ID A0A0F4YL45_TALEM Unreviewed; 479 AA.
AC A0A0F4YL45;
DT 24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT 24-JUN-2015, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=T310_7734 {ECO:0000313|EMBL:KKA18313.1};
OS Rasamsonia emersonii CBS 393.64.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Trichocomaceae; Rasamsonia.
OX NCBI_TaxID=1408163 {ECO:0000313|EMBL:KKA18313.1, ECO:0000313|Proteomes:UP000053958};
RN [1] {ECO:0000313|EMBL:KKA18313.1, ECO:0000313|Proteomes:UP000053958}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 393.64 {ECO:0000313|EMBL:KKA18313.1,
RC ECO:0000313|Proteomes:UP000053958};
RA Heijne W.H., Fedorova N.D., Nierman W.C., Vollebregt A.W., Zhao Z., Wu L.,
RA Kumar M., Stam H., van den Berg M.A., Pel H.J.;
RL Submitted (APR-2015) to the EMBL/GenBank/DDBJ databases.
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}.
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:KKA18313.1}.
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DR EMBL; LASV01000469; KKA18313.1; -; Genomic_DNA.
DR RefSeq; XP_013324925.1; XM_013469471.1.
DR AlphaFoldDB; A0A0F4YL45; -.
DR GeneID; 25320000; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000053958; 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:UP000053958};
KW Signal {ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209, ECO:0000313|EMBL:KKA18313.1}.
FT SIGNAL 1..20
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 21..479
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005117166"
FT REGION 420..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 479 AA; 51481 MW; 764CBF55AB684D7E CRC64;
MPSYSRLFAA LCGLATTAVA VNPLIVDGKD FVDSVTKDRF QIIGVDYQPG GSSGFSGDSD
PLSDKASCLR DAALMQRLGI NTIRVYNLAT NVSHDDCASI FNAAGIYMLL DVNSPLPNGS
LDRTAPWTTY DLDYLQRIFS VVEAFKNYPN TLGFFAGNEV INEQSTKEVP AYIRAVQRDL
KDYIAKNVQR PIPVGYSAAD VRDILVDTAN YMSCEISNAT SSRSDFFGLN SYSWCGDSSY
TKSGYDVLTA DFANASLPAF FSEYGCNLVE PRVFTEVQAL YGEDMTQAFS GGLVYEWTQE
ANNYGLVQIN DNNTVTLLID YDNLQKQFDK IDVKRIESSN TTQTSVKPVP CSADLITGNF
LNTFDLPARP QGVDDLIQNG VKGATVGKLV SVSSQEIPNT VYDYTGKVIS GIRLNALQNN
EVNTPGSNTS GSSSDGNGTS SATGTAASAT HTGAASRQHS SGVLSTFGAV VALAVSLAW
//
