ID V2YK16_MONRO Unreviewed; 767 AA.
AC V2YK16;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, 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=Moror_10328 {ECO:0000313|EMBL:ESK92044.1};
OS Moniliophthora roreri (strain MCA 2997) (Cocoa frosty pod rot fungus)
OS (Crinipellis roreri).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Agaricomycotina; Agaricomycetes;
OC Agaricomycetidae; Agaricales; Marasmiineae; Marasmiaceae; Moniliophthora.
OX NCBI_TaxID=1381753 {ECO:0000313|EMBL:ESK92044.1, ECO:0000313|Proteomes:UP000017559};
RN [1] {ECO:0000313|EMBL:ESK92044.1, ECO:0000313|Proteomes:UP000017559}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCA 2997 {ECO:0000313|EMBL:ESK92044.1,
RC ECO:0000313|Proteomes:UP000017559};
RX PubMed=24571091; DOI=10.1186/1471-2164-15-164;
RA Meinhardt L.W., Costa G.G.L., Thomazella D.P.T., Teixeira P.J.P.L.,
RA Carazzolle M.F., Schuster S.C., Carlson J.E., Guiltinan M.J.,
RA Mieczkowski P., Farmer A., Ramaraj T., Crozier J., Davis R.E., Shao J.,
RA Melnick R.L., Pereira G.A.G., Bailey B.A.;
RT "Genome and secretome analysis of the hemibiotrophic fungal pathogen,
RT Moniliophthora roreri, which causes frosty pod rot disease of cacao:
RT mechanisms of the biotrophic and necrotrophic phases.";
RL BMC Genomics 15:164-164(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}.
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:ESK92044.1}.
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DR EMBL; AWSO01000305; ESK92044.1; -; Genomic_DNA.
DR RefSeq; XP_007848667.1; XM_007850476.1.
DR AlphaFoldDB; V2YK16; -.
DR STRING; 1381753.V2YK16; -.
DR KEGG; mrr:Moror_10328; -.
DR HOGENOM; CLU_004624_6_1_1; -.
DR OrthoDB; 1431012at2759; -.
DR Proteomes; UP000017559; 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:0000313|EMBL:ESK92044.1};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000017559};
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 124..146
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 290..468
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..36
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..97
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 150..184
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 157..180
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 767 AA; 83395 MW; 42A91FA42C41A69B CRC64;
MAHQSQPSDH IYNRIPLEQH PPSPGPGSTF QNPHSRFAGQ ALYQDGSYAT SHQSMPSIGG
NSEYSASVYA LNDTRDNPSL SGHYRDDPNG HDVAMSPMGR SKWMDEKEAA YASPKAKTNH
KLKIIAVIVA GALVIIAIIV GVYFALSKKD SKDGNASKGT SSDASTGKNS NSNGNGNDKS
GVVLAVTGGD GSEVTLEDGT TFKYSNPHGG HWYYDPNEPF NNGAKAQSWS PALNETFNYG
VDRIRGVNVG GWLTIEPVSH PSAPALFEKY ATSVPTPVDE YTLHMAVAAD TANGGLAQIE
EHYKTFITEK DFAEIAGAGL NYVRIPLPYW AIDVRENEPF LPKTAWKYFL KAIGWARKYG
LRINLDLHAV PGSQNGWNHS GKLGDVNWLM GPMGLANAQR TLDYIRILAE FIAQPQYRDV
ITMFGIINEP RESYSGAEQI EAFYAEAYRI IREITGIGQG AWISYHDAFR PRSDWAGFMA
NADRIMLDDH PYIAFGGQDN RGWGAKVDQV CGWSADVKTS MSAFGMTAAG EFSLAINDCG
LWVTGVGDGT RYEGDYKPDP SFPRIGSCTQ WTDWTKFDAA TKAEMKQFAM ASFDALQNFF
FWTWKIGDSI NSGKVESPAW SYKLGLEQGW MPLDPREANG VCGDTAPFNR SIPHGNGNAN
LARYPWPPAT IRSAGPANRV PTYTATGVVP TLAGATLTVS GVTPTKTIDI GNGWANPQDQ
AGMMVPVAGC SYLDPWVGTR ASVPTPLCPG VRRDIEAHES EPTPPPL
//
