ID A0A0D2BR77_9EURO Unreviewed; 451 AA.
AC A0A0D2BR77;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=PV06_08526 {ECO:0000313|EMBL:KIW39967.1};
OS Exophiala oligosperma.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Chaetothyriomycetidae; Chaetothyriales; Herpotrichiellaceae; Exophiala.
OX NCBI_TaxID=215243 {ECO:0000313|EMBL:KIW39967.1, ECO:0000313|Proteomes:UP000053342};
RN [1] {ECO:0000313|EMBL:KIW39967.1, ECO:0000313|Proteomes:UP000053342}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 72588 {ECO:0000313|EMBL:KIW39967.1,
RC ECO:0000313|Proteomes:UP000053342};
RG The Broad Institute Genomics Platform;
RA Cuomo C., de Hoog S., Gorbushina A., Stielow B., Teixiera M.,
RA Abouelleil A., Chapman S.B., Priest M., Young S.K., Wortman J., Nusbaum C.,
RA Birren B.;
RT "The Genome Sequence of Exophiala oligosperma CBS72588.";
RL Submitted (JAN-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. {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; KN847339; KIW39967.1; -; Genomic_DNA.
DR RefSeq; XP_016260183.1; XM_016409875.1.
DR AlphaFoldDB; A0A0D2BR77; -.
DR STRING; 215243.A0A0D2BR77; -.
DR GeneID; 27360600; -.
DR VEuPathDB; FungiDB:PV06_08526; -.
DR HOGENOM; CLU_021855_1_0_1; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000053342; 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: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 Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW Membrane {ECO:0000256|RuleBase:RU361209};
KW Reference proteome {ECO:0000313|Proteomes:UP000053342};
KW Signal {ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209, ECO:0000313|EMBL:KIW39967.1}.
FT SIGNAL 1..18
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 19..451
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005112402"
FT REGION 369..419
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 384..419
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 451 AA; 47695 MW; 9CFB29FFE5E33FD2 CRC64;
MRTSTIAALA LGAGVASAAT VKRASSITSV TVKGNAFFAG NDRFYIRGVD YQPGGSSNVA
DPIADVDGCK RDIAEFKKLG LNTIRVYTVD NTANHDECMS ALADAGIYLV LDVNTPKYSL
NRADPNPSYN DVYLQSIFAT IDDFQKYDNV LAFFSGNEVI NDPESSAAAP YVKAVTRDMR
QYIRNRGYRT IPVGYSAADV SENRLEMAEY MNCGTSDERS DFFAFNDYSW CDPSSFTQSG
WDQKVKNFTG YGLPLFLSEY GCNTNTREFQ EVESLYSTQM TGVYSGGLVY EYSQEPSNYG
LVEINGNSVS ELPDFSALQS QFSKTPNPQG DGGYNSTGGA SGCPAYNNPN WLVKTDALPA
IPEGAKKFMT SGAGKGPGLS GAGSQNAGGA STGTATAGSG QASQTGSSSG GSSTSSSTNG
AIAMAVPEWS FAPMVCGAVL VMSSLFGATL L
//
