ID   A0A179EZR9_METCM        Unreviewed;       418 AA.
AC   A0A179EZR9;
DT   07-SEP-2016, integrated into UniProtKB/TrEMBL.
DT   07-SEP-2016, sequence version 1.
DT   27-MAR-2024, entry version 23.
DE   RecName: Full=cellulase {ECO:0000256|ARBA:ARBA00012601};
DE            EC=3.2.1.4 {ECO:0000256|ARBA:ARBA00012601};
GN   ORFNames=VFPPC_10925 {ECO:0000313|EMBL:OAQ58695.1};
OS   Pochonia chlamydosporia 170.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC   Hypocreomycetidae; Hypocreales; Clavicipitaceae; Pochonia.
OX   NCBI_TaxID=1380566 {ECO:0000313|EMBL:OAQ58695.1, ECO:0000313|Proteomes:UP000078397};
RN   [1] {ECO:0000313|EMBL:OAQ58695.1, ECO:0000313|Proteomes:UP000078397}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=170 {ECO:0000313|EMBL:OAQ58695.1};
RX   PubMed=27416025;
RA   Wang G., Liu Z., Lin R., Li E., Mao Z., Ling J., Yang Y., Yin W.B., Xie B.;
RT   "Biosynthesis of antibiotic leucinostatins in bio-control fungus
RT   Purpureocillium lilacinum and their inhibition on phytophthora revealed by
RT   genome mining.";
RL   PLoS Pathog. 12:E1005685-E1005685(2016).
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->4)-beta-D-glucosidic linkages in
CC         cellulose, lichenin and cereal beta-D-glucans.; EC=3.2.1.4;
CC         Evidence={ECO:0000256|ARBA:ARBA00000966};
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641, ECO:0000256|RuleBase:RU361153}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:OAQ58695.1}.
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DR   EMBL; LSBJ02000014; OAQ58695.1; -; Genomic_DNA.
DR   RefSeq; XP_018136814.1; XM_018289216.1.
DR   AlphaFoldDB; A0A179EZR9; -.
DR   STRING; 1380566.A0A179EZR9; -.
DR   GeneID; 28853210; -.
DR   KEGG; pchm:VFPPC_10925; -.
DR   OrthoDB; 1638835at2759; -.
DR   Proteomes; UP000078397; 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:0000272; P:polysaccharide catabolic process; IEA:UniProt.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR001547; Glyco_hydro_5.
DR   InterPro; IPR018087; Glyco_hydro_5_CS.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR34142:SF5; CBM1 DOMAIN-CONTAINING PROTEIN; 1.
DR   PANTHER; PTHR34142; ENDO-BETA-1,4-GLUCANASE A; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
DR   PROSITE; PS00659; GLYCOSYL_HYDROL_F5; 1.
PE   3: Inferred from homology;
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW   Hydrolase {ECO:0000256|RuleBase:RU361153};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000078397};
KW   Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|SAM:SignalP};
KW   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..418
FT                   /note="cellulase"
FT                   /evidence="ECO:0000256|SAM:SignalP"
FT                   /id="PRO_5008101056"
FT   TRANSMEM        394..417
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          58..307
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          345..391
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        347..390
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   418 AA;  44343 MW;  2186C6D65676F24C CRC64;
     MRSLSWLLAA LAASAGVMGK MKYLGVAMAG VDFGCDIDGS CPADHVQVPL ATLGGADSAG
     QMKHFVDDDG MNTFRLSMTW QYITAGQASG GLDKINFGNF DKLVQACLDT GAYCMLDLHN
     FARYDGGIVG QGGPTDDVFA GLWKQLATYY AKNDKIIFGL MNEPHDLDIK LWAKSCQAAV
     TAIRKAGATS QIILLPGTNF ASAETFVSTG SAEALAAITN PDGSTDNLLL DLHKYLDINN
     SGTHAECTTN NVAGFKTIAE WLRKNKRLGM VSESGASMDQ SCMTKFCEQN EFISKNDDVL
     VGFVGWGAGG FDSTYVLTLT PTKSGNSWTD NKLMKQCIIA PFGKAASSKP SPTTTSAPSS
     TSTEESTQKT PSAAPSGTKN NTNSNESAPE KDSGAGYIAI SHFYVFLASI AALHLYLH
//