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Database: UniProt
Entry: G3AJE9_SPAPN
LinkDB: G3AJE9_SPAPN
Original site: G3AJE9_SPAPN 
ID   G3AJE9_SPAPN            Unreviewed;       455 AA.
AC   G3AJE9;
DT   16-NOV-2011, integrated into UniProtKB/TrEMBL.
DT   16-NOV-2011, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   ORFNames=SPAPADRAFT_60044 {ECO:0000313|EMBL:EGW34608.1};
OS   Spathaspora passalidarum (strain NRRL Y-27907 / 11-Y1).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Spathaspora.
OX   NCBI_TaxID=619300 {ECO:0000313|Proteomes:UP000000709};
RN   [1] {ECO:0000313|EMBL:EGW34608.1, ECO:0000313|Proteomes:UP000000709}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NRRL Y-27907 / 11-Y1 {ECO:0000313|Proteomes:UP000000709};
RX   PubMed=21788494; DOI=10.1073/pnas.1103039108;
RA   Wohlbach D.J., Kuo A., Sato T.K., Potts K.M., Salamov A.A., LaButti K.M.,
RA   Sun H., Clum A., Pangilinan J.L., Lindquist E.A., Lucas S., Lapidus A.,
RA   Jin M., Gunawan C., Balan V., Dale B.E., Jeffries T.W., Zinkel R.,
RA   Barry K.W., Grigoriev I.V., Gasch A.P.;
RT   "Comparative genomics of xylose-fermenting fungi for enhanced biofuel
RT   production.";
RL   Proc. Natl. Acad. Sci. U.S.A. 108:13212-13217(2011).
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.
CC       {ECO:0000256|RuleBase:RU004453}.
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DR   EMBL; GL996500; EGW34608.1; -; Genomic_DNA.
DR   RefSeq; XP_007374192.1; XM_007374130.1.
DR   AlphaFoldDB; G3AJE9; -.
DR   STRING; 619300.G3AJE9; -.
DR   GeneID; 18873193; -.
DR   KEGG; spaa:SPAPADRAFT_60044; -.
DR   eggNOG; KOG4701; Eukaryota.
DR   HOGENOM; CLU_007818_7_2_1; -.
DR   InParanoid; G3AJE9; -.
DR   OMA; IAGRRTH; -.
DR   OrthoDB; 360175at2759; -.
DR   Proteomes; UP000000709; Unassembled WGS sequence.
DR   GO; GO:0008061; F:chitin binding; IEA:UniProtKB-KW.
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; 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; IPR001579; Glyco_hydro_18_chit_AS.
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; 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   Chitin-binding {ECO:0000256|ARBA:ARBA00022669};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU000489};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000256|RuleBase:RU000489};
KW   Polysaccharide degradation {ECO:0000256|ARBA:ARBA00023326};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000709};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..17
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           18..455
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003442439"
FT   DOMAIN          24..302
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          321..356
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   455 AA;  47735 MW;  7D2DE930AA2F015E CRC64;
     MLTRIISILT ILSTVIAFNA NSNSNVAAYW GQNAGGSQSS LGSYCSSSAA DIIILSFMNG
     FPNLELNFAN QCSDTYGDGL LHCSQIGSDI KSCQSQGKIV LLSLGGATGN YGFSSDSDAQ
     SFATTLWNKF GGGSDSERPF DDAVIDGFDF DMENKLQTGY AAMAAKLRQY FNSDSSKSYY
     LSAAPQCPYP DESVGDILSQ VDIDFAFIQF YNNYCSLGGS FNWDTWSSYA KSTSPNKNIK
     LYLGLPGSTA SAGSGYADLS TVQQAVSSIK GDPSFGGISI WDISSGENDG FLSGCKNALG
     SSSGGSAPSY SAPAFSAPST VVPASSASPS AEFGYPAPAP SSEAPASQEP STSSFQWIPA
     DAPATTESDE GTTTVTTLQT LYSTSDTPRH QHVVHKVYVT LTTTVLVPPP TNTPQLGDSP
     IQKRDEVATV SQGGATHLTT RLGLVLFSLI SVLFI
//
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