ID E3RTV7_PYRTT Unreviewed; 745 AA.
AC E3RTV7;
DT 11-JAN-2011, integrated into UniProtKB/TrEMBL.
DT 11-JAN-2011, sequence version 1.
DT 27-MAR-2024, entry version 50.
DE RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN ORFNames=PTT_12469 {ECO:0000313|EMBL:EFQ90841.1};
OS Pyrenophora teres f. teres (strain 0-1) (Barley net blotch fungus)
OS (Drechslera teres f. teres).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Pleosporineae; Pleosporaceae;
OC Pyrenophora.
OX NCBI_TaxID=861557 {ECO:0000313|Proteomes:UP000001067};
RN [1] {ECO:0000313|EMBL:EFQ90841.1, ECO:0000313|Proteomes:UP000001067}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0-1 {ECO:0000313|EMBL:EFQ90841.1,
RC ECO:0000313|Proteomes:UP000001067};
RX PubMed=21067574; DOI=10.1186/gb-2010-11-11-r109;
RA Ellwood S.R., Liu Z., Syme R.A., Lai Z., Hane J.K., Keiper F., Moffat C.S.,
RA Oliver R.P., Friesen T.L.;
RT "A first genome assembly of the barley fungal pathogen Pyrenophora teres f.
RT teres.";
RL Genome Biol. 11:R109.1-R109.14(2010).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Random endo-hydrolysis of N-acetyl-beta-D-glucosaminide
CC (1->4)-beta-linkages in chitin and chitodextrins.; EC=3.2.1.14;
CC Evidence={ECO:0000256|ARBA:ARBA00000822};
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 18 family. Chitinase
CC class V subfamily. {ECO:0000256|ARBA:ARBA00008682}.
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DR EMBL; GL535040; EFQ90841.1; -; Genomic_DNA.
DR RefSeq; XP_003301062.1; XM_003301014.1.
DR AlphaFoldDB; E3RTV7; -.
DR STRING; 861557.E3RTV7; -.
DR EnsemblFungi; EFQ90841; EFQ90841; PTT_12469.
DR KEGG; pte:PTT_12469; -.
DR eggNOG; KOG2806; Eukaryota.
DR HOGENOM; CLU_373032_0_0_1; -.
DR OrthoDB; 3203764at2759; -.
DR Proteomes; UP000001067; Unassembled WGS sequence.
DR GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR GO; GO:0008061; F:chitin binding; IEA:InterPro.
DR GO; GO:0004568; F:chitinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006032; P:chitin catabolic process; IEA:UniProtKB-KW.
DR GO; GO:0000272; P:polysaccharide catabolic process; IEA:UniProtKB-KW.
DR CDD; cd06548; GH18_chitinase; 1.
DR Gene3D; 3.10.50.10; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR011583; Chitinase_II.
DR InterPro; IPR029070; Chitinase_insertion_sf.
DR InterPro; IPR001223; Glyco_hydro18_cat.
DR InterPro; IPR001579; Glyco_hydro_18_chit_AS.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR PANTHER; PTHR11177; CHITINASE; 1.
DR PANTHER; PTHR11177:SF317; CHITINASE 11; 1.
DR Pfam; PF00704; Glyco_hydro_18; 1.
DR SMART; SM00636; Glyco_18; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR SUPFAM; SSF54556; Chitinase insertion domain; 1.
DR PROSITE; PS01095; GH18_1; 1.
DR PROSITE; PS51910; GH18_2; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|ARBA:ARBA00023277};
KW Chitin degradation {ECO:0000256|ARBA:ARBA00023024};
KW Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW Reference proteome {ECO:0000313|Proteomes:UP000001067};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT TRANSMEM 69..88
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 126..147
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT TRANSMEM 159..182
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 334..708
FT /note="GH18"
FT /evidence="ECO:0000259|PROSITE:PS51910"
FT REGION 273..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 745 AA; 81383 MW; 38EBCC6A363D7D06 CRC64;
MSTQPQYSSG HLNETQRHLL SPTLSSPGFS SGYHSPLMHQ GPPSPDFNAI KKAQKEDARL
KSLIRHLRII SRTLAFLLSL GVLIPITLTL TKFLSTKDTY RTVTLADGTS HTRTAWAKNT
RPWPTYMYFS VAVVSTVLHA VTLLAYCCSV GKANTVNTVT SVFSLIVMLG NVGVWAAAVG
VYRMQKDWHG ISNDLWGWTC SHGASKIQVE FEGVVDFEKY CSVQFANGDI PPLINETSFT
GPGVAESEPI VTSNSNYYST TFGTPGLPYV STFAPTKPST PTSSSNEVDQ PFTSSPASYA
TPSPTLPQPS STLLTLVPSH EPLAQSSNST HAGYRAVAYY GNWDIYNRNY QPQQIPASKL
THLLYSFANV NSNGTVFLTD TYADTDKHYS TDSWSEAGNN VYGSIKQLQL LKASNRNLKV
LLSIGGWTYT NTNRAMDTPM SSTRGIQRFA ASCVQLIRDY GFDGVDIDWE YPTTTEQGSA
FLGLLQEIRR QMDDYANTLV YGDEFGHEMK PSFLLSIAAP AGETNYRNMP LREISRVTDF
VNLMTYDYAG SWGNVTGHAS NLYASAEKPL STPYNTASVL AAYYAAGVPP AKLNLGMPLY
GRSFTNTQGL GLPYRGIGIG SWEAGVYDLK DLPLAGAQEF YDAEAGATYS YHNGSGMLVS
YDSVPMALRK ADYIAQQRLG GAMWWEISGD RTDEGSIVSN VVEKLGGLSG ANMESSANWL
LYPDSQFDNI RNGISGGQAQ RVGRV
//
