ID B6Q434_TALMQ Unreviewed; 947 AA.
AC B6Q434;
DT 16-DEC-2008, integrated into UniProtKB/TrEMBL.
DT 16-DEC-2008, sequence version 1.
DT 27-MAR-2024, entry version 60.
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=PMAA_030220 {ECO:0000313|EMBL:EEA28206.1};
OS Talaromyces marneffei (strain ATCC 18224 / CBS 334.59 / QM 7333)
OS (Penicillium marneffei).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC Talaromyces sect. Talaromyces.
OX NCBI_TaxID=441960 {ECO:0000313|EMBL:EEA28206.1, ECO:0000313|Proteomes:UP000001294};
RN [1] {ECO:0000313|Proteomes:UP000001294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 18224 / CBS 334.59 / QM 7333
RC {ECO:0000313|Proteomes:UP000001294};
RX PubMed=25676766; DOI=10.1128/genomea.01559-14;
RA Nierman W.C., Fedorova-Abrams N.D., Andrianopoulos A.;
RT "Genome sequence of the AIDS-associated pathogen Penicillium marneffei
RT (ATCC18224) and its near taxonomic relative Talaromyces stipitatus
RT (ATCC10500).";
RL Genome Announc. 3:E0155914-E0155914(2015).
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; DS995899; EEA28206.1; -; Genomic_DNA.
DR RefSeq; XP_002144721.1; XM_002144685.1.
DR AlphaFoldDB; B6Q434; -.
DR STRING; 441960.B6Q434; -.
DR VEuPathDB; FungiDB:PMAA_030220; -.
DR HOGENOM; CLU_004624_4_0_1; -.
DR OrthoDB; 1431012at2759; -.
DR PhylomeDB; B6Q434; -.
DR Proteomes; UP000001294; 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:0000256|ARBA:ARBA00023295};
KW Membrane {ECO:0000256|SAM:Phobius};
KW Reference proteome {ECO:0000313|Proteomes:UP000001294};
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 411..431
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 589..828
FT /note="Glycoside hydrolase family 5"
FT /evidence="ECO:0000259|Pfam:PF00150"
FT REGION 1..323
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 362..392
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 434..461
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 38..52
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 53..73
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 74..88
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 89..220
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 221..236
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 242..323
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 362..379
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 947 AA; 109136 MW; 85CEFC52F89E913C CRC64;
MPSHSRTRDR NYNRDRAERD YYSRHRRYNK DDRNRGDEVE VEIDDDEDDE REEYSRRQER
FAARRSQSRG YETIEVEEEE DDDEEEEVVD NSRSRHRSVP RQVAEYDDTP RTPRRKRPER
EERYRDEYTS RRRTRDKTPK AKESPATSPK KRLDREGYRR NTSRTREGSP IRERRQRHRD
DDGIRVVGDR DRPRDEDQDR EIRRQQRRKE RQDRELAAQK HTSADSTNSA SQLLSADALA
KLNDYYERER TKTRNQRDDD GHNKRRERRR QRTQDITAVE DEDNRIRVEK RRERRRPPSQ
QPERRPSYHK EKKTFYDDDN DAELVSRHNQ GRRLVSGAVM EEGRSNKLFF WKRIGRRNDP
AAEKDITDYH EDDGDDGHGG RGGGAFYNRG LKEPDDDDYD HVPFWRRKRN LIIAGVIVLL
LAIVIPVAII GSRKKSNGTS SSSGGNDSGS GRGSSSSYGP YNSSLSTISQ DSIPASARGT
ILDPFTWYDT RDFNLTYTNE TVGGLPIMGF NSTWDDSAQP NSNVPALNKN FTYGTTPIRG
VNIGGWLSIE PFITPSFFSK YSPIDGVIDE YTLTQKLGSA AAATIEEHYA TFIQEEDFAE
IAAAGLDHVR IPYSYWAVTT YDGDPYVKQI SWRYLLRAIE YCRKYGLRVN LDLHGLPGSQ
NGYNHSGRQG LIRWLNGTDG ALNAQRSLDI HNQLSQFFAQ PRYQNIVTIY GLANEPPLLS
LDVSTVLNWT VSATEIVQKN GIKAKISMGD GFLNLDKWEY IMKTDVPPNL LLDTHQYTIF
NINEINLNHT AKINLVCNSW LPMIGKVNST TNGFGQTICG EFSQADTDCT QYLNNVNTGT
RWEGTLSGST TPDCYTKSND CSCASANADV SSYSSDYKLW LQTYAEAQFS AFETAMGWFY
WTWQTESAPQ WSYKQARAAG FMPKLAYQPN FKCGATVPSF GRLPEYY
//
