ID   EGLX_ARTBC              Reviewed;         457 AA.
AC   D4AJR9;
DT   14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT   18-MAY-2010, sequence version 1.
DT   25-MAY-2022, entry version 43.
DE   RecName: Full=Endo-1,3(4)-beta-glucanase ARB_04519 {ECO:0000250|UniProtKB:Q5BAP5};
DE            EC=3.2.1.6 {ECO:0000250|UniProtKB:Q5BAP5};
DE   Flags: Precursor;
GN   ORFNames=ARB_04519;
OS   Arthroderma benhamiae (strain ATCC MYA-4681 / CBS 112371) (Trichophyton
OS   mentagrophytes).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Arthrodermataceae; Trichophyton.
OX   NCBI_TaxID=663331;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC MYA-4681 / CBS 112371 {ECO:0000312|Proteomes:UP000008866};
RX   PubMed=21247460; DOI=10.1186/gb-2011-12-1-r7;
RA   Burmester A., Shelest E., Gloeckner G., Heddergott C., Schindler S.,
RA   Staib P., Heidel A., Felder M., Petzold A., Szafranski K., Feuermann M.,
RA   Pedruzzi I., Priebe S., Groth M., Winkler R., Li W., Kniemeyer O.,
RA   Schroeckh V., Hertweck C., Hube B., White T.C., Platzer M., Guthke R.,
RA   Heitman J., Woestemeyer J., Zipfel P.F., Monod M., Brakhage A.A.;
RT   "Comparative and functional genomics provide insights into the
RT   pathogenicity of dermatophytic fungi.";
RL   Genome Biol. 12:R7.1-R7.16(2011).
CC   -!- FUNCTION: Mixed-linked glucanase involved in the degradation of complex
CC       natural cellulosic substrates. Active on laminarin. lichenan, soluble
CC       carboxymethyl cellulose but not on pustulan.
CC       {ECO:0000250|UniProtKB:Q5BAP5}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=Endohydrolysis of (1->3)- or (1->4)-linkages in beta-D-glucans
CC         when the glucose residue whose reducing group is involved in the
CC         linkage to be hydrolyzed is itself substituted at C-3.; EC=3.2.1.6;
CC         Evidence={ECO:0000250|UniProtKB:Q5BAP5};
CC   -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 16 family.
CC       {ECO:0000255|PROSITE-ProRule:PRU01098}.
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DR   EMBL; ABSU01000001; EFE36992.1; -; Genomic_DNA.
DR   RefSeq; XP_003017637.1; XM_003017591.1.
DR   AlphaFoldDB; D4AJR9; -.
DR   SMR; D4AJR9; -.
DR   EnsemblFungi; EFE36992; EFE36992; ARB_04519.
DR   GeneID; 9522482; -.
DR   KEGG; abe:ARB_04519; -.
DR   eggNOG; ENOG502QUM3; Eukaryota.
DR   HOGENOM; CLU_016972_4_3_1; -.
DR   OMA; VADISHM; -.
DR   Proteomes; UP000008866; Unassembled WGS sequence.
DR   GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
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:0030245; P:cellulose catabolic process; IEA:UniProtKB-KW.
DR   InterPro; IPR013320; ConA-like_dom_sf.
DR   InterPro; IPR000757; GH16.
DR   Pfam; PF00722; Glyco_hydro_16; 1.
DR   SUPFAM; SSF49899; SSF49899; 1.
DR   PROSITE; PS51762; GH16_2; 1.
PE   3: Inferred from homology;
KW   Carbohydrate metabolism; Cellulose degradation; Glycoprotein; Glycosidase;
KW   Hydrolase; Polysaccharide degradation; Reference proteome; Secreted;
KW   Signal.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000255"
FT   CHAIN           19..457
FT                   /note="Endo-1,3(4)-beta-glucanase ARB_04519"
FT                   /evidence="ECO:0000255"
FT                   /id="PRO_0000434494"
FT   DOMAIN          19..319
FT                   /note="GH16"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   REGION          318..397
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        335..388
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   ACT_SITE        130
FT                   /note="Nucleophile"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   ACT_SITE        135
FT                   /note="Proton donor"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01098"
FT   CARBOHYD        200
FT                   /note="N-linked (GlcNAc...) asparagine"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00498"
SQ   SEQUENCE   457 AA;  49506 MW;  B877A05CCE98F493 CRC64;
     MRTTGLLLLG ALAELGSATY ILEDDYQPNT WFDQFRFFSA KDPTHAYVNY LDQAEARSQN
     LIGVRNNAVY LGVDHKNVAT GEGRSSVRLE TKKVYNHGLI VADINHMPGG ECGTWPAFWT
     TSSAWPMEGE LDIIEGVNQQ KQNDYALHTA QGCSIPERGD FTGSVVTPNC DVKALGQAEN
     QGCLVEDTKG SRGYGPDFNN ATGGVFATEW TDQAISIWFF PREDIPKDVN SEHPDPSKWG
     KPSAFFGGGE CPIGKHVRNQ RIIFNTAFCG GWADGMWPGD PICSKKAPTC MEYVRENPSA
     FEDAYWSINY MKVYQQGTAP TKPSQAPAPP SSTPALPTMK STSTVSSMVS ATQPAPTASN
     PTGAPMQPSS SSSNNGPQPT GGNGNPGDSC PPPTQPACRT YVTTKTYTLV STMMPSGPQT
     TGGIVPVPSA ALEDIKDTAQ RLRRRDMERH SRRGHHN