ID V5EY72_KALBG Unreviewed; 569 AA.
AC V5EY72;
DT 22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT 22-JAN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=PSEUBRA_SCAF2g02697 {ECO:0000313|EMBL:EST07604.1};
OS Kalmanozyma brasiliensis (strain GHG001) (Yeast) (Pseudozyma brasiliensis).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Kalmanozyma.
OX NCBI_TaxID=1365824 {ECO:0000313|EMBL:EST07604.1, ECO:0000313|Proteomes:UP000019377};
RN [1] {ECO:0000313|Proteomes:UP000019377}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=GHG001 {ECO:0000313|Proteomes:UP000019377};
RX PubMed=24356824; DOI=10.1128/genomea.00920-13;
RA Oliveira J.V.D.C., dos Santos R.A.C., Borges T.A., Riano-Pachon D.M.,
RA Goldman G.H.;
RT "Draft genome sequence of Pseudozyma brasiliensis sp. nov. strain GHG001, a
RT high producer of endo-1,4-xylanase isolated from an insect pest of
RT sugarcane.";
RL Genome Announc. 1:E0092013-E0092013(2013).
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}.
CC -!- SIMILARITY: Belongs to the glycosyl hydrolase 72 family.
CC {ECO:0000256|ARBA:ARBA00007528, ECO:0000256|RuleBase:RU361209}.
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DR EMBL; KI545862; EST07604.1; -; Genomic_DNA.
DR RefSeq; XP_016292593.1; XM_016437094.1.
DR AlphaFoldDB; V5EY72; -.
DR STRING; 1365824.V5EY72; -.
DR GeneID; 27419766; -.
DR eggNOG; ENOG502QPST; Eukaryota.
DR HOGENOM; CLU_021855_2_2_1; -.
DR OMA; CMYDASA; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000019377; 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; 1,3-BETA-GLUCANOSYLTRANSFERASE GAS1; 1.
DR PANTHER; PTHR31468:SF2; 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};
KW Reference proteome {ECO:0000313|Proteomes:UP000019377};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209}.
FT SIGNAL 1..28
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 29..569
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005148743"
FT DOMAIN 402..496
FT /note="X8"
FT /evidence="ECO:0000259|SMART:SM00768"
FT REGION 511..542
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 569 AA; 59157 MW; 0D5A916674D985B2 CRC64;
MARHPLRPLG FLFALLGLIA LLAQPSSAIP SVTRRGKYLY QGSNRFYVKG VAYQEPAPVA
ASTAANDANG GFPEPDSFTD PLALPDACTR DVANFRDLGI NTIRVYSVNA SLNHDSCMST
FSNAGIYVIL DLALPLNGSI NRAEPSWDVG LLNLYATTID VFTRYDNLLA VNIANEVVTQ
SSNADSAPFI KAAVRDVKAY LQSKNSNVLV SYSSTDGANG VNQWRDQLAY YLTCGSAATS
IDLYGLNSYS WCGQSSYAQS GYNLLTSDLA DLPVPAYLAE FGCVEGVGTG NRPWTEVAAL
YSSPMTDTFS GGVAFSYFPQ SSGLDYGLVS VSGNSVSTRG DWTALKNAFA ATSSAPTSAP
AGASSNPSYP TCRGNTANFP ASTTLPPTPN PELCDCIESS AFSCALTTDA FNSPNIIGVL
TGQACMYLGE QGGSCASILA DGQTGTYGNY SGCSAGQRLE WAMSRYYEVT GFNAVSCDFA
GNGTVRAPPP GNQTSIRNAY QTCLGQNPVG VTTPRPDVSG SVNSTATGAA PTTSQTGTGG
NANSATSGAG VMGGMLMALA LAVAGWCIV
//
