GenomeNet

Database: UniProt
Entry: M3J3Y9_CANMX
LinkDB: M3J3Y9_CANMX
Original site: M3J3Y9_CANMX 
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
//
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