ID T5AI41_OPHSC Unreviewed; 458 AA.
AC T5AI41;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=OCS_02033 {ECO:0000313|EMBL:EQL02249.1};
OS Ophiocordyceps sinensis (strain Co18 / CGMCC 3.14243) (Yarsagumba
OS caterpillar fungus) (Hirsutella sinensis).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Sordariomycetes;
OC Hypocreomycetidae; Hypocreales; Ophiocordycipitaceae; Ophiocordyceps.
OX NCBI_TaxID=911162 {ECO:0000313|EMBL:EQL02249.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL02249.1, ECO:0000313|Proteomes:UP000019374}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Co18 / CGMCC 3.14243 {ECO:0000313|Proteomes:UP000019374};
RC TISSUE=Fruit-body {ECO:0000313|EMBL:EQL02249.1};
RX DOI=10.1007/s11434-013-5929-5;
RA Hu X., Zhang Y., Xiao G., Zheng P., Xia Y., Zhang X., St Leger R.J.,
RA Liu X., Wang C.;
RT "Genome survey uncovers the secrets of sex and lifestyle in caterpillar
RT fungus.";
RL Chin. Sci. Bull. 58:2846-2854(2013).
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. {ECO:0000256|RuleBase:RU361209}.
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 Membrane {ECO:0000256|ARBA:ARBA00004589}; Lipid-anchor, GPI-anchor
CC {ECO:0000256|ARBA:ARBA00004589}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR EMBL; KE652332; EQL02249.1; -; Genomic_DNA.
DR AlphaFoldDB; T5AI41; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_0_1; -.
DR Proteomes; UP000019374; 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:0016787; F:hydrolase activity; 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:SF5; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS5; 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 Hydrolase {ECO:0000313|EMBL:EQL02249.1};
KW Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW Membrane {ECO:0000256|RuleBase:RU361209};
KW Reference proteome {ECO:0000313|Proteomes:UP000019374};
KW Signal {ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 19..458
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005147256"
FT REGION 390..432
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 395..417
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 458 AA; 49467 MW; AD60F576EFCFA2A2 CRC64;
MKQSALISAL VALGAVSASP TATEKEPPSK RATLPTVTAS GNAFWAGKER FYLRGIDYQP
GGSSADTDPL ADTKTCTRDI KKFKELGVNT IRVYAVDNSV KHDDCMKALE DAGIYLVLDV
NTPKYSINRV KPGPSYNTNY LQNVFATVEM FAQYRNTLAF FSGNEVINHQ KGTDEAAPFV
KAVTRDMKNY MNSRGLRRVP VGYSAADVSS NRLQTANYMN CGSDDMRSDF FAFNDYSWCN
SDYETSGWSE KVKTFAEYGL PIFLSEWGCQ QAGNQRITRK FDEVKAMMSE QMTSVYSGGL
MYEYSIEKND YGLVKISGDD VDTKGDYDEF KAFASALKDN PAPTGAGGAA STTHAVTCPT
KESNWNVDPS LVPAMPQKAE KFMKSGAGNG LGLKGAGSQD SSDSGTSTTS VTEGKPSPSS
GKKDDDSAGM SLQAGMDKAP MVVCGLTLLF TLFGAALL
//
