ID G3Y7R0_ASPNA Unreviewed; 533 AA.
AC G3Y7R0;
DT 14-DEC-2011, integrated into UniProtKB/TrEMBL.
DT 14-DEC-2011, sequence version 1.
DT 27-MAR-2024, entry version 44.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=ASPNIDRAFT_50757 {ECO:0000313|EMBL:EHA21355.1};
OS Aspergillus niger (strain ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 /
OS NCTC 3858a / NRRL 328 / USDA 3528.7).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=380704 {ECO:0000313|EMBL:EHA21355.1, ECO:0000313|Proteomes:UP000009038};
RN [1] {ECO:0000313|EMBL:EHA21355.1, ECO:0000313|Proteomes:UP000009038}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 1015 / CBS 113.46 / FGSC A1144 / LSHB Ac4 / NCTC 3858a /
RC NRRL 328 / USDA 3528.7 {ECO:0000313|Proteomes:UP000009038};
RX PubMed=21543515; DOI=10.1101/gr.112169.110;
RA Andersen M.R., Salazar M.P., Schaap P.J., van de Vondervoort P.J.,
RA Culley D., Thykaer J., Frisvad J.C., Nielsen K.F., Albang R., Albermann K.,
RA Berka R.M., Braus G.H., Braus-Stromeyer S.A., Corrochano L.M., Dai Z.,
RA van Dijck P.W., Hofmann G., Lasure L.L., Magnuson J.K., Menke H.,
RA Meijer M., Meijer S.L., Nielsen J.B., Nielsen M.L., van Ooyen A.J.,
RA Pel H.J., Poulsen L., Samson R.A., Stam H., Tsang A., van den Brink J.M.,
RA Atkins A., Aerts A., Shapiro H., Pangilinan J., Salamov A., Lou Y.,
RA Lindquist E., Lucas S., Grimwood J., Grigoriev I.V., Kubicek C.P.,
RA Martinez D., van Peij N.N., Roubos J.A., Nielsen J., Baker S.E.;
RT "Comparative genomics of citric-acid-producing Aspergillus niger ATCC 1015
RT versus enzyme-producing CBS 513.88.";
RL Genome Res. 21:885-897(2011).
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:EHA21355.1}.
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DR EMBL; ACJE01000015; EHA21355.1; -; Genomic_DNA.
DR AlphaFoldDB; G3Y7R0; -.
DR STRING; 380704.G3Y7R0; -.
DR VEuPathDB; FungiDB:ASPNIDRAFT2_1220663; -.
DR HOGENOM; CLU_021855_2_1_1; -.
DR Proteomes; UP000009038; 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:0042123; F:glucanosyltransferase activity; IEA:UniProt.
DR GO; GO:0071840; P:cellular component organization or biogenesis; IEA:UniProt.
DR GO; GO:0071852; P:fungal-type cell wall organization or biogenesis; IEA:UniProt.
DR Gene3D; 1.20.58.1040; -; 1.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR004886; Glucanosyltransferase.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR InterPro; IPR012946; X8.
DR PANTHER; PTHR31468:SF9; 1,3-BETA-GLUCANOSYLTRANSFERASE; 1.
DR PANTHER; PTHR31468; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR Pfam; PF03198; Glyco_hydro_72; 1.
DR Pfam; PF07983; X8; 1.
DR SMART; SM00768; X8; 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, ECO:0000256|SAM:Phobius};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209};
KW Transmembrane {ECO:0000256|SAM:Phobius};
KW Transmembrane helix {ECO:0000256|SAM:Phobius}.
FT SIGNAL 1..17
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 18..533
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005132110"
FT TRANSMEM 511..532
FT /note="Helical"
FT /evidence="ECO:0000256|SAM:Phobius"
FT DOMAIN 370..458
FT /note="X8"
FT /evidence="ECO:0000259|SMART:SM00768"
FT REGION 466..490
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 533 AA; 56707 MW; 64561213E6754D2B CRC64;
MKLSLAVGAA LMGSALAVDI DPIVIKGSKF FYSSNNTQFY IRDDYTGNSS SGYTDPLANP
TLCKRDIPIL QELNTNVIRV YAIDPTKDHT TCMNLLAAAG IYVISDLSDP TQSIDRSDPT
WETSLYTRYT NVIDELIQYN NTLAFFAGNE VSNDVATTDA SAFVKAAVRD MKAYIKSQGY
RSIGVGYATN DDSDIRVNMA DYFNCGSEDE SIDFWGYNIY SWCGDSSYTK SGYDERTEEF
RNYSVPVFFS EYGCNTVQPR KFTDIKALFG DQMNDVWSGG IVYMYFQTDN DYGLVSAIDS
TSVSKLADFT YYSSQIASAT PSGTNKASYT PTNTALQSCP AVTSKSWLAT SSPLPPTPNQ
ELCTCMDNAS GCVVKDSVSS SDYDDLFSTV CGFTSCDGIF HNGTTGTYGA YSMCGAKQQL
NFVLDKYWKE QGKKADACGF DGSATTTATV KATGTCSALM KEAGTAGTGT VTSKPTGTAA
GSSSASGTGG VSAVGSVGSA SLGKGSAIIS IGAWQVGAYV VTGVVAGLGM VLL
//
