ID R9AHL6_WALI9 Unreviewed; 819 AA.
AC R9AHL6;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 38.
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=J056_003913 {ECO:0000313|EMBL:EOR01677.1};
OS Wallemia ichthyophaga (strain EXF-994 / CBS 113033).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Wallemiomycotina;
OC Wallemiomycetes; Wallemiales; Wallemiaceae; Wallemia.
OX NCBI_TaxID=1299270 {ECO:0000313|EMBL:EOR01677.1, ECO:0000313|Proteomes:UP000014064};
RN [1] {ECO:0000313|Proteomes:UP000014064}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=EXF-994 / CBS 113033 {ECO:0000313|Proteomes:UP000014064};
RX PubMed=24034603; DOI=10.1186/1471-2164-14-617;
RA Zajc J., Liu Y., Dai W., Yang Z., Hu J., Gostincar C., Gunde-Cimerman N.;
RT "Genome and transcriptome sequencing of the halophilic fungus Wallemia
RT ichthyophaga: haloadaptations present and absent.";
RL BMC Genomics 14:617-617(2013).
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; KE007229; EOR01677.1; -; Genomic_DNA.
DR RefSeq; XP_009267397.1; XM_009269122.1.
DR AlphaFoldDB; R9AHL6; -.
DR STRING; 1299270.R9AHL6; -.
DR GeneID; 20376865; -.
DR KEGG; wic:J056_003913; -.
DR eggNOG; ENOG502QRG8; Eukaryota.
DR HOGENOM; CLU_004624_6_2_1; -.
DR OMA; YAITIGQ; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000014064; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000014064};
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 185..209
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 350..544
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..102
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 159..179
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 211..245
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..31
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 72..102
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 819 AA; 91053 MW; 8913A774E3A7E04B CRC64;
MRFSPKRKTP PIDSASIESS LRLNGSDPSI RLVTEENDGL SADDRPSYEG TAPRNNEISS
NKADGFKSLG RPASFITTTS SNSENNYLTP EQPSSPQAAN NKTSYRNISQ SSLPRQSAEV
TGVGEIAQQP PYTYTHSFEQ KSMSANLTSS SELFDKGIQE KGLPEVQPDR SSKAPLGGAR
KQRKWLIAGA STLAAVVVIV LVIALPVTLT RNNDSSSSSS SSENKDGQPK TNASGNLVQT
SGGDGSEVTL ENGDTFIYNN TFGGNWTSIP FNNTARAQSY TKPLSETWDY NNDRILGVNL
GGWLVLEPFI VPALYEACED ADTPCVDEYT LSNYYRSQNK LEEVLDEHYD TFITEKDFAD
IAAAGLNWVR LPIPFWMIET QDDEPFYEGG CFKYFQKAVK WARKYGLRLN LDLHAVPGSQ
NGYNHSGHLG NIHWMASYMG LVNAQRTLNY IRTITELITE DEYKDVVAMF SVINEPFGPT
IGRDVVASFY FEAYNVIREI TGTGEGKGPW LAFHDAMVGG AQWSDFLRGA DRVALDIHPY
VAFNGQNNDP MSEQVRICLL TSFNAHSPFS YGVTIAGEFS LAINDCGTVN GVDEGTRYEG
TYTNDQGNVL QPNFGEGACD EFNNWQGWDD QFKSQIKTFG LSSMDALQNF FFWTWRIGKS
SKTNDFVNPF WSYQLGLQQD YMTTDPHSEP WGTCEKLSQE DQGRNWNSNP VQDYPEWMLG
GEGAGELFGD TSAYNTFPPQ SFFNVDDVDS LPQYTQTGDR IVLEPSPVEY MNEDGELESV
DNANGWYDDS DDTPFYSAIE GCDRYRSPYY EGDIIGGNC
//
