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Database: UniProt
Entry: B8MEP1_TALSN
LinkDB: B8MEP1_TALSN
Original site: B8MEP1_TALSN 
ID   B8MEP1_TALSN            Unreviewed;       479 AA.
AC   B8MEP1;
DT   03-MAR-2009, integrated into UniProtKB/TrEMBL.
DT   03-MAR-2009, sequence version 1.
DT   27-MAR-2024, entry version 62.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=TSTA_019840 {ECO:0000313|EMBL:EED16924.1};
OS   Talaromyces stipitatus (strain ATCC 10500 / CBS 375.48 / QM 6759 / NRRL
OS   1006) (Penicillium stipitatum).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Trichocomaceae; Talaromyces;
OC   Talaromyces sect. Talaromyces.
OX   NCBI_TaxID=441959 {ECO:0000313|EMBL:EED16924.1, ECO:0000313|Proteomes:UP000001745};
RN   [1] {ECO:0000313|Proteomes:UP000001745}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10500 / CBS 375.48 / QM 6759 / NRRL 1006
RC   {ECO:0000313|Proteomes:UP000001745};
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: Splits internally a 1,3-beta-glucan molecule and transfers
CC       the newly generated reducing end (the donor) to the non-reducing end of
CC       another 1,3-beta-glucan molecule (the acceptor) forming a 1,3-beta
CC       linkage, resulting in the elongation of 1,3-beta-glucan chains in the
CC       cell wall. Involved in cell wall morphogenesis.
CC       {ECO:0000256|ARBA:ARBA00025026}.
CC   -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000256|ARBA:ARBA00004609,
CC       ECO:0000256|RuleBase:RU361209}; Lipid-anchor, GPI-anchor
CC       {ECO:0000256|ARBA:ARBA00004609, ECO:0000256|RuleBase:RU361209}.
CC   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR   EMBL; EQ962656; EED16924.1; -; Genomic_DNA.
DR   RefSeq; XP_002484158.1; XM_002484113.1.
DR   AlphaFoldDB; B8MEP1; -.
DR   STRING; 441959.B8MEP1; -.
DR   GeneID; 8108795; -.
DR   VEuPathDB; FungiDB:TSTA_019840; -.
DR   eggNOG; ENOG502QRZZ; Eukaryota.
DR   HOGENOM; CLU_021855_1_2_1; -.
DR   InParanoid; B8MEP1; -.
DR   OMA; TQEANDY; -.
DR   OrthoDB; 2783940at2759; -.
DR   PhylomeDB; B8MEP1; -.
DR   Proteomes; UP000001745; Unassembled WGS sequence.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0098552; C:side of membrane; IEA:UniProtKB-KW.
DR   GO; GO:0016740; F:transferase activity; IEA:UniProtKB-KW.
DR   Gene3D; 3.20.20.80; Glycosidases; 1.
DR   InterPro; IPR004886; Glucanosyltransferase.
DR   InterPro; IPR017853; Glycoside_hydrolase_SF.
DR   PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR   PANTHER; PTHR31468:SF4; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS3-RELATED; 1.
DR   Pfam; PF03198; Glyco_hydro_72; 1.
DR   SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE   3: Inferred from homology;
KW   Glycoprotein {ECO:0000256|RuleBase:RU361209};
KW   GPI-anchor {ECO:0000256|RuleBase:RU361209};
KW   Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW   Membrane {ECO:0000256|RuleBase:RU361209};
KW   Reference proteome {ECO:0000313|Proteomes:UP000001745};
KW   Signal {ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209, ECO:0000313|EMBL:EED16924.1}.
FT   SIGNAL          1..21
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           22..479
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5005124096"
FT   REGION          425..454
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   479 AA;  50806 MW;  F39BB88E12524455 CRC64;
     MVASYAKIFA AVCGLASTAA AVNPVTVQGK DFVDTVTGDR FQIVGVDYQP GGSSAFKGTA
     DPLSDKDSCL RDAAILQYLG INTIRVYNLA PSANHDECAS IFNAAGIYMI LDVNSPLDNG
     SLNRGAPWES YNPIYMAQVF GVIEAFKNYP NTAGFFSGNE VINEDSVELV PNYIRAVQRD
     MHDYISKNSN RSIPVGYSAA DVRPLLVDTA YYLSCNLSNS TNSRSDFFGL NSYSWCGDAT
     YHSSGYDVLT QDFANISMPV FFSETGCNNV KPRVFSEIQA IYGPDMSQAL SGALVYEYSQ
     EANDYGLVSI NSNGSVTLLI DFENLKSQYN KLDFGSITAH NSSQTSIKAP TCDPKQITSN
     ITKSFDVPDR VAGIDKMIQN GVTTNVSVGA LVSVSSTKIS QTVYDYKGNV VSGIQLNVLD
     KGAVNTPSNS STVTSSSPSG TSTGTSASAS STGKGAASSV RVNALTGLGA MAAVAFFAL
//
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