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Database: UniProt
Entry: A0A0J8QR10_COCIT
LinkDB: A0A0J8QR10_COCIT
Original site: A0A0J8QR10_COCIT 
ID   A0A0J8QR10_COCIT        Unreviewed;       102 AA.
AC   A0A0J8QR10;
DT   14-OCT-2015, integrated into UniProtKB/TrEMBL.
DT   14-OCT-2015, sequence version 1.
DT   27-MAR-2024, entry version 21.
DE   RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE            EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN   ORFNames=CISG_04242 {ECO:0000313|EMBL:KMU74535.1};
OS   Coccidioides immitis RMSCC 3703.
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Onygenales; Onygenaceae; Coccidioides.
OX   NCBI_TaxID=454286 {ECO:0000313|EMBL:KMU74535.1, ECO:0000313|Proteomes:UP000054559};
RN   [1] {ECO:0000313|Proteomes:UP000054559}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RMSCC 3703 {ECO:0000313|Proteomes:UP000054559};
RX   PubMed=20516208; DOI=10.1101/gr.103911.109;
RA   Neafsey D.E., Barker B.M., Sharpton T.J., Stajich J.E., Park D.J.,
RA   Whiston E., Hung C.-Y., McMahan C., White J., Sykes S., Heiman D.,
RA   Young S., Zeng Q., Abouelleil A., Aftuck L., Bessette D., Brown A.,
RA   FitzGerald M., Lui A., Macdonald J.P., Priest M., Orbach M.J.,
RA   Galgiani J.N., Kirkland T.N., Cole G.T., Birren B.W., Henn M.R.,
RA   Taylor J.W., Rounsley S.D.;
RT   "Population genomic sequencing of Coccidioides fungi reveals recent
RT   hybridization and transposon control.";
RL   Genome Res. 20:938-946(2010).
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   -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC       {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR   EMBL; DS268136; KMU74535.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0J8QR10; -.
DR   STRING; 454286.A0A0J8QR10; -.
DR   Proteomes; UP000054559; 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:SF4; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS3-RELATED; 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:UP000054559};
KW   Transferase {ECO:0000256|RuleBase:RU361209}.
SQ   SEQUENCE   102 AA;  11862 MW;  101DC495EEF40D87 CRC64;
     MKSISKLQIS RPSLAAVHRL CRHPHRGSRI AVRQQQDQRS LPDHWRRVNT IRIYNLSPNV
     NHDECVSIFN AAGIYLLVDV NNPDYGQHIN RETLRQPTTR DT
//
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