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Database: UniProt
Entry: G8YKW0_PICSO
LinkDB: G8YKW0_PICSO
Original site: G8YKW0_PICSO 
ID   G8YKW0_PICSO            Unreviewed;       739 AA.
AC   G8YKW0;
DT   22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT   22-FEB-2012, sequence version 1.
DT   13-SEP-2023, entry version 44.
DE   RecName: Full=chitinase {ECO:0000256|ARBA:ARBA00012729};
DE            EC=3.2.1.14 {ECO:0000256|ARBA:ARBA00012729};
GN   Name=Piso0_001471 {ECO:0000313|EMBL:CCE88694.1};
GN   ORFNames=GNLVRS01_PISO0F07133g {ECO:0000313|EMBL:CCE88694.1};
OS   Pichia sorbitophila (strain ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC
OS   10061 / NRRL Y-12695) (Hybrid yeast).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC   Saccharomycetales; Debaryomycetaceae; Millerozyma.
OX   NCBI_TaxID=559304 {ECO:0000313|EMBL:CCE88694.1, ECO:0000313|Proteomes:UP000005222};
RN   [1] {ECO:0000313|Proteomes:UP000005222}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4447 / BCRC 22081 / CBS 7064 / NBRC 10061 / NRRL
RC   Y-12695 {ECO:0000313|Proteomes:UP000005222};
RX   DOI=10.1534/g3.111.000745;
RA   Leh Louis V., Despons L., Friedrich A., Martin T., Durrens P.,
RA   Casaregola S., Neuveglise C., Fairhead C., Marck C., Cruz J.A.,
RA   Straub M.L., Kugler V., Sacerdot C., Uzunov Z., Thierry A., Weiss S.,
RA   Bleykasten C., De Montigny J., Jacques N., Jung P., Lemaire M., Mallet S.,
RA   Morel G., Richard G.F., Sarkar A., Savel G., Schacherer J., Seret M.L.,
RA   Talla E., Samson G., Jubin C., Poulain J., Vacherie B., Barbe V.,
RA   Pelletier E., Sherman D.J., Westhof E., Weissenbach J., Baret P.V.,
RA   Wincker P., Gaillardin C., Dujon B., Souciet J.L.;
RT   "Pichia sorbitophila, an interspecies yeast hybrid reveals early steps of
RT   genome resolution following polyploidization.";
RL   G3 (Bethesda) 2:299-311(2012).
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};
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DR   EMBL; FO082054; CCE88694.1; -; Genomic_DNA.
DR   AlphaFoldDB; G8YKW0; -.
DR   STRING; 559304.G8YKW0; -.
DR   eggNOG; KOG4701; Eukaryota.
DR   HOGENOM; CLU_375564_0_0_1; -.
DR   InParanoid; G8YKW0; -.
DR   OMA; TARPCAK; -.
DR   Proteomes; UP000005222; Chromosome F.
DR   GO; GO:0110165; C:cellular anatomical entity; IEA:UniProt.
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   4: Predicted;
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:UP000005222};
KW   Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..24
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           25..739
FT                   /note="chitinase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5003519133"
FT   DOMAIN          26..309
FT                   /note="GH18"
FT                   /evidence="ECO:0000259|PROSITE:PS51910"
FT   REGION          309..368
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          399..637
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        399..429
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        446..637
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   739 AA;  75946 MW;  6FBB96ADA96160F7 CRC64;
     MLMQKQFRFA QLLLLLTHAA TILAQGKVAV YWGQASGGSQ KSLGDYCTDD VDIVILSFLN
     NFPSPWTLDF SSSCSEKFSN GVLHCSQIGS DIKKCQQKGK KVLLSLGGQN GKQGFSSDSE
     ATDFAQTLWN AFGGGSSKER PFDDAKIDGF DFDVENKQQT GYVALAKKLK DYYSQDSSKK
     YYLSASPQCV YPDESVGDVL SHVPIDFAFI QFYNNNCNLD KSFNFDTWQK YAESAPNKDI
     ELFIGLPGSS SAAGSGYVST DVVKSTVQKV SNDKNFAGIS LWDASAATSN TGSQGTSYLS
     EIKDILGSSS SPSSSGSSSS GSQAAQSSAE PSVQPSAQPS GQYSSASSEQ ASSSLIPHQS
     IAQQGTESSS SAATVAGYNA AATAGTTFAA GGYASTPANQ GASTSTNNNN NVYGSQAAPQ
     SNTIAGGSHQ AVADDSVVEA KKDSIAPAPS SQQFKSYSNS SSSTTSQSSK SVGATTGAND
     GNKMNAESVT SQGSAATDDA SQQSASVSES VSSDSTLTTT LRKTIMKAPF SNSTTNNGAH
     AAQTADTKPT SEANNNKNSY HYSAMVVGPS SNANSGSNKG QSGSNSGHSG SSGNQSGSNG
     NQSGSSSNST IPQSGSSNGQ DNANQGSDSG SNGDTTTTIY STISTTITSK SSSNTAAPSS
     FHAESVTSQL NSTANATSSS SSAMSSGFVS LSSYAPSSTS ANAQQKREVK GVAMNSEAKA
     SLTTVSWFSL LCLVVTSLF
//
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