ID   O60019_PHARH            Unreviewed;       424 AA.
AC   O60019;
DT   01-AUG-1998, integrated into UniProtKB/TrEMBL.
DT   01-AUG-1998, sequence version 1.
DT   22-FEB-2023, entry version 68.
DE   SubName: Full=Endo-1,3(4)-beta-glucanase {ECO:0000313|EMBL:AAC17104.1};
DE            EC=3.2.1.6 {ECO:0000313|EMBL:AAC17104.1};
DE   SubName: Full=Glycoside hydrolase family 16 protein {ECO:0000313|EMBL:CED84840.1};
GN   Name=bg1 {ECO:0000313|EMBL:AAC17104.1};
OS   Phaffia rhodozyma (Yeast) (Xanthophyllomyces dendrorhous).
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC   Cystofilobasidiales; Mrakiaceae; Phaffia.
OX   NCBI_TaxID=264483 {ECO:0000313|EMBL:AAC17104.1};
RN   [1] {ECO:0000313|EMBL:AAC17104.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Bang M.-L., Sandal T.;
RL   Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:AAC17104.1}
RP   NUCLEOTIDE SEQUENCE.
RX   PubMed=10091328; DOI=10.1007/s002530051384;
RA   Bang M.L., Villadsen I., Sandal T.;
RT   "Cloning and characterization of an endo-beta-1,3(4)glucanase and an
RT   aspartic protease from Phaffia rhodozyma CBS 6938.";
RL   Appl. Microbiol. Biotechnol. 51:215-222(1999).
RN   [3] {ECO:0000313|EMBL:CED84840.1}
RP   NUCLEOTIDE SEQUENCE.
RA   Sharma Rahul, Thines Marco;
RL   Submitted (AUG-2014) to the EMBL/GenBank/DDBJ databases.
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DR   EMBL; AF064870; AAC17104.1; -; mRNA.
DR   EMBL; LN483166; CED84840.1; -; Genomic_DNA.
DR   AlphaFoldDB; O60019; -.
DR   CAZy; GH16; Glycoside Hydrolase Family 16.
DR   CLAE; MLG16A_PHARH; -.
DR   GO; GO:0052861; F:glucan endo-1,3-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0052862; F:glucan endo-1,4-beta-glucanase activity, C-3 substituted reducing group; IEA:UniProtKB-EC.
DR   GO; GO:0005975; P:carbohydrate metabolic process; IEA:InterPro.
DR   CDD; cd02181; GH16_fungal_Lam16A_glucanase; 1.
DR   Gene3D; 2.60.120.200; -; 1.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   PANTHER; PTHR10963:SF24; GLYCOSIDASE C21B10.07-RELATED; 1.
DR   PANTHER; PTHR10963; GLYCOSYL HYDROLASE-RELATED; 1.
DR   SUPFAM; SSF49899; Concanavalin A-like lectins/glucanases; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   2: Evidence at transcript level;
KW   Glycosidase {ECO:0000313|EMBL:AAC17104.1};
KW   Hydrolase {ECO:0000313|EMBL:AAC17104.1}; Signal {ECO:0000256|SAM:SignalP}.
FT   SIGNAL          1..22
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           23..424
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007696980"
FT   DOMAIN          100..380
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
FT   REGION          25..96
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        45..61
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   424 AA;  45425 MW;  A236F6555326EF49 CRC64;
     MHLANVLLTL LPVSLLATES LAGSSSHSAH ALPARRRHNK GRALSPIKAS NSSSEHETNR
     IASAGASADD FSPVTGRRVS KRAQCGVSSP ATSSKTSSTI TVGAAVVPTA AATSSSKWKL
     DLEAKGNSFF DTFNFWAYDD PTHGTVTYVS QDEATKSNLA TVNGKGNAVL AVDTTQNVQK
     GRKAVRLHSS YIFNGGLILA DIVHMPTGCG TWPAWWSNGP DWPNKGEIDI LEGTHSWDRN
     QVSVHTSDGC TIPSNYGASA VLTTGSFVNT NCASYATSNQ GCGQRESASH QAYGEPFNQN
     GGGVYAMKWD TSGISVYFFP RNAIPADITQ GVPLPETWGT PMGNFPSTSC EPFKFFKDHH
     TIINTTFCGD WANSDWWTAG SAGNGQSCAA KTGYNSCSDY VLNNGDKFHE AYWEFASVKY
     YQPK
//