ID   K1WQJ7_MARBU            Unreviewed;       672 AA.
AC   K1WQJ7;
DT   28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT   28-NOV-2012, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   RecName: Full=glucan 1,3-beta-glucosidase {ECO:0000256|ARBA:ARBA00038929};
DE            EC=3.2.1.58 {ECO:0000256|ARBA:ARBA00038929};
DE   AltName: Full=Exo-1,3-beta-glucanase D {ECO:0000256|ARBA:ARBA00041260};
GN   ORFNames=MBM_06482 {ECO:0000313|EMBL:EKD15266.1};
OS   Marssonina brunnea f. sp. multigermtubi (strain MB_m1) (Marssonina leaf
OS   spot fungus).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC   Helotiales; Drepanopezizaceae; Drepanopeziza.
OX   NCBI_TaxID=1072389 {ECO:0000313|EMBL:EKD15266.1, ECO:0000313|Proteomes:UP000006753};
RN   [1] {ECO:0000313|EMBL:EKD15266.1, ECO:0000313|Proteomes:UP000006753}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MB_m1 {ECO:0000313|EMBL:EKD15266.1,
RC   ECO:0000313|Proteomes:UP000006753};
RX   PubMed=22876864; DOI=10.1186/1471-2164-13-382;
RA   Zhu S., Cao Y.-Z., Jiang C., Tan B.-Y., Wang Z., Feng S., Zhang L.,
RA   Su X.-H., Brejova B., Vinar T., Xu M., Wang M.-X., Zhang S.-G.,
RA   Huang M.-R., Wu R., Zhou Y.;
RT   "Sequencing the genome of Marssonina brunnea reveals fungus-poplar co-
RT   evolution.";
RL   BMC Genomics 13:382-382(2012).
CC   -!- FUNCTION: Glucosidase involved in the degradation of cellulosic
CC       biomass. Active on lichenan. {ECO:0000256|ARBA:ARBA00037126}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004401};
CC       Single-pass type II membrane protein {ECO:0000256|ARBA:ARBA00004401}.
CC       Membrane {ECO:0000256|ARBA:ARBA00004606}; Single-pass type II membrane
CC       protein {ECO:0000256|ARBA:ARBA00004606}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 5 (cellulase A) family.
CC       {ECO:0000256|ARBA:ARBA00005641}.
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DR   EMBL; JH921442; EKD15266.1; -; Genomic_DNA.
DR   RefSeq; XP_007294371.1; XM_007294309.1.
DR   AlphaFoldDB; K1WQJ7; -.
DR   STRING; 1072389.K1WQJ7; -.
DR   GeneID; 18762417; -.
DR   KEGG; mbe:MBM_06482; -.
DR   eggNOG; ENOG502QRG8; Eukaryota.
DR   HOGENOM; CLU_004624_4_2_1; -.
DR   InParanoid; K1WQJ7; -.
DR   OMA; WWYWTWK; -.
DR   OrthoDB; 1431012at2759; -.
DR   Proteomes; UP000006753; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0004553; F:hydrolase activity, hydrolyzing O-glycosyl compounds; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
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; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31297:SF22; GLUCAN 1,3-BETA-GLUCOSIDASE 2; 1.
DR   PANTHER; PTHR31297; GLUCAN ENDO-1,6-BETA-GLUCOSIDASE B; 1.
DR   Pfam; PF00150; Cellulase; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Cell membrane {ECO:0000256|ARBA:ARBA00022475};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Glycosidase {ECO:0000256|ARBA:ARBA00023295};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW   Membrane {ECO:0000256|SAM:Phobius};
KW   Reference proteome {ECO:0000313|Proteomes:UP000006753};
KW   Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW   Transmembrane {ECO:0000256|ARBA:ARBA00022692, ECO:0000256|SAM:Phobius};
KW   Transmembrane helix {ECO:0000256|ARBA:ARBA00022989,
KW   ECO:0000256|SAM:Phobius}.
FT   TRANSMEM        139..160
FT                   /note="Helical"
FT                   /evidence="ECO:0000256|SAM:Phobius"
FT   DOMAIN          310..546
FT                   /note="Glycoside hydrolase family 5"
FT                   /evidence="ECO:0000259|Pfam:PF00150"
FT   REGION          1..129
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          164..194
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        9..23
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        28..53
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        54..88
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   672 AA;  74996 MW;  8CE8A5F9EBA7B2EF CRC64;
     MAPHGSPRRP RERSHRHDKK RSARRSKYES TSSGASTQVL SANALAQLDH LNQQRLPRTR
     RAAEEVTPTK PRRKRHREVR DETVVVEKRR QRKRRKGRVV SGALLEEGNS SKLRGLRGGA
     RSEKDEEYED RAGGKRKKWI WIGVGLIIVI IIIIVVAVVV SQNNNSGSSS SSSSPTSSSG
     DSRPSNSNLD GISESSIPAA AKGTELDPFS WYDTTDFNVT YTDVTVGGLP IMGLMSDWDD
     SKSANSNTPP ISTPWGSYAD TPARGVNLGG WLSLEPFIAP SMFNYPGVVD EYTLTTHLGA
     DAKATLEKHY ATFVTEQTFK DIAAAGLDHV RIPFSYWAVT IYDGDPYVYR VSWRYLLRAI
     EWARKYGLRI NLDLHGFPGS QNGWNHSGRL GAIGWLNGPD GALNANRSLA IHDQLSQFFA
     QDRYKNIIAF YGLVNEPKMI SLPQSDVVSW TATAFDLVRK NGITAYVVFG DGFMGLDNWQ
     GQLTEYDGLV LDVHQYVIFN QNQIDFNRTK KIDYACSEWS SQAEQSMSVA TGFGPTIFAE
     WSQADTDCAP YLTNVGWGNR WEGTYDAGDP SLDVLTPDCP AQNDQCTCKQ ANADPSTYSP
     SYKKFLQMFA EAQMHSFEKG WGWFYWTWRT ESATQWSYEK GLAAGILPKK AYAPEFNCSA
     AIPSFSDLPE YQ
//