ID F8Q6H4_SERL3 Unreviewed; 500 AA.
AC F8Q6H4;
DT 21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT 21-SEP-2011, sequence version 1.
DT 27-MAR-2024, entry version 33.
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=SERLA73DRAFT_185852 {ECO:0000313|EMBL:EGN96212.1};
OS Serpula lacrymans var. lacrymans (strain S7.3) (Dry rot fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Boletales; Coniophorineae; Serpulaceae; Serpula.
OX NCBI_TaxID=936435 {ECO:0000313|Proteomes:UP000008063};
RN [1] {ECO:0000313|Proteomes:UP000008063}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=strain S7.3 {ECO:0000313|Proteomes:UP000008063};
RX PubMed=21764756; DOI=10.1126/science.1205411;
RA Eastwood D.C., Floudas D., Binder M., Majcherczyk A., Schneider P.,
RA Aerts A., Asiegbu F.O., Baker S.E., Barry K., Bendiksby M., Blumentritt M.,
RA Coutinho P.M., Cullen D., de Vries R.P., Gathman A., Goodell B.,
RA Henrissat B., Ihrmark K., Kauserud H., Kohler A., LaButti K., Lapidus A.,
RA Lavin J.L., Lee Y.-H., Lindquist E., Lilly W., Lucas S., Morin E.,
RA Murat C., Oguiza J.A., Park J., Pisabarro A.G., Riley R., Rosling A.,
RA Salamov A., Schmidt O., Schmutz J., Skrede I., Stenlid J., Wiebenga A.,
RA Xie X., Kuees U., Hibbett D.S., Hoffmeister D., Hoegberg N., Martin F.,
RA Grigoriev I.V., Watkinson S.C.;
RT "The plant cell wall-decomposing machinery underlies the functional
RT diversity of forest fungi.";
RL Science 333:762-765(2011).
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, ECO:0000256|RuleBase:RU361153}.
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DR EMBL; GL945484; EGN96212.1; -; Genomic_DNA.
DR AlphaFoldDB; F8Q6H4; -.
DR STRING; 936435.F8Q6H4; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_6_1_1; -.
DR InParanoid; F8Q6H4; -.
DR OMA; FAMSHME; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000008063; 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:0071704; P:organic substance metabolic process; IEA:InterPro.
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 Glycosidase {ECO:0000256|ARBA:ARBA00023295, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153, ECO:0000313|EMBL:EGN96212.1};
KW Membrane {ECO:0000256|ARBA:ARBA00022989};
KW Reference proteome {ECO:0000313|Proteomes:UP000008063};
KW Signal-anchor {ECO:0000256|ARBA:ARBA00022968};
KW Transmembrane {ECO:0000256|ARBA:ARBA00022692};
KW Transmembrane helix {ECO:0000256|ARBA:ARBA00022989}.
FT DOMAIN 10..170
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 421..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 421..440
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 500 AA; 53100 MW; F2C267424717FE72 CRC64;
MAADTSPGGG LQQLETHYST FITERDFAAI AGAGLNFVRI PVPWWAIETR GNEPFLPKVS
WTYFLKAIKW ARKYGLRINL DFHALPGSQN GWNHSGKLGS VNVLNGPMGL ANAQRSLDYV
RIFAEFISQP EYSDVVTIFG ITNEPQGTMV GQSQLSSYYV QAYNNVREAS GIGEGKGPYV
SFHDGFLGTA QWAGFLPNSD RSAIDTHPYI CFGGQSAAPM SSYAQTPCNA WGSMMNTSMG
AFGLSTAGEF SNAVTDCGLY VNGIGLGTRY EGTYTPGNWP AVGSCDPWTD WQAWNSTMKE
DIMQFALASM DALQNWFFWT WKIGNSSTTG VVESPQWSYS LGLENGWMPK DPRVAVGACG
NQNIWSPPLQ AWQTGGAGAG DLASGLSASY PWPPATISNA GAASLLPTYT PTGTVATLPG
PTFTLTSGSQ TKTASAGDGW ENPSDTAKGM VGIATCSYLD PWIGPSAAPP SPLCSAGGAA
SARAIANDVP RAQITTPPKA
//
