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Database: UniProt
Entry: I8A3C3_ASPO3
LinkDB: I8A3C3_ASPO3
Original site: I8A3C3_ASPO3 
ID   I8A3C3_ASPO3            Unreviewed;       457 AA.
AC   I8A3C3;
DT   03-OCT-2012, integrated into UniProtKB/TrEMBL.
DT   03-OCT-2012, sequence version 1.
DT   27-MAR-2024, entry version 36.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=Ao3042_04190 {ECO:0000313|EMBL:EIT79427.1};
OS   Aspergillus oryzae (strain 3.042) (Yellow koji mold).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Circumdati.
OX   NCBI_TaxID=1160506 {ECO:0000313|EMBL:EIT79427.1, ECO:0000313|Proteomes:UP000002812};
RN   [1] {ECO:0000313|EMBL:EIT79427.1, ECO:0000313|Proteomes:UP000002812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3.042 {ECO:0000313|EMBL:EIT79427.1,
RC   ECO:0000313|Proteomes:UP000002812};
RX   PubMed=22933657; DOI=10.1128/EC.00160-12;
RA   Zhao G., Yao Y., Qi W., Wang C., Hou L., Zeng B., Cao X.;
RT   "Draft genome sequence of Aspergillus oryzae strain 3.042.";
RL   Eukaryot. Cell 11:1178-1178(2012).
RN   [2] {ECO:0000313|Proteomes:UP000002812}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=3.042 {ECO:0000313|Proteomes:UP000002812};
RA   Zhao G., Hou L., Wang C., Cao X.;
RT   "Comparative genomic analyses of Aspergillus oryzae 3.042 and A. oryzae
RT   RIB40 for soy-sauce fermentation.";
RL   Submitted (JUN-2012) 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:EIT79427.1}.
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DR   EMBL; AKHY01000127; EIT79427.1; -; Genomic_DNA.
DR   AlphaFoldDB; I8A3C3; -.
DR   HOGENOM; CLU_021855_0_0_1; -.
DR   Proteomes; UP000002812; 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:SF8; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS2; 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   Signal {ECO:0000256|RuleBase:RU361209};
KW   Transferase {ECO:0000256|RuleBase:RU361209, ECO:0000313|EMBL:EIT79427.1}.
FT   SIGNAL          1..18
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT   CHAIN           19..457
FT                   /note="1,3-beta-glucanosyltransferase"
FT                   /evidence="ECO:0000256|RuleBase:RU361209"
FT                   /id="PRO_5005136333"
FT   REGION          354..427
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        354..369
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        396..427
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   457 AA;  49618 MW;  87739B920235C172 CRC64;
     MRPLSTVSAL AWLGGFQALP VNAIQTISTV GSKFFHEDGT QYFLKGIAYQ LIPDDPLVDT
     AQCKRDFALM AELGTNAIRV YHVDPKANHD GCMEALAAAG IYLFVDLDTF DTSINQDKPQ
     WTHSQFERYK AVLDEFQKYN NTAGVFVGNE VINTKEGSAA APYVLAAAHD IKSYRNEKGY
     RNIPVGYSAA DIAELRPMLQ NYLACRPDSA DRLDFFSLNA YEWCGPSSYE TSGYKRLQSQ
     ASDYPIPIFF SETGCNAARP RTFEDQAAIF GPEMANTWSG SMIYEWIQEA NDYGLIKYGP
     PSGASPDKML VQDGFPRQGE PIPVDPDFHN LKAQWARLRP TGVALSDYIK STSSIKPASC
     PTSTPGGWAV DSHQPLPTLQ RATSDVAAAG PNPGSGSGPD SGSRPEQLSA RVTSVAPSDY
     HSSRAVNGAS AGTRGFDRLA GGSLFLCMLI GALALWL
//
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