ID M3J3Y9_CANMX Unreviewed; 489 AA.
AC M3J3Y9;
DT 01-MAY-2013, integrated into UniProtKB/TrEMBL.
DT 01-MAY-2013, sequence version 1.
DT 24-JAN-2024, entry version 32.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
DE Flags: Fragment;
GN ORFNames=G210_3094 {ECO:0000313|EMBL:EMG46643.1};
OS Candida maltosa (strain Xu316) (Yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Saccharomycotina; Saccharomycetes;
OC Saccharomycetales; Debaryomycetaceae; Candida/Lodderomyces clade; Candida.
OX NCBI_TaxID=1245528 {ECO:0000313|EMBL:EMG46643.1, ECO:0000313|Proteomes:UP000011777};
RN [1] {ECO:0000313|EMBL:EMG46643.1, ECO:0000313|Proteomes:UP000011777}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Xu316 {ECO:0000313|Proteomes:UP000011777};
RA Yu J., Wang Q., Geng X., Bao W., He P., Cai J.;
RT "Genome sequence of Candida maltosa Xu316, a potential industrial strain
RT for xylitol and ethanol production.";
RL Submitted (FEB-2013) 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|RuleBase:RU361209};
CC Lipid-anchor, GPI-anchor {ECO:0000256|RuleBase:RU361209}. Membrane
CC {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}.
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:EMG46643.1}.
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DR EMBL; AOGT01001924; EMG46643.1; -; Genomic_DNA.
DR AlphaFoldDB; M3J3Y9; -.
DR STRING; 1245528.M3J3Y9; -.
DR eggNOG; ENOG502QRZZ; Eukaryota.
DR HOGENOM; CLU_021855_2_0_1; -.
DR OMA; HECMSAL; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000011777; 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; 1.20.58.1040; -; 1.
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:SF10; 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|ARBA:ARBA00022622,
KW ECO:0000256|RuleBase:RU361209};
KW GPI-anchor {ECO:0000256|ARBA:ARBA00022622, ECO:0000256|RuleBase:RU361209};
KW Lipoprotein {ECO:0000256|RuleBase:RU361209};
KW Membrane {ECO:0000256|RuleBase:RU361209};
KW Reference proteome {ECO:0000313|Proteomes:UP000011777};
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..489
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005140332"
FT REGION 420..476
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..442
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 443..467
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:EMG46643.1"
SQ SEQUENCE 489 AA; 55775 MW; 70F899C3560BE930 CRC64;
MLFLILILII FIQSVSCQIT IAGNKFFESD NQFFIKGIAY QKSRQEGEVY DTSKEPHYID
PLANPFTCLR DLEYLKELGV NVVRVYQISP TANHDVCMEA FGEAGIYVLA DLSEPYMSIR
RDYPHWDTEL FGRYKDVVDA MHKYDNMMGF FAGNEVTNSP SNMDASPYVR AAIRDTKKYI
ADKGYRNIPV GYASNDDASI RGELANYFTC GDEGRADFFA INVYEWCGYS TYTTSGYRDL
TLAFKGYPVP VFFSEFGCNI ISPRPFTEID TIYGSTMTKV WSGGIVYEYF EEVNHYGVVQ
AKPDGQVSKL PDFDTLKQKY NSVTPVGITI DEAGDTEYVE CTNEFVLPPT PDEDKCECLW
KKLSCVIRGD FDEESVLKDL CFKVDCAELT GNYSDCSPKV RVSYALSKYA NGRKDVCEER
GELREAEEEH GEEEEEEVPH KDEQQQEEEN EENEVPKKGK EKFPKENPSS RSGSYATSLN
NFYWLALFI
//