ID A0A0F4YYD6_TALEM Unreviewed; 336 AA.
AC A0A0F4YYD6;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 22-FEB-2023, entry version 20.
DE SubName: Full=Chitinase {ECO:0000313|EMBL:KKA23249.1};
GN ORFNames=T310_2742 {ECO:0000313|EMBL:KKA23249.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA23249.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA23249.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA23249.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: GPI-anchored chitinase involved in the degradation of chitin,
CC a component of the cell walls of fungi and exoskeletal elements of some
CC animals (including worms and arthropods). Required to reshape the cell
CC wall at the sites where cell wall remodeling and/or cell wall
CC maturation actively take place such as sites of conidia formation.
CC {ECO:0000256|ARBA:ARBA00024658}.
CC -!- SUBCELLULAR LOCATION: Secreted, cell wall
CC {ECO:0000256|ARBA:ARBA00004191}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class III subfamily. {ECO:0000256|ARBA:ARBA00025727}.
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:KKA23249.1}.
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DR EMBL; LASV01000107; KKA23249.1; -; Genomic_DNA.
DR RefSeq; XP_013329861.1; XM_013474407.1.
DR AlphaFoldDB; A0A0F4YYD6; -.
DR SMR; A0A0F4YYD6; -.
DR STRING; 1408163.A0A0F4YYD6; -.
DR GeneID; 25315093; -.
DR OrthoDB; 360175at2759; -.
DR Proteomes; UP000053958; Unassembled WGS sequence.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR CDD; cd02877; GH18_hevamine_XipI_class_III; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR045321; Cts1-like.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR45708; ENDOCHITINASE; 1.
DR PANTHER; PTHR45708:SF49; ENDOCHITINASE; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Cell wall {ECO:0000256|ARBA:ARBA00022512};
KW Reference proteome {ECO:0000313|Proteomes:UP000053958};
KW Secreted {ECO:0000256|ARBA:ARBA00022512}; Signal {ECO:0000256|SAM:SignalP}.
FT SIGNAL 1..19
FT /evidence="ECO:0000256|SAM:SignalP"
FT CHAIN 20..336
FT /evidence="ECO:0000256|SAM:SignalP"
FT /id="PRO_5002482127"
FT DOMAIN 34..333
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
SQ SEQUENCE 336 AA; 35552 MW; 9137B5C8CBA975EA CRC64;
MHFSKVLASL GLMATAASAA PHMLKTRNAT GTGAQNVVYW GQNGGGIVEN NDLATYCTST
SGIDIIVLAF LYEWGNGVTI PSGTIGQSCY ISTSGEGQNC DDLAKAIDTC KANGVKVILS
LGGASGSYSL QSQEQAETIG QNLWEAYGNA GNGSVPRPFG STFVNGWDFD IEANSGNQYY
QYLIAKLRSN FASDPSNTYY ITGAPQCPIP EPNMNVIVTN AQFDYLWIQF YNNPGCSVNG
NINFDQWKTN IANTPSANAK LFIGVPASPL GATGTESGAQ YYLQPSALAS LVGQYQSDPA
FGGVMMWNAG FSDSNVNNGC TYAQEAKHIL TTGSPC
//
