46..68
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..106
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT DISULFID 163..175
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
FT DISULFID 168..182
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU00261"
SQ SEQUENCE 971 AA; 107005 MW; CC7105EF1AA45BAD CRC64;
MAIAILFLCL ATFADAENTR QLHGSRARHH RRANVITKAP AWAKEITNSP GHQNPAMAPP
DPTVELELSD DSATSLDQYY KDAENATESS DVTPNKSHLS RRSLEKRGSG PLYCKDGPCA
DDSCCGPEKI CGYGPDYCGK GCSSNCDATA MCGEYSEEGE MPCGMNLCCS ASGWCGTTEV
FCDNADPVHK TLPCQAGYGS CNIASSPSCA KGSGSTNGRT IGYYQSWNVR ARKCDTKTPK
QLNTKGFTHL FYSFAFIDPV SFKVTPAHDD DVKQMREFTN LSKDVRAYMD EYGFQGVDLD
WEYPGEPKRG GRKLADTRNF SMLLKEMRAA YGSKYGISLT LAPDYWYLRW FDAKVMEPYV
DFFGFMAYDL HGYWDEDVKT LGKIIRGQAD IREIGNNTIP LWFGGLDPKK LNFGLALYGR
GYTVADKSCN NLGCSFVGPS KKGECTDSDG VMSLGEIKNL IKKGVKSTYL KDSMMKQITF
DDQWIGYDDE ETFADKKAWA DGYCFGGTMI WSIDFQPSDN STDGSGDVPA LPDLDGIGAI
PKDLQDKVLK KCDTGFSYDN YGDLPKLWYD SGAEQWADAY IKSQKDHTNW AQNLYRNLFE
KKDHTKFSCV TPNSRCDFDA SCVNVEFPYL HEGSQSTVRQ QDHSDPCHRL RDETYPRHQE
WSSSAFSMAS AIAAPIPAVG GPLAGISGLA SMIGTFTSTV GGNDNAVDAT DTLTFAVKTA
AVEGKRKIAS IVSSVYGDFG HAQNDLPKTM LVGGADNPAI KVFGYGAWLR DNDLTDLSGA
VERMSDKMNQ ALLWQMARLF KGFYVVIRDD LPINKCTHPN NAWDDRTGRC LDILSWWPKS
ASGRVGGDLA MEKVWDKWNM SPLWTLRNAV ECWENNGGKI GDAKVKALQS EWTNGVPPPC
FFAMPVLKGN WSKDAASDGA IWLAGDFVGQ EGQAGRLWPK DKCDKANREL DPITGGQVKK
CSSLNKVGGE K
//
