ID A0A094A899_9PEZI Unreviewed; 531 AA.
AC A0A094A899;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 13-SEP-2023, entry version 27.
DE RecName: Full=1,3-beta-glucanosyltransferase {ECO:0000256|RuleBase:RU361209};
DE EC=2.4.1.- {ECO:0000256|RuleBase:RU361209};
GN ORFNames=V493_07979 {ECO:0000313|EMBL:KFY19390.1};
OS Pseudogymnoascus sp. VKM F-4281 (FW-2241).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Leotiomycetes;
OC Leotiomycetes incertae sedis; Pseudeurotiaceae; Pseudogymnoascus.
OX NCBI_TaxID=1420906 {ECO:0000313|EMBL:KFY19390.1, ECO:0000313|Proteomes:UP000029327};
RN [1] {ECO:0000313|EMBL:KFY19390.1, ECO:0000313|Proteomes:UP000029327}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=VKM F-4281 (FW-2241) {ECO:0000313|Proteomes:UP000029327};
RA Leushkin E.V., Logacheva M.D., Penin A.A., Sutormin R.A., Gerasimov E.S.,
RA Kochkina G.A., Ivanushkina N.E., Vasilenko O.V., Kondrashov A.S.,
RA Ozerskaya S.M.;
RT "Population genomics of a fungus Geomyces pannorum provides evidence of
RT horizontal gene transfer but not of sexual reproduction.";
RL Submitted (JUL-2014) 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|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:KFY19390.1}.
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DR EMBL; JPJV01003554; KFY19390.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A094A899; -.
DR STRING; 1420906.A0A094A899; -.
DR HOGENOM; CLU_021855_2_1_1; -.
DR OrthoDB; 2783940at2759; -.
DR Proteomes; UP000029327; 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:UP000029327};
KW Signal {ECO:0000256|ARBA:ARBA00022729, ECO:0000256|RuleBase:RU361209};
KW Transferase {ECO:0000256|RuleBase:RU361209}.
FT SIGNAL 1..26
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT CHAIN 27..531
FT /note="1,3-beta-glucanosyltransferase"
FT /evidence="ECO:0000256|RuleBase:RU361209"
FT /id="PRO_5005107347"
FT DOMAIN 384..473
FT /note="X8"
FT /evidence="ECO:0000259|SMART:SM00768"
FT REGION 482..502
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 487..502
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 531 AA; 56568 MW; 27E29B1CEDAF2294 CRC64;
MKSFSLASAA ATAFAGAALL VSSVKAEVDP IVIKGSHFFY KTNGTEFFIK GIAYQQEAPA
NGSDSATTKI TDPLADIESC KRDVPLLAEL GTNVIRVYAI DPEKDHKECM TLLENAGIYV
IQDLSNPQNS IERDNPAWTT SIFEGYAAVI DEMQQFSNTL GFFAGNEVSN QANNTNASAF
VKASVRDSKA YIKAKGYRQI GVGYATNDDA EIRDDLADYF NCGPAEQSID FWGYNIYSWC
GKSSFQKSGF DVRTKEFKDY NVPVFFAEYG CNDPSPRVFT EVEAIYGPQM TDVWSGGIVY
MYFQEANNYG LVKVDGDNVK KLKDFSVLAS QVAKATPSVK TMSAYTPTNT AARTCPDVNA
GWAASSVLPP IANSKVCDCM VKSLKCKAKA DISGEDIATQ FDYVCGEDAK ACNGFAANAT
TGKYGAYSMC SAEQKLSFAF DQYFQAQGSA STACDFSGNG ETQAGSNEGD CTALLEAAGK
DGSGTVNDVP TEGSTGEGSG DNDNAAGSLA AFSMGSYVVA AMLAGLGMVL L
//
