ID A0A3N4IN81_ASCIM Unreviewed; 709 AA.
AC A0A3N4IN81;
DT 13-FEB-2019, integrated into UniProtKB/TrEMBL.
DT 13-FEB-2019, sequence version 1.
DT 27-MAR-2024, entry version 15.
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=BJ508DRAFT_411665 {ECO:0000313|EMBL:RPA85651.1};
OS Ascobolus immersus RN42.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Pezizomycetes;
OC Pezizales; Ascobolaceae; Ascobolus.
OX NCBI_TaxID=1160509 {ECO:0000313|EMBL:RPA85651.1, ECO:0000313|Proteomes:UP000275078};
RN [1] {ECO:0000313|EMBL:RPA85651.1, ECO:0000313|Proteomes:UP000275078}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RN42 {ECO:0000313|EMBL:RPA85651.1,
RC ECO:0000313|Proteomes:UP000275078};
RX PubMed=30420746; DOI=10.1038/s41559-018-0710-4;
RA Murat C., Payen T., Noel B., Kuo A., Morin E., Chen J., Kohler A.,
RA Krizsan K., Balestrini R., Da Silva C., Montanini B., Hainaut M.,
RA Levati E., Barry K.W., Belfiori B., Cichocki N., Clum A., Dockter R.B.,
RA Fauchery L., Guy J., Iotti M., Le Tacon F., Lindquist E.A., Lipzen A.,
RA Malagnac F., Mello A., Molinier V., Miyauchi S., Poulain J., Riccioni C.,
RA Rubini A., Sitrit Y., Splivallo R., Traeger S., Wang M., Zifcakova L.,
RA Wipf D., Zambonelli A., Paolocci F., Nowrousian M., Ottonello S.,
RA Baldrian P., Spatafora J.W., Henrissat B., Nagy L.G., Aury J.M.,
RA Wincker P., Grigoriev I.V., Bonfante P., Martin F.M.;
RT "Pezizomycetes genomes reveal the molecular basis of ectomycorrhizal
RT truffle lifestyle.";
RL Nat. Ecol. Evol. 2:1956-1965(2018).
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; ML119652; RPA85651.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3N4IN81; -.
DR STRING; 1160509.A0A3N4IN81; -.
DR Proteomes; UP000275078; 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:0000313|EMBL:RPA85651.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000275078};
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 171..197
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 352..588
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..165
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..71
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 709 AA; 80394 MW; D6B91C01C0CB0F31 CRC64;
MPRRTQREEE NESSEALYPR RSTHRDSRTS RDYGYEGGEG RPRRERSSTR RNSEHGRRRS
DSGRRRSSTE RRAAGAGGSQ RRQPERPDRH RSYRTVPAAP PVAAAPVVAP LLGGDADSPR
RSSTQQHRRS DTTTSRKYSG APVRNATMGE KGRRRRGGGA GGRKRKSRGT LFWAAIAAAI
IALLLIILVP IGVLVVGKNK DEELKGSPLS NQKRPAGFGL AGADGLPMDV PESAKGTLLD
PNDWLDTTDF NTTYTTATVG GLSVMGLLDD WQRYESTRPN ENVPPLNQPF PYGKQPIRGV
NVGGWLLIEP FITPSFFDDI NKNQKKPKVI DEYTLSMELG PEKAREKLER HYATYITEQD
FKEIKEAGLD HVRIPFGYWA VYPIKGEPYV PQVSWRYLLR AIEYCRKYGL RVKLDLHAVP
GGANGWNHSG RLYYLEWLNG ENGDENGKKA LEVHERLSKF FSQERYQNVV TMYGLVNEPR
IDMIGAEPVL EWAEKAYNLV QKNGFRGKIV MGDGFRGLEA WKDDFRGLDS MVLDVHNYQI
FNLGQIALTH TKKIEFTCTA WKDQLIDVID NGFGPVFVGE WGQADTDCTK HLNDIGEGTR
WEGTLGSGGP TKCPKESNRP CSCKEANAHP REYTDQYRAF LLMYAEAQMD SFENSWGWMY
WTWQTENAYQ WSYKKGIENG IMPKIAYERS FKCGDDVPDW EARGLPEHY
//
