ID T5AP31_OPHSC Unreviewed; 484 AA.
AC T5AP31;
DT 13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT 13-NOV-2013, sequence version 1.
DT 13-SEP-2023, entry version 26.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=OCS_00125 {ECO:0000313|EMBL:EQL04166.1};
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:EQL04166.1, ECO:0000313|Proteomes:UP000019374};
RN [1] {ECO:0000313|EMBL:EQL04166.1, 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:EQL04166.1};
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 -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR EMBL; KE652176; EQL04166.1; -; Genomic_DNA.
DR AlphaFoldDB; T5AP31; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_1_2_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: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 Hydrolase {ECO:0000313|EMBL:EQL04166.1};
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..17
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 18..484
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005147266"
FT REGION 423..459
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 431..445
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 484 AA; 52956 MW; 275AB3D3F67BE7FF CRC64;
MLILSVLVAL VTTLVGAVPS LEVHGTDFVN PKTGNKFQIV GVAYQPGGSA GYDPRGRKDP
LSHADVCLRD AALLQVMGVN TIRVYNVDPN INHDECASIF NAAGIYLIID VNSPLVGEAI
TSFEPWTSYY MEYLNHTFAV VEAFSNYPNT LLYFSGNEVI NDLPSAKEVP PYLRAITRDL
KNYIKNNIER KIPVGYSAAD VREVLWDTWN FMQCSEDGSP DDMSRADVFA LNSYSWCGPG
ATYESSTFKV LTERFKKSSV PVFFSEYGCN KPTPRYWNET KAIYGEMADV FSGGVVYEWT
EEENGYGLVK VKGSELSIMG DYNRLKSQLS KIDWKSVQSQ SAAGDKEATS PPKCKSSLVL
EKGFKSNFTL PAVPPGAQTL IKNGIQPKPR GKIVNVSDYD VQMAVKGVSG LKVVPLNDDE
FNWAGKNEAD TGSDPDQRTD EGDQNTGGKD QGGASGSDKE DAAVLMRPLL WVAALPLVAM
AFLA
//
