ID G9NXX1_HYPAI Unreviewed; 753 AA.
AC G9NXX1;
DT 22-FEB-2012, integrated into UniProtKB/TrEMBL.
DT 22-FEB-2012, sequence version 1.
DT 27-MAR-2024, entry version 49.
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=TRIATDRAFT_293559 {ECO:0000313|EMBL:EHK44300.1};
OS Hypocrea atroviridis (strain ATCC 20476 / IMI 206040) (Trichoderma
OS atroviride).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Hypocreaceae; Trichoderma.
OX NCBI_TaxID=452589 {ECO:0000313|EMBL:EHK44300.1, ECO:0000313|Proteomes:UP000005426};
RN [1] {ECO:0000313|EMBL:EHK44300.1, ECO:0000313|Proteomes:UP000005426}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 20476 / IMI 206040 {ECO:0000313|Proteomes:UP000005426};
RX PubMed=21501500; DOI=10.1186/gb-2011-12-4-r40;
RA Kubicek C.P., Herrera-Estrella A., Seidl-Seiboth V., Martinez D.A.,
RA Druzhinina I.S., Thon M., Zeilinger S., Casas-Flores S., Horwitz B.A.,
RA Mukherjee P.K., Mukherjee M., Kredics L., Alcaraz L.D., Aerts A., Antal Z.,
RA Atanasova L., Cervantes-Badillo M.G., Challacombe J., Chertkov O.,
RA McCluskey K., Coulpier F., Deshpande N., von Doehren H., Ebbole D.J.,
RA Esquivel-Naranjo E.U., Fekete E., Flipphi M., Glaser F.,
RA Gomez-Rodriguez E.Y., Gruber S., Han C., Henrissat B., Hermosa R.,
RA Hernandez-Onate M., Karaffa L., Kosti I., Le Crom S., Lindquist E.,
RA Lucas S., Luebeck M., Luebeck P.S., Margeot A., Metz B., Misra M.,
RA Nevalainen H., Omann M., Packer N., Perrone G., Uresti-Rivera E.E.,
RA Salamov A., Schmoll M., Seiboth B., Shapiro H., Sukno S.,
RA Tamayo-Ramos J.A., Tisch D., Wiest A., Wilkinson H.H., Zhang M.,
RA Coutinho P.M., Kenerley C.M., Monte E., Baker S.E., Grigoriev I.V.;
RT "Comparative genome sequence analysis underscores mycoparasitism as the
RT ancestral life style of Trichoderma.";
RL Genome Biol. 12:R40.1-R40.15(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}.
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:EHK44300.1}.
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DR EMBL; ABDG02000025; EHK44300.1; -; Genomic_DNA.
DR RefSeq; XP_013942516.1; XM_014087041.1.
DR AlphaFoldDB; G9NXX1; -.
DR STRING; 452589.G9NXX1; -.
DR GeneID; 25780317; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_4_1_1; -.
DR OMA; WWYWTWK; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000005426; 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:EHK44300.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000005426};
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 231..251
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 387..605
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..178
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 256..277
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..50
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 51..68
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 69..150
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 753 AA; 86216 MW; 07F52B7764B729A8 CRC64;
MSDTDIPRAH RSRNRSARGE SSRRDRPRKK ESRTRRGASS ADEGRADRRS RSQSLSANAL
AQLNQDNVRQ QRHADRERRK RDRERGEGHD ERARERLERQ QRRERERRRE REAERDRDRE
REMEWERDRQ REREREQRRT RGRDRSPSPD PETEPVIIPK KYQKPGRQKK KSRVVSGAVM
EEGRSKGWGF GFGGWGNHSR DGSYDSLRKE DLYSQPEKKK KKTTWSKRKK WIVGGICAVI
LLIIIVVAAV VGSKHKSGSS SDSSSPKASN SDVPAKWINT DLDPTTWAST EDFNTTFTDV
MVGGLPIMGL DSDWDDSAQA NDKVPALNKP WGNYSKTPAR GVNLGGWLSI EPFITPSLFN
YPLSAGVVDE WTLCIHLGSQ AASTIENHYN TFVTESTFQD IANAGLDHVR IPFSYWAVKV
YDGDQYIYRN SWRYLLRGIE WARKYGLRVN LDMHGLPGSQ NGWNHSGRQG AIGWLNGTNG
DLNAERSLDI HNSLSQFFAQ DRYKNIITHY GLANEPRMTF LKASTVVNWT ETAYKMVRKN
GFNGLVIFGD GFMGLNNWQG KMQGYDGLVL DVHQYVIFNQ NQIDFTHQKK VQYACQGWTQ
QAEQSQDTST GYGPTQFAEW SQADTDCAQY VTNVGQGNRW EGTLNTGNAS TAILTPDCPT
KDSKCSCDQA NADPSKWSSE YKQFLTMFAE AQMYSFEKGL GWWYWTWQTE TSPQWSYKAG
MQAGVLPQKA WDRSFNCDTD VPDFSKSGLP EYY
//
