ID A0A166LVV1_9PEZI Unreviewed; 603 AA.
AC A0A166LVV1;
DT 06-JUL-2016, integrated into UniProtKB/TrEMBL.
DT 06-JUL-2016, sequence version 1.
DT 27-MAR-2024, entry version 17.
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=CT0861_10487 {ECO:0000313|EMBL:KZL63986.1};
OS Colletotrichum tofieldiae.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Glomerellales; Glomerellaceae; Colletotrichum;
OC Colletotrichum spaethianum species complex.
OX NCBI_TaxID=708197 {ECO:0000313|EMBL:KZL63986.1, ECO:0000313|Proteomes:UP000076552};
RN [1] {ECO:0000313|EMBL:KZL63986.1, ECO:0000313|Proteomes:UP000076552}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=0861 {ECO:0000313|EMBL:KZL63986.1,
RC ECO:0000313|Proteomes:UP000076552};
RA Hacquard S., Kracher B., Hiruma K., Weinman A., Muench P., Garrido Oter R.,
RA Ver Loren van Themaat E., Dallerey J.-F., Damm U., Henrissat B.,
RA Lespinet O., Thon M., Kemen E., McHardy A.C., Schulze-Lefert P.,
RA O'Connell R.J.;
RT "Survival trade-offs in plant roots during colonization by closely related
RT pathogenic and mutualistic fungi.";
RL Submitted (JUN-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KZL63986.1}.
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DR EMBL; LFIV01000302; KZL63986.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A166LVV1; -.
DR STRING; 708197.A0A166LVV1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000076552; 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, ECO:0000256|RuleBase:RU361153};
KW Hydrolase {ECO:0000256|RuleBase:RU361153};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000076552};
KW Signal {ECO:0000256|ARBA:ARBA00022729};
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 46..68
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 247..484
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..22
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 79..132
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 603 AA; 65823 MW; 223E7BB01C4206D6 CRC64;
MAHSTNYNTS ADDIVAKPGP TTDGEWIVGD RNVGKTERGK GKRLRWILVG IVLALVAVIG
IVIGVLFAKN VIKTNSGSAK DASTVATASP GASGVGTDSS QPTATRGTGG AQTTAAGLPQ
STASCSTPDD IPTSARGTAM DVTSWLDLTD FNCTFTSELI GGLPLVGLNT AWDDSKRANP
NVPALDQPWG SYAQRPIRGV NIGGWLSLEP FITPSLFEYP SSAGVADEYT LCKHLGKDAT
EVLEKHYSTF VTEKDFKAIA DAGLDHIRIP FSYWAVRTYD SDPYPAGLSW RYLLRGIEWA
RKYGLRIKLD LHGLPGSQNG WNHSGRQGDV GWLKSSNGDV NLKRSLDIHD QLSKFFAQDR
YKNIVAFYGL ANEPALTIPL DDLVTWTGEA YDLVRKNGVG AIQVFSESMK SLEAWKGKLD
GHGDSLAIDV HQYTIFDVNV LKFNHADKIA FVCKTWTAQI KGSVDKTAGF GPTMVGEWSQ
ADTDCTKHLN GMGTGARWLG TFAGKTTPAC PTEDNQCSCE LANADPSTYT ANYKTFLLTW
AEAQMDIFEK SWGWFYWTWK TESAPLWSYQ AGLQGNFLPS LAYKRSWDCS KPIPSFGDLP
EYY
//
