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
//