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Database: UniProt
Entry: A0A165PN27_EXIGL
LinkDB: A0A165PN27_EXIGL
Original site: A0A165PN27_EXIGL 
ID   A0A165PN27_EXIGL        Unreviewed;       370 AA.
AC   A0A165PN27;
DT   06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT   06-JUL-2016, sequence version 1.
DT   24-JAN-2024, entry version 16.
DE   RecName: Full=GH16 domain-containing protein {ECO:0000259|PROSITE:PS51762};
GN   ORFNames=EXIGLDRAFT_734537 {ECO:0000313|EMBL:KZW02409.1};
OS   Exidia glandulosa HHB12029.
OC   Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC   Auriculariales; Exidiaceae; Exidia.
OX   NCBI_TaxID=1314781 {ECO:0000313|EMBL:KZW02409.1, ECO:0000313|Proteomes:UP000077266};
RN   [1] {ECO:0000313|EMBL:KZW02409.1, ECO:0000313|Proteomes:UP000077266}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=HHB12029 {ECO:0000313|EMBL:KZW02409.1,
RC   ECO:0000313|Proteomes:UP000077266};
RX   PubMed=26659563; DOI=10.1093/molbev/msv337;
RA   Nagy L.G., Riley R., Tritt A., Adam C., Daum C., Floudas D., Sun H.,
RA   Yadav J.S., Pangilinan J., Larsson K.H., Matsuura K., Barry K., Labutti K.,
RA   Kuo R., Ohm R.A., Bhattacharya S.S., Shirouzu T., Yoshinaga Y.,
RA   Martin F.M., Grigoriev I.V., Hibbett D.S.;
RT   "Comparative Genomics of Early-Diverging Mushroom-Forming Fungi Provides
RT   Insights into the Origins of Lignocellulose Decay Capabilities.";
RL   Mol. Biol. Evol. 33:959-970(2016).
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DR   EMBL; KV425888; KZW02409.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A165PN27; -.
DR   STRING; 1314781.A0A165PN27; -.
DR   InParanoid; A0A165PN27; -.
DR   OrthoDB; 1932445at2759; -.
DR   Proteomes; UP000077266; Unassembled WGS sequence.
DR   GO; GO:0016020; C:membrane; IEA:UniProtKB-KW.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
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   4: Predicted;
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000077266};
KW   Signal {ECO:0000256|SAM:SignalP}; Transmembrane {ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT   SIGNAL          1..19
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT   CHAIN           20..370
FT                   /note="GH16 domain-containing protein"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5007864105"
FT   TRANSMEM        349..369
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          41..307
FT                   /note="GH16"
FT                   /evidence="ECO:0000259|PROSITE:PS51762"
SQ   SEQUENCE   370 AA;  40526 MW;  F41386EA11EE61E4 CRC64;
     MLRLGLVLAF SALAVDVVAL SLSLPSLSMF SRRATTTIAE PSIIWIPQDV YRGDTFFDEW
     DFFSDKDPTN GMVNYLPREK AMAGDNAFAY LDKNDQVVMR VDNWTTLQPG QYRDSVRIST
     KKLYNRGLFI LDVAHSPYGC SVWPGYWTLG MAQQWPASGE IDILEGVHNN QHDQVTWHTA
     PGCNLTAPGN FSGTSISTNC YANEVGGCGI VDWSRASYGP LFNALGGGVY AMRWDESAID
     VWFFYRAAVP TDITLGAPDP TLENWGTPSA SLSNTGCDLD KYFVDHAIVF DITVCGDWAG
     ASYQQDGCPG SCIDRVMDPT SFDNASWVIN SLSVYQKKTV QGRVTNNGAF SSAPALYVLA
     IALSLLTSLL
//
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