ID J9VJM1_CRYNH Unreviewed; 829 AA.
AC J9VJM1;
DT 28-NOV-2012, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 2.
DT 27-MAR-2024, entry version 41.
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=CNAG_05138 {ECO:0000313|EMBL:AFR94403.2};
OS Cryptococcus neoformans var. grubii serotype A (strain H99 / ATCC 208821 /
OS CBS 10515 / FGSC 9487) (Filobasidiella neoformans var. grubii).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Tremellomycetes;
OC Tremellales; Cryptococcaceae; Cryptococcus;
OC Cryptococcus neoformans species complex.
OX NCBI_TaxID=235443 {ECO:0000313|EMBL:AFR94403.2, ECO:0000313|Proteomes:UP000010091};
RN [1] {ECO:0000313|EMBL:AFR94403.2, ECO:0000313|Proteomes:UP000010091}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H99 / ATCC 208821 / CBS 10515 / FGSC 9487
RC {ECO:0000313|Proteomes:UP000010091};
RX PubMed=24743168; DOI=10.1371/journal.pgen.1004261;
RA Janbon G., Ormerod K.L., Paulet D., Byrnes E.J.III., Yadav V.,
RA Chatterjee G., Mullapudi N., Hon C.C., Billmyre R.B., Brunel F., Bahn Y.S.,
RA Chen W., Chen Y., Chow E.W., Coppee J.Y., Floyd-Averette A., Gaillardin C.,
RA Gerik K.J., Goldberg J., Gonzalez-Hilarion S., Gujja S., Hamlin J.L.,
RA Hsueh Y.P., Ianiri G., Jones S., Kodira C.D., Kozubowski L., Lam W.,
RA Marra M., Mesner L.D., Mieczkowski P.A., Moyrand F., Nielsen K., Proux C.,
RA Rossignol T., Schein J.E., Sun S., Wollschlaeger C., Wood I.A., Zeng Q.,
RA Neuveglise C., Newlon C.S., Perfect J.R., Lodge J.K., Idnurm A.,
RA Stajich J.E., Kronstad J.W., Sanyal K., Heitman J., Fraser J.A.,
RA Cuomo C.A., Dietrich F.S.;
RT "Analysis of the genome and transcriptome of Cryptococcus neoformans var.
RT grubii reveals complex RNA expression and microevolution leading to
RT virulence attenuation.";
RL PLoS Genet. 10:E1004261-E1004261(2014).
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; CP003823; AFR94403.2; -; Genomic_DNA.
DR RefSeq; XP_012048519.1; XM_012193129.1.
DR AlphaFoldDB; J9VJM1; -.
DR GeneID; 23888481; -.
DR KEGG; cng:CNAG_05138; -.
DR VEuPathDB; FungiDB:CNAG_05138; -.
DR HOGENOM; CLU_004624_6_2_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000010091; Chromosome 4.
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 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 163..186
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 343..581
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..53
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 82..124
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..157
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..243
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 810..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 12..30
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 87..113
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 829 AA; 88407 MW; 4B0C3A0C6817F225 CRC64;
MPRPAYDPVA NPNFSPDSNT SPNPDRNSNF LDPEANLFGR PGSEYAPAPS LMSRDSTAAS
MNLMGGTPSL AGTHRDSWGS GIALTGAEGA TNGNRNPGRS GLANSTVPYG SGERLSTSDE
DDEHGHITPA VAAIGAGTAA RGISEKPRWA ESGSGKGKKN RKWLWAALAA LLIVAIGLGV
GLGVGLTRNR DSKTLAASSG NENSSPSSQV PSGASSASGS ATATSTSATA SATPTTGTQG
SLITLEDGST MTYDNPYGGK WVWDEANPFK NEAQANSWTP ALNQNWTWGQ DKVFGVNLGG
WLVIEPFIVP GLYEKYANGS AGTAIDEYTL SINMGDNLTA ALTEHYETFI TERDFAEIVA
AGLNWVRIPI PFFAIEVWEG EPYLPKVSWQ YFLKAIKWAR KYGLRVNLDL HSVPGSQNGW
NHSGRQGSVN WMNGVMGLAN AQRSLDYIRT LAQFIAQPEY APVIQMFGFL NEPNGNAISK
GPVASFYIEA HNIIRDITGI GSGNGPMLSM HDGFLGVTAW YGDLAGADRM MLDQHTYMVF
QDQPQGTLDT LKTMPCQWWA SSTNTTSQQW GPNTAGEWSA AWNDCGKWVN NVGSGSRYDG
TYDGYANKAT GSCDYWNDYT QWNQSTIDAL NHFVSGSMDA LQNFFFWTWK IGNSTDAIQQ
PNPFWHYRLG LEKGWIPKDP RTVAGTCQAD GVSMNNFDGT FSNAYVTGGA GAGTIAASAS
SSYPWPPASF TNVASDSMSL LPQYTQTGTP ITMPGPTFTS PGSSATIDAG NGWFNANAND
KQAYAAISGC SYPPEYSAAD LAVPTGACGA GLSQANKRSA EPTPAPTRR
//
